UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
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B2U3C9
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MMVIRPVERSDVSALMQLASKTGGGLTSLPANEATLSARIERAIKTWQGELPKSEQGYVFVLEDSETGTVAGICAIEVAVGLNDPWHNYRVGTLVHASKELNVYNALPTLFLSNDHTGSSELCTLFLDPDWRKEGNGYLLSKSRFMFMAAFRDKFNDKVVAEMRGVIDEHGYSPFWQSLGKRFFSMDFSRADFLCGTGQKAFIAELMPKHPIYTHFLSQEAQDVIGQVHPQTAPARAVLEKEGFRYRNYIDIFDGGPTLECDIDRVRAIRKSRLVEVAEGQPAQGDFPACLVANENYHHFRVVLARTDPATERLILTAAQLDALKCHAGERVRLVRLCAVEKTA
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Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. Belongs to the arginine N-succinyltransferase family.
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Q321N9
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MMVIRPVERSDVSALMQLASKTGGGLTSLPANEATLSARIERAIKTWQGELPKSEQGYVFVLEDSETGTVAGICAIEVAVGLNDPWHNYRVGTLVHASKELNVYNALPTLFLSNDHTGSSELCTLFLDPDWRKEGNGYLLSKSRFMFMAAFRDKFNDKVVAEMRGVIDEHGYSPFWQSLGKRFFSMDFSRADFLCGTGQKAFIAELMPKHPIYTHFLSQEAQDVIGQVHPQTAPARAVLEKEGFRYRNYIDIFDGGPTLECDIDRVRAIRKSRLVEVAEGQPAQGDFPACLVANENYHHFRVVLARTDPATERLILTAAQLDALKCHAGDRVRLVRLCAVEKTA
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Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. Belongs to the arginine N-succinyltransferase family.
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Q32G89
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MMVIRSVERSDVSALMQLASKTGGGLTSLPANEATLSARIERAIKTWQGELPKSEQGYVFVLEDSETGTVAGICAIEVAVGLNDPWYNYRVGTLVHASKELNVYNALPTLFLSNDHTGSSELCTLFLDPDWRKEGNGYLLSKSRFMFMAAFRDKFNDKVVAEMRGVIDEHGYSPFWQSLGKRFFSMDFSRADFLCGTGQKAFIAELMPKHPIYTHFLSQEAQDVIGQVHPQTAPARAVLEKEGFRYRNYIDIFDGGPTLECDIDRVRAIRKSRLVEVAEGQPAQGDFPACLVANENYHHFRVVLVRTDPATERLILTAAQLDALKCHAGDRVRLVRLCAEEKTA
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Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. Belongs to the arginine N-succinyltransferase family.
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Q0T4V4
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MMVIRPVERSDVSALMQLASKTGDGLTSLPANEATLSARIERAIKTWQGELPKSEQGYVFVLEDSETGTVPGICAIEVAVGLNDPWYNYRVGTLVHASKELNVYNALPTLFLSNDHTGSSELCTLFLDPDWRKEGNGYLLSKSRFMFMAAFRDKFNDKVVAEMRGVIDEHGYSPFWQSLGKRFFSMDFSRADFLCGTGQKAFIAELMPKHPIYTHFLSQEAQDVIGQVHPQTAPARAVLEKEGFRYRNYIDIFDGGPTLECDIDRVRAIRKSRLVEVAEGQPAQGDFPACLVANENYHHFRVVLARTDPATERLILTAAQLDALKCHAGDRVRLVRLCAEEKTA
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Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. Belongs to the arginine N-succinyltransferase family.
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Q7UCI8
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MMVIRPVERSDVSALMQLASKTGGGLTSLPANEATLSARIERAIKTWQGELPKSEQGYVFVLEDSETGTVAGICAIEVAVGLNDPWYNYRVGTLVHASKELNVYNALPTLFLSNDHTGSSELCTLFLDPDWRKEGNGYLLSKSRFMFMAAFRDKFNDKVVAEMRGVIDEHGYSPFWQSLGKRFFSMDFSRADFLCGTGQKAFIAELMPKHPIYTHFLSQEAQDVIGQVHPQTAPARAVLEKEGFRYRNYIDIFDGGPTLECDIDRVRAIRKSRLVEVAEGQPAQGDFPACLVANENYHHFRVVLARTDPATERLILTAAQLDALKCHAGDRVRLVRLCAEEKTA
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Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. Belongs to the arginine N-succinyltransferase family.
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Q3Z294
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MMVIRPVERSDVSALMQLASKTGGGLTSLPANEATLSARIERAIKTWQGELPKSEQGYVFVLEDSETGTVAGICAIEVAVGLNDPWYNYRVGTLVHASKELNVYNALPTLFLSNDHTGSSELCTLFLDPDWRKEGNGYLLSKSRFMFMAAFRDKFNDKVVAEMRGVIDEHGYSPFWQSLGKRFFSMDFSRVDFLCGTGQKAFIAELMPKHPIYTHFLSQEAQDVIGQVHPQTAPARAVLEKEGFRYRNYIDIFDGGPTLECDIDRVRAIRKSRLVEVAEGQPAQGDFPACLVANENYHHFRVVLARTDPATERLILTAAQLDALKCHAGDRVRLVRLCAEEKTA
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Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. Belongs to the arginine N-succinyltransferase family.
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A0A3Q9FEJ4
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MEQREIILLGLAALAVTYQVIVWIYNAWFHPLSGYPGPKLFGASYLPGLYHRIRGDYVLVHTALHERFGEVIRVSPNELSYINPQAWKDITGQGSGRQDMEKDPLSFGRPMPNAPSIFNAHRMDHSRIRRTMSHAFSASALRRQESLIQSHVKMMIQCLREHNEEVVDMVSWYNFTTFDMFGDLAFGESFGCLTNSLYHPWVKMLIMSMKAGYFIIQAQKYPIFEKVLMSFIPRMMRQRRRDHLALTQAKLAKRMAKPEERPDFLSFILRHQDEATGMSLPELEINASTLIVAGSETTATLLSGCTYYLLRNPRVMEKLLNEVRTTFKSEDEIDITTVNGLKYMLAVLDEALRVYPPAPGNFHRLVPKEGSVICEKFVPGETQVSVCHYAAYHSPCNFHQPDEFIPERFLGESKFENDRRDVLQPFGTGSRACLGRNLAYFEMRLILTHVLWNFDLELMPQSKYWANQKVFAIWDKPELYVKLKPRAGLEVRA
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Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the asperterpenoids, sesterterpenes that exhibit anti-tuberculosis activity (PubMed:30548032). The first step of the pathway is performed by the sesterterpene synthase astC that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and further converting GFPP into preasperterpenoid A, respectively (PubMed:30548032). The cytochrome P450 monooxygenase astB then dually oxidizes preasperterpenoid A to produce asperterpenoid A along with a minor product, asperterpenoid B (PubMed:30548032). Finally, the cytochrome P450 monooxygenase astA converts asperterpenoid A into asperterpenoid C (PubMed:30548032). asperterpenoid A + O2 + reduced [NADPH--hemoprotein reductase] = asperterpenoid C + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] Secondary metabolite biosynthesis; terpenoid biosynthesis. Asperterpenoids A and B, but not the final product asperterpenoid C, exhibit potent inhibitory activity against Mycobacterium tuberculosis protein tyrosine phosphatase B with IC(50) values of 3 to 6 uM. Belongs to the cytochrome P450 family.
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A1JS43
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MMRVRPVERRDLADILELAGKTGVGMTSLPQNEQHLAARIERALNTWQGSLAVGEQGYLFVLEDTEREKVVGVSAIEVAVGMNDPWYNFRVGTLVHASKTLNVYKSVPTLFLSNDHTGYSELCTLFLDPEYRKDKNGPFLSKVRFLFIAAFRQHFSRKLIAEMRGYTDEQGRSPFWENVGRHFFSIEFAKADYLSGTGQKAFIAELMPKHPLYVDFLAEEARAVIGQVHPHTAPARAVLETEGLQYQGYVDIFDGGPTLEANTDEVRAVRDSSQRKVVIDDIDIDPSGSAYLVANDRYQEFRSILINTHLSDEFLHLTPDNAAALGVVAGDVVRIISLFAPETKK
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Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. Belongs to the arginine N-succinyltransferase family.
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Q1C8B0
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MMKVRPVERRDLADIFELAGKTGVGMTSLPQNEQHLAARIERALNTWQGSLDPGEQGYLFVLEDSEQQKVVGVSAIEVAVGLNDPWYNFRVGTLVHASKALNVYKSVPTLFLSNDHTGYSELCTLFLDPDYRKDKNGPFLSKVRFLFIAAFRQYFSRKVIAEMRGYTDEQGRSPFWESVGRHFFSIEFAKADYLSGTGQKAFIAELMPKHPLYVDFLAEEARAVIGQVHPHTAPARAVLETEGLQYQGYVDIFDGGPTLEANTDDVRVVRDSSKRTVVIKDYDIEDYDIDPNGRLYLVANDHYHHFRAILMNTHLSDERLRLTPESAEALGVAAGDSVRIVSLFAPETKR
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Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. Belongs to the arginine N-succinyltransferase family.
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B2K295
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MMKVRPVERRDLADIFELAGKTGVGMTSLPQNEQHLAARIERALNTWQGSLDPGEQGYLFVLEDSEQQKVVGVSAIEVAVGLNDPWYNFRVGTLVHASKALNVYKSVPTLFLSNDHTGYSELCTLFLDPDYRKDKNGPFLSKVRFLFIAAFRQYFSRKVIAEMRGYTDEQGRSPFWESVGRHFFSIEFAKADYLSGTGQKAFIAELMPKHPLYVDFLAEEARAVIGQVHPHTAPARAVLETEGLQYQGYVDIFDGGPTLEANTDDVRAVRDSSKRTVVIKDYDIEDYDIDPNGRLYLVANDHYHHFRAILMNTHLSDERLRLTPESAEALGVAAGDSVRIVSLFAPETKR
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Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. Belongs to the arginine N-succinyltransferase family.
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Q7CI71
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MMKVRPVERRDLADIFELAGKTGVGMTSLPQNEQHLAARIERALNTWQGSLDPGEQGYLFVLEDSEQQKVVGVSAIEVAVGLNDPWYNFRVGTLVHASKALNVYKSVPTLFLSNDHTGYSELCTLFLDPDYRKDKNGPFLSKVRFLFIAAFRQYFSRKVIAEMRGYTDEQGRSPFWESVGRHFFSIEFAKADYLSGTGQKAFIAELMPKHPLYVDFLAEEARAVIGQVHPHTAPARAVLETEGLQYQGYVDIFDGGPTLEANTDDVRVVRDSSKRTVVIKDYDIEDYDIDPNGRLYLVANDHYHHFRAILMNTHLSDERLRLTPESAEALGVAAGDSVRIVSLFAPETKR
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Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. Belongs to the arginine N-succinyltransferase family.
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A9QZ62
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MMKVRPVERRDLADIFELAGKTGVGMTSLPQNEQHLAARIERALNTWQGSLDPGEQGYLFVLEDSEQQKVVGVSAIEVAVGLNDPWYNFRVGTLVHASKALNVYKSVPTLFLSNDHTGYSELCTLFLDPDYRKDKNGPFLSKVRFLFIAAFRQYFSRKVIAEMRGYTDEQGRSPFWESVGRHFFSIEFAKADYLSGTGQKAFIAELMPKHPLYVDFLAEEARAVIGQVHPHTAPARAVLETEGLQYQGYVDIFDGGPTLEANTDDVRVVRDSSKRTVVIKDYDIEDYDIDPNGRLYLVANDHYHHFRAILMNTHLSDERLRLTPESAEALGVAAGDSVRIVSLFAPETKR
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Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. Belongs to the arginine N-succinyltransferase family.
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A4TJU6
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MMKVRPVERRDLADIFELAGKTGVGMTSLPQNEQHLAARIERALNTWQGSLDPGEQGYLFVLEDSEQQKVVGVSAIEVAVGLNDPWYNFRVGTLVHASKALNVYKSVPTLFLSNDHTGYSELCTLFLDPDYRKDKNGPFLSKVRFLFIAAFRQYFSRKVIAEMRGYTDEQGRSPFWESVGRHFFSIEFAKADYLSGTGQKAFIAELMPKHPLYVDFLAEEARAVIGQVHPHTAPARAVLETEGLQYQGYVDIFDGGPTLEANTDDVRVVRDSSKRTVVIKDYDIEDYDIDPNGRLYLVANDHYHHFRAILMNTHLSDERLRLTPESAEALGVAAGDSVRIVSLFAPETKR
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Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. L-arginine + succinyl-CoA = CoA + H(+) + N(2)-succinyl-L-arginine Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 1/5. Belongs to the arginine N-succinyltransferase family.
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P77581
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MSQPITRENFDEWMIPVYAPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPELREALNEQASKFWHTGNGYTNEPVLRLAKKLIDATFADRVFFCNSGAEANEAALKLARKFAHDRYGSHKSGIVAFKNAFHGRTLFTVSAGGQPAYSQDFAPLPADIRHAAYNDINSASALIDDSTCAVIVEPIQGEGGVVPASNAFLQGLRELCNRHNALLIFDEVQTGVGRTGELYAYMHYGVTPDLLTTAKALGGGFPVGALLATEECARVMTVGTHGTTYGGNPLASAVAGKVLELINTPEMLNGVKQRHDWFVERLNTINHRYGLFSEVRGLGLLIGCVLNADYAGQAKQISQEAAKAGVMVLIAGGNVVRFAPALNVSEEEVTTGLDRFAAACEHFVSRGSS
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. Is involved in the utilization of arginine as a nitrogen source, via the AST pathway, and seems also to play a role in ornithine catabolism (PubMed:9696779). 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Its expression is under nitrogen control; a nitrogen-limited medium highly increases succinylornithine transaminase activity. Cells lacking this gene lose the ability to grow on arginine as the nitrogen source. The disruption of this gene also impairs ornithine catabolism. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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B7N584
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MSQPITRENFDEWMIPVYAPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPELREALNEQASKFWHTGNGYTNEPVLRLAKKLIDATFADRVFFCNSGAEANEAALKLARKFAHDRYGSHKSGIVAFKNAFHGRTLFTVSAGGQPAYSQDFAPLPPDIRHAAYNDINSASALIDDSTCAVIVEPIQGEGGVVPASNAFLHGLRELCDRHNALLIFDEVQTGVGRTGELYAYMHYGVTPDLLTTAKALGGGFPVGALLATEECASVMTVGTHGTTYGGNPLASAVAGKVLDLINTPEMLNGVKQRHDWFVERLNTVNHRCGLFSEVRGLGLLIGCVLNADYAGQAKQISQEAAKAGVMVLIAGGNVVRFAPALNVSEEEVTTGLDRFAAACDHFVSRGSS
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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B6IBG8
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MSQPITRENFDEWMIPVYAPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPELREALNEQASKFWHTGNGYTNEPVLRLAKKLIDATFADRVFFCNSGAEANEAALKLARKFAHDRYGSHKSGIVAFKNAFHGRTLFTVSAGGQPAYSQDFAPLPADIRHAAYNDINSASALIDDSTCAVIVEPIQGEGGVVPASNAFLQGLRELCNRHNALLIFDEVQTGVGRTGELYAYMHYGVTPDLLTTAKALGGGFPVGALLATEECARVMTVGTHGTTYGGNPLASAVAGKVLELINTPEMLNGVKQRHDWFVERLNTINHRYGLFSEVRGLGLLIGCVLNADYAGQAKQISQEAAKAGVMVLIAGGNVVRFAPALNVSEEEVTTGLDRFAAACEHFVSRGSS
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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B1LDY3
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MSQPITRENFDEWMIPVYAPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPELREALNEQASKFWHTGNGYTNEPVLRLAKKLIDATFADRVFFCNSGAEANEAALKLARKFAHDRYGSHKSGIVAFKNAFHGRTLFTVSAGGQPAYSQDFAPLPPDIHHAAYNDINSASALIDDATCAVIVEPIQGEGGVVPASNAFLQGLRELCDRHNALLIFDEVQTGVGRTGELYAYMHYGVTPDLLTTAKALGGGFPVGALLATEECASVMTVGTHGTTYGGNPLASAVAGKVLDLINTPEMLNGVKQRHDWFVERLNSINHHYGLFSEVRGLGLLIGCVLNADYAGQAKQISQEAAKAGVMVLIAGGNVVRFAPALNVSEEEVTTGLDRFAAACEHFVSRGSS
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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Q1RB45
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MSQPITRENFDEWMIPVYAPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPELREALNEQASKFWHTGNGYTNEPVLRLAKKLIDATFADRVFFCNSGAEANEAALKLARKFAHDRYGSHKSGIVAFKNAFHGRTLFTVSAGGQPAYSQDFAPLPPDIRHAAYNDINSASALIDDATCAVIVEPIQGEGGVVPASNAFLQGLRELCDRHNALLIFDEVQTGVGRTGELYACMHYGVTPDLLTTAKALGGGFPVGALLATEECASVMTVGTHGTTYGGNPLASAVAGKVLDLINTPEMLNGVKQRHDWFVERLNSINHHYSLFSEVRGLGLLIGCVLNADYAGQAKQISQEAVKAGVMVLIAGGNVVRFAPALNVSEEEVTTGLDRFAAACEHFVSRGSS
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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B7LQ44
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MSQPITRENFDEWMLPVYAPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPELREALNEQASKFWHTGNGYTNEPVLRLAKKLIDATFADRVFFCNSGAEANEAALKLARKFAHDRYGSHKSGIVAFKNAFHGRTLFTVSAGGQPAYSQDFAPLPPDIRHAAYNDLNSASALIDDSTCAVIVEPIQGEGGVVPASNAFLQGLRELCDRHNALLIFDEVQTGVGRTGELYAYMHYGVTPDLLTTAKALGGGFPVGALLATEECASVMTVGTHGTTYGGNPLASAVAGKVLDLINTPEMLIGVKQRHDWFVERLNTINHRYGLFSEVRGLGLLIGCVLNADYAGQAKQISQEAAKAGVMVLIAGGNVVRFAPALNVSEEEVTTGLDRFAVACERFVSGGSS
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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Q7N2G7
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MLENIQRSWFEHYMVPCFSPAKFIPVRAKGSKVWDQDGKEYIDFAGGIAVNSLGHAHPELKDELIYQIDKIWHIGNGYTNEPVLKLAKRLVENTFADKAFFCNSGAEANEAALKLARKYAADKYGKNKNEIISFKDSFHGRTLFTVTVGGQPKYSQDYAPLPQEITHLPYNNLSAIREHISENTCAVIVEPIIGEGGVIPADPAFLQELRTLCDRFQALLIFDEIQTGVGRTGYLYAYQEYGVEPDILTSAKGLGGGFPIGAMLTKQHIAAVFQPGTHGTTFGGNPLATAVANKVLSIVNQAELLTGVLQRHDYFMDKLSKLNQRYQIFSCLRGKGLLLGAELDKAWQGKAKQLTNLAAEEGLIALIAGPDVLRFAPALNIEFADIDEGLVRLESAIMRFVG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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B5F846
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MSLSVTRENFDEWMVPVYIPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQANRFWHTGNGYTNEPALRLAKKLIDATFAERVFFCNSGAEANEAALKLARKYAHDRVGNHKSGIVAFKNAFHGRTLFTVSAGGQPTYSQDFAPLPPDIRHAAYNDLNSASALIDDNTCAVIVEPVQGEGGVIPATKAFLQGLRELCDRHQALLIFDEVQTGVGRTGELYAYMHYGVTPDILTTAKALGGGFPIGAMLTTQDYASVMTPGTHGTTYGGNPLATAVAGKVLDIINTPEMQNGVRQRHDAFIERLNTLNVRFGMFSEIRGLGLLLGCVLQTKFAGKAKLIAQEAAKAGVMVLIAGGDVVRFAPALNVSDEEIATGLDRFALACERLQAGGASCG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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Q57PX9
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MSLSVTRENFDEWMVPVYVPAPFIPVRGEGSRLWEQQGKEYIDFAGGIAVNALGHAHPALREALNEQANRFWHTGNGYTNEPALRLAKKLIDATFAERVFFCNSGAEANEAALKLARKYAHDRVGNHKSGIVAFKNAFHGRTLFTVSAGGQPTYSQDFAPLPPDIRHAAYNDLNSASALIDDNTCAVIVEPVQGEGGVIPATKAFLQGLRELCDRHQALLIFDEVQTGVGRTGELYAYMHYGVTPDILTTAKALGGGFPIGAMLTTQDYASVMTPGTHGTTYGGNPLATAVAGKVLDIINTPEMQNGVRQRHDAFIERLNTINVRFGMFSEIRGLGLLLGCVLQTEFAGKAKLIAQEAAKAGVMVLIAGGDVVRFAPALNVSDEEIATGLDRFALACERLQTGGASCG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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B5FJD8
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MSLSVTRENFDEWMVPVYVPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQANRFWHTGNGYTNEPALRLAKKLIDATFAERVFFCNSGAEANEAALKLARKYAHDRVGNHKSGIVAFKNAFHGRTLFTVSAGGQPTYSQDFAPLPPDIRHAAYNDLNSASALIDDNTCAVIVEPVQGEGGVIPATKAFLQGLRELCDRHQALLIFDEVQTGVGRTGELYAYMHYGVTPDILTTAKALGGGFPIGAMLTTQDYASVMTPGTHGTTYGGNPLATAVAGKVLDIINTPEMQNGVRQRHDAFIERLNTINVRFGMFSEIRGLGLLLGCVLQTEFAGKAKLIAQEAAKAGVMVLIAGGDVVRFAPALNVSDEEIATGLDRFALACERLQAGGASCG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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B5QWJ0
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MSLSVTRENFDEWMVPVYVPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQANRFWHTGNGYTNEPALRLAKKLIDATFAERVFFCNSGAEANEAALKLARKYAHDRVGNHKSGIVAFKNAFHGRTLFTVSAGGQPTYSQDFAPLPPDIRHAAYNDLNSASALIDDNTCAVIVEPVQGEGGVIPATKAFLQGLRELCDRHQALLIFDEVQTGVGRTGELYAYMHYGVTPDILTTAKALGGGFPIGAMLTTQDYASVMTPGTHGTTYGGNPLATAVAGKVLDIINTPEMQNGVRQRHDAFIERLNTINARFGMFSEIRGLGLLLGCVLQTEFAGKAKLIAQEAAKAGVMVLIAGGDVVRFAPALNVSDEEIATGLDRFALACERLQTGGASCG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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B5RB01
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MSLSVTRENFDEWMVPVYVPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQANRFWHTGNGYTNEPALRLAKKLIDATFAERVFFCNSGAEANEAALKLARKYAHDRVGNHKSGIVAFKNAFHGRTLFTVSAGGQPTYSQDFAPLPPDIRHAAYNDLNSASALIDDNTCAVIVEPVQGEGGVIPATKAFLQGLRELCDRHQALLIFDEVQTGVGRTGELYAYMHYGVTPDILTTAKALGGGFPIGAMLTTQDYASVMTPGTHGTTYGGNPLATAVAGKVLDIINTPEMQNGVRQRHDAFIERLNTINARFGMFSEIRGLGLLLGCVLQTEFAGKAKLIAQEAAKAGVMVLIAGGDVVRFAPALNVSDEEIATGLDRFALACERLQTGGASCG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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B4TGE0
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MSLSVTRENFDEWMVPVYVPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQANRFWHTGNGYTNEPALRLAKKLIDATFAERVFFCNSGAEANEAALKLARKYAHDRVGNHKSGIVAFKNAFHGRTLFTVSAGGQPTYSQDFAPLPPDIRHAAYNDLNSASALIDDNTCAVIVEPVQGEGGVIPATKAFLQGLRELCDRHQALLIFDEVQTGVGRTGELYAYMHYGVTPDILTTAKALGGGFPIGAMLTTQDYASVMTPGTHGTTYGGNPLATAVAGKVLDIINTPEMQNGVRQRHDAFIERLNTINVRFGMFSEIRGLGLLLGCVLQTEFAGKAKLIAQEAAKAGVMVLIAGGDVVRFAPALNVSDEEIATGLDRFALACERLQTGGASCG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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B4T3Z4
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MSLSVTRENFDEWMVPVYVPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQANRFWHTGNGYTNEPALRLAKKLIDATFAERVFFCNSGAEANEAALKLARKYAHDRVGNHKSGIVAFKNAFHGRTLFTVSAGGQPTYSQDFAPLPPDIRHAAYNDLNSASALIDDNTCAVIVEPVQGEGGVIPATKAFLQGLRELCDRYQALLIFDEVQTGVGRTGELYAYMHYGVTPDILTTAKALGGGFPIGAMLTTQNYASVMTPGTHGTTYGGNPLATAVAGKVLDIINTPEMQNGVRQRHDAFIERLNTLNVRFGMFSEIRGLGLLLGCVLQTEFAGKAKLIAQEAAKAGVMVLIAGGDVVRFAPALNVSDEEIATGLDRFALACERLQTGGAPCG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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Q5PHC8
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MSLSVTRENFDEWMVPVYVPAPLIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQANRFWHTGNGYTNEPALRLAKKLIDATFAERVFFCNSGAEANEAALKLARKYAHDRVGNHKSGIVAFKNAFHGRTLFTVSAGGQPTYSQDFAPLPPDIRHAAYNDLNSASALIDDNTCAVIVEPVQGEGGVIPATKAFLQGLRELCDRHQALLIFDEVQTGVGRTGKLYAYMHYGVTPDILTTAKALGGGFPIGAMLTTQDYASVMTPGTHGTTYGGNPLATAVAGKVLDIINTPEMQNGVRQRHDAFIERLNTLNVRFGMFSEIRGLGLLLGCVLQTEFAGKAKLIAQEAAKAGVMVLIAGGDVVRFAPALNVSDEEIATGLDRFALACERLQTGGASCG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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A9N278
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MSLSVTRENFDEWMVPVYVPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQANRFWHTGNGYTNEPALRLAKKLIDATFAERVFFCNSGAEANEAALKLARKYAHDRIGNHKSGIVAFKNAFHGRTLFTVSAGGQPSYSQDFAPLPPDIRHAAYNDLNSASALIDDNTCAVIVEPVQGEGGVIPATKAFLQGLRELCDRHQALLIFDEVQTGVGRTGELYAYMHYGVTPDILTTAKALGGGFPIGAMLTTQDYASVMTPGTHGTTYGGNPLATAVAGKVLDIINTPEMQNGVRQRHDAFIERLNTINVRFGMFSEIRGLGLLLGCVLQTEFAGKAKLIAQEAAKAGVMVLIAGGDVVRFAPALNVSDEEIATGLDRFALACERLQTGGAPCG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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C0Q6X9
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MSLSVTRENFDEWMVPVYVPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQANRFWHTGNGYTNEPALRLAKKLIDATFAERVFFCNSGAEANEAALKLARKYAHDRVGNHKSGIVAFKNAFHGRTLFTVSAGGQPTYSQDFAPLPPDIRHAAYNDLNSASALIDDNTCAVIVEPVQGEGGVIPATKAFLQGLRELCDRHQALLIFDEVQTGVGRTGELYAYMHYGVTPDILTTAKALGGGFPIGAMLTTQDYASVMTPGTHGTTYGGNPLATAVAGKVLDIINTPEMQNGVRQRHDAFIERLNTINVRFGMFSEIRGLGLLLGCVLQTEFAGKAKLIAQEAAKAGVMVLIAGGDVVRFAPALNVSDEEIATGLDRFALACERLQTGGASCG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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B5BA72
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MSLSVTRENFDEWMVPVYVPAPLIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQANRFWHTGNGYTNEPALRLAKKLIDATFAERVFFCNSGAEANEAALKLARKYAHDRVGNHKSGIVAFKNAFHGRTLFTVSAGGQPTYSQDFAPLPPDIRHAAYNDLNSASALIDDNTCAVIVEPVQGEGGVIPATKAFLQGLRELCDRHQALLIFDEVQTGVGRTGKLYAYMHYGVTPDILTTAKALGGGFPIGAMLTTQDYASVMTPGTHGTTYGGNPLATAVAGKVLDIINTPEMQNGVRQRHDAFIERLNTLNVRFGMFSEIRGLGLLLGCVLQTEFAGKAKLIAQEAAKAGVMVLIAGGDVVRFAPALNVSDEEIATGLDRFALACERLQTGGASCG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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Q8Z6F9
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MSLSVTRENFDEWMVPVYVPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQANRFWHTGNGYTNEPALRLAKKLIDATFAERVFFCNSGAEANEAALKLARKYAHDRVGNHKSGIVAFKNAFHGRTLFTVSAGGQPTYSQDFAPLPPDIRHAAYNDLNSASALIDDNTCAVIVEPVQGEGGVIPATNAFLQGLRELCDRHQALLIFDEVQTGVGRTGELYAYMHYGVTPDILTTAKALGGGFPIGAMLTTQDYASVMTPGTHGTTYGGNPLATAVAGKVLDIINTPEMQNGVRQRHDAFIERLNTINVRFGMFSEIRGLGLLLGCVLQTEFAGKAKLIAQEAAKAGVMVLIAGGDVVRFAPALNVSDEEIATGLDRFALACERLQAGGASCG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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Q8ZPV2
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MSLSVTRENFDEWMVPVYVPAPFIPVRGEGSRLWDQQGKEYIDFAGGIAVNALGHAHPALREALNEQANRFWHIGNGYTNEPALRLAKKLIDATFAERVFFCNSGAEANEAALKLARKYAHDRVGNHKSGIVAFKNAFHGRTLFTVSAGGQPTYSQDFAPLPPDIRHAAYNDLNSASALIDDNTCAVIVEPVQGEGGVIPATKAFLQGLRELCDRHQALLIFDEVQTGVGRTGELYAYMHYGVTPDILTTAKALGGGFPIGAMLTTQDYASVMTPGTHGTTYGGNPLATAVAGKVLDIINTPEMQNGVRQRHDAFIERLNTLNVRFGMFSEIRGLGLLLGCVLQTEFAGKAKLIAQEAAKAGVMVLIAGGDVVRFAPALNVSDEEIATGLDRFALACERLQTGGVPCG
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Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. 2-oxoglutarate + N(2)-succinyl-L-ornithine = L-glutamate + N-succinyl-L-glutamate 5-semialdehyde Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 3/5. By nitrogen and carbon starvation, and arginine, via the ArgR and Crp transcriptional regulators. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.
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B2VEK5
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MQDFLQLTLSGGQPEQKEGRNGLLRWRWLNVGILELTPLHSVPRALVVSSGIHGNETAPVEIVEQLVNALLRGELALQARLLVIYGNPAALRLNRRYVHGDMNRMFGGRWQQYEDCPEARRAWILEQAMDNFWQAGDYEEVRWHLDLHTAIRGSYHAQFGVLPQRMTPWPEDFMHWLASAGLEALVFHRATGGTFTNYSSRHFQAASCTLELGTALPFGHNDLTQFAAVRLALRQLIAGGENIPAAAQPRRYRVSQQITRRSDRFVLHMSDEVLNFTAFPQGTLLAEDGEDRVYVQQAREYVLFPNPNVATGLRAGLMLVEDNVHNKAL
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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B7LQ48
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MDNFLALTLTGKKPVITEREINGVRWRWLGDGVLELTPLTPPQGALVISAGIHGNETAPVEMLDALLGAISHGEIPLRWRLLVIFGNPPALKQGKRYCHSDMNRMFGGRWQLFAESGETCRARELEQCLEDFFDQGKESVRWHLDLHTAIRGSLHPQFGVLPQRDIPWDEKFLTWLGTAGLEALVFHQAPGGTFTHFSARHFGALACTLELGKALPFGQNDLRQFAVTASAIAARVSGESVGVVRTPPIRYRVVSQITRHSPSFEMHMASDTLNFMPFKKGTLLAQDGEERFTVTHDVEYVLFPNPLVALGLRAGLMLEKIS
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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Q5QUK3
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MNKVFSDFLAWTREHEWGCDESYNLTLSNGTKLSVWDSGVLEVSPASPGHKDVVLSCAVHGNETAPIEICRDIINDIIDEKQTVTHRTLFLIANPASINKGERFVEENMNRLFSGEHGKGSTQNKERERAAKMENYVERFYQSAPEGSRERFHYDLHTAIRDSKREKFAVYPFTHGAPYSRQQLQFLLACGVDTVLLNQAPTTTFSYFSARQFNAHAFTVELGKVRPFGENDRAKFAAAETTLRDLISQTELDFGPFEPEQHYVFKEAQTINRTQPDFELNFADDVANFTSFNKGELLAWDGDKACYAQHDGEHIIFPNAKVALGHRALLTVVRVPTESLDLV
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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Q141D1
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MPVSLLDDFLAYTLAGTRPAASEAQGTCAGGVRWSWLDDGVLLMEPAVQEEGMRSVLVSAGVHGDETAPIELLAFLVRDIAHGTAALTGRLLVILGNVDAMRDACRYRDDDLNRLFSGRHLQLPQSHEAPRAAALERAATRFFAAAPDNPGARWHIDMHTAIRASAFEQFALLPHTGKPFSRAMFEWLGEARISAVLLHTTRGNTYSHFTAQACGALACTLELGKVRPFGQNDLTRFAGADHAVRHLLAGMRGEVRAPMPRAFTVIDQITRQSEAFELLVAPDVANFTPFAKDTVLARDGDYRYVVRHDEERLVFPNATVKPGLRAGLMVIETTQDTLSKLV
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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Q7N2H1
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MDLLTLLLEKKLADHLTFPETINAHWLAEGVLQLIPHEEGNRSLVISAGIHGNETAPIEILIQLLAQLAEGTLALKNNVLIIFGNLPAMRTNRRYLHDDLNRMFGGRYLNFPLGNERSRAAELENVVNRFFAEPSVSSTNIRWHIDLHTAIRASHHEQFALLPAQNRPFSAEFMQWLHDSDIDALVYHREKAGTFSHFLSEKFGADSCTMEMGKAMPFGENDLTRFQKITDALYGLISLSQITARIKFELKHYQVINSIIKSHDSFQLHIPADTLNFTELPEGFEIASQHDHHWKIKFPAKFILFPNAEVANGLRAGLLLALNKK
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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Q48G22
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MLALGKLLELTLAGREPAEKTQLTVEGVRMRWMGEGALEVRPPQVRDNGTDLLLSAGIHGNETAPIELLDELIRSIARGDLKPRARILFLFGNPDAMRRGTRFVEQDVNRLFNGRHEQSGGAEALRACELEHLAASFFSLPDRYRLHYDLHTAIRGSKIEQFALYPWKEGRQHSRLELARLRAAGMSAVLLQNKPSIVFSAYTYDQLGAEAFTLELGKARPFGQNQQVNLAPLRLRLEQIIEGREPELDENLEELQLFSVAREVIKRTDAFTFNLADAVENFSPLEKGYVLAEDAGGSRWVVEEDGARIIFPNPKVKNGLRAGILIVPTDAGSLG
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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Q15TS5
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MQTVNTHKLISHLQQQGQFLTLSRCSGELVQNPISFTLYEHTQVSIISPGIISFSPKIKSDKAIVLSSGIHGNETAPIEICDQYVIDILTGKIRVAHRILFIFGNLPAMDRATRFVDENLNRLFSHAHASESVDQNSYECARAKEIEEAVAEFYGSGHGEESRYHYDLHTAIRPSKNEKFAVYPFLHGEKHDKEQISFLLACGIDTFLLSGSPTTTFSYYSSRQFGAHAFTVELGKVQAFGQNDMSRFTQVNDTLKRFISGQPLNLKSFNDQDVLIYQVNQVINKHAEDFELDFSDDLPNFSDFPKGTLLAHETGNEYRAEFDGEAVVFPNANVAIGQRAILTVIPTTLD
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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A6VA73
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MLALGKLLDLTLAGREPTEKIQLTADGTRLHWLAEGALEVTPIGARDNGVDLLLSAGIHGNETAPIELLERLVRKLASGELKPAARVLFLLGNPEAIRRGERFVEQDMNRLFNGRHEEGSGNEAFRAAELERLAQVFFSRGERDRLHYDLHTAIRGSRIEQFALYPWAEGREHSRAELARLRDAGIEAVLLQNKPGITFSAYTYGQLGAEAFTLELGKARPFGQNQQVNLERLERRLEMLIDGSEERPDGAHLDGLKLFSVSREVIKHSDHFRLHLDDDVANFTELSPGYLLAEDIGGTRWVVDEVGARIIFPNPRVKNGLRAGILVVPAKL
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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B7UY33
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MLALGKLLDLTLAGREPTEKIQLTADGTRLHWLAEGALEVTPIGARDNGVDLLLSAGIHGNETAPIELLERLIRKVAAGTLKPAARVLFLFGNPEAIRRGERYVEQDMNRLFNGRHEEGSGNEAFRAAELERLAQVFFSKTERVHLHYDLHTAIRGSKIEQFALYPWAEGRQHSRSELARLRDAGIEAVLLQNKPGITFSAYTYGQLGAEAFTLELGKARPFGENQEVNLERLERSLELLIDGSEEQPDGSRLDGLKLFSVSREVIKHSDHFRLHLDDDVANFTELSPGYLLAEDIGGTRWVVDEVGARIIFPNPRVKNGLRAGILVVPAKL
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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Q02I61
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MLALGKLLDLTLAGREPTEKIQLTADGTRLHWLAEGALEVTPIGARDNGVDLLLSAGIHGNETAPIELLERLIRKVAAGTLKPAARVLFLFGNPEAIRRGERYVEQDMNRLFNGRHEEGSGNEAFRAAELERLAQVFFSKTERVHLHYDLHTAIRGSKIEQFALYPWAEGREHSRSELARLRDAGIEAVLLQNKPGITFSAYTYGQLGAEAFTLELGKARPFGENQEVNLERLERSLELLIDGSEEQPDGSRLDGLKLFSVSREVIKHSDHFRLHLDDDVANFTELSPGYLLAEDIGGTRWVVEEVGARIIFPNPRVKNGLRAGILVVPAKL
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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O50177
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MLALGKLLDLTLAGREPTEKIQLTADGTRLHWLAEGALEVTPIGARDNGVDLLLSAGIHGNETAPIELLERLIRKVAAGTLKPAARVLFLFGNPEAIRRGERYVEQDMNRLFNGRHEEGSGNEAFRAAELERLAQVFFSKTERVHLHYDLHTAIRGSKIEQFALYPWAEGRQHSRSELARLRDAGIEAVLLQNKPGITFSAYTYGQLGAEAFTLELGKARPFGENQEVNLERLERSLELLIDGSEEQPDGSRLDGLKLFSVSREVIKHSDHFRLHLDDDVANFTELSPGYLLAEDIGGTRWVVDEVGARIIFPNPRVKNGLRAGILVVPAKL
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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Q4K840
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MLALGKLLELTLAGREPAEKTQLTVDGVRMRWLSEGALEVRPPEARDNGLDLLLSAGIHGNETAPIELLDRLLHDIARGDLKPRARILFLFGNPEAMRRGERFVEQDVNRLFNGRHESSSGFEALRACELERLAASFFSQPDRQRLHYDLHTAIRGSKIEQFALYPWKDGRQHSRRELARLRAAGMEAVLLQNKPSIVFSAYTYDQLGAESFTLELGKARPFGQNQGVNVERLETRLKQIIDGSEPPAEQDSLDGLQLFSVAREVIKHSDSFHLHLPADIENFSELEVGYLLAEDIAQTRWVIEETGARIIFPNPKVKNGLRAGILIVPATADGLA
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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C3JXY4
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MLALGKLLELTLAGREPAQKIQLTVDGVQMRWLSEGALEVRPPEARDNGSDLLLSSGIHGNETAPIELLDRLLHGIARGEIKPRSRVLFLFGNTEAMRRGERYLELDVNRLFNGRHEKNIGPEAMRAAELEQLARSFFSLPGRSRLHYDLHTAIRGSKIEQFALYPWKEGRQHSRHQLARLNAAGMQAVLLQNKTSITFTAFTYEQLEAEAFTLELGKARPFGQNQGVNVSRLELRLKQIIEGTEPETDSLDGLKLFAVSREVIKHSDAFLLHLPADVENFSELEKGYLLAEDVAKTRWVIEEEGARIIFPNPKVKNGLRAGILIVPTTDAVLG
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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A4XWE4
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MLALGKLLELTLAGHEPSAKIQLTPDGTRLRWLDEGALEITPPAARDNGLDLLLSAGIHGNETAPIELLDRLLRGIARNELHPAARILFLFGNPEAMRRGERFVEQDINRLFNGRHEQSSGFEAIRACDLEHLAATFFGKDTGRTRLHYDLHTAIRGSKIEQFALYPWHEGRTHSRRELQRLRAAGIEAVLLQNKGSITFSSYTYGQLGAEAFTLELGKARAFGQNQLVNLDLLENALQALIEGREVIDDEPTLDGLQLFAVSREIIKHSDSFQLHLPADIENFTELEPGYLLAEDIADTRWVVEEQNARIIFPNPKVKNGLRAGILIVPDDGAGLA
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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A5W0D8
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MLALGKLLELTLTAHEPAEKTQVTPGGARLRWLGEGALEVRPAESEDCGLDLLLSAGIHGNETAPIELLERLLHGVANGKIKPRARVLFLFGNPAAIRKGERFIEQDINRLFNGRHELSSGFEALRAAELEQFARVFFSKPGRNRLHYDLHTAIRGSKIEQFALYPYKEGRKHSRRELARLAAAGMEAVLLQSKSSITFSAFTYEQLEAEAFTLELGKARPFGQNEQVNLDKLEERLIRIIEATEPENESSLDGLQLFSVSREIIKHSDSFHLHLPADIENFSELSKGYLLAEDLAEMRWVVEEEGARIIFPNPKVKNGLRAGILIVPDSGQRLG
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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Q3K888
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MLALGKLLELTLAGREPAEKTQLTVEGVRMRWLSEGALEVRPPEARDNGLDLLLSAGIHGNETAPIELLDRLLHDIARGDLKPRARILFLFGNPEAIRKGERFVEQDVNRLFNGRHEQSSGSEALRACELERLAASFFSLPDRQRLHYDLHTAIRGSKIEQFALYPWKEGRQHSRLELARLRAAGMEAVLLQNKPSIVFSSYTYDKLGAESFTLELGKARPFGQNAGVNVSLLETRLKQIIEGTEPEMAEQGLDGLQLFSVAREIIKHSDAFRLNLPADIENFSELDVGYVLAEDLANTRWIIEEQGARIIFPNPKVKNGLRAGILIVPTTDENLA
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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B0KR44
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MLALGKLLELTLTDHEPAEKTQVTPKGARLRWLGEGALEVRPAESEDCGLDLLLSAGIHGNETAPIELLERLLHGVANGKIKPRARLLFLFGNPVAIRKGERFIEQDINRLFNGRHELSSGFEALRAAELEQFARVFFSKPGRSRLHYDLHTAIRGSKIEQFALYPYKEGRKHSRRELARLAAAGMEAVLLQSKSSITFSAFTYEQLDAEAFTLELGKARPFGQNEQVNLDKLEERLIRIIEATEPEGESSLDGLQLFSVSREIIKHSDSFHLHLPADIENFSELSKGYLLAEDLAEMRWVVEEEGARIIFPNPKVRNGLRAGILIVPDSGQRLG
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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Q88EI7
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MLALGKLLELTLTDHEPAEKTQVTPKGARLRWLGEGALEVRPAESDDCGLDLLLSAGIHGNETAPIELLERLLHGVANGKIRPRARVLFLFGNPAAIRKGERFIEQDINRLFNGRHELSSGFEALRAAELEQFARVFFSKPGRNRLHYDLHTAIRGSKIEQFALYPYKEGRKHSRRELARLAAAGMEAVLLQSKSSITFSAFTYEQLEAEAFTLELGKARPFGQNEQVNLDKLEERLIRIIEATEPEDESSLDGLQLFSVSREIIKHSDSFHLHLPADIENFSELSKGYLLAEDLAEMRWVVEEEGARIIFPNPKVKNGLRAGILIVPDSGQRLG
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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B1JCH0
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MLALGKLLELTLTDHEPAEKTQVTPKGVRLRWLGEGALEVRPPEGDDCGLDLLLSAGIHGNETAPIELLERLLHGVANGKIKPRSRVMFLFGNPAAIRKGERFIEQDINRLFNGRHELSSGFEALRAAELEQFARVFFSKPERARLHYDLHTAIRGSKIEQFALYPYKEGRKHSRRELARLAAAGMEAVLLQSKSSITFSAFTYEQLDAEAFTLELGKARPFGQNEQVNLDKLEERLIQIIEGNEPEAGDSLDGLKLFSVAREIIKHSEGFRLHLPVDIENFSELSKGYLLAEDLAEMRWVVEEEGARIIFPNPKVKNGLRAGILIVPDSGQRLD
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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Q885J4
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MLALGKLLELTLAGREPAEKTQLTVEGVRMRWLAEGALEVRPPQARDNGTDLLLSAGIHGNETAPIELLDELIRSIARGDLKPRARILFLFGNPAAMRLGARYVEQDVNRLFNGRHEQSGGAEALRACELERLAASFFSLPDRYRLHYDLHTAIRGSKIEQFALYPWKEGRQHSRFELARLRAAGISAVLLQNKPSIVFSAYTYEQLGAEAFTLELGKARPFGQNRHVNLAPLRLRLEQIIEGSEPQPDERLEGLQLFSVAREVIKRSDAFTFNLADDVENFSELEKGYVLAEDVSDSRWVVKEEGARIIFPNPKVKNGLRAGIVIVPADADGLG
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Transforms N(2)-succinylglutamate into succinate and glutamate. H2O + N-succinyl-L-glutamate = L-glutamate + succinate Binds 1 zinc ion per subunit. Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 5/5. Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.
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P50997
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MGKGVGRDKYEPAAVSEHGDKKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTTARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVIGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVKGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKSSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRDRYAKIVEIPFNSTNKYQLSIHKNPNTSEPRHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDALQNAYLELGGLGERVLGFRHLFLPDEQFPEGFQFDTDDVNFPVENLCFVGFISMIGPPRAAVPDAVGKCRGAGIKVIMVTGDHPITAKAIAKGAGIISEGNETVEDIAARLNIPVRQVNPRDAKACVVHGSDLKDMTSEQLDGILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIVGSDASKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPTHLLGLRVDWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1 (PubMed:16943195, PubMed:21454534). Interacts with regulatory subunit FXYD3 (By similarity). Interacts with SIK1 (By similarity). Interacts with SLC35G1 and STIM1 (By similarity). Interacts with CLN3; this interaction regulates the sodium/potassium-transporting ATPase complex localization at the plasma membrane (By similarity). Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-941 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity). Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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P25489
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MGVGDGRDQYELAAMSEQSGKKKSKNKKEKKEKDMDELKKEVDLDDHKLSLEELHHKYGTDLSKGLSNSRAEEILARDGPNALTPPPTTPEWVKFCKQMFGGFSMLLWTGAVLCFLAYGILAAMEDEPANDNLYLGVVLSAVVIITGCFSYYQDAKSSKIMDSFKNLVPQQALVVRDGEKKQINAEEVVIGDLVEVKGGDRIPADLRIISSHGCKVDNSSLTGESEPQTRSPDFSNDNPLETKNIAFFSTNCVEGTARGIVISTGDRTVMGRIATLASGLEVGRTPISIEIEHFIHIITGVAVFLGVSFLLLSLVLGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMAKKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGTSFDRSSDTWASLARIAGLCNRAVFLAEQIDVPILKRDVAGDASESALLKCIELCCGSVKEMREKFTKVAEIPFNSTNKYQLSVHKIPSGGKESQHLLVMKGAPERILDRCATIMIQGKEQLLDDEIKESFQNAYLELGGLGERVLGFCHFYLPDEQFPEGFQFDADDVNFPTENLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVNEVNPRDAKACVVHGGDLKDLSCEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRTGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLFFIIANIPLPLGTVTILCIDLGTDMLPAISLAYEAAESDIMKRQPRNPKTDKLVNERLISIAYGQIGMIQALAGFFTYFVILAENGFLPPRLLGIRMNWDDKYINDLEDSYGQQWTYEQRKIVEFTCHTAFFTSIVIVQWADLIICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMDVALRMYPLKPNWWFCAFPYSLLIFIYDEIRKLILRRNPGGWMERETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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P09572
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MGKGAGRDKYEPTATSEHGTKKKKAKERDMDELKKEISMDDHKLSLDELHRKYGTDLSRGLTTARAAEILARDGPNTLTPPPTTPEWVKFCRQLFGGFSLLLWIGSLLCFLAYGITSVMEGEPNSDNLYLGVVLAAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVVRNGEKMSINAEGVVVGDLVEVKGGDRIPADLRIISAHGCKVDNSSLTGESEPQTRSPDFSNENPLETRNIAFFSTNCVEGTAVGIVISTGDRTVMGRIASLASGLEGGKTPIAMEIEHFIHLITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVGTLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGASFDKSSATWLALSRIAGLCNRAVFQANQENVPILKRAVAGDASESALLKCIELCCGSVKEMRERYPKVVEIPFNSTNKYQLSIHKNANAGESRHLLVMKGAPERILDRCDSILIHGKVQPLDEEIKDAFQNAYLELGGLGERVLGFCHLALPDDQFPEGFQFDTDEVNFPVEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISDGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDILLHHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTCTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVIMAENGFLPSGLVGIRLQWDDRWINDVEDSYGQQWTFEQRKIVEFTCHTAFFVSIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMDVALRMYPLKPTWWFCAFPYSLLIFLYDEIRKLIIRRNPGGWVERETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Phosphorylation on Tyr-10 modulates pumping activity. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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P18907
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MGKGGGRDKYEPAAISEHGNKKKAKKERDMDELKKEVSMDDHKLSLDELQRKYGTDLSRGLTTARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVVRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVTFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLSLSRIAGLCNRAVFQANQENIPILKRAVAGDASESALLKCIELCCGSVKEMRDRYPKIVEIPFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRCSSILLNGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPLENLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTPEQLDDILRHHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVDWDDRWVNDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1. Interacts with regulatory subunit FXYD3. Interacts with SIK1. Interacts with SLC35G1 and STIM1. Interacts with CLN3; this interaction regulates the sodium/potassium-transporting ATPase complex localization at the plasma membrane (By similarity). Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-941 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity). Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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Q9UJ21
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MGKGVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYAKIVEIPFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPIDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVDWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1 (By similarity). Interacts with regulatory subunit FXYD3 (PubMed:21454534). Interacts with SIK1 (By similarity). Binds the HLA class II histocompatibility antigen DR1 (PubMed:1380674). Interacts with SLC35G1 and STIM1 (PubMed:22084111). Interacts with CLN3; this interaction regulates the sodium/potassium-transporting ATPase complex localization at the plasma membrane (Probable). Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity). The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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Q91Z09
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MGKGVGRDKYEPAAVSEHGDKKGKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTPARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIRSATEEEPPNDDLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEDVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAEEIEHFIHLITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWFALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIEVCCGSVMEMREKYSKIVEIPFNSTNKYQLSIHKNPNASEPKHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLLLPDEQFPEGFQFDTDDVNFPVDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVNQVNPRDAKACVVHGSDLKDMTSEELDDILRYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIVGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPFHLLGIRETWDDRWVNDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGAALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1 (PubMed:17283221). Interacts with regulatory subunit FXYD3 (PubMed:15743908). Interacts with SIK1 (By similarity). Interacts with SLC35G1 and STIM1 (By similarity). Interacts with CLN3; this interaction regulates the sodium/potassium-transporting ATPase complex localization at the plasma membrane (By similarity). Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity). Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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Q9YH26
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MGLGKGKDEYKLAATSEDGGKKDKKAKAKKDMDDLKKEVDLDDHKLTLDELHRKYGTDLTRGLSSSRAKEILARDGPNALTPPPTTPEWVKFCKQLFGGFSMLLWIGAILCFLAYGIQAASEDEPANDNLYLGIVLSAVVIITGCFSYYQEAKSSKIMESFKNLVPRQALGIRDGEKKNINAEEVVLGDLVEVKGGDRIPADLRIISAHGCKVDNSSLTGESEPQTRSPDFSNENPLETRNISFFSTNCIEGTARGIVINTEDRTVMGRIATLASSLEGGKTPIAIEIEHFIHIITGVAVFLGVSFFILSLILGYNWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMAKKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGTSFDRSSATWANLSRIAGLCNRAVFLADQSNIPILKRDVAGDASEAALLKCIELCCGSVNEMREKYPKIAEIPFNSTNKYQLSIHKNTTPGETKHLLVMKGAPERILDRCNSIVLQGKVQALDDEMKDAFQNAYVELGGLGERVLGFCHYHLPDDEFPEGFAFDTDEVNFPTENLCFVGLMAMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNVPVSEVNPRDAKACVVHGSELKDMTSEELDDLLKHHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEISPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEKAESDIMKRQPRNPKTDKLVNERLISIAYGQIGMMQATAGFFTYFVILAENGFLPMDLIGVRVLWDDKYVNDLEDSYGQQWTYERRKIVEYSCHTAFFASIVIVQWADLIICKTRRNSIVQQGMTNRILIFGLFEETALAAFLSYCPGMDVALRMYPMKPLWWFCAFPYSLLIFLYDEARRYILRRNPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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P18874
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MGKGVGRDKYEPAAVSEHGDKKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTPARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWSDNQIHEADTTENQSGVSFDKTSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYTKIVEIPFNSTNKYQLSIHKNPNTAEPRHLLVMKGAPERILDRCSSILIHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPLDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPASKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNEQLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVNWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTPFFVTIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1 (PubMed:15563542). Interacts with regulatory subunit FXYD3 (By similarity). Interacts with SIK1 (By similarity). Interacts with SLC35G1 and STIM1 (By similarity). Interacts with CLN3; this interaction regulates the sodium/potassium-transporting ATPase complex localization at the plasma membrane (By similarity). Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-941 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity). Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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Q5RBX4
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MAFKVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEAGTTENQSGVSFDKTSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYAKIVEIPFNSTNKYQLSIHKNPNTSEPRHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPIDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISTAYGQIGMIQALGGFFTYFVILAENGFLPLHLLGLRVDWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1. Interacts with regulatory subunit FXYD3. Interacts with SIK1. Interacts with SLC35G1 and STIM1. Interacts with CLN3; this interaction regulates the sodium/potassium-transporting ATPase complex localization at the plasma membrane (By similarity). Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity). Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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Q9N0Z6
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MGKGVGRDKYEPAAVSEHGDKKGKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTTARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGILAATEEDFDNDNLYLGVVLAAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEDVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVIYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYTKIVEIPFNSTNKYQLSIHKNLNANEPRHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLLLPDEQFPEGFQFDTDEVNFPVDNLCFIGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPFHLLGIRVDWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEIRKLIIRRRPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (By similarity). May contribute to blood-heart barrier properties of endocardial endothelium and may control cardiac performance via endothelial Na(+)/H(+) exchange (PubMed:11738066). ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1. Interacts with regulatory subunit FXYD3. Interacts with SIK1. Interacts with SLC35G1 and STIM1. Interacts with CLN3; this interaction regulates the sodium/potassium-transporting ATPase complex localization at the plasma membrane (By similarity). Expressed in endocardial endothelial cells. Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity). Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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Q64609
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MGKGVGRDKYEPAAVSEHGDKKSKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTPARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIRSATEEEPPNDDLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEDVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAEEIEHFIHLITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWFALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIEVCCGSVMEMREKYTKIVEIPFNSTNKYQLSIHKNPNASEPKHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLLLPDEQFPEGFQFDTDEVNFPVDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVNQVNPRDAKACVVHGSDLKDMTSEELDDILRYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIVGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPFHLLGIRETWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGAALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1 (PubMed:17283221, PubMed:19339511, PubMed:23532852). Interacts with regulatory subunit FXYD3 (PubMed:15743908). Interacts with SLC35G1 and STIM1 (By similarity). Interacts with SIK1 (PubMed:17939993). Interacts with CLN3; this interaction regulates the sodium/potassium-transporting ATPase complex localization at the plasma membrane (By similarity). Expressed in the central nervous system, in most motor and sensory axons of the ventral and dorsal roots, as well as in the large motor neurons of the ventral horn (at protein level). Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1 to PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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P30714
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MGYGAGRDKYEPAATSEHGGKKGKGKGKDRDMEELKKEVTMEDHKMTLEELHRKYGTDLTRGLTTARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIRKASDLEPDNDNLYLGVVLSAVVIITGCFSYYQEAKSSRIMESFKNMVPQQALVIRNGEKLSINAENVVQGDLVEVKGGDRIPADLRIISAHGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVINTGDRTVMGRIATLASGLEGGQTPIAVEIGHFIHIITGVAVFLGVSFFILSLILHYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGASFDKSSPTWTALARIAGLCNRAVFPAGQENTPILKRDVVGDASESALLKCIELCCGSVKDMREKNQKVAEIPFNSTNKYQLSVHKNANPSESRYLLVMKGAPERILDRCSSILLQGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLLLDDEQFPDGFSFDTEDVNFPTEGLCFVGLISMIDPPRAAVPDRVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVNQVNPRDAKACVIHGTDLKDMNADQIDDILRHHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIADIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKKDKLVNERLISMAYGQIGMIQALGGFFAYFVILAENGFLPSTLLGIRVAWEDRYVNDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMDVALRMYPLKPTWWFCAFPYSLLIFIYDEVRKLILRRSPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate This alpha subunit is resistant to ouabain. The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Mainly expressed in kidney. Found in bladder, colon, eye, and testis. Found in low levels in brain, heart, spleen and liver. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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P04074
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MGKGVGRDKYEPAAVSEHGDKKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLNRGLTTARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAVLCFLAYGIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLALSRIAGLCNRAVFQANQDNLPILKRAVAGDASESALLKCIEVCCGSVKEMRERYAKIVEIPFNSTNKYQLSIHKNANAGEPRHLLVMKGAPERILDRCSSILIHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLMLPDEQFPEGFQFDTDDVNFPVDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDARACVVHGSDLKDMTPEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPQTDKLVNERLISMAYGQIGMIQALGGFFTYFVIMAENGFLPNHLLGIRVTWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate Specifically inhibited by cardiac glycosides such as digoxin or ouabain. The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1. Interacts with regulatory subunit FXYD3. Interacts with SIK1. Interacts with SLC35G1 and STIM1. Interacts with CLN3; this interaction regulates the sodium/potassium-transporting ATPase complex localization at the plasma membrane (By similarity). Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-941 by PKA modulates the response of ATP1A1 to PKC (By similarity). Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity). Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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Q92127
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MGYGAGRDKYEPAATSEQGGKKKKGKGKGKEKDMDELKKEVTMEDHKLSLDELHRKFGTDMQRGLTTARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIQAAMEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRSGEKLSINAEEVVLGDLVEVKGGDRIPADLRVISSHGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVNTGDRTVMGRIATLASGLDGGRTPIAIEIEHFIHIITGVAVFLGVSFFILSLILQYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGASFDKSSPTWTALSRVAGLCNRAVFQAGQENTPILKRDVAGDASESALLKCIELCCGSVRDMREKNHKVAEIPFNSTNKYQLSVHKNANPSESRYILVMKGAPERILDRCTSIILQGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLALPDDQFPDGFQFDTEEVNFPTENLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVNQVNPRDAKACVIHGTDLKDMTEEQIDDILRHHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPWTLLGIRVNWDDRWTNDVEDSYGQQWTYEQRKIVEFTCHTSFFISIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMDVALRMYPLKPTWWFCAFPYSLIIFIYDEVRKLIIRRSPGGWVEKESYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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A2VDL6
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MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAFGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVVREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSSILVQGKEIPLDKEMQDAFQNAYLELGGLGERVLGFCQLNLPSAKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPREAKACVVHGSDLKDMTSEQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRSMNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrients (By similarity). ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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P24797
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MDGREYSPAATTSENGGGRRKQKEKELDELKKEVNLDDHKLSLDELGRKYQVDLSRGLSNARAAEVLAQDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKIQINAENVVVGDLVEVKGGDRVPADMRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVISTGDRTVMGRIASLASGLEVGRTPIAMEIEHFIRLITGVAVFLGLSFFILSLILGYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWAALSRIAGLCNRAVFKPGQENISISKRDTAGDASESALLKCIQLSCGSVKKMRDKNPKVTEIPFNSTNKYQLSIHEREEDPQGHILVMKGAPERILERCSRILLQGQEVPLDEEMKEAFQNAYLELGGLGERVLGFCHLYLPPDKFPRGFRFDADEVNFPTSDLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPREAKACVVHGSDLKDMTAEQLDEILRNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPRTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPARLLGVRLAWDDRSTNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFAYDEVRKLILRRYPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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Q9UQ25
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MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDVLARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPMSQVNPREAKACVVHGSDLKDMTSEQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTMNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrients. ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. Extended N-terminus.
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Q80UZ8
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MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGALLCFLAYGILAAMEDEPSNDNLYLGIVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGQTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPREAKACVVHGSDLKDMTSEQLDEILRDHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTTNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (By similarity). ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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D2WKD8
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MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVVREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDNPQSHVLVMKGAPERILDRCSSILVQGKEIPLDKEMQDAFQNAYLELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPREAKACVVHGSDLKDMTSEQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRSMNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrients (By similarity). ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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Q5RCD8
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MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDVLARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFPGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIREADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCPTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPMSQVNPREAKACVVHGSDLKDMTSEQLDEILKNHTEIVFARTSPQQKLVIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLVFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTMNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
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This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrients (By similarity). ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate The sodium/potassium-transporting ATPase is composed of a catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an additional regulatory subunit. Interacts with regulatory subunit FXYD1. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.
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Q7Z4Y8
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MAPFVRNLVEKTPALVNAAVTYLKPRLAAFWYYTTVELVPPTPAEIPRAIQSLKKIVSSAQTGSFKQLTVKEALLNGLVATEVSTWFYVREITGKRGIIG
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Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(0) seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Belongs to the ATPase g subunit family. Could be the product of a pseudogene.
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Q0DJH7
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MVAVTVMRKSRNFVGPSPPTPPAEITTTLELSSIDRVPGLRHNVRSLHVFRRHKNSGPVVDGDSRRPAAVIRAALARALADYPAFAGRFVGSLLAGDACVACTGEGAWFVEAAADCSLDDVNGLEYPLMISEEELLPAPEDGVDPTSIPVMMQVTEFTCGGFILGLVAVHTLADGLGAAQFITAVAELARGMDKLRVAPVWDRSLIPNPPKLPPGPPPSFQSFGFQHFSTDVTSDRIAHVKAEYFQTFGQYCSTFDVATAKVWQARTRAVGYKPEIQVHVCFFANTRHLLTQVLPKDGGYYGNCFYPVTVTAIAEDVATKELLDVIKIIRDGKARLPMEFAKWASGDVKVDPYALTFEHNVLFVSDWTRLGFFEVDYGWGTPNHIIPFTYADYMAVAVLGAPPMPKKGTRIMTQCVENKCIKEFQDEMKAFI
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Involved in the incorporation of ferulate into the cell wall. May act as arabinoxylan feruloyl transferase. Plants over-expressing AT5 have significant increase of ferulate in leaf cell wall. Belongs to the plant acyltransferase family.
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O04035
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MVNEKKMLPKRIILMRHGESAGNIDAGAYATTPDHKIPLTEEGRAQAREAGKKMRALISTQSGGACGENWRVYFYVSPYERTRTTLREVGKGFSRKRVIGVREECRIREQDFGNFQVEERMRVVKETRERFGRFFYRFPEGESAADVYDRVSSFLESMWRDVDMNRHQVDPSSELNLVIVSHGLTSRVFLTKWFKWTVAEFERLNNFGNCEFRVMELGASGEYTFAIHHSEEEMLDWGMSKDMIDDQKDRVDGCRVTTSNDSCSLHLNEYFDLLDVTDDEE
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May play a role in carbohydrates metabolism. Belongs to the phosphoglycerate mutase family.
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Q0WMW9
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MSPDNKLLPKRIILVRHGESEGNLDTAAYTTTPDHKIQLTDSGLLQAQEAGARLHALISSNPSSPEWRVYFYVSPYDRTRSTLREIGRSFSRRRVIGVREECRIREQDFGNFQVKERMRATKKVRERFGRFFYRFPEGESAADVFDRVSSFLESLWRDIDMNRLHINPSHELNFVIVSHGLTSRVFLMKWFKWSVEQFEGLNNPGNSEIRVMELGQGGDYSLAIHHTEEELATWGLSPEMIADQKWRANAHKGEWKEDCKWYFGDFFDHMADSDKECETEATEDREEEEEEEGKRVNLLTSSEYSNEPELYNGQCC
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Phosphoglycerate mutase-like protein lacking PGM activity. May play a role in carbohydrates metabolism. Expressed in roots, leaves, stems, flowers and siliques. By sucrose. Belongs to the phosphoglycerate mutase family.
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Q8N2T0
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MTSERSRIPCLSAAAAEGTGKKQQEGRAMATLDRKVPSPEAFLGKPWSSWIDAAKLHCSDNVDLEEAGKEGGKSREVMRLNKEDMHLFGHYPAHDDFYLVVCSACNQVVKPQVFQSHCERRHGSMCRPSPSPVSPASNPRTSLVQVKTKACLSGHHSASSTSKPFKTPKDNLLTSSSKQHTVFPAKGSRDKPCVPVPVVSLEKIPNLVKADGANVKMNSTTTTAVSASSTSSSAVSTPPLIKPVLMSKSVPPSPEKILNGKGILPTTIDKKHQNGTKNSNKPYRRLSEREFDPNKHCGVLDPETKKPCTRSLTCKTHSLSHRRAVPGRKKQFDLLLAEHKAKSREKEVKDKEHLLTSTREILPSQSGPAQDSLLGSSGSSGPEPKVASPAKSRPPNSVLPRPSSANSISSSTSSNHSGHTPEPPLPPVGGDLASRLSSDEGEMDGADESEKLDCQFSTHHPRPLAFCSFGSRLMGRGYYVFDRRWDRFRFALNSMVEKHLNSQMWKKIPPAADSPLPSPAAHITTPVPASVLQPFSNPSAVYLPSAPISSRLTSSYIMTSAMLSNAAFVTSPDPSALMSHTTAFPHVAATLSIMDSTFKAPSAVSPIPAVIPSPSHKPSKTKTSKSSKVKDLSTRSDESPSNKKRKPQSSTSSSSSSSSSSLQTSLSSPLSGPHKKNCVLNASSALNSYQAAPPYNSLSVHNSNNGVSPLSAKLEPSGRTSLPGGPADIVRQVGAVGGSSDSCPLSVPSLALHAGDLSLASHNAVSSLPLSFDKSEGKKRKNSSSSSKACKITKMPGMNSVHKKNPPSLLAPVPDPVNSTSSRQVGKNSSLALSQSSPSSISSPGHSRQNTNRTGRIRTLP
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Truncated N-terminus. Contaminating sequence. Sequence of unknown origin in the N-terminal part.
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Q8JFU1
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MKMEDMSLSGLDNTKLEALAHDVYSDLVEDACLGLCFEVHRAVKQGYFFLDETDQESMKDFEIVDQPGVDIFGQVYNQWKNKECVCPNCSRSIAASRFAPHLEKCLGMGRNSSRIANRRIASSNNTSKSESDQEDNDDINDNDWSYGSEKKAKKRKSEKNPNSPRRSKSLKHKNGELSGSVNPDMYKYNYSSGISYETLGPEELRSILTTQCGVVSEHTKKMCTRSQRCPQHTDEQRRAVRVFLLGPSASTLPDADTMLENEAYEPPDGQLIMSRLHWDASSDISPSDSASSKASTNNSESKRPKKKKPSTLSLTPAGERDKAQERDRIAGSGSSGSSSQNALGLSSRKKRPKLAVPPAPSIYDDLN
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Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histone H2B. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription. Component of some SAGA transcription coactivator-HAT complexes. Within the SAGA complex, participates in a subcomplex of SAGA called the DUB module (deubiquitination module) (By similarity). The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module. The C-terminal SGF11-type zinc-finger domain forms part of the 'catalytic lobe' of the SAGA deubiquitination module. Belongs to the SGF11 family.
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Q9NPU5
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MKMEEMSLSGLDNSKLEAIAQEIYADLVEDSCLGFCFEVHRAVKCGYFFLDDTDPDSMKDFEIVDQPGLDIFGQVFNQWKSKECVCPNCSRSIAASRFAPHLEKCLGMGRNSSRIANRRIANSNNMNKSESDQEDNDDINDNDWSYGSEKKAKKRKSDKNPNSPRRSKSLKHKNGELSNSDPFKYNNSTGISYETLGPEELRSLLTTQCGVISEHTKKMCTRSLRCPQHTDEQRRTVRIYFLGPSAVLPEVESSLDNDSFDMTDSQALISRLQWDGSSDLSPSDSGSSKTSENQGWGLGTNSSESRKTKKKKSHLSLVGTASGLGSNKKKKPKPPAPPTPSIYDDIN
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Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B (PubMed:18206972, PubMed:21746879). The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. Within the complex, it is required to recruit USP22 and ENY2 into the SAGA complex (PubMed:18206972). Regulates H2B monoubiquitination (H2Bub1) levels. Affects subcellular distribution of ENY2, USP22 and ATXN7L3B (PubMed:27601583). Component of some SAGA transcription coactivator-HAT complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H, TAF10, TRRAP and USP22. Within the SAGA complex, ENY2, ATXN7, ATXN7L3, and USP22 form an additional subcomplex of SAGA called the DUB module (deubiquitination module) (PubMed:18206972, PubMed:21746879, PubMed:27601583). Interacts directly with ENY2 and USP22 (PubMed:18206972). The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module. The C-terminal SGF11-type zinc-finger domain together with the C-terminal catalytic domain of USP22 forms the 'catalytic lobe' of the SAGA deubiquitination module. Belongs to the SGF11 family.
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Q8C1T7
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MKMEEMSLSGLDNSKLEAIAQEIYADLVEDSCLGFCFEVHRAVKCGYFFLDDTDPDSMKDFEIVDQPGLDIFGQVFNQWKSKECVCPNCSRSIAASRFAPHLEKCLGMGRNSSRIANRRIANSNNMNKSESDQEDNDDINDNDWSYGSEKKAKKRKSDKNPNSPRRSKSLKHKNGELSNSDPFKYSNSTGISYETLGPEELRSLLTTQCGVISEHTKKMCTRSLRCPQHTDEQRRTVRIYFLGPSAVLPEVESSLDNDGFDMTDSQALISRLQWDGSSDLSPSDSGSSKTSENQGWGLGTNSSESRKTKKKKSHLSLVGTASGLGSNKKKKPKPPAPPTPSIYDDIN
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Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B. The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. Within the complex, it is required to recruit USP22 and ENY2 into the SAGA complex. Regulates H2B monoubiquitination (H2Bub1) levels. Affects subcellular distribution of ENY2, USP22 and ATXN7L3B. Component of some SAGA transcription coactivator-HAT complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H, TAF10, TRRAP and USP22. Within the SAGA complex, ENY2, ATXN7, ATXN7L3, and USP22 form an additional subcomplex of SAGA called the DUB module (deubiquitination module). Interacts directly with ENY2 and USP22. The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module. The C-terminal SGF11-type zinc-finger domain together with the C-terminal catalytic domain of USP22 forms the 'catalytic lobe' of the SAGA deubiquitination module. Belongs to the SGF11 family.
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Q0DKA5
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MAAAAPDKAVERLSQKLVHPSSPTPSAPLRLSWLDRYPTQMALIESLHVFKPDPARDAAGQGLAPARAIETALARALVEYYPLAGRLAVSRDSGELQVDCCGGAGGHGGVWFIEAAVPCRLEDVDYLEYPLAISKDELLPHPRPRPTRDEEDKLILLVQVTTFACGGFVVGFRFSHAVADGPGAAQFMGAVGELARGGERITVAPSWGRDAVPDPAGAMVGALPEPAGASRLEYLAIDISADYINHFKSQFAAATGGARCSAFEVLIAKAWQSRTRAAAFDPSTPINLSFAMNARPLLLPRGGAGFYGNCYYIMRVASTAGRVATASVTDVVRMIREGKKRLPSEFARWAAGEMAGVDPYQITSDYRTLLVSDWTRLGFAEVDYGWGPPGHVVPLTNLDYIATCILVKPWAHKPGARLITQCVTPDRVTAFHDAMVDIN
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Involved in the incorporation of ferulate into the cell wall. May act as arabinoxylan feruloyl transferase. No visible phenotype under normal growth conditions, but mutant plants have significant reduction of ferulate in leaf cell wall. Belongs to the plant acyltransferase family.
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Q29449
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MPTMRRTVSEIRSRAEGYEKTDDVSEKTSLADQEEIRTIFINQPQLTKFCNNHVSTAKYNIITFLPRFLYSQFRRAANSFFLFIALLQQIPDVSPTGRYTTLVPLLFILAVAAIKEIIEDIKRHKADNAVNKKQTQVLRNGAWEIVHWEKVNVGDIVIIKGKEYIPADTVLLSSSEPQAMCYIETSNLDGETNLKIRQGLPATSDIKDIDSLMRLSGRIECESPNRHLYDFVGNIRLDGRSTVPLGADQILLRGAQLRNTQWVHGIVVYTGHDTKLMQNSTSPPLKLSNVERITNVQILILFCILIAMSLVCSVGSAIWNRRHSGRDWYLNLNYGGANNFGLNFLTFIILFNNLIPISLLVTLEVVKFTQAYFINWDLDMHYEPTDTAAMARTSNLNVELGQVKYIFSDKTGTLTCNVMQFKKCTIAGVAYGQNSQFGDEKTFSDSSLLENLQNNHPTAPIICEFLTMMAVCHTAVPEREGDKIIYQAASPDEGALVRAAKQLNFVFTGRTPDSVIIDSLGQEERYELLNVLEFTSARKRMSVIVRTPSGKLRLYCKGADTVIYDRLAETSKYKEITLKHLEQFATEGLRTLCFAVAEISESDFQEWRAVYHRASTSVQNRLLKLEESYELIEKNLQLLGATAIEDKLQDQVPETIETLMKADIKIWILTGDKQETAINIGHSCKLRRKNMGMIVINEGSLDGTRETLSRHCTTLGDALRKENDFALIIDGKTLKYALTFGVRQYFLDLALSCKAVICCRVSPLQKSEVVEMVKKQVKVITLAIGDGANDVSMIQTAHVGVGISGNEGLQAANSSDYSIAQFKYLKNLLMVHGAWNYNRGSKCILYCFYKNIVLYIIEIWFAFVNGFSGQILFERWCIGLYNVMFTAMPPLTLGIFERSCRKEYMLKYPELYKTSQNALDFNTKVFWVHCLNGLFHSVILFWFPLKALQYGTVFENGRTSDYLLLGNFVYTFVVITVCLKAGLETSYWTWFSHIAIWGSIALWVVFFGIYSSLWPAVPMAPDMSGEAAMLFSSGVFWMGLLFIPVASLLLDVVYKVIKRTAFKTLVDEVQELEAKSQDPGAVVLGKSLTERAQLLKNVFKKNHVNLYRSESLQQNLLHGYAFSQDENGIVSQSEVIRAYDTTKQRPDEW
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Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (By similarity). Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. In vitro, its ATPase activity is selectively and stereospecifically stimulated by phosphatidylserine (PS) (By similarity). The flippase complex ATP8A1:TMEM30A seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane (By similarity). Acts as aminophospholipid translocase at the plasma membrane in neuronal cells (By similarity). ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2. a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. Interacts with TMEM30A to form a flippase complex; this complex forms an intermediate phosphoenzyme. Interacts with TMEM30B; this interaction is reported conflictingly. Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B. In the presence of TMEM30A, predominantly located in cytoplasmic punctate structures and localizes to the plasma membrane (By similarity). Localizes to plasma membranes of red blood cells (By similarity). Kidney. Cleaved by calpain in a caspase- and calcium influx-dependent manner during platelet apoptosis leading to a 100 kDa polypeptide. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
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Q4W5P2
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MPTMRRTVSEIRSRAEGYEKTDDVSEKTSLADQEEVRTIFINQPQLTKFCNNHVSTAKYNIITFLPRFLYSQFRRAANSFFLFIALLQQIPDVSPTGRYTTLVPLLFILAVAAIKEIIEDIKRHKADNAVNKKQTQVLRNGAWEIVHWEKVAVGEIVKVTNGEHLPADLISLSSSEPQAMCYIETSNLDGETNLKIRQGLPATSDIKDVDSLMRISGRIECESPNRHLYDFVGNIRLDGHGTVPLGADQILLRGAQLRNTQWVHGIVVYTGHDTKLMQNSTSPPLKLSNVERITNVQILILFCILIAMSLVCSVGSAIWNRRHSGKDWYLNLNYGGASNFGLNFLTFIILFNNLIPISLLVTLEVVKFTQAYFINWDLDMHYEPTDTAAMARTSNLNEELGQVKYIFSDKTGTLTCNVMQFKKCTIAGVAYGHVPEPEDYGCSPDEWQNSQFGDEKTFSDSSLLENLQNNHPTAPIICEFLTMMAVCHTAVPEREGDKIIYQAASPDEGALVRAAKQLNFVFTGRTPDSVIIDSLGQEERYELLNVLEFTSARKRMSVIVRTPSGKLRLYCKGADTVIYDRLAETSKYKEITLKHLEQFATEGLRTLCFAVAEISESDFQEWRAVYQRASTSVQNRLLKLEESYELIEKNLQLLGATAIEDKLQDQVPETIETLMKADIKIWILTGDKQETAINIGHSCKLLKKNMGMIVINEGSLDGTRETLSRHCTTLGDALRKENDFALIIDGKTLKYALTFGVRQYFLDLALSCKAVICCRVSPLQKSEVVEMVKKQVKVVTLAIGDGANDVSMIQTAHVGVGISGNEGLQAANSSDYSIAQFKYLKNLLMIHGAWNYNRVSKCILYCFYKNIVLYIIEIWFAFVNGFSGQILFERWCIGLYNVMFTAMPPLTLGIFERSCRKENMLKYPELYKTSQNALDFNTKVFWVHCLNGLFHSVILFWFPLKALQYGTAFGNGKTSDYLLLGNFVYTFVVITVCLKAGLETSYWTWFSHIAIWGSIALWVVFFGIYSSLWPAIPMAPDMSGEAAMLFSSGVFWMGLLFIPVASLLLDVVYKVIKRTAFKTLVDEVQELEAKSQDPGAVVLGKSLTERAQLLKNVFKKNHVNLYRSESLQQNLLHGYAFSQDENGIVSQSEVIRAYDTTKQRPDEW
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Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:31416931). Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. In vitro, its ATPase activity is selectively and stereospecifically stimulated by phosphatidylserine (PS) (PubMed:31416931). The flippase complex ATP8A1:TMEM30A seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane (By similarity). Acts as aminophospholipid translocase at the plasma membrane in neuronal cells (By similarity). ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2. a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate ATPase activity is stimulated by phosphatidylserine (PS) and minimally by phosphatidylethanolamine (PE). ATPase activity is inhibited by beryllium fluoride and aluminum trifluoride (PubMed:31416931). Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit (PubMed:31416931). Interacts with TMEM30A to form a flippase complex; this complex forms an intermediate phosphoenzyme (PubMed:20947505, PubMed:20961850, PubMed:21914794, PubMed:31416931). Interacts with TMEM30B; this interaction is reported conflictingly (PubMed:20961850). Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B (PubMed:20947505). In the presence of TMEM30A, predominantly located in cytoplasmic punctate structures and localizes to the plasma membrane (PubMed:20947505). Localizes to plasma membranes of red blood cells (By similarity). Found in most adult tissues except liver, testis and placenta. Most abundant in heart, brain and skeletal muscle. Also detected in fetal tissues. Isoform 1 is only detected in brain, skeletal muscle and heart and is the most abundant form in skeletal muscle. Highly expressed in platelets (PubMed:30674456). Cleaved by calpain in a caspase- and calcium influx-dependent manner during platelet apoptosis leading to a 100 kDa polypeptide. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. Truncated N-terminus. Truncated N-terminus.
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Q8BR88
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MPTMRRTVSEIRSRAEGYEKTDDVSEKTSLADQEEVRTIFINQPQLTKFCNNHVSTAKYNVITFLPRFLYSQFRRAANSFFLFIALLQQIPDVSPTGRYTTLVPLLFILAVAAIKEIIEDIKRHKADNAVNKKQTQVLRNGAWEIVHWEKVAVGEIVKVTNGEHLPADLLSLSSSEPQAMCYIETSNLDGETNLKIRQGLPATSDIKDIDSLMRISGRIECESPNRHLYDFVGNIRLDGHGTVPLGADQILLRGAQLRNTQWVHGIVVYTGHDTKLMQNSTSPPLKLSNVERITNVQILILFCILIAMSLVCSVGSAIWNRRHSGKDWYLHLHYGGASNFGLNFLTFIILFNNLIPISLLVTLEVVKFTQAYFINWDLDMHYEPTDTAAMARTSNLNEELGQVKYIFSDKTGTLTCNVMQFKKCTIAGVAYGHVPEPEDYGCSPDEWQSSQFGDEKTFNDPSLLDNLQNNHPTAPIICEFLTMMAVCHTAVPEREGDKIIYQAASPDEGALVRAAKQLNFVFTGRTPDSVIIDSLGQEERYELLNVLEFTSARKRMSVVVRTPSGKLRLYCKGADTVIYERLAETSKYKEITLKHLEQFATEGLRTLCFAVAEISESDFEEWRAVYHRASTSVQNRLLKLEESYELIEKNLQLLGATAIEDKLQDQVPETIETLMKADIKIWILTGDKQETAINIGHSCRLLKRNMGMIVINEGSLDGTRETLSRHCTTLGDALRKENDFALIIDGKTLKYALTFGVRQYFLDLALSCKAVICCRVSPLQKSEVVEMVKKQVKVITLAIGDGANDVSMIQTAHVGVGISGNEGLQAANSSDYSIAQFKYLKNLLMVHGAWNYNRVSKCILYCFYKNIVLYIIEIWFAFVNGFSGQILFERWCIGLYNVMFTAMPPLTLGIFERSCRKENMLKYPELYKTSQNALDFNTKVFWVHCLNGLFHSVILFWFPLKALQYGTVFGNGKTSDYLLLGNFVYTFVVITVCLKAGLETSYWTWFSHIAIWGSIALWVVFFGIYSSLWPAVPMAPDMSGEAAMLFSSGVFWVGLLSIPVASLLLDVLYKVIKRTAFKTLVDEVQELEAKSQDPGAVVLGKSLTERAQLLKNVFKKNHVNLYRSESLQQNLLHGYAFSQDENGIVSQSEVIRAYDTTKQRPDEW
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Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:20224745, PubMed:16618126). Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. In vitro, its ATPase activity is selectively and stereospecifically stimulated by phosphatidylserine (PS) (PubMed:20224745, PubMed:16618126). The flippase complex ATP8A1:TMEM30A seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane (PubMed:23269685). Acts as aminophospholipid translocase at the plasma membrane in neuronal cells; the activity is associated with hippocampus-dependent learning (PubMed:22007859). May play a role in brain connectivity (PubMed:27287255). ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2. a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate ATPase activity is stimulated by phosphatidylserine (PS) and minimally by phosphatidylethanolamine (PE) (PubMed:16618126, PubMed:20224745). ATPase activity is inhibited by the vanadate and by the presence of calcium (PubMed:20224745). Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit (PubMed:23269685). Interacts with TMEM30A to form a flippase complex; this complex forms an intermediate phosphoenzyme (PubMed:23269685). Interacts with TMEM30B; this interaction is reported conflictingly (By similarity). Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B. In the presence of TMEM30A, predominantly located in cytoplasmic punctate structures (By similarity). Localizes to plasma membranes of red blood cells (PubMed:16643453). Localizes predominantly in the intracellular membranes, rather than the plasma membrane of platelets (PubMed:30674456). Found in most tissues except liver and testis. Most abundant in brain and lung. Also detected in fetal tissues. Isoform 1 is expressed in brain. Isoform 2 and isoform 3 are expressed in reticulocytes (PubMed:16643453). Expressed in mouse hippocampus in both dentate gyrus (DG) and the CA3 regions. Expressed in both neuronal as well as non-neuronal cells within the DG (PubMed:27287255). Highly expressed in platelets (PubMed:30674456). Cleaved by calpain in a caspase- and calcium influx-dependent manner only during platelet apoptosis and may lead to inactivation. Mice overexpressing ATP8A1 in brain display an autistic-like behavior but no difference in hippocampus-dependent learning. Unlike the mice overexpressing ATP8A1,homozygous knockout mice for ATP8A1 do not show any deficits in sociability behavior. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. Initial characterization studies with purified Atp8a1 enzyme demonstrated similar but distinct properties compared to the plasma membrane aminophospholipid flippase; however, the flippase complex accessory beta subunit was not included in the assays.
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C7EXK4
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MSRATSVGDQLDVPARTIYLNQPHLNKFCDNQISTAKYSVVTFLPRFLYEQIRRAANAFFLFIALLQQIPDVSPTGRYTTLVPLIIILTIAGIKEIVEDFKRHKADNAVNKKKTIVLRNGMWQTIVWKEVAVGDIVKVVNGQYLPADVVLLSSSEPQAMCYVETANLDGETNLKIRQGLSHTADMQTREVLMKLSGTIECEGPNRHLYDFTGNLNLDGKSPVALGPDQILLRGTQLRNTQWGFGIVVYTGHDTKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSVGALYWNGSQGGKNWYIKKMDATSDNFGYNLLTFIILYNNLIPISLLVTLEVVKYTQALFINWDTDMYYLGNDTPAMARTSNLNEELGQVKYLFSDKTGTLTCNIMNFKKCSIAGVTYGHFPELTREPSSDDFSRIPPPPSDSCDFDDPRLLKNIEDHHPTAPCIQEFLTLLAVCHTVVPERDGDSIVYQASSPDEAALVKGARKLGFVFTARTPYSVIIEAMGQEQTFGILNVLEFSSDRKRMSVIVRTPSGQLRLYCKGADNVIFERLSKDSKYMEETLCHLEYFATEGLRTLCVAYADLSERDYEEWLKVYQEASTILKDRAQRLEECYEIIEKNLLLLGATAIEDRLQAGVPETIATLLKAEIKIWVLTGDKQETAINIGYSCRLVSQNMALILLKEDSLDATRAAITQHCADLGSLLGKENDAALIIDGHTLKYALSFEVRRSFLDLALSCKAVICCRVSPLQKSEIVDVVKKRVKAITLAIGDGANDVGMIQTAHVGVGISGNEGMQATNNSDYAIAQFSYLEKLLLVHGAWSYNRVTKCILYCFYKNVVLYIIELWFAFVNGFSGQILFERWCIGLYNVIFTALPPFTLGIFERSCSQESMLRFPQLYKITQNAEGFNTKVFWGHCINALVHSLILFWFPMKALEHDTVLANGHATDYLFVGNIVYTYVVVTVCLKAGLETTAWTKFSHLAVWGSMLIWLVFFGIYSTIWPTIPIAPDMKGQATMVLSSAHFWLGLFLVPTACLIEDVAWRAAKHTCKKTLLEEVQELEMKSRVMGRAMLRDSNGKRMNERDRLLKRLSRKTPPTLFRGSSLQQSMPHGYAFSQEEHGAVTQEEIVRAYDTTKQKSRKK
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Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:19778899, PubMed:24706822, PubMed:31371510, PubMed:26592152). Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Reconstituted to liposomes, the ATP8A2:TMEM30A flippase complex predominantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE) (PubMed:19778899, PubMed:24706822, PubMed:31371510, PubMed:26592152). Phospholipid translocation is not associated with a countertransport of an inorganic ion or other charged substrate from the cytoplasmic side toward the exoplasm in connection with the phosphorylation from ATP (PubMed:31371510). ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth. Proposed to function in the generation and maintenance of phospholipid asymmetry in photoreceptor disk membranes and neuronal axon membranes. May be involved in vesicle trafficking in neuronal cells. Required for normal visual and auditory function; involved in photoreceptor and inner ear spiral ganglion cell survival. ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2. a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ADP + H(+) + phosphate ATPase activity is stimulated by phosphatidylserine (PS) and minimally by phosphatidylethanolamine (PE). ATPase activity is inhibited by N-ethylmaleimide (NEM) and vanadate. Flippase activity is inhibited by NEM and 1,2-dioleoyl-sn-glycero-3-phospho-L-serine (DOPS). Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit (PubMed:21454556, PubMed:26592152). Interacts with TMEM30A to form a flippase complex (PubMed:21454556). Localizes to the Golgi and endosomes in photoreceptor cells (By similarity). Localizes to disk membranes of rod photoreceptor outer segments (ROS) (PubMed:21454556). Expressed in retinal photoreceptor cells and testis. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. Extended N-terminus.
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Q9NYM3
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MLNGAGLDKALKMSLPRRSRIRSSVGPVRSSLGYKKAEDEMSRATSVGDQLEAPARTIYLNQPHLNKFRDNQISTAKYSVLTFLPRFLYEQIRRAANAFFLFIALLQQIPDVSPTGRYTTLVPLIIILTIAGIKEIVEDFKRHKADNAVNKKKTIVLRNGMWHTIMWKEVAVGDIVKVVNGQYLPADVVLLSSSEPQAMCYVETANLDGETNLKIRQGLSHTADMQTREVLMKLSGTIECEGPNRHLYDFTGNLNLDGKSLVALGPDQILLRGTQLRNTQWVFGIVVYTGHDTKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSAGALYWNRSHGEKNWYIKKMDTTSDNFGYNLLTFIILYNNLIPISLLVTLEVVKYTQALFINWDTDMYYIGNDTPAMARTSNLNEELGQVKYLFSDKTGTLTCNIMNFKKCSIAGVTYGHFPELAREPSSDDFCRMPPPCSDSCDFDDPRLLKNIEDRHPTAPCIQEFLTLLAVCHTVVPEKDGDNIIYQASSPDEAALVKGAKKLGFVFTARTPFSVIIEAMGQEQTFGILNVLEFSSDRKRMSVIVRTPSGRLRLYCKGADNVIFERLSKDSKYMEETLCHLEYFATEGLRTLCVAYADLSENEYEEWLKVYQEASTILKDRAQRLEECYEIIEKNLLLLGATAIEDRLQAGVPETIATLLKAEIKIWVLTGDKQETAINIGYSCRLVSQNMALILLKEDSLDATRAAITQHCTDLGNLLGKENDVALIIDGHTLKYALSFEVRRSFLDLALSCKAVICCRVSPLQKSEIVDVVKKRVKAITLAIGDGANDVGMIQTAHVGVGISGNEGMQATNNSDYAIAQFSYLEKLLLVHGAWSYNRVTKCILYCFYKNVVLYIIELWFAFVNGFSGQILFERWCIGLYNVIFTALPPFTLGIFERSCTQESMLRFPQLYKITQNGEGFNTKVFWGHCINALVHSLILFWFPMKALEHDTVLTSGHATDYLFVGNIVYTYVVVTVCLKAGLETTAWTKFSHLAVWGSMLTWLVFFGIYSTIWPTIPIAPDMRGQATMVLSSAHFWLGLFLVPTACLIEDVAWRAAKHTCKKTLLEEVQELETKSRVLGKAVLRDSNGKRLNERDRLIKRLGRKTPPTLFRGSSLQQGVPHGYAFSQEEHGAVSQEEVIRAYDTTKKKSRKK
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Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (Probable). Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules (By similarity). Reconstituted to liposomes, the ATP8A2:TMEM30A flippase complex predominantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE) (By similarity). Phospholipid translocation is not associated with a countertransport of an inorganic ion or other charged substrate from the cytoplasmic side toward the exoplasm in connection with the phosphorylation from ATP (By similarity). ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth (By similarity). Proposed to function in the generation and maintenance of phospholipid asymmetry in photoreceptor disk membranes and neuronal axon membranes (By similarity). May be involved in vesicle trafficking in neuronal cells (By similarity). Required for normal visual and auditory function; involved in photoreceptor and inner ear spiral ganglion cell survival (By similarity). ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2. a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ADP + H(+) + phosphate Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. Interacts with TMEM30A to form a flippase complex. Localizes to the Golgi and endosomes in photoreceptor cells (By similarity). Localizes to disk membranes of rod photoreceptor outer segments (ROS) (By similarity). Strongly expressed in the brain, cerebellum, retina and testis. The disease is caused by variants affecting the gene represented in this entry. A chromosomal aberration disrupting ATP8A2 has been found in a patient with severe intellectual disability and major hypotonia. Translocation t(10;13)(p12.1;q12.13) (PubMed:20683487). Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
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B2RQF2
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MSRATSVGDQLEAPARIIYLNQSHLNKFCDNRISTAKYSVLTFLPRFLYEQIRRAANAFFLFIALLQQIPDVSPTGRYTTLVPLVIILTIAGIKEIIEDFKRHKADNAVNKKKTIVLRNGMWHTIMWKEVAVGDIVKVLNGQYLPADMVLFSSSEPQGMCYVETANLDGETNLKIRQGLSHTTDMQTRDVLMKLSGRIECEGPNRHLYDFTGNLHLDGKSSVALGPDQILLRGTQLRNTQWVFGVVVYTGHDSKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSVGALFWNGSHGGKSWYIKKMDTNSDNFGYNLLTFIILYNNLIPISLLVTLEVVKYTQALFINWDMDMYYIENDTPAMARTSNLNEELGQVKYLFSDKTGTLTCNIMNFKKCSIAGVTYGHFPELAREQSSDDFCRMTSCTNDSCDFNDPRLLKNIEDQHPTAPCIQEFLTLLAVCHTVVPEKDGDEIIYQASSPDEAALVKGAKKLGFVFTGRTPYSVIIEAMGQEQTFGILNVLEFSSDRKRMSVIVRLPSGQLRLYCKGADNVIFERLSKDSKYMEETLCHLEYFATEGLRTLCVAYADLSENEYEEWLKVYQEASIILKDRAQRLEECYEIIEKNLLLLGATAIEDRLQAGVPETIATLLKAEIKIWVLTGDKQETAINIGYSCRLVSQNMALILLKEDSLDATRAAITQHCTDLGNLLGKENDVALIIDGHTLKYALSFEVRRSFLDLALSCKAVICCRVSPLQKSEIVDVVKKRVKAITLAIGDGANDVGMIQTAHVGVGISGNEGMQATNNSDYAIAQFSYLEKLLLVHGAWSYNRVTKCILYCFYKNVVLYIIELWFAFVNGFSGQILFERWCIGLYNVIFTALPPFTLGIFERSCTQESMLRFPQLYRITQNAEGFNTKVFWGHCINALVHSLILFWVPMKALEHDTPVTSGHATDYLFVGNIVYTYVVVTVCLKAGLETTAWTKFSHLAVWGSMLIWLVFFGVYSTIWPTIPIAPDMKGQATMVLSSAYFWLGLFLVPTACLIEDVAWRAAKHTCKKTLLEEVQELETKSRVMGKAMLRDSNGKRMNERDRLIKRLSRKTPPTLFRTGSIQQCVSHGYAFSQEEHGAVTQEEIVRAYDTTKENSRKK
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Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:22912588). Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Reconstituted to liposomes, the ATP8A2:TMEM30A flippase complex predominantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE) (PubMed:22912588). Phospholipid translocation is not associated with a countertransport of an inorganic ion or other charged substrate from the cytoplasmic side toward the exoplasm in connection with the phosphorylation from ATP (By similarity). ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth (PubMed:22641037). Proposed to function in the generation and maintenance of phospholipid asymmetry in photoreceptor disk membranes and neuronal axon membranes. May be involved in vesicle trafficking in neuronal cells. Required for normal visual and auditory function; involved in photoreceptor and inner ear spiral ganglion cell survival (PubMed:24413176). ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2. a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ADP + H(+) + phosphate Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit. Interacts with TMEM30A to form a flippase complex. Localizes to the Golgi and endosomes in photoreceptor cells (PubMed:24413176). Localizes to disk membranes of rod photoreceptor outer segments (ROS) (By similarity). Found in testis, heart and brain. Most abundant in testis. Also detected in fetal tissues. Expressed in retinal photoreceptor cells; detected in retina outer nuclear layer and inner segment (at protein level). Defects in Atp8a2 are the cause of Wabbler-lethal (wl) phenotype. Homozygotes show severe neurological annormalities that include ataxia and body tremors linked to progressive axonal degeneration in several areas of the nervous system. Atp8a2 and Atp8a1 double mutant mice die soon after birth. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
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Q9BTP8
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MSTERDSETTFDEDSQPNDEVVPYSDDETEDELDDQGSAVEPEQNRVNREAEENREPFRKECTWQVKANDRKYHEQPHFMNTKFLCIKESKYANNAIKTYKYNAFTFIPMNLFEQFKRAANLYFLALLILQAVPQISTLAWYTTLVPLLVVLGVTAIKDLVDDVARHKMDKEINNRTCEVIKDGRFKVAKWKEIQVGDVIRLKKNDFVPADILLLSSSEPNSLCYVETAELDGETNLKFKMSLEITDQYLQREDTLATFDGFIECEEPNNRLDKFTGTLFWRNTSFPLDADKILLRGCVIRNTDFCHGLVIFAGADTKIMKNSGKTRFKRTKIDYLMNYMVYTIFVVLILLSAGLAIGHAYWEAQVGNSSWYLYDGEDDTPSYRGFLIFWGYIIVLNTMVPISLYVSVEVIRLGQSHFINWDLQMYYAEKDTPAKARTTTLNEQLGQIHYIFSDKTGTLTQNIMTFKKCCINGQIYGDHRDASQHNHNKIEQVDFSWNTYADGKLAFYDHYLIEQIQSGKEPEVRQFFFLLAVCHTVMVDRTDGQLNYQAASPDEGALVNAARNFGFAFLARTQNTITISELGTERTYNVLAILDFNSDRKRMSIIVRTPEGNIKLYCKGADTVIYERLHRMNPTKQETQDALDIFANETLRTLCLCYKEIEEKEFTEWNKKFMAASVASTNRDEALDKVYEEIEKDLILLGATAIEDKLQDGVPETISKLAKADIKIWVLTGDKKETAENIGFACELLTEDTTICYGEDINSLLHARMENQRNRGGVYAKFAPPVQESFFPPGGNRALIITGSWLNEILLEKKTKRNKILKLKFPRTEEERRMRTQSKRRLEAKKEQRQKNFVDLACECSAVICCRVTPKQKAMVVDLVKRYKKAITLAIGDGANDVNMIKTAHIGVGISGQEGMQAVMSSDYSFAQFRYLQRLLLVHGRWSYIRMCKFLRYFFYKNFAFTLVHFWYSFFNGYSAQTAYEDWFITLYNVLYTSLPVLLMGLLDQDVSDKLSLRFPGLYIVGQRDLLFNYKRFFVSLLHGVLTSMILFFIPLGAYLQTVGQDGEAPSDYQSFAVTIASALVITVNFQIGLDTSYWTFVNAFSIFGSIALYFGIMFDFHSAGIHVLFPSAFQFTGTASNALRQPYIWLTIILAVAVCLLPVVAIRFLSMTIWPSESDKIQKHRKRLKAEEQWQRRQQVFRRGVSTRRSAYAFSHQRGYADLISSGRSIRKKRSPLDAIVADGTAEYRRTGDS
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Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phospholipids, in particular phosphatidylcholines (PC), from the outer to the inner leaflet of the plasma membrane (PubMed:25315773, PubMed:17948906). May participate in the establishment of the canalicular membrane integrity by ensuring asymmetric distribution of phospholipids in the canicular membrane (By similarity). Thus may have a role in the regulation of bile acids transport into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both and protect hepatocytes from bile salts (By similarity). Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity (PubMed:20512993). Participates in correct apical membrane localization of CDC42, CFTR and SLC10A2 (PubMed:25239307, PubMed:27301931). Enables CDC42 clustering at the apical membrane during enterocyte polarization through the interaction between CDC42 polybasic region and negatively charged membrane lipids provided by ATP8B1 (By similarity). Together with TMEM30A is involved in uptake of the synthetic drug alkylphospholipid perifosine (PubMed:20510206). Required for the preservation of cochlear hair cells in the inner ear (By similarity). May act as cardiolipin transporter during inflammatory injury (By similarity). ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2. a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit ATP8B1 and an accessory beta subunit TMEM30A (PubMed:17948906, PubMed:25239307). The flippase ATP8B1:TMEM30A complex can form an intermediate phosphoenzyme in vitro (PubMed:20947505, PubMed:20961850, PubMed:21914794). Also interacts with beta subunit TMEM30B (PubMed:20947505, PubMed:20961850, PubMed:21914794). Exit from the endoplasmic reticulum requires the presence of TMEM30A or TMEM30B (PubMed:20947505). Localizes to apical membranes in epithelial cells (PubMed:20512993). Found in most tissues except brain and skeletal muscle. Most abundant in pancreas and small intestine. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease may be caused by variants affecting the gene represented in this entry. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
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Q6R964
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MSTERDSETTFDEESQPNDEVVPYSDDETEDELEDQGSTVEPEQNRVNREAEKKRETFRKDCTWQVKANDRKFHEQPHFMNTKFFCIKESKYASNAIKTYKYNGFTFLPMNLFEQFKRAANFYFLILLILQAIPQISTLAWYTTLVPLLLVLGITAIKDLVDDVARHKMDKEINNRTCEVIKDGRFKIIKWKDIQVGDVIRLKKNDFIPADILLLSSSEPNSLCYVETAELDGETNLKFKMALEITDQYLQIEDNLATFDGFIECEEPNNRLDKFTGTLFWKNQSFPLDADKILLRGCVIRNTDVCHGLVIFAGADTKIMKNSGKTRFKRTKIDYLMNYMVYTIFIVLILVSAGLAIGHAYWEAQVGNYSWYLYDGENATPSYRGFLNFWGYIIVLNTMVPISLYVSVEVIRLGQSHFINWDLQMYYAEKDTPAKARTTTLNEQLGQIHYIFSDKTGTLTQNIMTFKKCCINGTIYGDHRDASQHSHSKIELVDFSWNTFADGKLAFYDHYLIEQIQSGKEPEVRQFFFLLSICHTVMVDRIDGQINYQAASPDEGALVNAARNFGFAFLARTQNTITVSELGSERTYNVLAILDFNSDRKRMSIIVRTPEGSIRLYCKGADTVIYERLHRMNPTKQETQDALDIFASETLRTLCLCYKEIEEKEFTEWNNKFMAASVASSNRDEALDKVYEEIEKDLILLGATAIEDKLQDGVPETISKLAKADIKIWVLTGDKKETAENIGFACELLTEDTTICYGEDINSLLHTRMENQRNRGGVSAKFAPPVYEPFFPPGENRALIITGSWLNEILLEKKTKRSKILKLKFPRTEEERRMRSQSRRRLEEKKEQRQKNFVDLACECSAVICCRVTPKQKAMVVDLVKRYKKAITLAIGDGANDVNMIKTAHIGVGISGQEGMQAVMSSDYSFAQFRYLQRLLLVHGRWSYIRMCKFLRYFFYKNFAFTLVHFWYSFFNGYSAQTAYEDWFITLYNVLYSSLPVLLMGLLDQDVSDKLSLRFPGLYVVGQRDLLFNYKRFFVSLLHGVLTSMVLFFIPLGAYLQTVGQDGEAPSDYQSFAVTVASALVITVNFQIGLDTSYWTFVNAFSIFGSIALYFGIMFDFHSAGIHVLFPSAFQFTGTASNALRQPYIWLTIILTVAVCLLPVVAIRFLSMTIWPSESDKIQKHRKRLKAEEQWKRRQSVFRRGVSSRRSAYAFSHQRGYADLISSGRSIRKKRSPLDAIIADGTAEYRRTVES
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Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phospholipids, in particular phosphatidylcholines (PC), from the outer to the inner leaflet of the plasma membrane (By similarity). May participate in the establishment of the canalicular membrane integrity by ensuring asymmetric distribution of phospholipids in the canicular membrane (PubMed:21820390). Thus may have a role in the regulation of bile acids transport into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both and protect hepatocytes from bile salts (PubMed:14976163, PubMed:21820390, PubMed:20126555). Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity (By similarity). Participates in correct apical membrane localization of CDC42, CFTR and SLC10A2 (PubMed:26416959). Enables CDC42 clustering at the apical membrane during enterocyte polarization through the interaction between CDC42 polybasic region and negatively charged membrane lipids provided by ATP8B1 (PubMed:26416959). Together with TMEM30A is involved in uptake of the synthetic drug alkylphospholipid perifosine (By similarity). Required for the preservation of cochlear hair cells in the inner ear (PubMed:19478059). According PubMed:20852622 is proposed to act as cardiolipin transporter during inflammatory injury; the function is questioned by PubMed:21475228 (PubMed:20852622, PubMed:21475228). ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2. a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit ATP8B1 and an accessory beta subunit TMEM30A (PubMed:30018401). The flippase ATP8B1:TMEM30A complex can form an intermediate phosphoenzyme in vitro. Also interacts with beta subunit TMEM30B. Exit from the endoplasmic reticulum requires the presence of TMEM30A or TMEM30B. Localizes to apical membranes in epithelial cells. Hepatocytes, bile duct, intestinal epithelial cells (cholangiocytes and ileocytes), and pancreatic acinar cells. Mice have unimpaired bile secretion, and no liver damage, but show mild abnormalities including depressed weight at weaning and elevated serum bile salt levels. Do not suffer from jaundice or diarrhea and have normal serum bilirubin levels and normal liver enzyme activities, except for mildly elevated serum AST (aspartate aminotransferase) activity. Display unimpaired transhepatic bile salt transport and are resistant to bile salt-induced cholestasis. Upon bile salt feeding, demonstrate serum bile salt accumulation, hepatic injury and expansion of the systemic bile salt pool and this failure of bile salt homeostasis occurs in the absence of any defect in hepatic bile secretion (PubMed:14976163). Mutant mice with B6 background show greater abnormalities than 129 and/or F1 background ones. Pups of B6 background gain less weight. In adult B6 background has lower serum cholesterol levels, higher serum alkaline phosphatase levels, and larger livers. After challenge with cholate-supplemented diet, these mice exhibit higher serum alkaline phosphatase and bilirubin levels, greater weight loss and larger livers (PubMed:20126555). Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily.
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P34379
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MVNEYDTYNKWLKFFSVRMVQSIIQSRLGDEIESKCVPYSENAVDWFNMRIDELGEISAYLKSNIKSYPPVGTLTLEFLLYTPSGQLLPLEAWILSSSEGTDDCSRNELYHDMSTLLRSAIVSARMTPMHRLYVKKQHLETFVIMYRVFENDISSDMGKGKKTRKIGELVSKFGNISLDLHYRTSMHFEEPEIAPVTPVEDVEEEIDDGEKTVVDENIQTRTVSECVPIADAKKRKASGSVESATSAGSSTSREAAPRFILGQSTSSEDSRHSDVQNSYEEDHKPSLADLRNHSFPFVNLLQSAYNPANGTKKNSSSTCLNSPKSTPEDKEPTIEKVAESFRAAKIDEVVFEEDEDEELPLDSMELSEDSFVHFNQLSDFGGAPSLGNELGDYLKQLKTAPDMTESGDIDICNMDLKTELEKISSQTANFNNFLKHVNSFSDE
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Component of the unc-51/atg-13 complex required for autophagosome formation (PubMed:19377305, PubMed:26687600). Required for the degradation of germ cell specific P-granule components such as sepa-1 by autophagy in somatic cells (PubMed:19377305). This ensures exclusive localization of the P-granules in germ cells (PubMed:19377305). May function downstream of the let-363 (Tor) signaling pathway to mediate sepa-1 degradation (PubMed:19377305). Plays a role in survival during limited food availability (PubMed:19377305). Interacts with unc-51 (via C-terminus) (PubMed:19377305). Interacts with lgg-1; the interaction is direct (PubMed:26687600). Under starvation conditions, is localized to punctate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. Recruited to preautophagosomes by lgg-1 (PubMed:26687600). Expressed from the 8-cell stage and subsequently throughout embryogenesis. After hatching, highly expressed in neurons including nerve ring cells, neurons in the tail and DD/VD motor neurons in the ventral nerve cord. Also expressed in body wall muscle and pharyngeal muscle. Belongs to the ATG13 family. Metazoan subfamily.
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Q5A245
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MLSDFKQQQQQKHHSHNPPNSHDDTQTKLQVAKLTQVIQKFFTKAAQIILESRAYPETSTPSLYPTKEESSKINKWFNLYMTNIPDSCKDDLKLWKGVDLTTIPPMIIETYIDLRSLPADQTLVLMDDEKHPWTVAKSRGKKQEVVLERWLIEFEPNTTDATVMVEELPLSYKQAIVLFRSIYGFTRLMPAFKVKKNLQNKLPLGNKILDGNQPISSKGRIGLSKPIINTRTNESHMTQKYFQPVHTSLGTLKISVAYRMDSEFCLHENEELLSSHFHKRDEEETKKKVSSSVSPLSSGTSLKETSTSPRKSQPPIRIQPFKVGSMSTSPPVQSPSISQPGTAPIQNQPSVPSSSLERRVSITSNKSTSNASLAAFLRNARSSTPSANNIPIINANPISGTSVPRSFSSSTGHEDSIFVNPDSASNTPRFASSFGSRASRRYSSTSIRQQTPQSDLMGQTNSVDAALSGIDADDDISDFVRMIDSKSDLRLGGGGGGGNSSVHNMSINESSYHGDALNKFQSLRSQYQQLSDSVSASLILQSRHSSRKSSLNSPAGSFDSHHHQHQQQQQQQQNQQQSQSPHTNTTSSIHSHAHSYSHSRMKDARPRSEDHQQTKFSAARRSSNISPTTAVPSSIGTPSSISSRIPHVTTIISSSDVSSTGGNRTKSAATTAIVSGMATSPSIYDYRSPRYQNVFDDDDEDDNDEEEGDREGNQLHEGRNSTESSQNQSKRIMKHIKKDEEDSEDDEDLLFTMSDMNSRNF
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Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity). Interacts with ATG1 to form the ATG1-ATG13 kinase complex. Belongs to the ATG13 family. Fungi subfamily.
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Q6FSJ9
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MSNGNDNQVIELIQNFFLKSAGLVTTVESNRYSLDDTSIEFDDEWFDMNIDVLHDLPPIIDKWTNFDGTQELPPLVIETFLDLHLLPSSYTVRLRDDESHLWAVSKGNKKSEIVLERWLIELDKESTSFKNHVQSGSGVSPEKLDQQLRLLFRYLFTLLQLLPSNDLMMALNNQSESHNTPIPVDIKTRILDGSQPILSKGRIGLSRPIISSYSNIINNSNIPAHLEQKKITPVWTKYGLLRISVSYRRDCQFIFQDLNEDNSPNTQITNQPAKTNEISISLSPRSKNDLNQISHPSWQKKFISSSKQFQPFIVGSVGSANTPNQNSSRNPSNSSVVGPHYHPQHRLSIGSSTSVSTQPNYEGTSVGSTSKFASSFNNLRRHSSVRYHESTEKLAKTDKNNYEDTDDLMEFVRLIEAKPELQPKKGLSGLQDKNLSGSILRYQKLRPSNDMLSEDLALSVSIDPIHGSQRRNSNSHSHSPVASFSPSGHFSSINSKLSQPHLAVRGSSSTVNSRRNSVDKVLASALSPIYGGDIPEYHTKSHNPVFNEVDDEEEGNDDLLVNKIPININKHKMSTSPRSIDSISNSLTRNRTPFRQPYQYSQPTTIATQAYAKMHRPTVRSSDAISEINSRKGDNFHQLINDNDEDDLVFFMSDMNLPRE
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Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity). Interacts with ATG1 to form the ATG1-ATG13 kinase complex. Belongs to the ATG13 family. Fungi subfamily.
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J3KIX9
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MHQHRRTSSAVASPVSSPHPSSSRPITRDRGTARFGPNVSRGLGIDRQMDASDQEQTIESPEKSPSQKLDQIIQNYHTKAALVILHSRVDLSPATYHGVIRTNKWFNVEVNETEDLKDSLGVWKYSNCTDSRPPPLIIEVYLDLTQLTNNQSLVIIDDSGKRWDVVEALATYGCLDNSRTSKSGVILERWRIDLGPGPDDLPLDMGSILPTVYKKSIVVFRSLYAYSKLLPAWKYSKRHSKIRPNPALSLKYRILQGPGGQIRSTNDPLTVPLHPGNGPVVDTYSFGVTDSPAGPLSALVTYRTNCDFRVDDSEALLSSRFMGVDERFFKPSLPSEDNFAAAGQEHGSLPVQKRDVGRPDLGQAYGSMSTFHQVGATTGASPISALRAARELAAGSPSSPTRPSHSPRPSQAGRVAALSGEGNHLIQRRPSISIQPFKAPPLSASPALVDSPVGSQPKNSAPRVGPMDITSSARQMPPPHGTPTTSRRSAHVSESAIASSTSGSPRPAPISKYSSSFSHRRGRLSSGGASKTDDDNNSSGRVSVSSSTVHPGSGTSADPATTSSGSLQADEDNISDFLKMLEMGKDLLSRKDSKSLDKNTKRTSAALSRFQKMRDSNAVLSDSMSSSLLLQPSSISSSKQLPNAATSVAGASISVSSSPGKAISPHTQHIPAVPSRLSSNSVVDYSHSHEDRHERRHRLSHESRRSPSEERANDEPRLKRDESTANAIDIPTSPRPFIPSFRRSSSAAQRRSSPPVEDDLGDFLPFGMRSLSLGAEDRSTLSLSELVRQQESSVPASDTNALQQQNQKDTRTGQSIVDESPSRIDNVPGTSSPRQYQPRFAHGRGRGSFGHPQPHVSAASSLGRASPIPNVTDADREGYIGSGNNGGTAVPPDTRRGSSHRFSFNRHLGTPANMDEDEPLLFAMSDFGASRRSLEEGRKGATTAGADHGGAPSTELQPAAETRSEGGPPSVSRGRYRAWP
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Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity). Interacts with ATG1 to form the ATG1-ATG13 kinase complex. Belongs to the ATG13 family. Fungi subfamily.
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Q7SYE0
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MDSDLSPQDKKDLDKFIKFFALKTVQVIVQARLGEKISTCSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPGIGRSMCVEISLKTSEGDSMELETWCLEMNEKCDKDIKVSYTVYNRLSLLLKSLLAITRVTPAYKLSRQQGHDYVILYRIYFGDVQLTGLGEGFQTVRVGIVGTPIGTITLSCAYRTNLALVSSRQFERTGPIMGIIIDHFVERPFTNMAHTHPCSYRAPGEDDGGTYAGIEDSQEVCTTSFSTSPPSQLYSSRLSYQTPPLGTVDLCHPTACTGAAHPHQMVVPGKDGGIPQVPAQPNHGTGAEQGRIPSCPTGQPPQLPPPTSCSSEVKTVSPSDVLETTFTRKVGAFVNKATTQVTTTGLDLPFAAFAPRSYDMEENDPMVHPPPSPIPSSPLQGSLHSNNSSHSGGQPNDDFVMVDFKPAFSKDDLLPMDLGTFYREFQNPPQLASLSIDVSAQSMAEDLDSLPEKLAVYEKNIDEFDAFVDTLQ
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Autophagy factor required for autophagosome formation. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. Phosphorylated under nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. Belongs to the ATG13 family. Metazoan subfamily.
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B5RTX9
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MVSPGQNDLSSDKSQIDPFVKKQNAKLTQVIQNFFSKSVQIVLQSRIQSESHNKEEQLKVGGDVGGHNVSSKINKWFNLHMYNDNLPKEELKLWKNINDVSQMPPMIIEVYLDLRQLTAIQTVILRDDNGNPWTVAKGGSKKHEVVLERWLIEFDANTVSGTIVDELPLIYKQAIILFRSLYGYTRLMPTFKLKKNLNKSNLNIGCKILDGKQPISSKGRIGLSKSIIPHQMLTTESHMSHKHFLPIQTTLGTLKISIAYRNHHEFSIHDNEELLSTHFVNIDDNDKDSEITPVEIEFKEELKIDRDSTTNEKVNEPEDDESHHADVESSQEHLQSEEPDESFEQDAKHISGSRKKFSISNNASMSLSPCSSGPQTVTEDSPSHNKPSANTTPIVSQRPTINPFKVGSISTSPPATTNFGGSSLERKVSITSNKSASNASLAAMLRNPRSSTSSTNTTANIPIANNNSNNQYNSTFPRSVSSSHGSNLAHDNDNLLGFSNPDNTSNTPRFSSSFGSRASRRFSNTSGRQSSLPSGNMNDTSLLATSAGSASSDAPMSGLYIDDDIGDFVRMIDSKSDLRFSGYNSNNDSKISYNQGSNSQIDALNKFQMLKNQHQQLSDSVSASLILHHNQLSGSRPSSRKSSHSIHSPPPSLPSGSYDNSHLPSINSKLRENSSTSGNDDNLARDSGTPSSRKNSFDYSTNSNTTFLKSPITNKLVSSPVTSTTPIHSCLHKTNNESGVISGLATTPSIYNDRRQIHYESVFDDDDDDYANNTADNRDQDDSLKLYLTNKLANAPKSNTNSRSLKSSTNPPNIGEDDDDDDDDLLFTMSDMNLAKH
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Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity). Interacts with ATG1 to form the ATG1-ATG13 kinase complex. Belongs to the ATG13 family. Fungi subfamily.
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Q9VHR6
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MSAQRLNAAERDLEKFIKFLVLKSTQVVVQSRLGEKMQTQCNPLAGSDWFNIAVQDHPEVLDETKRALNLKTGESILQRLPLCVEISLKTTEGDQMVLEVWSLDLLQPQNGASPATNDLNPEGQTLKAAHAIYNRMGIMLKSLISLTRTTPAYKLSRRQCPDSYGIFYRIYVDRPQVHTLGEGHKHVKIGQLSTIVGSLVMSVAYRTKLTISPTAAQSESNTIMLKSDHFRPATDANTPGNQQQTQNGTVVAKKLGLGALNPAQGTADRRFIDIEKPLRPGAFTDMGKLKQYTEDDFVLPETPPFEWLLRGRGSVESLNRLDNNSVASVNISNNNNSTQDSKFNQISNLNNNSAGFKSFEKNSENSVSPIKSLLIPASATATYRHHSEPSLQPPPDDDNLLKELHFPFASPTSHVNDLAKFYRECYHAPPLKGLNELQAEISSISSTPPASSGSGGVAACGPTAAATAIATSSADASAMDDLSRQLEQFETSLEDYDKLVSQFGLTGSSSTGSRSSGGLQMSN
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Autophagy factor required for autophagosome formation. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of Atg13 and Atg1. The Atg1-Atg13 complex functions at multiple levels to mediate and adjust nutrient-dependent autophagic signaling. Involved in the autophagic degradation of dBruce which controls DNA fragmentation in nurse cells. Interacts with Atg1. Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome. Phosphorylated in a nutrient-, TOR- and Atg1 kinase-dependent manner. Results in late stage egg chambers that contain persisting nurse cell nuclei without fragmented DNA and attenuation of caspase-3 cleavage. Belongs to the ATG13 family. Metazoan subfamily.
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C8VLQ3
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MHQQPRSPAPAASTSSARRSQDYDRRSDSPAFDLRTHTNRGLGIETENDTAEPEQSSQPGPEAISKVNQIVTNYHTKAALIILHSRVELPPSYAKNSNVPRVNRWFNVELEETDALKDQLKTWRTCDATDNRPPPMIIETYLDTAGLTNNQTLVALDDNGKRWDVTESLAASQSSRPAKASSSRAVDVILERWRVELGDMPGKLPSDLGAILPTVYKKSIILFRSLFTYSKFLPAWKFIKRNGRSRAHPALRVKYRIFSGHARDLSKQDHLTMPLFEGDTKVVDTYSFGVTDSPAGPFSVQVTYRTCCDFRVDDSEALLSSQFMGADDEIFQPSLPSGGLDARVTPEVGSAPLTRRTVEDPDLSRAYGSLSTFHHVGPTTGASPISALRAAREARASSPSPPTSSHRNSFAAARASPVGRAATLANDTNPNVARRPSISFQPFKAPPLSASPSLVDPPLSASPRTTGAGRTSLSDSRHMPPPSVTTSSRKPPSFGPDNANSSPNSASPRPTPMSRYSSAFSHRRGRPSSGGINKLEDDNSSGRASATSSGAQPGSGLLAEITGTSSDSIHADDENISEFLKMLDLRKDLLSPSSQTAMDNHSRRMTAASAALSRFRGMKDSNAALSDSMSSSLLMNRSSATSSKQLSGVPGIAGTSISTASSPGGKAISPHTPHTPAIPSRLSSNSIVDNTTTRLHGDNGSPVEEDASDETTTERLPSTVTAIPIPTSPATIFPSTFRRSSSAANRRSSHAIDDDEIFTMRSVSLGAEEPSHTTLGALQRQQDYEPIGTNIAPLESGARSSGGDDGNVLRGPTRRGPGAHRDASLSGPTVATSPYSHHPLHQRRISHSRGRGFSGGPHSLSSGSSSIARGGLIHPYPAEREAERDANAGASHSGTEDRRGTGRGSGGGRHNLPQAAQVEEDEPLLFAMSDFGASRRSFEEGRQGNHGPDSSGNTGSSRRGSGKRGTLSGFHLWP
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Activates the atg1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, atg13 is also required for glycogen storage during stationary phase (By similarity). Interacts with atg1 to form the atg1-atg13 kinase complex. Belongs to the ATG13 family. Fungi subfamily.
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I1RW37
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MHQQPRGPARVSSPGATTQPNLPSRSNSTREAALGSRPRAGSNLVGRDVPNSPSLESPPIPAPPADSVRKLDQIIQNFYAKAAVLVLDSRIKSRPARGANGARKPNKWFQIETDEIDDFRDELKIWKNCGSLDNRPPPMVIEVYLDASRLKDSQSLVIVDENGKRWDVMEQLNSYGSSTDSSGASRRNNEVVIERWQVELKHSGMTSVDFGPILPTVYKKAIVFFRSLFITTRLLPAWKFASQGAAKNSHPALIPRCRIRLSQPDRPRYDQLRLPIDGRPDPVTEYVFGDLEVPVGRLSTLVTYRSDCNFRVDDSEALLSSRFMGVDENFFRPSLPQQHATSRAPAAEAGSLRDHRSKPNLNDIQQAYGSLSTFHGNVPIGTSPISALRSVRQPGSDTSSPPESIPAQHDVGGPSSLPVRQGTARPHLPALEGLGRRPSVSFQPFKAGSLSGSPVPRQLDAEPASPQSLTRPGIPSLRQAGNRTSLTAGMPASLRGGPPTSSGETAVAGSPRPASTSRYSSSFTHRRGRLSFGGASKAGDDEQGSSGRQSLASSVAQPGSGLLAEVAGTSSESLRDDNEQLEDFIKALDSKKTLQSFGPSKTGESATNKTVAQLSRFHMMRDSNNALTESMTSSVQMQRSSSSSSRQLTSVPGMTAPASVSASSSPGKPLSPHTPHTPAIPSRLSENSIIDYSGQGRITSRQGRTSDNTQPGTIRENTITQDGTTAIDIPLSPRLATYQRRASSVAIQNRSMADDDDTDSAFAHRSISLGADDREPPTLSILLGRQMQLEEDSTQRPSDRLEPAADTGSTETPDMLRQGLSEENPPEGLIPAATSSSPFGRRRYMGMASHKQTPPQSSRGSFNGSLNRQVRGDDDSVNEEPLVFDLSEMDPQGRRSIEEARSGASGGPNIGPDRGGYESRNASRRGW
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Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy (By similarity). Involved in ATG9 and ATG23 cycling through the pre-autophagosomal structure (By similarity). Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation (By similarity). Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy (By similarity). Finally, ATG13 is also required for glycogen storage during stationary phase (By similarity). Autophagy is required for proper vegetative growth, asexual/sexual reproduction, and full virulence (PubMed:28894236). Autophagy is particularly involved in the biosynthesis of deoxynivalenol (DON), an important virulence determinant (PubMed:28894236). Hypophosphorylated form interacts with ATG1 to form the ATG1-ATG13 kinase complex (By similarity). The ATG1-ATG13 complex interacts with the ATG17-ATG29-ATG31 complex through direct interaction with ATG17 (By similarity). Does not significantly decrease the growth rate under nutrient-rich conditions (PubMed:28894236). Strongly reduces conidiation (PubMed:28894236). Causes only mild infection in point-inoculated spikelets of flowering wheat heads and impairs the spreading to nearby spikelets (PubMed:28894236). Reduces also strongly the production of deoxynivalenol (DON), an important virulence determinant (PubMed:28894236). Belongs to the ATG13 family. Fungi subfamily.
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Q9H8B0
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METDLNSQDRKDLDKFIKFFALKTVQVIVQARLGEKICTRSSSSPTGSDWFNLAIKDIPEVTHEAKKALAGQLPAVGRSMCVEISLKTSEGDSMELEIWCLEMNEKCDKEIKVSYTVYNRLSLLLKSLLAITRVTPAYRLSRKQGHEYVILYRIYFGEVQLSGLGEGFQTVRVGTVGTPVGTITLSCAYRINLAFMSTRQFERTPPIMGIIIDHFVDRPYPSSSPMHPCNYRTAGEDTGVIYPSVEDSQEVCTTSFSTSPPSQLSSSRLSYQPAALGVGSADLAYPVVFAAGLNATHPHQLMVPGKEGGVPLAPNQPVHGTQADQERLATCTPSDRTHCAATPSSSEDTETVSNSSEGRASPHDVLETIFVRKVGAFVNKPINQVTLTSLDIPFAMFAPKNLELEDTDPMVNPPDSPETESPLQGSLHSDGSSGGSSGNTHDDFVMIDFKPAFSKDDILPMDLGTFYREFQNPPQLSSLSIDIGAQSMAEDLDSLPEKLAVHEKNVREFDAFVETLQ
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Autophagy factor required for autophagosome formation and mitophagy. Target of the TOR kinase signaling pathway that regulates autophagy through the control of the phosphorylation status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1 complex. Through its regulation of ULK1 activity, plays a role in the regulation of the kinase activity of mTORC1 and cell proliferation. Part of a complex consisting of ATG13, ULK1 and RB1CC1 (PubMed:19597335, PubMed:19211835, PubMed:19225151, PubMed:24290141). Interacts with ATG101 (PubMed:19597335, PubMed:19287211, PubMed:26299944). Interacts with ULK1 (via C-terminus); this interaction is increased in the absence of TMEM39A (PubMed:19287211, PubMed:21855797, PubMed:18936157, PubMed:31806350). Interacts with ULK2 (via C-terminus) (PubMed:19225151, PubMed:18936157). Interacts (via the LIR motif) with GABARAP, GABARAPL, GABARAPL2 (PubMed:23043107). Interacts (via the LIR motif) with MAP1LC3A, MAP1LC3B and MAP1LC3C (PubMed:24290141). Interacts with TAB2 and TAB3 (PubMed:21976705). Interacts with C9orf72 (PubMed:27334615). Interacts with RB1CC1; this interaction is increased in the absence of TMEM39A (PubMed:31806350). Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane; the isolation membrane sequesters a portion of the cytoplasm resulting in autophagosome formation. Experimental confirmation may be lacking for some isoforms. The LIR motif (LC3-interacting region) is required for the interaction with the ATG8 family proteins GABARAP, GABARAPL, GABARAPL2, and MAP1LC3A. Phosphorylated by ULK1, ULK2 and mTOR. Phosphorylation status depends on nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. ULK1-mediated phosphorylation of ATG13 at Ser-355 is required for efficient clearance of depolarized mitochondria. Belongs to the ATG13 family. Metazoan subfamily. Extended N-terminus. Extended N-terminus.
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