UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
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30.7k
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Q9NP48
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MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQVKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHVEGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPTQ
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Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively (PubMed:15939762). Does not phosphorylate sphingosine (PubMed:15939762). Phosphorylates ceramide (By similarity). Phosphorylates 1,2-dioleoylglycerol more rapidly than 2,3-dioleoylglycerol (By similarity). Independently of its lipid kinase activity, acts as a component of the TIM22 complex (PubMed:28712724, PubMed:28712726). The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force (PubMed:28712724, PubMed:28712726). In the TIM22 complex, required for the import of a subset of metabolite carriers into mitochondria, such as ANT1/SLC25A4 and SLC25A24, while it is not required for the import of TIMM23 (PubMed:28712724). Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth (PubMed:15939762). a monoacylglycerol + ATP = ADP + H(+) + monoacyl-sn-glycero-3-phosphate a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+) an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine 1-phosphate + H(+) 1-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+) 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+) a 1-acyl-sn-glycerol + ATP = a 1-acyl-sn-glycero-3-phosphate + ADP + H(+) 1-hexadecanoyl-sn-glycerol + ATP = 1-hexadecanoyl-sn-glycero-3-phosphate + ADP + H(+) 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + ATP = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+) 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+) ATP + N-(hexanoyl)sphing-4-enine = ADP + H(+) + N-hexanoylsphing-4-enine 1-phosphate Lipid metabolism; glycerolipid metabolism. Component of the TIM22 complex, which core is composed of TIMM22, associated with TIMM10 (TIMM10A and/or TIMM10B), TIMM9, AGK and TIMM29 (PubMed:28712724, PubMed:28712726). Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane (PubMed:28712724). It is unclear whether the N-terminal hydrophobic region forms a transmembrane region or associates with the membrane without crossing it (PubMed:28712724, PubMed:28712726). Highly expressed in muscle, heart, kidney and brain. Overexpressed in prostate cancer, suggesting that it may play a role in initiation and progression of prostate cancer, processes in which lysophosphatidic acid (LPA) plays key roles. The disease is caused by variants affecting the gene represented in this entry. The TIM22 complex and import of proteins into mitochondrion are affected in patients suffering of MTDPS10 (PubMed:28712726). The disease is caused by variants affecting the gene represented in this entry. Belongs to the AGK family. According to a report, the N-terminal hydrophobic region forms a transmembrane region that crosses the mitochondrion inner membrane (PubMed:28712726). According to another report, the N-terminal hydrophobic region associates with the membrane without crossing it (PubMed:28712724).
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Q9D087
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MTAFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQVKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTVVKTDYEGQAKKLLELMESTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGQTSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVYAMTGLRWGSFRDAGVKVSKYWYLGPLKTKAAHFFSTLQEWPQTHQASISYTGPRERPPIEPEETPPRPSLYRRILRRLASFWAQPQDASSREVSPEVWKDVQLSTIELSITTRNTQLDLMSKEDFMNICIEPDTVSKGDFIIIGSKKVRDPGLRAAGTECLQASHCTLVLPEGTEGSFSIDSEEYEAMPVEVKLLPRKLRFFCDPRKREQMLPSTSQ
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Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively (PubMed:15252046). Phosphorylates ceramide but not sphingosine (PubMed:15252046). Phosphorylates 1,2-dioleoylglycerol more rapidly than 2,3-dioleoylglycerol (PubMed:18004883). Independently of its lipid kinase activity, acts as a component of the TIM22 complex (By similarity). The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force (By similarity). In the TIM22 complex, required for the import of a subset of metabolite carriers into mitochondria, such as ANT1/SLC25A4 and SLC25A24, while it is not required for the import of TIMM23 (By similarity). Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth (By similarity). a monoacylglycerol + ATP = ADP + H(+) + monoacyl-sn-glycero-3-phosphate a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+) an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine 1-phosphate + H(+) 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+) 1-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+) 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+) a 1-acyl-sn-glycerol + ATP = a 1-acyl-sn-glycero-3-phosphate + ADP + H(+) 1-hexadecanoyl-sn-glycerol + ATP = 1-hexadecanoyl-sn-glycero-3-phosphate + ADP + H(+) 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + ATP = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+) ATP + N-(hexanoyl)sphing-4-enine = ADP + H(+) + N-hexanoylsphing-4-enine 1-phosphate Both the ceramide and diacylglycerol kinase activities are inhibited by sphingosine and stimulated by cardiolipin (PubMed:15252046). Both activities are stimulated by calcium when magnesium concentrations are low but inhibited by calcium when magnesium concentrations are high (PubMed:15252046). Lipid metabolism; glycerolipid metabolism. Component of the TIM22 complex, which core is composed of TIMM22, associated with TIMM10 (TIMM10A and/or TIMM10B), TIMM9, AGK and TIMM29. Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane. It is unclear whether the N-terminal hydrophobic region forms a transmembrane region or associates with the membrane without crossing it. Ubiquitously expressed. Belongs to the AGK family. Was originally (PubMed:15252046) thought to have ceramide kinase activity. Such activity is however unlikely in vivo.
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Q5RED7
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MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQVKKATVFLNPAACKGKARTLFEKNAAPILHLCGMDVTIVKTDYEGQAKKLLELMENTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPSEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHAEGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPAQ
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Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively (By similarity). Phosphorylates ceramide but not sphingosine (By similarity). Phosphorylates 1,2-dioleoylglycerol more rapidly than 2,3-dioleoylglycerol (By similarity). Independently of its lipid kinase activity, acts as a component of the TIM22 complex (By similarity). The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force (By similarity). In the TIM22 complex, required for the import of a subset of metabolite carriers into mitochondria, such as ANT1/SLC25A4 and SLC25A24, while it is not required for the import of TIMM23 (By similarity). Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth (By similarity). a monoacylglycerol + ATP = ADP + H(+) + monoacyl-sn-glycero-3-phosphate a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+) an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine 1-phosphate + H(+) 1-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+) 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+) a 1-acyl-sn-glycerol + ATP = a 1-acyl-sn-glycero-3-phosphate + ADP + H(+) 1-hexadecanoyl-sn-glycerol + ATP = 1-hexadecanoyl-sn-glycero-3-phosphate + ADP + H(+) 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + ATP = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+) 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+) ATP + N-(hexanoyl)sphing-4-enine = ADP + H(+) + N-hexanoylsphing-4-enine 1-phosphate Lipid metabolism; glycerolipid metabolism. Component of the TIM22 complex, which core is composed of TIMM22, associated with TIMM10 (TIMM10A and/or TIMM10B), TIMM9, AGK and TIMM29. Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane. It is unclear whether the N-terminal hydrophobic region forms a transmembrane region or associates with the membrane without crossing it. Belongs to the AGK family.
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Q7ZYJ3
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MARVVRIFKTLRNHWKKSTVGFCLLAYGSHWLYGKHCDNLLRRAACEEAQVFGNHQILPHSAIKKATVFLNPAACKGKARTLFEKNAAPVLHLAGIDITVVKTDYEGQAKKLLELMEKTDLIIVAGGDGTVQEVITGLLRRDDEASFSKIPIGFIPLGGTNTLSHTLYPERENKVEQITEATLSILKGETVPLDVLQIKGEQDQPVFAVQGIRWGSYRDASVKVSKYWYLGPLKARAAHLFSALKEWPQQHQASISYLGPAERPPEEPEQKPSRPPLYVRIYRRLALYWSPPKVEVPVEPTPEPWEEAQLSAVELSITTQNHQPDLLRTLDSMSIHIEPDTISKGKFIQLGAQKMTDPLLHPEDSQVLLASRCSLHLPQGTEGHFSIDSEEYEAMSVDVTLLPRKLHFLCHPTRKQELLQSPTATAQS
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Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively (By similarity). Phosphorylates ceramide but not sphingosine (By similarity). Phosphorylates 1,2-dioleoylglycerol more rapidly than 2,3-dioleoylglycerol (By similarity). Independently of its lipid kinase activity, acts as a component of the TIM22 complex (By similarity). The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force (By similarity). a monoacylglycerol + ATP = ADP + H(+) + monoacyl-sn-glycero-3-phosphate a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+) an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine 1-phosphate + H(+) 1-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+) 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+) a 1-acyl-sn-glycerol + ATP = a 1-acyl-sn-glycero-3-phosphate + ADP + H(+) 1-hexadecanoyl-sn-glycerol + ATP = 1-hexadecanoyl-sn-glycero-3-phosphate + ADP + H(+) 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + ATP = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+) 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+) ATP + N-(hexanoyl)sphing-4-enine = ADP + H(+) + N-hexanoylsphing-4-enine 1-phosphate Lipid metabolism; glycerolipid metabolism. Component of the TIM22 complex. Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane. It is unclear whether the N-terminal hydrophobic region forms a transmembrane region or associates with the membrane without crossing it. Belongs to the AGK family.
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D4GU63
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MPYCLYDNTCKVQQTMLDDLSIIIVNYKSEEDIKNLYSRISGVAEFVVVDNSSSSELRQWCSHDDIHYIDSGGNHGYSGGNNMGIRYSLDELNRESVLVLNPDLEINKEDIRELYTIHQSTNYSIISPRILNREGIPVNESPTPEGTLFRSIGLLPALPGKEHNLKPVDHAHGSCMMISESVFEQIGYLNESFFMYYEEIEFCYRARRENINIGQCQVVDAIHNQPVDQTRFESSYQVYLDFRNRFLASNSIFSKSIDRIQYTTLSILISGWMVVRMLFEKKIEYIAPAIFGALHGIQNRTGKPERM
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Hexosyltransferase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier. Protein modification; protein glycosylation. Cell surface structure biogenesis; S-layer biogenesis. Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg. Belongs to the glycosyltransferase 2 family.
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Q8VZ36
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MGRGKIEIKRIENSTNRQVTFCKRRNGLLKKAYELSVLCDAEVALIVFSTRGRLYEYANNNIRSTIERYKKACSDSTNTSTVQEINAAYYQQESAKLRQQIQTIQNSNRNLMGDSLSSLSVKELKQVENRLEKAISRIRSKKHELLLVEIENAQKREIELDNENIYLRTKVAEVERYQQHHHQMVSGSEINAIEALASRNYFAHSIMTAGSGSGNGGSYSDPDKKILHLG
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Probable transcription factor (Probable). Is required, together with TT16/AGL32 for the maternal control of endothelium formation, which is essential for female gametophyte development and fertilization, and seed formation (PubMed:22176531). Interacts with AGL15 and AGL16. May be due to exon skipping.
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D4GU70
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MKGVLLSGGTGSRLRPITHTGPKQLVPVANKPVLEYAVEDLKEAGITEIGVILGHKGREEIQNLLGDGSDYGVEITYIVQGNPLGLAHAAGCAKDFVGDDDFVMYLGDNILKEGVVDLVESFESGDFGAGIALQEVENPQQFGIADVDDQGNVTQLIEKPDEPPTNLALIGMYVFSPAVFDAIEQLEPSWRGELEITDAIQSLLEDGYAIDSHVVEGWWKDTGKPEDILEANQLVLEDKSLKKRGTVSDDATVDGRIELAESATIEDGAVVRGPVSIADGAVIKSGTYVGPYTSVGPNSTLEGVHIENSVVIGESSINTSGRIVDSLLGKGANIGSADDFLPEGRRLVVGENSQLKL
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Nucleotidyltransferase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier. Binds 1 Mg(2+) ion per subunit. Protein modification; protein glycosylation. Cell surface structure biogenesis; S-layer biogenesis. Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg. Belongs to the glucose-1-phosphate thymidylyltransferase family.
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Q9SF79
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MARGKIQLKRIENPVHRQVTFCKRRTGLLKKAKELSVLCDAEIGVVIFSPQGKLFELATKGTMEGMIDKYMKCTGGGRGSSSATFTAQEQLQPPNLDPKDEINVLKQEIEMLQKGISYMFGGGDGAMNLEELLLLEKHLEYWISQIRSAKMDVMLQEIQSLRNKEGVLKNTNKYLLEKIEENNNSILDANFAVMETNYSYPLTMPSEIFQF
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Probable transcription activator that regulates root development by controlling cell proliferation in root meristem. May mediate responses to auxin in the root. May act as promoter of the flowering transition through up-regulation of SOC, FT and LFY. Preferentially expressed in roots (PubMed:7549482). In root meristem, expressed in external cells of columella, lateral root cap and atrichoblasts. In mature root, expressed in the central cylinder (PubMed:11855641). Expressed in leaf vasculature, young floral meristems and nectaries (PubMed:18203871). During embryo development, expressed in a punctate pattern from the globular stage to the torpedo stage. By auxin in root phloem. Retarded root growth, and altered root meristem size and stem-cell patterning. Late flowering phenotype. XAANTAL is the Mayan word for 'go slower' in recognition of the retarded root growth phenotypes of xaantal mutants.
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D4GU72
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MDVLVTGGAGFIGSNFVRYLLDNSDDSVVTLDALTYAGSRDNLAGYLDHPNHRFVEGDIRDRELVDDLVADADVIVNFAAESHVDRSIGGAEPFVSTNVQGTQTLLDAALDADIDRFLQISTDEVYGEIHDGKFTEDDPLAPRNPYSATKAGADLLVRSYRETHDLPTLITRTCNNFGPRQHPEKLIPKFIQRAANGETLPVYGDGSNVREWIYVEDNCAALDVVLREGDIGEVYNIGSGVELSNLETTEKILEAVGGSEDQIEFVEDRAGHDQRYAIDATKTKALGWEPEWSFEDGLEACVDYYLGDDE
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Lyase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier. Binds 1 NAD(+) per subunit. Protein modification; protein glycosylation. Cell surface structure biogenesis; S-layer biogenesis. Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg. Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily.
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Q9M2F0
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MGRGKVEVKRIENKITRQVTFSKRKSGLLKKAYELSVLCDAEVSLIIFSTGGKLYEFSNVGVGRTIERYYRCKDNLLDNDTLEDTQGLRQEVTKLKCKYESLLRTHRNLVGEDLEGMSIKELQTLERQLEGALSATRKQKTQVMMEQMEELRRKERELGDINNKLKLETEDHDFKGFQDLLLNPVLTAGCSTDFSLQSTHQNYISDCNLGYFLQIGFQQHYEQGEGSSVTKSNARSDAETNFVQ
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Probable transcription factor.
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D4GU69
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MPNIHDVEVRDLQVNADQRGHLVEVFRSDWDEYEIDPEMSYYSMTYPGVVRAWHRHLEGQIDHFVCPKGRITVGIYDDREDSPTQGELDTFVIGEHNQQVIRIPGDCWHGFKAIGDEPSLLINYPTNLYDYEDPDEERIPYDDDRIPYDWNAEIHG
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Epimerase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier. Protein modification; protein glycosylation. Cell surface structure biogenesis; S-layer biogenesis. Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg. Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
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Q9T056
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MVRGKTEMKRIENATSRQVTFSKRRNGLLKKAFELSVLCDAEVALIIFSPRGKLYEFSSSSSIPKTVERYQKRIQDLGSNHKRNDNSQQSKDETYGLARKIEHLEISTRKMMGEGLDASSIEELQQLENQLDRSLMKIRAKKYQLLREETEKLKEKERNLIAENKMLMEKCEMQGRGIIGRISSSSSTSELDIDDNEMEVVTDLFIGPPETRHFKKFPPSN
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Transcriptional activator that regulates root development by controlling meristem size and patterning of the root apical meristem. Regulates auxin transport and gradients in the root meristematic cells via direct regulation of the auxin efflux carrier PIN1 and PIN4 gene expression. Binds specifically to the CArG-box DNA sequences in the promoter regions of PIN1 and PIN4 genes (PubMed:24121311). Involved in the regulation of shoot apical meristem (SAM) cell identities and transitions. Promotes flowering transition and participates in flower meristem maintenance and determinacy. Positively regulates TFL1 and WUS expression. Binds directly to the TFL1 regulatory sequences (PubMed:25636918). Interacts with AGL16. Preferentially expressed in roots (PubMed:7549482). Expressed in lateral root cap, root epidermis, root endodermis, columella of the root meristematic region, the vascular cylinder in differentiated zones of the primary root and in emerged lateral root primordia (PubMed:24121311). Expressed in pollen (PubMed:12949148). During floral transition, expressed very early at the flanks of the inflorescence meristem in the anlagens upon the transition to flowering Subsequently, expression levels increase in the first and second stages of the floral meristem and at stage 3, expression is restricted to the L1 and L2 layers. Later on, expressed in the gynoecium and stamen primordia at stage 6. By auxin. Retarded root growth, and altered root meristem size and stem-cell patterning (PubMed:24121311). Late flowering phenotype (PubMed:25636918). XAANTAL is the Mayan word for 'go slower' in recognition of the retarded root growth phenotypes of xaantal mutants. Plants over-expressing AGL14/XAL2 show early flowering phenotype and flowers have vegetative traits.
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L9V9H5
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MYAFVTGANGLLGSVVVRTLREQGHAVVGSYHSEEPTFDCPLHQVDITDTERVVELLDEYDVDLVINCAAYTDVDGCESNPEVATAVNGTAPGDLAAVCDDREIPFIHYSTDYVFDGETDGFYEEGDEPAPIQEYGRSKLTGEHAVRDVNPDALILRLSFVYGARGDTSDLVGFPQWVASTLAAGDTVPLFTDQTMTPSRAGNVATTTLELLDAGVSGTFHVASQSAVTPSDFGEKICEVIGGDATLIESSVMADLDRPAARPRRSCLDVSNVEGELGCSQPTLEDDLAALEAAFSDYSS
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Reductase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Involved in the addition of final rhamnose (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier. Protein modification; protein glycosylation. Cell surface structure biogenesis; S-layer biogenesis. Impaired formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and 'Asn-117' glycosylation of S-layer glycoprotein Csg. Belongs to the dTDP-4-dehydrorhamnose reductase family. Truncated N-terminus.
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Q38839
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MGRGKIEIKRIENANSRQVTFSKRRSGLLKKARELSVLCDAEVAVIVFSKSGKLFEYSSTGMKQTLSRYGNHQSSSASKAEEDCAEVDILKDQLSKLQEKHLQLQGKGLNPLTFKELQSLEQQLYHALITVRERKERLLTNQLEESRLKEQRAELENETLRRQVQELRSFLPSFTHYVPSYIKCFAIDPKNALINHDSKCSLQNTDSDTTLQLGLPGEAHDRRTNEGERESPSSDSVTTNTSSETAERGDQSSLANSPPEAKRQRFSV
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Transcription factor involved in the negative regulation of flowering, probably through the photoperiodic pathway. Acts as both an activator and a repressor of transcription. Binds DNA in a sequence-specific manner in large CArG motif 5'-CC (A/T)8 GG-3'. Participates probably in the regulation of programs active during the early stages of embryo development. Prevents premature perianth senescence and abscission, fruits development and seed desiccation. Stimulates the expression of at least DTA4, LEC2, FUS3, ABI3, AT4G38680/CSP2 and GRP2B/CSP4. Can enhance somatic embryo development in vitro. Homodimer. Interacts with SVP, AGL24, AP1, AGL6, AG, AGL1, AGL11, AGL5, AGL16, SOC1 and AGL21. Associated with the chromosomes during mitosis. Accumulates in the egg cytoplasm before fertilization but moves into the nucleus of the fertilized egg. Expressed at low levels in flowers and siliques. Also present in seedlings. Detected during embryogenesis and accumulates during early seed development (at protein level). Expressed in shoot apices and the base of leaf petioles. During the reproductive phase, accumulates in immature buds and at the base of the floral organs, and in the receptacle, ovules, anther filaments, and stigma and style of open flowers. Accumulates before fertilization in the cytoplasm in the cells of the egg apparatus and moves into the nucleus during early stages of development following fertilization in the suspensor, embryo, and endosperm, mainly double fertilization derived tissues (at protein level). Highly expressed in developing embryos. In young seedlings, present in the shoot and root apices, lateral root primordia and throughout the vascular system. By auxin (2,4-D). Feedback loop leading to direct down-regulation by itself. Early flowering under short-days conditions (SD) when combined with AGL18 disruption. Decreased ability to produce somatic embryos in vitro.
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A0A5Q0QRK8
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MQIILPDILQTWAYARLLNPHYDGAKLESSLWIHPLVAKLFDQKGQKAFQNDYTSLLASLMYSHQGKVPSRRCDMMNLFFVYDEYTDVVSPEIAHRLSKIVVDAMKNSDEMSPCGEHPIGDKAKEFWRLATTLLPATGSNSDVCKSRFINLTEEYLNAVTVEARDRNEGTIHSVKEYLTMRRATSGAGLMLALIEFELDLPKAVLEHKFVQALEEIYTRTRVSSGQANHNLITVVMHENPGLSLQGAFDWLGSYAAGVVECFQTNVRNLPSFCDVEGPACESVDGTLQERVDKYISGLGQAVRAEDDWAFETTRYYGEDGPKVRETRVLVIRPVKRITRRHLLQSLEIKYSMVRG
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Belongs to the terpene synthase family. Does not functions as a sesquiterpene synthase since it does not contain a functional DDXXD metal-binding motif.
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P12284
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MDSAGLHINFRLSHVLTVVTCILYILPPTTTAYSLPAPGKAAFQHQLSKRDVSDGSAERRPYTRMGSGGLKLHCQVHPANCPGGLMVTKKSDLLGALLSRNSPSSYGLPSRDMSTAYKRQDVRQQLRMFDDLVQLRKLIETPSVYPSEEDEARLYD
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The alpha-1 peptide acts as an osmoregulatory peptide, increasing blood volume, and also modulates the activity of a set of cardiac motor neurons that control heart rate. A number of isoforms are produced. Expressed within the abdominal ganglion in neurons R15, RB(HE), the two L9(G) gill motoneurons, and L40 interneuron, all are parts of autonomic control circuit that contributes to implementing a central command to coordinate autonomic activity with escape locomotion. R15 alpha-1. R15 alpha-2. Isoform R15-1 produces peptide R15 alpha-2 which is a 24 aa long spliced form of peptide R15 alpha-1 which is produced by isoform R15-2.
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A0A5Q0QRJ3
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MCASATRPQPSASNNVKKIILPDLVSHCTFKLRHNRHRKQVTTETKKWLFKDGNLLGQKERAYHGLKCGLLTSMCYPDAGYPQLRVVNDFLTYLFHLDNLSDEMDNRGTTTTADEVLNSLYHPHTWRSSARVGKMTRDFYKRLVLTASPGAQQRFIETFDFFFQSVTQQALDRASGVIPDLESYISLRRDTSGCKPCWAMIEYANNLDIPDEVMDHPIIRSLGEATNDLVTWSNDIFSYSVEQSKGHTHNMIPVVMYQEGLDLQAAVDFVGDMCRQSINRFVEEKARLPSWGPKIDQDVAIYVQGLADWIVGSLHWSFETERYFGKSGRQVKASRIVDLLPRQRLP
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Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including alpha-muurolene, gamma-muurolene, alpha-selinene, beta-selinene, delta-cadinene, alpha-cadinol and delta-cadinol (PubMed:32233445). Delta-cadinene is the major product of Agr1 (PubMed:32233445). (2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate (2E,6E)-farnesyl diphosphate = alpha-muurolene + diphosphate (2E,6E)-farnesyl diphosphate = diphosphate + gamma-muurolene (2E,6E)-farnesyl diphosphate = alpha-selinene + diphosphate The DDXXD motif is important for the catalytic activity, presumably through binding to Mg(2+). Belongs to the terpene synthase family.
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Q90Y05
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METVLKSLFFLLVATSFTLAKERKPQTLSRGWGDNLEWVQTYEEGLFKAKSENKPLLLINHRNDCPHSQALKKAFAEHQGIQKLAEEFILLNVVYDPTDKNLQLDGQYVPKVVFVDPSLVVRADLPGKYSNHQYTYEPADIDHLFENMKKALVLLKTEL
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Monomer and homodimer. Expression begins at the end of gastrulation within the anterior ectoderm and by the end of neurulation is located within the cement gland placode. At stage 32 (tailbud), expressed in the cells surrounding the cement gland and in the otic vesicle. In addition, at the end of neurulation and afterwards, expressed within the notochord. Belongs to the AGR family.
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Q7ZZH4
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MESVLKSLFVLLVATSFTLAKEIPAKVSKPQTLSRGWGDNLEWVQTYEEGLYKAKAENKPLMLINHRNDCPHSLALKKAFAEHQGIQKLAEEFILLNVVYDPTDKNLQLDGQYVPKIIFVDPSLVVRADLPGKYSNHQYTYEPADIDHLFENMKKALVLLKTEL
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Monomer and homodimer. Belongs to the AGR family.
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A0A5Q0QNJ2
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MVWDFVLSLFHSLLAAFQTLTSWLTGSFLFNNKMAPAPNPAPVTFILPDLEKTFNSLPDDGLNPHHDVACAESREWFAKYNKKVLGAQMQEFFRRCKFELITSYTYPYVDKEGLRATMDWHNILWFFDEVTDTETGKDAHKSAIITIRTLREPDFDDGSSLCRMVRDFRLSHLSRAGPECTRRFLEHCDVAFHAGAVEAELREKGEVLSIEGYLKLRRETSGARTCFDMAEYLMDIDLPQDMYDDPVFQKGYIAALDLIFLANDLYSYNMEQAKGHNGANVLTVVMKETKLNLQSAADYVGVLCEKLIKQFQEAKSTLENRLAKEKNPAKAAALKDAIRSLVGYGHWVRGNVEWSFETERYFGKKNKEIKKSRVVTLTPTNSVNRALKA
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Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to viridiflorene. (2E,6E)-farnesyl diphosphate = diphosphate + viridiflorene The DDXXD motif is important for the catalytic activity, presumably through binding to Mg(2+). Belongs to the terpene synthase family.
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A7MCE1
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MLKGLLSVLLVMVALSSALGKPEKTTPKKEKEKRVPQTLSRGWGDQLIWAQTYEEALFWSRSKNKPLMVIFHLEDCPHSQALKKAFAEDKEIQKLADEDFVILNLVYETTDKHLSPDGQYVPRIIFVDPSMTVRADITGRYSNRMYAYEPADMKLLLSNMQRALKFLKTEL
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Monomer and homodimer. Expressed in most developing organs which contain mucus-secreting cells, including the epidermis, olfactory bulbs, otic vesicles, pharynx, esophagus, pneumatic duct, swim bladder, and intestine. Expressed in the gill, pharynx/esophagus, swim bladder/pneumatic duct, and intestine in the adult. Expressed after the segmentation stage. Belongs to the AGR family.
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O95994
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MEKIPVSAFLLLVALSYTLARDTTVKPGAKKDTKDSRPKLPQTLSRGWGDQLIWTQTYEEALYKSKTSNKPLMIIHHLDECPHSQALKKVFAENKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIMFVDPSLTVRADITGRYSNRLYAYEPADTALLLDNMKKALKLLKTEL
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Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. Promotes cell adhesion (PubMed:23274113). Monomer and homodimer (PubMed:23274113). Interacts with LYPD3 and DAG1 (alphaDAG1). Interacts with MUC2; disulfide-linked. Expressed strongly in trachea, lung, stomach, colon, prostate and small intestine. Expressed weakly in pituitary gland, salivary gland, mammary gland, bladder, appendix, ovary, fetal lung, uterus, pancreas, kidney, fetal kidney, testis, placenta, thyroid gland and in estrogen receptor (ER)-positive breast cancer cell lines. Belongs to the AGR family.
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A2CGA2
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MEKFSVSAILLLVAISGTLAKDTTVKSGAKKDPKDSRPKLPQTLSRGWGDQLIWTQTYEEALYRSKTSNRPLMVIHHLDECPHSQALKKVFAEHKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIVFVDPSLTVRADITGRYSNRLYAYEPSDTALLYDNMKKALKLLKTEL
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Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells. Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth (By similarity). Promotes cell adhesion (By similarity). Monomer and homodimer. Interacts with LYPD3 and DAG1 (alphaDAG1). Interacts with MUC2; disulfide-linked. Expressed in lung, skeletal muscle, testis, liver, stomach, colon, small intestine, the goblet cells of the intestine and the mucuous neck cells of the stomach. Expressed in embryo at 15 dpc onwards. Mice are viable but display altered production of mucus with loss of production of MUC2 despite expression of its mRNA. They also display an increase in mast cells in the intestine, an increased expression of inflammation-specific genes, and frequent rectal prolapse. This is associated with a higher susceptibility to colitis. Belongs to the AGR family.
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Q5R7P1
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MEKISVSAFLLLVALSYTLARDTTVKPAAKKDTKDSRPKLPQTLSRGWGDQLIWTQTYEEALYKSKTSNKPLMIIHHLDECPHSQALKKVFAENKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIMFVDPSLTVRADITGRYSNRLYAYEPTDTALLLDNMKKALKLLKTEL
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Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells. Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth (By similarity). Promotes cell adhesion (By similarity). Monomer and homodimer. Interacts with LYPD3 and DAG1 (alphaDAG1). Interacts with MUC2; disulfide-linked. Belongs to the AGR family.
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Q28ID5
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METVLKTLFVLLVATSLTLAKDLPQATRVLQTLSRGWGDNLEWVQTYEEGLYKAKTENKPLILINHRNDCPHSLALKKAFAEHQGIQKLAEEFVLLNVVYDPTDKNLQLDGQYVPKVVFVDPSLVVRADLPGKYSNHQYTYEPADIDLLFENMKKALILLKTEL
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Monomer and homodimer. Belongs to the AGR family.
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A0A5Q0QU70
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MNASPFLNESSPTRPTSFVLPDLVSHCKFPLSYHPNGDEIAQESVDWLDSSCPDLTAKQRRALRVLQSGELTAYCYNQATSPERLRVVSDFLTYLFHLDNISDGMMTRETDVLADVVMNAFWFTDKYMPTRGPGKEQLDEELNPGKLARDFWSRAIADCGVGVQARFKETMGLFFEAVNIQARMRDEDTIPDLESYIDVRRDTSGCKPSWVLIEYALGIDLPDHVVDHPIMQALNQGTNDLVTWSNDIFSYNVEQSRGDTHNMIVILMEYHGHTLQSAVDYVGELCAQTIDTFCENKERLPSWGPEIDDMVARYVKGLQDWIVGSLHWSFQTQRYFGKDGLDIKKHRFVKLLPLEAAK
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Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including alpha-muurolene, gamma-muurolene, germacrene, delta-cadinene, delta-cadinol and cubenol. (2E,6E)-farnesyl diphosphate = alpha-muurolene + diphosphate (2E,6E)-farnesyl diphosphate = diphosphate + gamma-muurolene (2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate The DDXXD motif is important for the catalytic activity, presumably through binding to Mg(2+). Belongs to the terpene synthase family.
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A4D120
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MMLHSALGLCLLLVTVSSNLAIAIKKEKRPPQTLSRGWGDDITWVQTYEEGLFYAQKSKKPLMVIHHLEDCQYSQALKKVFAQNEEIQEMAQNKFIMLNLMHETTDKNLSPDGQYVPRIMFVDPSLTVRADIAGRYSNRLYTYEPRDLPLLIENMKKALRLIQSEL
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Required for calcium-mediated regulation of ciliary beat frequency and mucociliary clearance in the airway. Might be involved in the regulation of intracellular calcium in tracheal epithelial cells. Interacts with LYPD3 and DAG1 (alphaDAG1). Found in the cytoplasm, which could include the endoplasmic reticulum. Expressed in the lung, in the ciliated cells of the airway epithelium (PubMed:25751668). Expression increased with differentiation of airway epithelial cells (PubMed:25751668). Not detected in the mucous cells (PubMed:25751668). Expressed in ciliated cells in the oviduct (PubMed:26170690). Also detected in stomach, colon, prostate and liver (PubMed:25751668). Expressed in breast, ovary, prostate and liver cancer (PubMed:26170690). Expression is associated with the level of differentiation of breast cancer (at protein level) (PubMed:26170690). Not induced as part of the cellular response to endoplasmic reticulum stress (PubMed:25751668). Up-regulated by androgens and by estrogens in prostate cancer cells (PubMed:23294566) Up-regulated by a hormone (estrogen-receptor alpha) independent mechanism in ovarian cancer (PubMed:22361111). Belongs to the AGR family.
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Q8BW95
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MLHSALALCLLLITVSSNLAIAIKKEKRPPQTLSRGWGDDITWVQTYEEGLFHARKSNKPLMVIHHLEDCQYCQALKKEFAKNEEIQEMAQNDFIMLNLMHETTDKNLSPDGQYVPRIMFVDPSLTVRADITGRYSNRLYTYEPQDLPMLVDNMKKALRLIQSEL
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Required for calcium-mediated regulation of ciliary beat frequency and mucociliary clearance in the airway. Might be involved in the regulation of intracellular calcium in tracheal epithelial cells. Interacts with LYPD3 and DAG1 (alphaDAG1). Expressed in the ciliated cells of the airway epithelium. Not detected in the mucous cells. Knockout mice develop ciliated cells with normal-appearing cilia and histology. However, ciliary beat frequency was lower in airways from knockout mice compared with control mice in presence of calcium (20% lower in the absence of stimulation, 35% lower after ATP stimulation). Knockout mice show reduced mucociliary clearance. Knockout mice do not seem to show endoplasmic reticulum stress response. Belongs to the AGR family.
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Q6DJ58
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MYFPMIELTLVLLASSNLAMSVRKEIRAPQTLSRGWGDDISWVQTYEEGLYNAKKRNKPLMVIHHLEDCQYCQALKKVFAESDEAQTLAQEQFIMLNLMHETTDKNLSPDGQYVPRIMFIDPTLTVRADITGRYSNRRYTYEPQDLPLLIENMNKAIHLLQTEL
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Required for calcium-mediated regulation of ciliary beat frequency in the airway. Belongs to the AGR family. Truncated N-terminus.
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A0A5Q0QP64
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MSALPSQFKLPDLLSTCPLKDGTNPAYKKAAAESRAWIGSYNMFADRKRAFFIQGQNELLCSHVYCYAGYEQLRTTCDFVNLLFVVDEVSDEQSGEDARATGQVFVNAMKYADWHDGSKLAKLTKDFRVRFLRLAGPKNVARFVALCESYTACVGKEAELRESGQVLGVKEFIPLRRQNSAVLLCFSLVEYILGIDLDDEVYRDENFLNAYWAACDHVCWANDVYSYDMEQSKGLSNNNIVTVLMEENHTSLQDTSDYIGEKCAEFVQIYLTSKKRLSPSLGPDAALFLESIGSWMVGNLAWSFETSRYFGSRHLEVKETGIVILRPRELPEDGSSSDSDEE
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Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including beta-copaene, alpha-cubebene, cadina-1(6),4-diene, gamma-muurolene, delta-cadinene, epizonarene, epicubenol and cubenol (PubMed:32233445). Agr4 is also able to use the monoterpene precursor geranyl diphosphate (GPP) as substrates to synthesize the monoterpene beta-myrcene (PubMed:32233445). Delta-cadinene is the major product of Agr4 (PubMed:32233445). (2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate (2E,6E)-farnesyl diphosphate = diphosphate + gamma-muurolene (2E,6E)-farnesyl diphosphate = beta-copaene + diphosphate (2E)-geranyl diphosphate = beta-myrcene + diphosphate The DDXXD motif is important for the catalytic activity, presumably through binding to Mg(2+). Belongs to the terpene synthase family.
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A0A5Q0QSI8
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MASSLLEPSLAAIALVILLASVSLSRKKRPAAPEPQGLSVLGNLFDIPKRASSIIYLALGKPYNTLTKRAVSQLQGYTPGSHIDATSHSPRVFRLPNLEETFSVFPDHGLNPNYTSARTDSRAWINQYTKVVCGPKMVAFMNNCEFELSNSHCYPYAGYKGLKATMDLTNILWLYDEYTDTGSGAEAVKAAGIVARALREPDYDDGTWVCRMMKSFKQNHIDKAGPGVARRFIDNFCNYVEVVGREAELREKNEVLDIPNYVTFRRETSAVRTCFDLVEYCLDLDLPQYVHDDPVFISGYNAGMDLVFWANDLVSYNMEQSKGHSGANVVTVIMKSKGVDLQTAVDFLGGYCEALTAQLLEAKRILQARSDAAYSRDVVRLMDAFGDWVRGNVAWSFETERYFGKENKRVKETLLVELKEPFVGALALKE
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Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to viridiflorene and viridiflorol. (2E,6E)-farnesyl diphosphate = diphosphate + viridiflorene The DDXXD motif is important for the catalytic activity, presumably through binding to Mg(2+). Belongs to the terpene synthase family.
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A0A5Q0QN66
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MPGSANWTADRFYIPDTLANWPWPRAINPAYEECKAASAAWCEKYGAFSARAQKAFNLCDFNLLASLAYAGLPADVNRVGCDLMNLFFVVDEHTDAMDARSVQDWVDIVVDALHHPHTPRPAGEPKVGEIARTFWENGIKCMGPTAQRRFVETFTTYLQSVVTQAQDRDKHLFRDVDSYMEVRRDTIGAKPSFALLEHDMELPDDVFYHPLLEKLREWAIDMLILGNDLCSYNVEQSRGDDGHNIIRLAMLQENTNVHGALRFVSKMHDDLAEKFLSNYQGMPSFTPQIDAWVTRYIDGLGNWVRANDSWSFESWRYFKGDVLRVQAERWVELLPPAPKDELTSSIPPESRWIKPAVEPSRARPNNVGIVALDTYTPTSEDDFQTLAVKTVSSLLSKYNINPVSVGRLDICIERAADPYIIYALRDAFASAGNTDVEAIVSSSKSVVGLFNAINWVESSSWDGRYAIVFAGDLSSGVSAALVGPDAPIVVEPTRGTYLGDPIASTDEAQGSYIDSLFQSYSHYRKKHPQFSKTSGAPNGAHTPTTTNGSIKSNGFVSGDTNGHANGNGHVQTRSSTPSSSSSSTSSPSFDYMILHDRHGKIPTGAGSIYLGLASLITDIAPETLAGKSIGVFGFANSTSTFFGIRVAGDCSVICKQLQA
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Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to delta(6)-protoilludene. (2E,6E)-farnesyl diphosphate = Delta(6)-protoilludene + diphosphate The DDXXD motif is important for the catalytic activity, presumably through binding to Mg(2+). Belongs to the terpene synthase family.
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A0A5Q0QNH9
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MSFFKSSQPTIYIPDTLRNWPWPREINPHYEECKRESAAWVEKFGAFSAKAQKAFNKCDFNLLASLAWSRVNRDGCRIGCDLMNLFFVFDEWSDVSDAEETRRMADIIMDALYDPHKPRPTGEWVGGEVTRQYWLNAIRTATPSAQKRFIKAFKLYTDSVVQQSADRDKHLIRDIDSYFEVRRDTIGAKPSFAINEVHMNLPDYVMEHPVIKNLTAYCIDMLCIGNDLCSYNVEQSRGDDGHNLVTIVMHQLNLDVQGAFDWIGKLHDELVDKFLEEYKNVPTFKDKQVTKECAEYAFGLGNWVRGNDQWSFESERYFRKDGMRVLTERTVVLLPKKREPPPKPLDEDPIYSALPWWGWTALFGFLATAFTFSARQLSTRISANLIA
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Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to delta(6)-protoilludene. (2E,6E)-farnesyl diphosphate = Delta(6)-protoilludene + diphosphate The DDXXD motif is important for the catalytic activity, presumably through binding to Mg(2+). Belongs to the terpene synthase family.
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A0A5Q0QMX1
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MSEQQYTLPDLLQNWPWNRHLSPYYEEAKRESSAWVESFKPFDQDGQRAFDAYLLASLTYSHGSREFVRLGCDLMNFYFVYDEYTDVSDSAVADRLANIVIDAMRNPENSSQSGDHLLGKMTKHFWTRALAMAPAGSPCFEHFITTSETYLRAVTQEAEDRANKRVRKVDDYLRLRRDTCGARPTLALIEFGLNLPNEVVRHPSLVALTEAAVDLIILVNDMHSYVRELSCGHENHNLITAIMLEHRLNRQDAFHWLGSHCSRVVDQFLSDLDELPSWGEPTDSGVRDYINGLGQWVRGNDDWSTESKRYYGEDGETIRQERLVTTRSGESNYIKFGQVGVQDSVRIQPIEAN
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Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including beta-elemene, gamma-muurolene, alpha-selinene, beta-selinene, beta-cadinene, delta-cadinene and alpha-cadinol. (2E,6E)-farnesyl diphosphate = diphosphate + gamma-muurolene (2E,6E)-farnesyl diphosphate = alpha-selinene + diphosphate (2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate The DDXXD motif is important for the catalytic activity, presumably through binding to Mg(2+). Belongs to the terpene synthase family.
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Q8IZF1
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MATPRGLGALLLLLLLPTSGQEKPTEGPRNTCLGSNNMYDIFNLNDKALCFTKCRQSGSDSCNVENLQRYWLNYEAHLMKEGLTQKVNTPFLKALVQNLSTNTAEDFYFSLEPSQVPRQVMKDEDKPPDRVRLPKSLFRSLPGNRSVVRLAVTILDIGPGTLFKGPRLGLGDGSGVLNNRLVGLSVGQMHVTKLAEPLEIVFSHQRPPPNMTLTCVFWDVTKGTTGDWSSEGCSTEVRPEGTVCCCDHLTFFALLLRPTLDQSTVHILTRISQAGCGVSMIFLAFTIILYAFLRLSRERFKSEDAPKIHVALGGSLFLLNLAFLVNVGSGSKGSDAACWARGAVFHYFLLCAFTWMGLEAFHLYLLAVRVFNTYFGHYFLKLSLVGWGLPALMVIGTGSANSYGLYTIRDRENRTSLELCWFREGTTMYALYITVHGYFLITFLFGMVVLALVVWKIFTLSRATAVKERGKNRKKVLTLLGLSSLVGVTWGLAIFTPLGLSTVYIFALFNSLQGVFICCWFTILYLPSQSTTVSSSTARLDQAHSASQE
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Orphan receptor that regulates migration of lymphatic endothelial cells in vitro via the small GTPases RhoA and CDC42 (PubMed:24178298). Regulates B-cell development (By similarity). Seems to signal through G-alpha(q)-proteins (PubMed:22575658). Expressed in cultured primary dermal lymphatic endothelial cells. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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Q3U2Q3
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MATARSLGLLFFLLLTSDEETTEEPRNVCRRLQEGHEYDTFDLNDTAQCFTKCGQSEHSPCDVGNLQRYWLNYESYLLENSMETVDMPFVKALIQNISTDVSEDLLYSLMLSQIPRQVMQGEDEPADGVRLPKSLFGALPGNRSAVRLAITVLDIGAGNVFKGPKLLEDKGSSVLNNRMVGLSVGQMHATGLSEPVEITFSHERQPPNVILTCVFWDMAKGDWDSHGCSTVPGDGRTVCRCDHLTFFALLLRPILDLATAQTLTRISQAGSAVSMIFLAFTMVLYVAFRFSLQRFKSEDAPKIHMALSISLFLLNLTFLINVGSSSQGPPASCWVRAAIFHYFLLCVFTWMGLEAFHLYLLAIRVFNTYFGHYFLKLSLLAWGLPVLVVIGAGSSNSYGVYTIRDQENRTSLELCWFQKEPALYATVHGYFLVTFLFGAVVLALVAWKIFTLPSVTAGKGQGPTWKSVLTVLGLSSLVGMTWGLAVLTPLGLSTIYVFTLLNSLQGLFIFCWFIILYFPTQSTTASSSGTARLDQAHSVSQE
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Orphan receptor that regulates migration of lymphatic endothelial cells via the small GTPases RhoA and CDC42 (By similarity). Regulates B-cell development (PubMed:24113187). Seems to signal through G-alpha(q)-proteins (By similarity). Specifically expressed in intestinal lymphatic endothelium. No visible phenotype. Mutant mice show altered follicular-versus-marginal zone B-lymphocyte fate decision in the spleen and decreased numbers of B220+ lymphocytes in the bone marrow. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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Q86SM6
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MKEHIIYQKLYGLILMSSFIFLSDTLSLKGKKLDFFGRGDTYVSLIDTIPELSRFTACIDLVFMDDNSRYWMAFSYITNNALLGREDIDLGLAGDHQQLILYRLGKTFSIRHHLASFQWHTICLIWDGVKGKLELFLNKERILEVTDQPHNLTPHGTLFLGHFLKNESSEVKSMMRSFPGSLYYFQLWDHILENEEFMKCLDGNIVSWEEDVWLVNKIIPTVDRTLRCFVPENMTIQEKSTTVSQQIDMTTPSQITGVKPQNTAHSSTLLSQSIPIFATDYTTISYSNTTSPPLETMTAQKILKTLVDETATFAVDVLSTSSAISLPTQSISIDNTTNSMKKTKSPSSESTKTTKMVEAMATEIFQPPTPSNFLSTSRFTKNSVVSTTSAIKSQSAVTKTTSLFSTIESTSMSTTPCLKQKSTNTGALPISTAGQEFIESTAAGTVPWFTVEKTSPASTHVGTASSFPPEPVLISTAAPVDSVFPRNQTAFPLATTDMKIAFTVHSLTLPTRLIETTPAPRTAETELTSTNFQDVSLPRVEDAMSTSMSKETSSKTFSFLTSFSFTGTESVQTVIDAEATRTALTPEITLASTVAETMLSSTITGRVYTQNTPTADGHLLTLMSTRSASTSKAPESGPTSTTDEAAHLFSSNETIWTSRPDQALLASMNTTTILTFVPNENFTSAFHENTTYTEYLSATTNITPLKASPEGKGTTANDATTARYTTAVSKLTSPWFANFSIVSGTTSITNMPEFKLTTLLLKTIPMSTKPANELPLTPRETVVPSVDIISTLACIQPNFSTEESASETTQTEINGAIVFGGTTTPVPKSATTQRLNATVTRKEATSHYLMRKSTIAAVAEVSPFSTMLEVTDESAQRVTASVTVSSFPDIEKLSTPLDNKTATTEVRESWLLTKLVKTTPRSSYNEMTEMFNFNHTYVAHWTSETSEGISAGSPTSGSTHIFGEPLGASTTRISETSFSTTPTDRTATSLSDGILPPQPTAAHSSATPVPVTHMFSLPVNGSSVVAEETEVTMSEPSTLARAFSTSVLSDVSNLSSTTMTTALVPPLDQTASTTIVIVPTHGDLIRTTSEATVISVRKTSMAVPSLTETPFHSLRLSTPVTAKAETTLFSTSVDTVTPSTHTLVCSKPPPDNIPPASSTHVISTTSTPEATQPISQVEETSTYALSFPYTFSGGGVVASLATGTTETSVVDETTPSHISANKLTTSVNSHISSSATYRVHTPVSIQLVTSTSVLSSDKDQMTISLGKTPRTMEVTEMSPSKNSFISYSRGTPSLEMTDTGFPETTKISSHQTHSPSEIPLGTPSDGNLASSPTSGSTQITPTLTSSNTVGVHIPEMSTSLGKTALPSQALTITTFLCPEKESTSALPAYTPRTVEMIVNSTYVTHSVSYGQDTSFVDTTTSSSTRISNPMDINTTFSHLHSLRTQPEVTSVASFISESTQTFPESLSLSTAGLYNDGFTVLSDRITTAFSVPNVPTMLPRESSMATSTPIYQMSSLPVNVTAFTSKKVSDTPPIVITKSSKTMHPGCLKSPCTATSGPMSEMSSIPVNNSAFTPATVSSDTSTRVGLFSTLLSSVTPRTTMTMQTSTLDVTPVIYAGATSKNKMVSSAFTTEMIEAPSRITPTTFLSPTEPTLPFVKTVPTTIMAGIVTPFVGTTAFSPLSSKSTGAISSIPKTTFSPFLSATQQSSQADEATTLGILSGITNRSLSTVNSGTGVALTDTYSRITVPENMLSPTHADSLHTSFNIQVSPSLTSFKSASGPTKNVKTTTNCFSSNTRKMTSLLEKTSLTNYATSLNTPVSYPPWTPSSATLPSLTSFVYSPHSTEAEISTPKTSPPPTSQMVEFPVLGTRMTSSNTQPLLMTSWNIPTAEGSQFPISTTINVPTSNEMETETLHLVPGPLSTFTASQTGLVSKDVMAMSSIPMSGILPNHGLSENPSLSTSLRAITSTLADVKHTFEKMTTSVTPGTTLPSILSGATSGSVISKSPILTWLLSSLPSGSPPATVSNAPHVMTSSTVEVSKSTFLTSDMISAHPFTNLTTLPSATMSTILTRTIPTPTLGGITTGFPTSLPMSINVTDDIVYISTHPEASSRTTITANPRTVSHPSSFSRKTMSPSTTDHTLSVGAMPLPSSTITSSWNRIPTASSPSTLIIPKPTLDSLLNIMTTTSTVPGASFPLISTGVTYPFTATVSSPISSFFETTWLDSTPSFLSTEASTSPTATKSTVSFYNVEMSFSVFVEEPRIPITSVINEFTENSLNSIFQNSEFSLATLETQIKSRDISEEEMVMDRAILEQREGQEMATISYVPYSCVCQVIIKASSSLASSELMRKIKSKIHGNFTHGNFTQDQLTLLVNCEHVAVKKLEPGNCKADETASKYKGTYKWLLTNPTETAQTRCIKNEDGNATRFCSISINTGKSQWEKPKFKQCKLLQELPDKIVDLANITISDENAEDVAEHILNLINESPALGKEETKIIVSKISDISQCDEISMNLTHVMLQIINVVLEKQNNSASDLHEISNEILRIIERTGHKMEFSGQIANLTVAGLALAVLRGDHTFDGMAFSIHSYEEGTDPEIFLGNVPVGGILASIYLPKSLTERIPLSNLQTILFNFFGQTSLFKTKNVTKALTTYVVSASISDDMFIQNLADPVVITLQHIGGNQNYGQVHCAFWDFENNNGLGGWNSSGCKVKETNVNYTICQCDHLTHFGVLMDLSRSTVDSVNEQILALITYTGCGISSIFLGVAVVTYIAFHKLRKDYPAKILINLCTALLMLNLVFLINSWLSSFQKVGVCITAAVALHYFLLVSFTWMGLEAVHMYLALVKVFNIYIPNYILKFCLVGWGIPAIMVAITVSVKKDLYGTLSPTTPFCWIKDDSIFYISVVAYFCLIFLMNLSMFCTVLVQLNSVKSQIQKTRRKMILHDLKGTMSLTFLLGLTWGFAFFAWGPMRNFFLYLFAIFNTLQGFFIFVFHCVMKESVREQWQIHLCCGWLRLDNSSDGSSRCQIKVGYKQEGLKKIFEHKLLTPSLKSTATSSTFKSLGSAQGTPSEISFPNDDFDKDPYCSSP
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Orphan receptor. Detected in fetal retina. Highly expressed in normal enterochromaffin cells and in neuroendocrine carcinoma. Detected in normal liver; highly expressed in primary liver carcinoma. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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B7ZCD0
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MRKHILHQRLCGLILVSSFIFLTDSLSLKGKRLDFYGEGKAYVSLTYTMPELSRLTACIDLISMTNSSHYWMAFIYITNNTLLGREDVDLGLAGDHQQLILYSFGKTFYVSYHLIPFHWHTLCLVWDGVKGRLELFRNKERILAIMDQPHRLSPNGTLVLGHFPRNGEGQIKTVIPRFTSSLYYFQLWDRILENEEFMTCFYGNVVSWEDDVWLIHKISPTVDRRLRCFVSENMTIQETSTNVSQQIDLTTSSQTTGLNPHKTSHSSTLLPEGMADSTINSTAISYANTVPSPLATVSAAKDLKTSTTETATFLTDTLFTSTATPLPTQTVTEHSYLGKTRTSKRVEAMATEIFHSATATDLIDTSVFTKNYTVSETSTTKSKSAVGKTTLFLNESTSIAPTPCPKHKSTDVAILHTSKSGQEFLVSSAARTVSWSTLEETSPITTDVGIVSTFPPESLLTSTASPVSSTFPEIQLASTLSTTDSEMASTVHSVLPMQTIPTPRTVKPESGSTNFQDVFSPSMEDALSVSMPKETTFMAFSSITSSPITRTQDEQIAIDAESTHLTIIPGTKFVPTLAEASLFPTIEGQAYTQDTPTTDEPMLTLTSTKSPSTYNASESVLTSITIKSDYQFFTNETTWTSKSGQNLLTSMNTTTIPTFTSNKTLTLPFQGNATNRDHSSMTTNVSPIEASTESKVTTSSDATTASYTTALFKPTSQWLSHFTSVSGITSIASQPESKLTTLLLKSNSMPTVATNEFPSIPSEPVAPSVNTSTLTDIKPNFSTEKSISETIQIETNGVSSFGDTLAPLPMSATTQRVYTTVTKETTSRHPKVKSTISTVAEASPFSTMLEVTDESEQMVTASVTISPFTDIEKLTTALSKETATAEVGVSWLSTKLKESMPESSHNGTTESFNSTHTYTVDWTSEKSKGNSASSPNSASTQALPELPSSSTMKTMGVTFSTNSSQRTAASLSAGILSPQTASTHALVTPQLLTHTFSLPVNISAVTSPKTTMVFFDETKVTLSQPSTLARDFTTSMPSVGSTLPTVTMTTELVPPVSPTASTISDSMFTHRDLLHTTSEVTTISSTTAHMAISSLRETLVSSLRPPTPVITKAISTIPSISSDSVSPSIHTLVCSRPSPNNVTIVSSTYVSSTTSTSVATPSESHFSFPYAFSSGGDVTMASGPTGTSAGGEAMPPNTFVNKFITSVDHESTTYFVNTPVSTQSVFATSMVSSDKEQTNISMEKTLRTTGVAEISPSKNSFILDSQSTFPWEMTDTELSETTEISSHQTHLPSEILPGYSDSGNLTTFSTSGSTQSAQTLSSSTIIGVRVSEGSTSLEKTALPSQVQTVTKSLTHDKERTSALSEYPPRTVEKIMSSSPVTHQATGHLATSIVDASRTTRISHPVLINTTLSYLLSLKTKPEATQIASSTSGSTENFPNSFSPFTTGLLSTNFTMITPNGSTTVLSIPNEPTNLPKKTSMEASTPISQMDLLALNVTAFTSKKVSDTHTMLMTKSSRTIHIGTLKSVSIGTFGLKSEKSEMPVNNSDFSTTVLYSDTSTRLGEFFTSSSSLPPKATKTTQASTLNTTPVAHAGPTSQRTVFSSTFSNSSVVEVPLNYTTAHFSSPTQRGFLSMKTIPTTSMAGISTSVIGATSSSLSSSKNTEPISSIPKTMFSLLLSTTQQPSQENGAPTLDILPGITVSSGGATDLINANSRATIPANELSTTPSDNFYTFLNTQDSPTLTNSKVTPRPTESVKSTPTHLSFDTRKMNILTELTKSGPCVTTPVLYPLWTQTSTAPPLTSHLYSPHSTKAKFPLASQMAEYPAWATGITPSITQALLTTSRNTQRVEDSPFPVFTTKVMTPNRMEVETLHSPSGTLATSTTSQIGLVSRDVTVMPLISTSESLPSLGISESTSLSISSTFPPTTLAAILPTFEKTAMPVTPGITLSSNPSVNSRATSPTWSSSSLPSDSRASIFTPSRLLTSSSGEMSESTFPASDIIATYSNFTVAPLSDGSATIATQATSTTTLDIITANSLTSPPIPSKDKDGSLHTSTFLESSLRTTGADSSTDMSERMSFGRTSISPSLTRHDLSIGSLTVSSPTNTSPWSKVPVTSESHTLFPSKSTLDSVMSTATTTSTAIGTSFPLMSTEMAHPSTATGFSLVSSSFETTWMDSIFSSLFTQPSTSPTAKESTVSFYNIKMSFSVFDEEPRVLVTTVIHDLTKDWLNFMFQNSEFSLANLAIQIKSRKTSKEETAMYRYILEQKKGQGMDAIFHVPYSCACWVIIKAKSSLESVELISSIRTKIHGNLTHGNFTQDQLTLLVKSDHVVVEKLEPGKCEADETPSKYKGTYKWPLTDPTETAQERCIKNENRNATRICSISIQTGKCQWEKPRLKQCKLLQGLPDKIVDLANITISDENADDVAEHILNLVNESPPLDEEETKIIVSKVADISNCDEISINLTQIILQILNTVTEKQSDSASNLPPVSNEILRIIERVGHKMEFAGRTANLTVAKLALAVLRVDHKFEGMAFSIQSSEEVIAPQIFLGDIPLRKALASIYLPKSLREKVPLDGLQTILFNFFGQTSLFKAKTITSELMTYVVSASISNTSIQNLADPVIIILKHIQGDWNYDQVYCAFWDFDTNNGLGGWNPSGCKLKESNINYTICQCNHLTHFGVLMDLSRSTVDAVNERILVIITYTGCGISSIFLGIAMVTYIAFHKLRKDYPSKILINLCTALLMLNLAFLVNSWLTSFQKVGLCITAAVALHYFLLVSLTWMGLEAVHMYFALVKVFNTYIPNYILKFCLAGWGIPAITVAIILSVRKDLYGTLSPTTPFCWIKDDHIFYISVVAYFCLIFLMNLSMFCTVLVQLTSVKSQSQKTRKKMILNDLKGTISLTFLLGLTWGFAFFAWGPVRIFFLYLFAICNTLQGFLIFVFYCVMKESVREQWHMPLHCRWLRLENFAGWINVRHKQKRLKKNNESKLLTPSLMSTTTFKSIGSVPSIPSEINFSNGDFDDSPDTFSFLSCKAAPTFIRRALPAEIQTNSTQKQRSFPINVSRDTHLTPSSGLGEMFNL
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Orphan receptor. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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Q8IZ14
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MDHCGALFLCLCLLTLQNATTETWEELLSYMENMQVSRGRSSVFSSRQLHQLEQMLLNTSFPGYNLTLQTPTIQSLAFKLSCDFSGLSLTSATLKRVPQAGGQHARGQHAMQFPAELTRDACKTRPRELRLICIYFSNTHFFKDENNSSLLNNYVLGAQLSHGHVNNLRDPVNISFWHNQSLEGYTLTCVFWKEGARKQPWGGWSPEGCRTEQPSHSQVLCRCNHLTYFAVLMQLSPALVPAELLAPLTYISLVGCSISIVASLITVLLHFHFRKQSDSLTRIHMNLHASVLLLNIAFLLSPAFAMSPVPGSACTALAAALHYALLSCLTWMAIEGFNLYLLLGRVYNIYIRRYVFKLGVLGWGAPALLVLLSLSVKSSVYGPCTIPVFDSWENGTGFQNMSICWVRSPVVHSVLVMGYGGLTSLFNLVVLAWALWTLRRLRERADAPSVRACHDTVTVLGLTVLLGTTWALAFFSFGVFLLPQLFLFTILNSLYGFFLFLWFCSQRCRSEAEAKAQIEAFSSSQTTQ
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Adhesion G protein-coupled receptor (GPCR). Transduces intracellular signals through coupling to guanine nucleotide-binding protein G(s) subunit alpha and activation of adenylate cyclase pathway. Isoform 1, but not isoform 2, is constitutively active, as evidenced by elevated basal cAMP levels, and responds to mechanical activation (shaking). Expressed in immune cells. Primarily found in granulocytes. Found in eosinophils. Autoproteolysis between residues Leu-226 and Thr-227 occurs in the lumen of the endoplasmic reticulum during receptor biosynthesis. The N-terminal fragment (NTF) subsequently reassociates with the C-terminal fragment (CTF) either in a homogeneric heterodimerization, or with another family member through heterogeneric heterodimerization. Autocatalytic cleavage is thought to be critical for the maturation, stability, trafficking, and function. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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G5E8G8
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MDPHGALFFYLCLLAAQVVLVETLSDLLVLMKRLEQPVGRGLSSRARHIHSLEQKLLNASFGGHNLTLQTNSIQSLVFKLSCDFPGLSLSSTTLTNVSQVRAPHAMQFPAELTKGACVTSRPAELRLICIYFFTAHLFQDDRNSSLLNNYVLGAQLDHRPVNNLQKPVNISFWHNRSLEGYTVSCVFWKEGASKSSWGAWSPEGCYTEQPSATQVLCHCNHLTYFAVLMQLSGDPVPAELQVPLEYISFVGCSISIVASLLTILLYAQSRKQSDSTTRIHMNLNGSVLLLNVTFLLSSQMTLPTMPRPVCKVLAAVLHYALLSSLTWMAIEGFNLYLFLGRVYNAYIRRYLLKLCMLGWGFPALLVLLLLMIKSSVYGPCVTSLSKSQENGTGFQNVSMCWIRSPMVHSILVMGYGGFTSLFNLVVLAWALWILCRLRAREKALSPWAYRDTAMVLGLTVLLGTTWTLAFFSFGVFLLPQLFLFTIFNSLYGFFLFLWFCSQKRYSDAEAKAEMEAVSSSQMTH
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Adhesion G protein-coupled receptor (GPCR). Transduces intracellular signals through coupling to guanine nucleotide-binding protein G(s) subunit alpha and activation of adenylate cyclase pathway (PubMed:22575658). Isoform 1, but not isoform 2, is constitutively active, as evidenced by elevated basal cAMP levels, and responds to mechanical activation (shaking) (PubMed:26499266). Expressed at least in kidney, heart, brain and spleen. In the kidney, both isoform 1 and isoform 2 are expressed at similar levels. Isoform 1 is predominant in spleen, while isoform 2 is the major form in heart and brain. Autoproteolysis between residues Leu-222 and Thr-223 occurs in the lumen of the endoplasmic reticulum during receptor biosynthesis. The N-terminal fragment (NTF) subsequently reassociates with the C-terminal fragment (CTF) either in a homogeneric heterodimerization, or with another family member through heterogeneric heterodimerization. Autocatalytic cleavage is thought to be critical for the maturation, stability, trafficking, and function. May be due to competing acceptor splice site. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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C6KFA3
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MISFISGRWWRWKFQNTLAVFLLLICLSTSVAQSCQSSTSCNVVLTDSQGSFTSPCYPNDYPPSQSCNWTIQAPAGFIVQITFLDFELEEAQGCIYDRVVVKTGTSDAKFCGLTANGLTLNSTGNVMEVFFNSDFSVQKKGFHISYKQVAVTLRNQKVTMPKSSKTILRVSNSISIPVLTAFTVCFEIARTAQKATETIFTLSDAAGTSILAFEKTSNGMELFIGASYCSVDNLLTSSDITATMKPLCLTWTKSSGLIGVYFGGHYFSSICSASQIYTLQSGGLLQIAGKGSSSVSVDDQNLDGFIYNFRLWDHAMLSSELSALTCDTVGNVVDWDHSYWTIPGSSTQTDSTLSCSTAITTLSPGTAGCASGLGCPATLTVTITSIATTNIIPTNATTHEDIFYRSTLVVTDEQTPDRDATAIISQWLNQTFQNWMYRVYVDGISLQLITVLSRITTTRQTYLALLVYKNTTDVNLAEVEIESMLRSAPAIGNGLTLDSVTVNLMENCQADEFPVHYRWPESRPTVTQYVPCFPYKDRNASRTCMINRDNYTSFWALPDRGNCTNITSITVSQENAMDVAVQLADISNNGLSKEELTQVVTKVMELVNIAKINATLASTVVTIISNVMVSSEDAQKDASETALKAVDELVQKIEFDGPSLTISSKNLVVGVSALDTTNFNGSTLSAFIATNTTDPQIDFDSEAHNALAVVTLPPTLLQNLSLSQIEKVSRINFMFFGRTGLFQDHQNNGLTLNSYVVASSVGNFTIKNLQDPVRIEIAHLEYQKDPNPQCVFWDFNLQNYSGGCNSDGCKVGSDSNSNRTVCLCNHLTHFGILMDVSRAAELIDEKNNRVLTFITYIGCGISAIFSAATLLTYIAFEKLRRDYPSKILMNLSTSLLFLNMVFLLDGWLASYEIKELCVTVAVFLHFFLLTSFTWMGLESIHMYIALVKVFNTYIRRYILKFCIVGWGVPAAIVGIVLAVSKDSYGKNYYGKGKDGQGTSEFCWILNPVVFYVTCVAYFSIIFLMNVAMFIVVMIQICGRNGKRSNRTLREDILRNLRSVVSLTFLLGMTWGFAFFAWGPVSLAFMYLFTIFNSLQGLFIFVFHCALKENVQKQWRRYLCCGKLRLADNSDWSKTATNNTKKVSSDNLGKSLSSSSFGSTTANWTSKAKATLNPFARHSNADSTLQ
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G-protein coupled receptor which is activated by type IV collagen, a major constituent of the basement membrane. Couples to G(i)-proteins as well as G(s)-proteins (PubMed:25118328). Essential for normal differentiation of promyelinating Schwann cells and for normal myelination of axons (PubMed:19745155). Also plays a role in inner ear development (PubMed:24067352). Plays an important role in heart development (PubMed:24082093). Necessary and sufficient for axon sorting by Schwann cells independently of the ADGRG6-CTF (PubMed:25695270). Expressed in Schwann cells of the posterior lateral line nerve and in brain. Detected from 30 hours post-fertilization to 4 days post-fertilization in Schwann cells of the posterior lateral line nerve. A short peptide sequence (termed the Stachel sequence) in the C-terminal part of the extra-cellular domain (ECD) functions as a tethered agonist. Upon structural changes within the ECD, e.g. due to extracellular ligand binding or mechanical movements, this intramolecular agonist is exposed to the 7TM domain, triggering G-protein activation. Morpholino knockdown of the protein results in defects in semicircular canal formation inner ear (PubMed:24067352). Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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Q96JW0
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MMFRSDRMWSCHWKWKPSPLLFLFALYIMCVPHSVWGCANCRVVLSNPSGTFTSPCYPNDYPNSQACMWTLRAPTGYIIQITFNDFDIEEAPNCIYDSLSLDNGESQTKFCGATAKGLSFNSSANEMHVSFSSDFSIQKKGFNASYIRVAVSLRNQKVILPQTSDAYQVSVAKSISIPELSAFTLCFEATKVGHEDSDWTAFSYSNASFTQLLSFGKAKSGYFLSISDSKCLLNNALPVKEKEDIFAESFEQLCLVWNNSLGSIGVNFKRNYETVPCDSTISKVIPGNGKLLLGSNQNEIVSLKGDIYNFRLWNFTMNAKILSNLSCNVKGNVVDWQNDFWNIPNLALKAESNLSCGSYLIPLPAAELASCADLGTLCQATVNSPSTTPPTVTTNMPVTNRIDKQRNDGIIYRISVVIQNILRHPEVKVQSKVAEWLNSTFQNWNYTVYVVNISFHLSAGEDKIKVKRSLEDEPRLVLWALLVYNATNNTNLEGKIIQQKLLKNNESLDEGLRLHTVNVRQLGHCLAMEEPKGYYWPSIQPSEYVLPCPDKPGFSASRICFYNATNPLVTYWGPVDISNCLKEANEVANQILNLTADGQNLTSANITNIVEQVKRIVNKEENIDITLGSTLMNIFSNILSSSDSDLLESSSEALKTIDELAFKIDLNSTSHVNITTRNLALSVSSLLPGTNAISNFSIGLPSNNESYFQMDFESGQVDPLASVILPPNLLENLSPEDSVLVRRAQFTFFNKTGLFQDVGPQRKTLVSYVMACSIGNITIQNLKDPVQIKIKHTRTQEVHHPICAFWDLNKNKSFGGWNTSGCVAHRDSDASETVCLCNHFTHFGVLMDLPRSASQLDARNTKVLTFISYIGCGISAIFSAATLLTYVAFEKLRRDYPSKILMNLSTALLFLNLLFLLDGWITSFNVDGLCIAVAVLLHFFLLATFTWMGLEAIHMYIALVKVFNTYIRRYILKFCIIGWGLPALVVSVVLASRNNNEVYGKESYGKEKGDEFCWIQDPVIFYVTCAGYFGVMFFLNIAMFIVVMVQICGRNGKRSNRTLREEVLRNLRSVVSLTFLLGMTWGFAFFAWGPLNIPFMYLFSIFNSLQGLFIFIFHCAMKENVQKQWRQHLCCGRFRLADNSDWSKTATNIIKKSSDNLGKSLSSSSIGSNSTYLTSKSKSSSTTYFKRNSHTDNVSYEHSFNKSGSLRQCFHGQVLVKTGPC
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G-protein coupled receptor which is activated by type IV collagen, a major constituent of the basement membrane (By similarity). Couples to G(i)-proteins as well as G(s)-proteins (PubMed:24227709). Essential for normal differentiation of promyelinating Schwann cells and for normal myelination of axons (PubMed:24227709). Regulates neural, cardiac and ear development via G-protein- and/or N-terminus-dependent signaling (By similarity). May act as a receptor for PRNP which may promote myelin homeostasis (By similarity). Interacts with Laminin-2; this interaction stabilizes the receptor in an inactive state. Laminin-2 polymerization could facilitate ADGRG6-NTF removal, thereby exposing the tethered agonist to drive myelination. Interacts with PRNP. Detected on the cell surface of activated but not resting umbilical vein. Expressed in placenta and to a lower extent in pancreas and liver. Detected in aortic endothelial cells but not in skin microvascular endothelial cells. Up-regulated by bacterial lipopolysaccharides (LPS) and thrombin, but not by other inflammatory stimuli in primary umbilical veins. A short peptide sequence (termed the Stachel sequence) in the C-terminal part of the extra-cellular domain (ECD) functions as a tethered agonist. Upon structural changes within the ECD, e.g. due to extracellular ligand binding or mechanical movements, this intramolecular agonist is exposed to the 7TM domain, triggering G-protein activation. Proteolytically cleaved into 2 conserved sites: one in the GPS domain (S1 site) and the other in the middle of the extracellular domain (S2 site). The proteolytic cleavage at S1 site generates an extracellular subunit and a seven-transmembrane subunit. Furin is involved in the cleavage of the S2 site generating a soluble fragment. Processing at the GPS domain occurred independent of and probably prior to the cleavage at the S2 site. Proteolytic cleavage is required for activation of the receptor. Highly glycosylated. Genetic variations in ADGRG6 influences stature as a quantitative trait (STQTL) [MIM:606255]. Adult height is an easily observable and highly heritable complex continuous trait. Because of this, it is a model trait for studying genetic influence on quantitative traits. The disease is caused by variants affecting the gene represented in this entry. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily. Sequencing errors. Truncated N-terminus. Truncated N-terminus. Extended N-terminus.
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Q811E4
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MMFDTLGKRCCPWRLKPSALLFLFVLCVTCVPLSVCGCGSCRLVLSNPSGTFTSPCYPNDYPNTQSCSWTLRAPAGYIIQITFNDFDIEEAPNCIYDSLSLDNGESQTKFCGATAKGLSFNSSVNEMHVSFSSDFSIQKKGFNASYIRVAVSLRNQKVILPQTLDAYQVSVAKSISIPELKAFTLCFEASKVGNEGGDWTAFSYSDESLTQLLSLEKASNGYFLSISGSRCLLNNALPVKDKEDIFTENLEQLCLVWNNSWGSIGINFKKNYETVPCDSTISAVVPGDGTLLLGSDRDEVASLRGSIYNFRLWNFTMDLKALSNLSCSVSGNVIDWHNDFWSISTQALKAEGNLSCGSYLIQLPAAELTNCSELGTLCQDGIMYRISVVIHNDFNHPEVKVQTKVAEWLNSTFQNWNYTVYVVNISFHQKVGEDRMKVKRDIMDDDKRLVLWALLVYNATNNVSLNEEKIKQKLMTNNASLEDGLRLCEVDVNQLGMCSALEDPDGFSWPATLPSVYKQPCPNKPGFFMTRACLSNGTSTFWGPVDTSNCSRQSNEVANEILNQTGDGQNLTSANINSIVEKVKRIVNKEENIDITLGSTLMNIFSNILSSSDSDLLESSTEALKTIDELAFKIDLNSTPHVNIETQNLALGVSSLIPGTNAPSNFSIGLPSNNESYFQMDFGNGQTDPLASVILPPNLLENLSPEDSVLVRRAQFTFFNKTGLFQDVGSQRKVLVSYVMACSIGNITIQNLKDPVQIKIKHTRTQEVHHPICAFWDMNKNKSFGGWNTSGCVAHSDLDAGETICLCSHFTHFGVLMDLPRSASQIDGRNTKVLTFITYIGCGISAIFSAATLLTYVAFEKLRRDYPSKILMNLSSALLFLNLIFLLDGWVTSFGVAGLCTAVAALLHFFLLATFTWMGLEAIHMYIALVKVFNTYIHRYILKFCIIGWGLPALVVSIILVSRRQNEVYGKESYGKDQDDEFCWIQDPVVFYVSCAGYFGVMFFLNVAMFIVVMVQICGRNGKRSNRTLREEVLRNLRSVVSLTFLLGMTWGFAFFAWGPLNIPFMYLFSIFNSLQGLFIFIFHCAMKENVQKQWRRHLCCGRFRLADNSDWSKTATNIIKKSSDNLGKSLSSSSIGSNSTYLTSKSKSSSTTYFKRNSHSDNFS
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G-protein coupled receptor which is activated by type IV collagen, a major constituent of the basement membrane. Essential for normal differentiation of promyelinating Schwann cells and for normal myelination of axons these functions are mediated via G-protein-signaling pathways (PubMed:24227709, PubMed:21613327). Regulates also neural, cardiac and ear development via G-protein- and/or N-terminus-dependent signaling. May act as a receptor for PRNP which may promote myelin homeostasis (PubMed:27501152). Plays an important role in heart developmention (PubMed:24082093). Necessary and sufficient for axon sorting by Schwann cells independently of the ADGRG6-CTF (PubMed:25695270). Interacts with Laminin-2; this interaction stabilizes the receptor in an inactive state (PubMed:25695270). Laminin-2 polymerization could facilitate ADGRG6-NTF removal, thereby exposing the tethered agonist to drive myelination (PubMed:25695270). Interacts with PRNP (PubMed:27501152). Expressed at high levels in the heart, somite and otic vesicle during embryogenesis and in adult lung. Proteolytically cleaved into 2 conserved sites: one in the GPS domain (S1 site) and the other in the middle of the extracellular domain (S2 site). The proteolytic cleavage at S1 site generates an N-terminal fragment (NTF) and a seven-transmembrane-containing C-terminal fragment (CTF). The membrane-bound CTF can act as an independent receptor and the soluble NTF can act as a ligand or coreceptor. Furin is involved in the cleavage of the S2 site generating a soluble fragment. Processing at the GPS domain occurred independent of and probably prior to the cleavage at the S2 site. Proteolytic cleavage is required for activation of the receptor (By similarity). Deficient mice die during organogenesis. Mutant embryos show signs of myocardial wall thinning, hypotrabeculation, defective mitochondrial and circulatory failure. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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Q86SQ2
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MASCRAWNLRVLVAVVCGLLTGIILGLGIWRIVIRIQRGKSTSSSSTPTEFCRNGGTWENGRCICTEEWKGLRCTIANFCENSTYMGFTFARIPVGRYGPSLQTCGKDTPNAGNPMAVRLCSLSLYGEIELQKVTIGNCNENLETLEKQVKDVTAPLNNISSEVQILTSDANKLTAENITSATRVVGQIFNTSRNASPEAKKVAIVTVSQLLDASEDAFQRVAATANDDALTTLIEQMETYSLSLGNQSVVEPNIAIQSANFSSENAVGPSNVRFSVQKGASSSLVSSSTFIHTNVDGLNPDAQTELQVLLNMTKNYTKTCGFVVYQNDKLFQSKTFTAKSDFSQKIISSKTDENEQDQSASVDMVFSPKYNQKEFQLYSYACVYWNLSAKDWDTYGCQKDKGTDGFLRCRCNHTTNFAVLMTFKKDYQYPKSLDILSNVGCALSVTGLALTVIFQIVTRKVRKTSVTWVLVNLCISMLIFNLLFVFGIENSNKNLQTSDGDINNIDFDNNDIPRTDTINIPNPMCTAIAALLHYFLLVTFTWNALSAAQLYYLLIRTMKPLPRHFILFISLIGWGVPAIVVAITVGVIYSQNGNNPQWELDYRQEKICWLAIPEPNGVIKSPLLWSFIVPVTIILISNVVMFITISIKVLWKNNQNLTSTKKVSSMKKIVSTLSVAVVFGITWILAYLMLVNDDSIRIVFSYIFCLFNTTQGLQIFILYTVRTKVFQSEASKVLMLLSSIGRRKSLPSVTRPRLRVKMYNFLRSLPTLHERFRLLETSPSTEEITLSESDNAKESI
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Orphan receptor. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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Q80T42
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MRSCRSCNVRVLVAIVCGLLTGIVLGLGIWRMVIRINRGIFVPVPSIPVQFCRNGGTWQNGRCICTEEWKGLRCTIANFCENSTDGEFTFGSIPVGRYGPSLQTCEPGTLNAGSPKATRLCNVSEFGNIELQNVTKGSCNINLQTLEIQINNQTASAENISREAQVLTADASKLTAQNITSATTVVGQIFGKANNESQAKKTAIATVSQILDASEDVFQKAAEMDNSKSFSNLIKQMENYSYSQGDQTVVEPNIAIQSVTRDDNSGPSVLFSVQKGSSNSLVSGRILINKTANGLNPDGQTELQILLNTGENRKSCGFMVYQNHKLFQSKTFTATSDFSQKIISSKINESEQQRQNKVSVEMVFNPTYDKRELRLHSYACVYWNFLINDWDTQGCQKTGNTTEFLRCNCSHTTNFAVLMSFKKDYKYPKSLDILSNIGCALSIAGLALTILFQILTRKIRKTSVTWVLVSLCSSMLIFNLLFVFGIENSNKNLKTSDSDINVKPENNKIPESDTIETPNPSCTAIAALLHYFLLVTFTWNGLSATQLYFLLIRTMKPLPRHFIIFISLVGWGVPAIIVGVTIGSIYALSGNKRYWELDYRQEEICWLAVPKDNDYARSPLLWSFIIPVTIILITNITIFVIITVKVLWKNNQNLTSTKKVSSLKKVFSTLSIAVVFGVTWILAYAMLISNDDIRIVFSYIFCLFNTTQGLQIFILYTVRTKVFQSEASKILKSLSSSFDRTKPMPSITPLKLRVRMYNMLRSLPSLNERFRLLEPSGMTEETSLS
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Orphan receptor. Selectively expressed in the intestinal tissues. Deficient mice exhibit less body weight gain and an increase in intestinal contraction frequency. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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Q90685
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MGGSGAAATLALGLALGLALGGWANCPERELQRREEEANVVLTGTVEEIMNVDPVHHTYSCKVRVWRYLKGKDIVTHEILLDGGNKVVIGGFGDPLICDNQVSTGDTRIFFVNPAPQYMWPAHRNELMLNSSLMRITLRNLEEVEHCVEEHRKLLADKPNSYFTQTPPTPRDACRGMLCGFGAVCERSPTDPSQASCVCKKTACPVVVAPVCGSDYSTYSNECELEKAQCNQQRRIKVISKGPCGSKDPCAEVTCSFGSTCVRSADGQTAGCVCPASCSGVAESIVCGSDGKDYRSECDLNKHACDKQENVFKKFDGACDPCKGILNDMNRVCRVNPRTRRVELLSRPENCPSKREPVCGDDGVTYASECVMGRTGAIRGLEIQKVRSGQCQHQDKCKDECKFNAVCLKRWHARCSCDRITCDGTYRPVCARDSRTYSNDCERQKAECHQKAAIPVKHSGPCDLGTPSPCLSVECTFGATCVVKNREPVCECQQVCQGRYDPVCGSDNRTYGNPCELNAMACVLKREIRVKHKGPCDRCGKCQFGAICEAETGRCVCPTECVPSSQPVCGTDGNTYGSECELHVRACTQQKNILVAAQGDCKSCGTTVCSFGSTCVGGQCVCPRCEQQPLAQVCGTDGLTYDNRCELRAASCQQQKSIEVAKMGPCEDECGSGGSGSGDGSECEQDRCRHYGGWWDEDAEDDRCVCDFTCLAVPRSPVCGSDDVTYANECELKKTRCEKRQNLYVTSQGACRALTTTPPPLPVVHCSQTIYGCCPDNMTLALGVGAAGCPSTCQCNPYGSYGGTCDPATGQCSCKPGVGGLKCDRCEPGFWNFRGIVTDSKSGCTPCNCDPVGSVRDDCEQMTGLCSCKTGITGMKCNQCPNGSKMGMAGCEKDPSAPKSCEEMSCEFGATCVEVNGFAHCECPSPLCSEANMTKVCGSDGVTYGDQCQLKTIACRQGQLITVKHVGQCHESITHTSHTMPPTPLPTLPLDKLIVPPPLQLTTQAPEPTELATTSLLMEASPTTRSHPTTRRVTTTRPVTTPWMTHGVLKTTVRPLSTSPVVLATTQPPYAESGSAEGSGDQEMSISGDQESSGAGSAGEEEVEESQVTPTPAIERATCYNTPLGCCSDGKTAAADAEGSNCPATKVFQGVLILEEVEGQELFYTPEMADPKSELFGETARSIESALDELFRNSDVKNDFKSIRVRDLGQSSAVRVIVESHFDPATSYTAADVQAASLKQIRASKKRTILVKKPQQEHVKFMDFDWIPRIFTTTITTTTATTMAPATTRRHTTASAATTAHILRQDTVGHPSAKLAAPASTRRPTSTLPTTARRKPTRQPPSTTKKPSRPCDSHPCLHGGTCEDDGREFTCRCPAGKGGAVCEKPIRYFIPSFGGKSYLAFKMMKAYHTVRIAMEFRATELSGLLLYNGQNRGKDFISLALVGGFVELRFNTGSGTGVITSKVRVEPGKWHQLVVNRNRRSGMLAVDGEHVSGESPTGTDGLNLDTDLFVGGAPEDQMAVVAERTAATVGLKGSIRLLDVNNQMYDLREKGSDVLYGSGVGECGNDPCHPNPCHHGASCHVKEAEMFHCECLHSYTGPTCADERNPCDPTPCHISATCLVLPEGGAMCACPMGREGEFCERVTEQDHTMPFLPEFNGFSYLELNGLQTLFLTCRQMSMEVVFLAKSPSGMIFYNGQKTDGKGDFVSLALHDGYLEYRYDLGKGAAVLRSKEPVPLNTWISVLLERSGRKGVMRINNGERVMGESPKSRKVPHAFLNLKEPFYVGGAPDFSKLARAAAISTSFYGAVQRISIKGVPLLKEQHIRSAVEISTFRAHPCTQKPNPCQNGGTCSPRLESYECACQRGFSGAHCEKVIIEKAAGDAEAIAFDGRTYMEYHNAVTKSHLSNEIPAPDALDYPAEPSEKALQSNHFELSIKTEATQGLILWSGKGLERSDYIALAIVDGFVQMMYDLGSKPVVLRSTVPINTNHWTHIKAYRVQREGSLQVGNEAPITGSSPLGATQLDTDGALWLGGMERLSVAHKLPKAYSTGFIGCIRDVIVDRQELHLVEDALNNPTILHCSAK
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Heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. Transmembrane agrin (TM-agrin), the predominant form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases. Isoform 2, isoform 4 and isoform 7: muscle agrin isoforms, which lack the 8-amino acid insert at the 'B' site, but with the insert at the'A' site have no AChr clustering activity nor MUSK activation but bind heparin. Bind alpha-dystroglycan with lower affinity. Muscle agrin A0B0 lacking inserts at both 'A' and 'B' sites has no heparin-binding nor AChR clustering activity but binds strongly alpha-dystroglycan. Is involved in modulation of growth factor signaling (By similarity). Involved also in the regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling. This released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'B' splice variants of this fragment also show an increase in the number of filopodia. Monomer (By similarity). Interacts (N-terminal subunit) with TGF-beta family members, BMP2 AND BMP4; the interactions inhibit the activity of these growth factors. Interacts with TGFB1; the interaction enhances the activity of TGFB1. Component of the AGRN-LRP4 complex that consists of a tetramer of two AGRN-LRP4 heterodimers. Interacts (via the laminin G-like 3 domain) directly with LRP4; the interaction is required for activation of MUSK and clustering of AChR and requires the 'B8' insert present in the B8 isoforms. Interacts with DAG1; the interaction is influenced by cell surface glycosaminoglycans and by alternative splicing of AGRN. Synaptic basal lamina at the neuromuscular junction. Many isoforms exist including secreted and transmembrane forms, isoforms with different length inserts produced at the 'B' splice site, B0, B8, B11 and B19, with or without the 'A' splice site insert. Detected in embryonic brain, spinal cord, skeletal muscle, vitreous humor and liver (at protein level). The 4 amino acid insert at the 'A' site is required for efficient binding of heparin. The NtA domain, absent in TM-Agrin, is required for binding laminin and connecting to basal lamina. Both laminin G-like 2 (G2) and laminin G-like 3 (G3) domains are required for alpha-dystroglycan binding. G3 domain is required for C-terminal heparin, heparan sulfate and sialic acid binding. Contains heparan and chondroitin sulfate chains and alpha-dystroglycan as well as N-linked and O-linked oligosaccharides. Glycosaminoglycans (GAGs), present in the N-terminal 110 kDa fragment, are required for induction of filopodia in hippocampal neurons. The first cluster (Gly/Ser-rich) for GAG attachment contains heparan sulfate (HS)chains and the second cluster (Ser/Thr-rich), contains chondroitin sulfate (CS) chains (By similarity). C-terminal heparin and heparin sulfate binding is independent of calcium ions. Binds heparin with a stoichiometry of 2:1. Binds sialic acid with a stoichiometry of 1:1 and binding requires calcium ions. Inserts at the 'B' site have no effect on sialic acid binding. At synaptic junctions, cleaved at two conserved sites, alpha and beta, by neurotrypsin. Cleavage at the alpha-site produces the N- and C- terminal 110-kDa subunits. Further cleavage of the C-terminal at the beta site produces C-terminal fragments, C22 and C90, of 90 kDa and 22 kDa respectively (By similarity). Proteolytically cleaved in vitro in both the N-terminal and C-terminal by several matrix metalloproteinases (MMPs). Transmembrane isoform produced by usage of an alternative first exon.
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Q90404
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VPLSPVCGSDGVTYDSECALKLMRCMIQKDLHVVMLSPCKDASPSSVPELHCSRSVYGCCRDNVTAAQGVGLAGCPSTCECNRYGSYSKTCSPSSGQCSCKPGVGGLKCDRCEPGFWNFRGIVTDEKSGCTPCNCYPLGAVRDDCEQMSGLCSCKAGISGMKCNQCPNGSKLGPSGCDQDPSVSRTCSDLHCQYGATCVQSIGRAYCECPPSICPKNKQFKVCGSDGVTYANECQLKTIACRQGSVINILHQGPCQGTTPSTGNIQTTDLTPSPKEHTNLSKIVSLETIPILKAIFPVTDNTTGPQVHKMYTVTASPGVIGHPTAGWPPSSLTSSEPPDLSGSGDFSGDTDLEASGNLEGSGVEPMGFNESSTGPPTPVPNERSTCDNTEFGCCSDGKTPSVDGEGSNCPPTKLFQGVLIVEEVEGQELFYTPEMDDPKSELFGETARSIENALNELFGNSNVKKDFKSVRVHGLGPSDPVRIIVEVHFDPRTSYNSHDVQRALLQQVKQSRRKSIVVKKPEQDNVKIVDFDWAPLLFTTTSTTAARTTVPITTASALPVTRRPPPATTRWPKVLPHAKVPSTTTKPATTRRPPFSRKVEVRPATVKVHRPCDSQPCLHGGTCEDDGVSYTCSCPAGRGGAVCERTIVYFIPEFGGRSYLAFKTMKAYYTVRISMEFRASNLDGLPLVQWTEKGKGLHFYRPSEGYVELRFNHGVWDGVITSKTLIKPGNWHHVVGNRNRRSGMLSVDGEPHLIGESPPGTDGLNLDTDLFLGGTPEDEMTLVTERTTATKGLQGCIRLLDVNNLIYDLQERSNDVLYGSGVGECGNNPCSPNPCKNRGKCHMKEAEMFHCESVGEFSGPTCADKHNPCDPNPCHQSANCMVLPEGGSKCECPMGREGELCERVSEAEQDQGKAFIPEFNGLSYLEMNGIHTFVSDLLQKLSMEVIFLAKDPNGMIFYNGQKTDGRGDFVSLNLRDGYLEFKYDLGKGAAVLRSKAPIPLNVWNVVTVERNGRKGLMKINKDELVSGESPKSRKAPHTALNLKEAFYVGGAPDFNKFARAAGIISGFTGAIQKLSLKSIPLLKKENIRNAMEISNFRWHACTKTRNPCQNGGVCSPRLREYDCMCQRGFSGPQCEKALEEKSASGSESVAFNGRTFIEYHNTVTRSEKAVQVNYFEMSIKTEATKGLILWSGKIAEKSDYIALAVVDGFVQMTYDLGSKPVTLRSTIPVNTNQWVRIKANRIHGYGTLQVGNEAPVTGSSPFAATQLDTDGALWLGGIEKLAPGNRLPKAYSTGFIGCIKDVVIDRQELQLVEDALNNPTILHCPAKK
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Plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between motor neuron and skeletal muscle. Ligand of the MUSK signaling complex that induces the phosphorylation of MUSK, the kinase of the complex. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane (By similarity). Synaptic basal lamina at the neuromuscular junction.
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Q9BTD4
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MAGRSHPGPLRPLLPLLVVAACVLPGAGGTCPERALERREEEANVVLTGTVEEILNVDPVQHTYSCKVRVWRYLKGKDLVARESLLDGGNKVVISGFGDPLICDNQVSTGDTRIFFVNPAPPYLWPAHKNELMLNSSLMRITLRNLEEVEFCVEDKPGTHFTPVPPTPPDACRGMLCGFGAVCEPNAEGPGRASCVCKKSPCPSVVAPVCGSDASTYSNECELQRAQCSQQRRIRLLSRGPCGSRDPCSNVTCSFGSTCARSADGLTASCLCPATCRGAPEGTVCGSDGADYPGECQLLRRACARQENVFKKFDGPCDPCQGALPDPSRSCRVNPRTRRPEMLLRPESCPARQAPVCGDDGVTYENDCVMGRSGAARGLLLQKVRSGQCQGRDQCPEPCRFNAVCLSRRGRPRCSCDRVTCDGAYRPVCAQDGRTYDSDCWRQQAECRQQRAIPSKHQGPCDQAPSPCLGVQCAFGATCAVKNGQAACECLQACSSLYDPVCGSDGVTYGSACELEATACTLGREIQVARKGPCDRCGQCRFGALCEAETGRCVCPSECVALAQPVCGSDGHTYPSECMLHVHACTHQISLHVASAGPCETCGDAVCAFGAVCSAGQCVCPRCEHPPPGPVCGSDGVTYGSACELREAACLQQTQIEEARAGPCEQAECGSGGSGSGEDGDCEQELCRQRGGIWDEDSEDGPCVCDFSCQSVPGSPVCGSDGVTYSTECELKKARCESQRGLYVAAQGACRGPTFAPLPPVAPLHCAQTPYGCCQDNITAARGVGLAGCPSACQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNFRGIVTDGRSGCTPCSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDGRALGPAGCEADASAPATCAEMRCEFGARCVEESGSAHCVCPMLTCPEANATKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPCQEAVAPSTHPTSASVTVTTPGLLLSQALPAPPGALPLAPSSTAHSQTTPPPSSRPRTTASVPRTTVWPVLTVPPTAPSPAPSLVASAFGESGSTDGSSDEELSGDQEASGGGSGGLEPLEGSSVATPGPPVERASCYNSALGCCSDGKTPSLDAEGSNCPATKVFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGKSVRAIVDVHFDPTTAFRAPDVARALLRQIQVSRRRSLGVRRPLQEHVRFMDFDWFPAFITGATSGAIAAGATARATTASRLPSSAVTPRAPHPSHTSQPVAKTTAAPTTRRPPTTAPSRVPGRRPPAPQQPPKPCDSQPCFHGGTCQDWALGGGFTCSCPAGRGGAVCEKVLGAPVPAFEGRSFLAFPTLRAYHTLRLALEFRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGESPSGTDGLNLDTDLFVGGVPEDQAAVALERTFVGAGLRGCIRLLDVNNQRLELGIGPGAATRGSGVGECGDHPCLPNPCHGGAPCQNLEAGRFHCQCPPGRVGPTCADEKSPCQPNPCHGAAPCRVLPEGGAQCECPLGREGTFCQTASGQDGSGPFLADFNGFSHLELRGLHTFARDLGEKMALEVVFLARGPSGLLLYNGQKTDGKGDFVSLALRDRRLEFRYDLGKGAAVIRSREPVTLGAWTRVSLERNGRKGALRVGDGPRVLGESPKSRKVPHTVLNLKEPLYVGGAPDFSKLARAAAVSSGFDGAIQLVSLGGRQLLTPEHVLRQVDVTSFAGHPCTRASGHPCLNGASCVPREAAYVCLCPGGFSGPHCEKGLVEKSAGDVDTLAFDGRTFVEYLNAVTESELANEIPVPETLDSGALHSEKALQSNHFELSLRTEATQGLVLWSGKATERADYVALAIVDGHLQLSYNLGSQPVVLRSTVPVNTNRWLRVVAHREQREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPKAYGTGFVGCLRDVVVGRHPLHLLEDAVTKPELRPCPTP
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Heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This secreted isoform forms a bridge, after release from motor neurons, to basal lamina through binding laminin via the NtA domain. Transmembrane form that is the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases. Isoform 1, isoform 4 and isoform 5: neuron-specific (z+) isoforms that contain C-terminal insertions of 8-19 AA are potent activators of AChR clustering. Isoform 5, agrin (z+8), containing the 8-AA insert, forms a receptor complex in myotubules containing the neuronal AGRN, the muscle-specific kinase MUSK and LRP4, a member of the LDL receptor family. The splicing factors, NOVA1 and NOVA2, regulate AGRN splicing and production of the 'z' isoforms. Isoform 3 and isoform 6: lack any 'z' insert, are muscle-specific and may be involved in endothelial cell differentiation. Is involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity). This released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia. Monomer (By similarity). Interacts (N-terminal subunit) with TGF-beta family members, BMP2 AND BMP4; the interactions inhibit the activity of these growth factors. Interacts with TGFB1; the interaction enhances the activity of TGFB1 (By similarity). Component of the AGRN-LRP4 complex that consists of a tetramer of two AGRN-LRP4 heterodimers. Interacts (via the laminin G-like 3 domain) directly with LRP4; the interaction is required for activation of MUSK and clustering of AChR and requires the 'z8' insert present in the z(+8) isoforms. Interacts with DAG1; the interaction is influenced by cell surface glycosaminoglycans and by alternative splicing of AGRN. Synaptic basal lamina at the neuromuscular junction. Many isoforms may exist depending on the occurrence and length of inserts at the x, y or z splice site. Four 'z' isoforms can be produced with inserts of 0, 8, 11 or 19 AA. Isoforms differ in their acetylcholine receptor clustering activity and tissue specificity. Expressed in basement membranes of lung and kidney. Muscle- and neuron-specific isoforms are found. Isoforms (y+) with the 4 AA insert and (z+8) isoforms with the 8 AA insert are all neuron-specific. Isoforms (z+11) are found in both neuronal and non-neuronal tissues. The NtA domain, absent in TM-agrin, is required for binding laminin and connecting to basal lamina. Both laminin G-like 2 (G2) and laminin G-like 3 (G3) domains are required for alpha-dystroglycan/DAG1 binding. G3 domain is required for C-terminal heparin, heparan sulfate and sialic acid binding (By similarity). Contains heparan and chondroitin sulfate chains and alpha-dystroglycan as well as N-linked and O-linked oligosaccharides. Glycosaminoglycans (GAGs), present in the N-terminal 110 kDa fragment, are required for induction of filopodia in hippocampal neurons. The first cluster (Gly/Ser-rich) for GAG attachment contains heparan sulfate (HS) chains and the second cluster (Ser/Thr-rich), contains chondroitin sulfate (CS) chains. Heparin and heparin sulfate binding in the G3 domain is independent of calcium ions. Binds heparin with a stoichiometry of 2:1. Binds sialic acid with a stoichiometry of 1:1 and binding requires calcium ions (By similarity). At synaptic junctions, cleaved at two conserved sites, alpha and beta, by neurotrypsin. Cleavage at the alpha-site produces the agrin N-terminal 110-kDa subunit and the agrin C-terminal 110-kDa subunit. Further cleavage of agrin C-terminal 110-kDa subunit at the beta site produces the C-terminal fragments, agrin C-terminal 90 kDa fragment and agrin C-terminal 22 kDa fragment. Excessive cleavage at the beta-site releases large amounts of the agrin C-terminal 22 kDa fragment leading to destabilization at the neuromuscular junction (NMJ). The disease is caused by variants affecting the gene represented in this entry. Cleaved C-terminal fragments may be used as a biomarker for sarcopenia, age-related progressive loss of skeletal muscle. Produced by usage of an alternative first exon. The unknown residue 'x' in the transmembrane isoform is probably a proline residue by similarity to mouse and rat sequences. Leiden Open Variation Database (LOVD)
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B2RWU1
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MPPLPLEHRPRQQPGASVLVRYFMIPCNICLILLATSTLGFAVLLFLSNYKPGIHFTAAPSMPPDVCRGMLCGFGAVCEPSVEDPGRASCVCKKNVCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPCGSRDPCANVTCSFGSTCVPSADGQTASCLCPTTCFGAPDGTVCGSDGVDYPSECQLLRHACANQEHIFKKFDGPCDPCQGSMSDLNHICRVNPRTRHPEMLLRPENCPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQCQTRDQCPETCQFNSVCLSRRGRPHCSCDRVTCDGAYRPVCAQDGHTYDNDCWRQQAECRQQQTIPPKHQGPCDQTPSPCRGAQCAFGATCTVKNGKAVCECQRVCSGGYDPVCGSDGVTYGSVCELESMACTLGREIRVARRGPCDRCGQCRFGSLCEVETGRCVCPSECVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHCQTCGETVCTFGAVCSAGQCVCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEARAGPCEPAECGSGGSGSGEDNACEQELCRQHGGVWDEDSEDGPCVCDFSCQSVLKSPVCGSDGVTYSTECHLKKARCEARQELYVAAQGACRGPTLAPLLPMASPHCAQTPYGCCQDNVTAAQGVGLAGCPSTCHCNPHGSYSGTCDPVTGQCSCRPGVGGLRCDRCEPGFWNFRGIVTDGHSGCTPCSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDGQALGHLGCEADPTTPVTCVEMHCEFGASCVEEAGFAQCVCPTLTCPEANSTKVCGSDGVTYGNECQLKTIACRQRLDISIQSLGPCRESVAPGVSPTSASMTTPRHILSRTLASPHSSLPLSPSTTAHDWPTPLPTSPQTVVGTPRSTAATPSDVASLATAIFRESGSTNGSGDEELSGDEEASGGGSGGLEPPVGSVVVTHGPPIERASCYNSPLGCCSDGKTPSLDSEGSNCPATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSIRLRELGPGKLVRAIVDVHFDPTTAFQAPDVGQALLQQIQVSRPWALAVRRPLREHVRFLDFDWFPTFFTGAATGTTAAVATARATTVSRLSASSVTPRVYPSYTSRPVGRTTAPLTTRRPPTTTASIDRPRTPGPQRPPKSCDSQPCLHGGTCQDLDSGKGFSCSCTAGRAGTVCEKVQLPSVPAFKGHSFLAFPTLRAYHTLRLALEFRALETEGLLLYNGNARGKDFLALALLDGHVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGEAPVVGESPSGTDGLNLDTKLYVGGLPEEQVATVLDRTSVGIGLKGCIRMLDINNQQLELSDWQRAVVQSSGVGECGDHPCSPNPCHGGALCQALEAGVFLCQCPPGRFGPTCADEKNPCQPNPCHGSAPCHVLSRGGAKCACPLGRSGSFCETVLENAGSRPFLADFNGFSYLELKGLHTFERDLGEKMALEMVFLARGPSGLLLYNGQKTDGKGDFVSLALHNRHLEFRYDLGKGAAIIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVLGESPKSRKVPHTMLNLKEPLYVGGAPDFSKLARGAAVASGFDGAIQLVSLRGHQLLTQEHVLRAVDVAPFAGHPCTQAVDNPCLNGGSCIPREATYECLCPGGFSGLHCEKGIVEKSVGDLETLAFDGRTYIEYLNAVTESELTNEIPAPETLDSRALFSEKALQSNHFELSLRTEATQGLVLWIGKVGERADYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRVRAHREHREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLQKLPVGQALPKAYGTGFVGCLRDVVVGHRQLHLLEDAVTKPELRPCPTL
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Heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. This neuron-specific (z+) isoform is a component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This transmembrane agrin (TM-agrin) isoform, the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases. Isoform 2 and isoform 3: these isoforms lacking the 'z' insert (z0) are muscle-specific, have no AChR clustering ability and may be involved in nervous system endothelial cell differentiation. Involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity). This released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia. Monomer (By similarity). Interacts (N-terminal subunit) with TGF-beta family members, BMP2 AND BMP4; the interactions inhibit the activity of these growth factors. Interacts with TGFB1; the interaction enhances the activity of TGFB1. Interacts with DAG1; the interaction is influenced by cell surface glycosaminoglycans and by alternative splicing of AGRN (By similarity). Component of the AGRN-LRP4 complex that consists of a tetramer of two AGRN-LRP4 heterodimers. Interacts (via the laminin G-like 3 domain) directly with LRP4; the interaction is required for activation of MUSK and clustering of AChR and requires the 'z8' insert present in the z(+8) isoforms. Many isoforms exist depending on the occurrence and length of inserts at the x, y or z splice site. There are 4 'z' isoforms produced with inserts of 0, 8, 11 or 19 AA. Isoforms differ in their acetylcholine receptor clustering activity and tissue specificity. In addition, a secreted isoform is produced by alternative usage of the first exon. Expressed in central nervous system (CNS) synapses such as in the cerebral cortex and hippocampus. Localizes to basal lamina of hippocampal blood vessels. Both (z+) and (z-) isoforms found in kidney, heart and cerebral vasculature. All (z+), (z-), (y+) and (y-) isoforms present throughout muscle fiber basal laminae in neonatal animals. Both laminin G-like 2 (G2) and laminin G-like 3 (G3) domains are required for alpha-dystroglycan binding. G3 domain is required for C-terminal heparin, heparan sulfate and sialic acid binding (By similarity). Contains heparan and chondroitin sulfate chains and alpha-dystroglycan as well as N-linked and O-linked oligosaccharides. Heparin and heparin sulfate binding in the G3 domain is independent of calcium ions. Binds heparin with a stoichiometry of 2:1. Binds sialic acid with a stoichiometry of 1:1 and binding requires calcium ions (By similarity). Glycosaminoglycans (GAGs), present in the N-terminal 110 kDa fragment, are required for induction of filopodia in hippocampal neurons. The first cluster (Gly/Ser-rich) for GAG attachment contains heparan sulfate (HS) chains and the second cluster (Ser/Thr-rich), contains chondroitin sulfate (CS) chains. At synaptic junctions, cleaved at two conserved sites, alpha and beta, by neurotrypsin. Cleavage at the alpha-site produces the agrin N-terminal 110-kDa subunit and the agrin C-terminal 110-kDa subunit. Further cleavage of agrin C-terminal 110-kDa subunit at the beta site produces the C-terminal fragments, agrin C-terminal 90 kDa fragment and agrin C-terminal 22 kDa fragment. Excessive cleavage at the beta-site releases large amounts of the agrin C-terminal 22 kDa fragment leading to destabilization at the neuromuscular junction (NMJ). Cleavage is developmentally regulated. In developing brain, neurotrypsin-mediated cleavage occurs mainly during late fetal days and in the first postnatal week. Z(-)/z(-) mice lacking the 'z' insert are stillborn or die immediately after birth. They did not inflate their lungs and were never seen to move spontaneously. An intramuscular nerve is formed and axons leave the nerve and branch but do not stop and arborize. AChR clusters were fewer in number, about 30% smaller in size and lower in density. Transgenic null (Tg/Agrn -/-) mice, exhibit atrophied muscle due to denervation and are smaller than normal littermates. There is impairment of locomotory behavior and half the mice die after 50 days. There is a greatly reduced number of synapses and about 30% loss of postsynaptic spines and a decrease in the length of dendrites in cortical neurons. Mice that have excessive neurotrypsin-mediated agrin cleavage, exhibit pathological symptoms characteristic of precocious sarcopenia, with fragmentation and disassembly of the neuromuscular junction (NMJ).
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Q63034
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MPPLPLEHRPRQEPGASMLVRYFMIPCNICLILLATSTLGFAVLLFLSNYKPGIHFTPAPPTPPDVCRGMLCGFGAVCEPSVEDPGRASCVCKKNACPATVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPCGSRDPCANVTCSFGSTCVPSADGQTASCLCPTTCFGAPDGTVCGSDGVDYPSECQLLSHACASQEHIFKKFNGPCDPCQGSMSDLNHICRVNPRTRHPEMLLRPENCPAQHTPICGDDGVTYENDCVMSRIGATRGLLLQKVRSGQCQTRDQCPETCQFNSVCLSRRGRPHCSCDRVTCDGSYRPVCAQDGHTYNNDCWRQQAECRQQRAIPPKHQGPCDQTPSPCHGVQCAFGAVCTVKNGKAECECQRVCSGIYDPVCGSDGVTYGSVCELESMACTLGREIQVARRGPCDPCGQCRFGSLCEVETGRCVCPSECVESAQPVCGSDGHTYASECELHVHACTHQISLYVASAGHCQTCGEKVCTFGAVCSAGQCVCPRCEHPPPGPVCGSDGVTYLSACELREAACQQQVQIEEAHAGPCEPAECGSGGSGSGEDDECEQELCRQRGGIWDEDSEDGPCVCDFSCQSVPRSPVCGSDGVTYGTECDLKKARCESQQELYVAAQGACRGPTLAPLLPVAFPHCAQTPYGCCQDNFTAAQGVGLAGCPSTCHCNPHGSYSGTCDPATGQCSCRPGVGGLRCDRCEPGFWNFRGIVTDGHSGCTPCSCDPRGAVRDDCEQMTGLCSCRPGVAGPKCGQCPDGQVLGHLGCEADPMTPVTCVEIHCEFGASCVEKAGFAQCICPTLTCPEANSTKVCGSDGVTYGNECQLKAIACRQRLDISTQSLGPCQESVTPGASPTSASMTTPRHILSKTLPFPHNSLPLSPGSTTHDWPTPLPISPHTTVSIPRSTAWPVLTVPPTAAASDVTSLATSIFSESGSANGSGDEELSGDEEASGGGSGGLEPPVGSIVVTHGPPIERASCYNSPLGCCSDGKTPSLDSEGSNCPATKAFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFWSVRLRELGPGKLVRAIVDVHFDPTTAFQASDVGQALLRQIQVSRPWALAVRRPLQEHVRFLDFDWFPTFFTGAATGTTAAMATARATTVSRLPASSVTPRVYPSHTSRPVGRTTAPPTTRRPPTTATNMDRPRTPGHQQPSKSCDSQPCLHGGTCQDQDSGKGFTCSCTAGRGGSVCEKVQPPSMPAFKGHSFLAFPTLRAYHTLRLALEFRALETEGLLLYNGNARGKDFLALALLDGRVQFRFDTGSGPAVLTSLVPVEPGRWHRLELSRHWRQGTLSVDGETPVVGESPSGTDGLNLDTNLYVGGIPEEQVAMVLDRTSVGVGLKGCIRMLDINNQQLELSDWQRAAVQSSGVGECGDHPCLPNPCHGGALCQALEAGMFLCQCPPGRFGPTCADEKSPCQPNPCHGAAPCRVLSSGGAKCECPLGRSGTFCQTVLETAGSRPFLADFNGFSYLELKGLHTFERDLGEKMALEMVFLARGPSGLLLYNGQKTDGKGDFVSLALHNRHLEFCYDLGKGAAVIRSKEPIALGTWVRVFLERNGRKGALQVGDGPRVLGESPKSRKVPHTMLNLKEPLYIGGAPDFSKLARGAAVSSGFSGVIQLVSLRGHQLLTQEHVLRAVDVSPFADHPCTQALGNPCLNGGSCVPREATYECLCPGGFSGLHCEKGLVEKSVGDLETLAFDGRTYIEYLNAVIESELTNEIPAPETLDSRALFSEKALQSNHFELSLRTEATQGLVLWIGKAAERADYMALAIVDGHLQLSYDLGSQPVVLRSTVKVNTNRWLRIRAHREHREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLQKLPVGQALPKAYGTGFVGCLRDVVVGHRQLHLLEDAVTKPELRPCPTP
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Heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. This neuron-specific (z+) isoform is a component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This transmembrane agrin (TM-agrin) isoform, the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases. Isoform 1, isoform 4, isoform 5 and isoform 6: neuron-specific (z+) isoforms that contain C-terminal insertions of 8-19 AA are potent activators of AChR clustering. Isoform 5, agrin (z+8), containing the 8-AA insert, forms a receptor complex in myotubules containing the neuronal AGRN, the muscle-specific kinase MUSK and LRP4, a member of the LDL receptor family. The splicing factors, NOVA1 and NOVA2, regulate AGRN splicing and production of the 'z' isoforms. Is involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity). This released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia. Monomer. Component of the AGRN-LRP4 complex that consists of a tetramer of two AGRN-LRP4 heterodimers. Interacts (via the laminin G-like 3 domain) directly with LRP4; the interaction is required for activation of MUSK and clustering of AChR and requires the 'z8' insert present in the z(+8) isoforms. Interacts (N-terminal subunit) with TGF-beta family members, BMP2 AND BMP4; the interactions inhibit the activity of these growth factors. Interacts with TGFB1; the interaction enhances the activity of TGFB1. Interacts with DAG1; the interaction is influenced by cell surface glycosaminoglycans and by alternative splicing of AGRN. Many isoforms exist depending on the occurrence and length of inserts at the x, y or z splice site. There are 4 'z' isoforms produced with inserts of 0, 8, 11 or 19 AA. Isoforms differ in their acetylcholine receptor clustering activity and tissue specificity. In addition, a secreted isoform may be produced by alternative usage of the first exon. Embryonic nervous system and muscle. More abundant early in development. At E13, highly expressed in the developing nervous system. Isoform y(+4)z(0), containing the 'y' insert but no 'z' insert, is the most prevelant at this stage with pronounced expression in developing spinal and sympathetic ganglia. Isoforms with no 'y' insert (y0) localized to peripheral tissue. At E15, y(+4) isoform continues to be highly expressed in neural tissue predominantly in the spinal column and developing brain. The y(0) isoform is weakly expressed in capillaries and meninges and the y(0)(z0) in non-neural tissues, predominantly in epithelial cells lining the developing lung bronchioles and kidney tubules. Isoforms Z(+8) and z(+19) are highly expressed in ventral motor columns and facial nerve with weaker expression throughout spinal cord tissue. At later stages of development, isoform y(4)z(0) is the most prominent form in developing cortex, corpus striatum, hippocampus and cerebellum. Isoform y(0)z(0) expression is still detected in brain capillaries at stage P1. The z(+19) isoform is most highly expressed from E15 to E18 and declines slightly to P1. Isoforms y(1)4z(0) and y(+4)z(+8) are still expressed in adulthood, the former scattered throughout the spinal cord gray matter and, the latter, in motor neurons of the ventral spinal cord. Both laminin G-like 2 (G2) and laminin G-like 3 (G3) domains are required for alpha-dystroglycan binding. G3 domain is required for C-terminal heparin, heparan sulfate and sialic acid binding. Contains heparan and chondroitin sulfate chains and alpha-dystroglycan as well as N-linked and O-linked oligosaccharides. Glycosaminoglycans (GAGs), present in the agrin N-terminal 110 kDa fragment, are required for induction of filopodia in hippocampal neurons. The first cluster (Gly/Ser-rich) for GAG attachment contains heparan sulfate (HS) chains and the second cluster (Ser/Thr-rich), contains chondroitin sulfate (CS) chains. Heparin and heparin sulfate binding in the G3 doamin is independent of calcium ions. Binds heparin with a stoichiometry of 2:1. Binds sialic acid with a stoichiometry of 1:1 and binding requires calcium ions. At synaptic junctions, cleaved at two conserved sites, alpha and beta, by neurotrypsin. Cleavage at the alpha-site produces the agrin N-terminal 110-kDa subunit and the agrin C-terminal 110-kDa subunit. Further cleavage of agrin C-terminal 110-kDa subunit at the beta site produces the C-terminal fragments, agrin C-terminal 90 kDa fragment and agrin C-terminal 22 kDa fragment. Excessive cleavage at the beta-site releases large amounts of the agrin C-terminal 22 kDa fragment leading to destabilization at the neuromuscular junction (NMJ).
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O97830
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MARLAAVLWSLCVTAILVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYKVKQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYVDDDSEAAGNRVDYAFNTNANREEPVSLAFPNPYQFVSSVDYNPRDNQLYVWNNYFVVRYSLEFGPPDPSAGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPAPSTRRPPAPNLHVSPELFCEPREVRRVQWPATQQGMLVERPCPKGTRGIASFQCLPALGLWNPRGPDLSNCTSPWVNQVAQKIKSGENAANIASELARHTRGSIYAGDVSSSVKLMEQLLDILDAQLQALRPIERESAGKNYNKMHKRERTCKDYIKAVVETVDNLLRPEALESWKDMNATEQAHTATMLLDVLEEGAFLLADNVREPARFLAAKQNVVLEVTVLNTEGQVQELVFPQEYPSENSIQLSANTIKQNSRNGVVKVVFILYNNLGLFLSTENATVKLAGEAGSGGPGGASLVVNSQVIAASINKESSRVFLMDPVIFTVAHLEAKNHFNANCSFWNYSERSMLGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREIYQGRINELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHKMVRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRHSYCCIRSPPGGAHGSLKTSAMRSNARYYTGTQSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQPRGGTSPYNTLIAESVGFNPSSPPVFNSPGSYREPKHPLGGREACGMDTLPLNGNFNNSYSLRSGDFPPGDGAPEPPRGRNLADAAAFEKMIISELVHNNLRGGSSGAKGPPPPEPPVPPVPGGSGEEEAGGPGADRAEIELLYKALEEPLLLPRAQSVLYQSDLDESESCTAEDGATSRPLSSPPGRDSLYASGANLRDSPSYPDSSPEGPSEALPPPPPAPPGPPEIYYTSRPPALVARNPLQGYYQVRRPSHEGYLAAPGLEGPGPDGDGQMQLVTSL
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Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Receptor probably implicated in the regulation of exocytosis (By similarity). Forms a heterodimer, consisting of a large extracellular region (p120) non-covalently linked to a seven-transmembrane moiety (p85). Interacts with syntaxin and with proteins of the SHANK family via the PDZ domain. Interacts (via extracellular domain) with FLRT1, FLRT2 and FLRT3 (via extracellular domain) (By similarity). Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts. Brain-specific expression but low levels are also detected in kidney, lung and spleen. The extracellular domain coupled to the a single transmembrane region are sufficient for full responsiveness to alpha-latrotoxin. Autoproteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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Q9HAR3
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MARLAAVLWNLCVTAVLVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYKVEQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYVDDDSEAAGNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPRDNQLYVWNNYFVVRYSLEFGPPDPSAGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPVPSTRRPPAPNLHVSPELFCEPREVRRVQWPATQQGMLVERPCPKGTRGIASFQCLPALGLWNPRGPDLSNCTSPWVNQVAQKIKSGENAANIASELARHTRGSIYAGDVSSSVKLMEQLLDILDAQLQALRPIERESAGKNYNKMHKRERTCKDYIKAVVETVDNLLRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKENVVLEVTVLNTEGQVQELVFPQEEYPRKNSIQLSAKTIKQNSRNGVVKVVFILYNNLGLFLSTENATVKLAGEAGPGGPGGASLVVNSQVIAASINKESSRVFLMDPVIFTVAHLEDKNHFNANCSFWNYSERSMLGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREIYQGRINELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRHSYCCIRSPPGGTHGSLKTSAMRSNTRYYTGTQSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQPRGGTSPYNTLIAESVGFNPSSPPVFNSPGSYREPKHPLGGREACGMDTLPLNGNFNNSYSLRSGDFPPGDGGPEPPRGRNLADAAAFEKMIISELVHNNLRGSSSAAKGPPPPEPPVPPVPGGGGEEEAGGPGGADRAEIELLYKALEEPLLLPRAQSVLYQSDLDESESCTAEDGATSRPLSSPPGRDSLYASGANLRDSPSYPDSSPEGPSEALPPPPPAPPGPPEIYYTSRPPALVARNPLQGYYQVRRPSHEGYLAAPGLEGPGPDGDGQMQLVTSL
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Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Receptor probably implicated in the regulation of exocytosis (By similarity). Forms a heterodimer, consisting of a large extracellular region (p120) non-covalently linked to a seven-transmembrane moiety (p85). Interacts with syntaxin and with proteins of the SHANK family via the PDZ domain. Interacts (via extracellular domain) with FLRT1, FLRT2 and FLRT3 (via extracellular domain) (By similarity). Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts. The extracellular domain coupled to the a single transmembrane region are sufficient for full responsiveness to alpha-latrotoxin. Autoproteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus (By similarity). Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily. Extended N-terminus.
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Q80T49
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MARLAAALWSLCVTTVLVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYIFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYVDDDSEAAGNRVDYAFNTNANREEPVSLAFPNPYQFVSSVDYNPRDNQLYVWNNYFVVRYSLEFGPPDPSAGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPAPSTRRPPAPNLHVSPELFCEPREVRRVQWPATQQGMLVERPCPKGTRGIASFQCLPALGLWNPRGPDLSNCTSPWVNQVAQKIKSGENAANIASELARHTRGSIYAGDVSSSVKLMEQLLDILDAQLQALRPIERESAGKNYNKMHKRERTCKDYIKAVVETVDNLLRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKQNVVLEVTVLNTEGQVQELVFPQEYPSENSIQLSANTIKQNSRNGVVKVVFILYNNLGLFLSTENATVKLAGEAGTGGPGGASLVVNSQVIAASINKESSRVFLMDPVIFTVAHLEAKNHFNANCSFWNYSERSMLGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREIYQGRINELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEVACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRHSYCCIRSPPGGTHGSLKTSAMRSNTRYYTGTQSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQPRGGTSPYNTLIAESVGFNPSSPPVFNSPGSYREPKHPLGGREACGMDTLPLNGNFNNSYSLRSGDFPPGDGGPEPPRGRNLADAAAFEKMIISELVHNNLRGASGGAKGPPPEPPVPPVPGVSEDEAGGPGSADRAEIELLYKALEEPLLLPRAQSVLYQSDLDESESCTAEDGATSRPLSSPPGRDSLYASGANLRDSPSYPDSSPEGPNEALPPPPPAPPGPPEIYYTSRPPALVARNPLQGYYQVRRPSHEGYLAAPSLEGPGPDGDGQMQLVTSL
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Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Receptor probably implicated in the regulation of exocytosis (By similarity). Forms a heterodimer, consisting of a large extracellular region (p120) non-covalently linked to a seven-transmembrane moiety (p85). Interacts with syntaxin and with proteins of the SHANK family via the PDZ domain (By similarity). Interacts (via extracellular domain) with FLRT1, FLRT2 and FLRT3 (via extracellular domain) (PubMed:22405201). Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts. The extracellular domain coupled to the a single transmembrane region are sufficient for full responsiveness to alpha-latrotoxin. Autoproteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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O88916
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MARLAAALWSLCVTTVLVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYKVEQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYVDDDSEAAGNRVDYAFNTNANREEPVSLAFPNPYQFVSSVDYNPRDNQLYVWNNYFVVRYSLEFGPPDPSAGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPAPSTRRPPAPNLHVSPELFCEPREVRRVQWPATQQGMLVERPCPKGTRGIASFQCLPALGLWNPRGPDLSNCTSPWVNQVAQKIKSGENAANIASELARHTRGSIYAGDVSSSVKLMEQLLDILDAQLQALRPIERESAGKNYNKMHKRERTCKDYIKAVVETVDNLLRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKQNVVLEVTVLSTEGQVQELVFPQEYASESSIQLSANTIKQNSRNGVVKVVFILYNNLGLFLSTENATVKLAGEAGTGGPGGASLVVNSQVIAASINKESSRVFLMDPVIFTVAHLEAKNHFNANCSFWNYSERSMLGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREIYQGRINELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEVACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRHSYCCIRSPPGGAHGSLKTSAMRSNTRYYTGTQVPGQGRHIHQVSLGPRGRSALPESQKDPGGQSGPGDPLTFGLCPSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQPRGGTSPYNTLIAESVGFNPSSPPVFNSPGSYREPKHPLGGREACGMDTLPLNGNFNNSYSLRSGDFPPGDGGPEPPRGRNLADAAAFEKMIISELVHNNLRGASGGAKGPPPEPPVPPVPGVSEDEAGGPGGADRAEIELLYKALEEPLLLPRAQSVLYQSDLDESESCTAEDGATSRPLSSPPGRDSLYASGANLRDSPSYPDSSPEGPNEALPPPPPAPPGPPEIYYTSRPPALVARNPLQGYYQVRRPSHEGYLAAPSLEGPGPDGDGQMQLVTSL
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Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor probably implicated in the regulation of exocytosis. Receptor for TENM2 that mediates heterophilic synaptic cell-cell contact and postsynaptic specialization. Forms a heterodimer, consisting of a large extracellular region (p120) non-covalently linked to a seven-transmembrane moiety (p85). Interacts with syntaxin and with proteins of the SHANK family via the PDZ domain (PubMed:9208860, PubMed:10958799). Isoform 2 interacts with TENM2 (PubMed:21724987). Interacts (via extracellular domain) with FLRT1, FLRT2 and FLRT3 (via extracellular domain) (By similarity). Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts. Expressed in the brain (at protein level). Brain specific distribution but low levels are also detected in most tissues. The extracellular domain coupled to the a single transmembrane region are sufficient for full responsiveness to alpha-latrotoxin. Autoproteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily.
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Q9LXA3
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MMAPMTNWLTFSLSPMEMLRSSDQSQFVSYDASSAASSSPYLLDNFYGWSNQKPQEFFKEEAQLAAAASMADSTILTTFVDPQSHHSQNHIPKLEDFLGDSSSIVRYSDNSQTDTQDSSLTQIYDPRHHHNQTGFYSDHHDFKTMAGFQSAFSTNSGSEVDDSASIGRTHLAGDYLGHVVESSGPELGFHGGSTGALSLGVNVNNNTNHRNDNDNHYRGNNNGERINNNNNNDNEKTDSEKEKAVVAVETSDCSNKKIADTFGQRTSIYRGVTRHRWTGRYEAHLWDNSCRREGQARKGRQGGYDKEDKAARAYDLAALKYWNATATTNFPITNYSKEVEEMKHMTKQEFIASLRRKSSGFSRGASIYRGVTRHHQQGRWQARIGRVAGNKDLYLGTFATEEEAAEAYDIAAIKFRGINAVTNFEMNRYDVEAIMKSALPIGGAAKRLKLSLEAAASSEQKPILGHHQLHHFQQQQQQQQLQLQSSPNHSSINFALCPNSAVQSQQIIPCGIPFEAAALYHHHQQQQQHQQQQQQQNFFQHFPANAASDSTGSNNNSNVQGTMGLMAPNPAEFFLWPNQSY
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Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways. Expressed in roots, seedlings, hypocotyl, inflorescence, siliques, and pistils. Also detected at low levels in leaves. Detected in inflorescence and youg floral mersitems, and in stem procambial cells. In floral mersitems, mostly expressed in the central dome. Disappears progressively from sepal primordia, but accumulates in second, third and fourth whorl organ primordia. Later, confined to occasional patches in stamens and in petal before disparearing progressively from flowers. Belongs to the AP2/ERF transcription factor family. AP2 subfamily.
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Q9LSM4
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MAPPMTNCLTFSLSPMEMLKSTDQSHFSSSYDDSSTPYLIDNFYAFKEEAEIEAAAASMADSTTLSTFFDHSQTQIPKLEDFLGDSFVRYSDNQTETQDSSSLTPFYDPRHRTVAEGVTGFFSDHHQPDFKTINSGPEIFDDSTTSNIGGTHLSSHVVESSTTAKLGFNGDCTTTGGVLSLGVNNTSDQPLSCNNGERGGNSNKKKTVSKKETSDDSKKKIVETLGQRTSIYRGVTRHRWTGRYEAHLWDNSCRREGQARKGRQVYLGGYDKEDRAARAYDLAALKYWGSTATTNFPVSSYSKELEEMNHMTKQEFIASLRRKSSGFSRGASIYRGVTRHHQQGRWQARIGRVAGNKDLYLGTFATEEEAAEAYDIAAIKFRGINAVTNFEMNRYDIEAVMNSSLPVGGAAAKRHKLKLALESPSSSSSDHNLQQQQLLPSSSPSDQNPNSIPCGIPFEPSVLYYHQNFFQHYPLVSDSTIQAPMNQAEFFLWPNQSY
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Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways. Interacts with HDG2, and possibly with HDG3, HDG7, ANL2, ATML1 and PDF2. Expressed in roots, seedlings, inflorescence, and siliques. Also detected at low levels in leaves. Confined to the central region of inflorescence ane floral meristems, progressively restricted to the innermost cells of the dome. Also detected in developing stamen locules and later in sporogonous cells within locules. In carpel primordia, found in placenta and in young ovule primordia. Belongs to the AP2/ERF transcription factor family. AP2 subfamily.
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Q9FCY3
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MKKTLLASSLIACLSIASVNVYAASESSISIGYAQSHVKENGYTLDNDPKGFNLKYRYELDDNWGVIGSFAYTHQGYDFFYGSNKFGHGDVDYYSVTMGPSFRINEYVSLYGLLGAAHGKVKASVFDESISASKTSMAYGAGVQFNPLPNFVIDASYEYSKLDSIKVGTWMLGAGYRF
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Promotes the invasion of pathogenic bacteria into eukaryotic cells by an unknown mechanism. Belongs to the outer membrane OOP (TC 1.B.6) superfamily. Ail family.
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Q667X3
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MVFMNKTLLVSSLIACLSIASVNVYAEGESSISIGYAQSRVKEDGYKLDKNPRGFNLKYRYEFNNDWGVIGSFAQTRRGFEESVDGFKLIDGDFKYYSVTAGPVFRINEYVSLYGLLGAGHGKAKVSSIFGQSESRSKTSLAYGAGLQFNPHPNFVIDASYEYSKLDDVKVGTWMLGAGYRF
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Promotes the invasion of pathogenic bacteria into eukaryotic cells by an unknown mechanism. Belongs to the outer membrane OOP (TC 1.B.6) superfamily. Ail family.
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Q75D07
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MSLAIIPFITIGWLRCTRKSRDTMSSSPEPQAPMHVTQRQISVFSDEFRQRRRQQMLRFFGATAFTLLSARLAFRGTINRKYVPNMFQLNHRVPLASSQGEALHAFAYGSGLATGGFAMLILGTCWLADVSTVPEFSLRIKALLGESDTQSGRLESAHQDKETRELAAMLDSLLQEKKD
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Belongs to the AIM11 family.
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A0A1D8PJ55
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MSDLLHKLNFKIADASPEYKQRRKIQMIRFFTASAVTIFASRFAYRATVSRQYIPTLFQGNHSPPLSYNFTTDAAVAVGTGTLLCGSVTGMTVFGLCWILDVSNIKEFGWRMKSMLGGWESEKKLSEAPMDEESSYIQDSLNDILDGKYDFENDTEEVAGELKTN
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Belongs to the AIM11 family.
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C4YPM0
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MSDLLHKLNFKIADASPEYKQRRKIQMIRFFTASAVTIFASRFAYRATVSRQYIPTLFQGNHSPPLSYNFTTDAAVAVGTGTLLCGSVTGMTVFGLCWILDVSNIKEFGWRMKSMLGGWESEKKLSEAPMDEESSYIQDSLNDILDGKYDFENDTEEVAGELKTN
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Belongs to the AIM11 family.
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B9WD58
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MTDLLHKLNFKIADASPEYKQRRKIQMIRFFTASAVTIFASRFAYRATVSRQYIPTLFQGNHSPPLSYNFTTDAAVAVGTGTLLCGSVTGMTVFGLCWILDVSNIQEFGWRMKSMLGGWESEKKLSEAPMDEESSYIQDSLNDILDGKYDFEEDTEEVHTAEMKTK
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Belongs to the AIM11 family.
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Q6FQN0
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MTVPEIISDGKSTRRNLQKLLFFGATSATLAIAALTSRSIATRKYIPTFFQLNTKIPTFSSKSEAQAALGLSSGLSLGIFAITTTGFCWALDISSASDFKQRMKTLFNTIDEKEYMNDSDPETNKIIEELEALINKK
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Belongs to the AIM11 family.
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C5M8B9
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MSTFLQSFKISQASDEYKQRRKTQMLKFFTASAITILTSRFAYRSTIARQYVPTLFQGNHSPPLSYNFTTDAAVAVATGTILCGSVSSMLVLGGFWILDVSNLGEFGWRMKEKLGGLEKEKHLGEMEMDEESRYIQDSLNDLLDGKYDFEEEGGNNSVA
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Belongs to the AIM11 family.
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C4XZH2
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MDLLRQYNFKIADASPEYLERRKKQAVLFMTAAAVTIFTSRFAYKSTITRQYIPTLFQGNHSPPLGYNFTSDAAVAVGTGTMLCASVSSMICFGTCWVLDVSTFREFGWKMKSLMGGTQKEQELADMPMDEDSAYIQDGLNDILDGKVELNFDDE
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Belongs to the AIM11 family.
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Q6BYM1
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MSAEPSQFNKLLTKYDFKLASASEEYRNRRKRQMMLFMGSAAITIFTSRLAYKSTITRQYVPSLFQGNHAPPLSYNFTSDAAVAVGTGTLLCGSVSSMVIFGTCWIIDVSNFQEFGWKMKSLMGGYEKQKELAKLPMDEESAFLQDSLNDILDGKYDFDETTPAEK
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Belongs to the AIM11 family.
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Q6CMH6
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MSEVASVTDAQIEKFSLLYKERRKVQMMRFFGVTALTLISARLAFKGVASRKYIPTMFQLNHKPPPFSYKGEVVNALAYGTALSTGGFAMLGFGLCWIWDVSTLKELGNKLKELMGDGSEKDKLVSTNMDLDEDTQKVADALEAMLSTKK
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Belongs to the AIM11 family.
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C4R7Q4
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MRILLIFFVPSGILDQLFPRISILSTLRVNLTNSPLLTPNLTLYSMVNGFDFSKMFGRKDPELVSKEVKQYNERRFKQMALFYGFTVATFICSKIAYRGVIKRRYVPNYYQHNHVAPPFSFYRDALSAVFHSTSLAITSLGMASTGVLWYYDISSVAEFSFKLKQALGGHDKEQELKKLPEDETVQEIQNSINSYLGDR
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Belongs to the AIM11 family.
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C5DE77
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MASVQLSSRDISVFSNEYKERRRLQMMRFFGATAFTLISARLAFRGVQSRKYVPNMFQLNHKPPTYSFQGEAVSALAFGTGLATGTFSMLVFGTCWVWDISSLAEFTLKMKKLMGEPVTDQALLENTPMDEDTRKVAEALEDMLKGSRKD
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Belongs to the AIM11 family.
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A5E5Y6
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MTSTTRDVLHKLNFSIADASPEYIDRRKLQMAKFFTFAALSIFSTRFIYKQTIARQYVPLLFQQNHQPPTSYNFTADAMVAVGAGTLACGSISGMLMFGTAWILDVSNLKEFGYRMKALMGGDVKEKELSEMKMDDETRALQDGLNDLLEGKI
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Belongs to the AIM11 family.
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A5DJS9
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MSFTNLLEKYDFKLASASEEYKQRRKYQMALFMASGAATIFAARFAFKSTMARQYVPTLFQGNHQPPTSYNFTTDAAVAVGTGTVLCGSVSSMIIFGTCWMMDVSTFKEFGWRMKTVMGGYEKQKQLAQMPLDEESEIIQNGLNDILEGKYDDIE
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Belongs to the AIM11 family.
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A3LP48
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MSVEAASNSSDQSGLKPFLAKYNFKLGEASDEYIARRKRQMVLFMSSAALTIFASRFAYKSTISRQYIPTLFQGNHAPPLSYNFATDAAVAVGTGTLLCGSVSSMVIFGSCWILDVSNFKEFGWKMKSMMGGYEKERELSKLPMDEESAYIQDGLNDILEGKYDFDEDGTEEGK
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Belongs to the AIM11 family.
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A7TQD5
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MVDVVSEGIPVQDVEEFTEKYKNRRKQQMMRFIGSTAVTLISCRLAITRAKARHYVPNMFQLNYKPPVVTYKGETGPALVLATGITVGTLSMLVSGSCWIWDISTMKEFREIKGFSSEKVEHPRLANMPLESDSMRNVYERLELLNGKK
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Belongs to the AIM11 family.
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Q6C0R5
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MKFRFGEGAEGTLNTSVTTAMIDQEKRAADLKRRKNQMLLFGGATLATLASCRLTARGISSRRYIPKMFQANHMPPQSDMVKEAAMAVVFATTMALSSFSMVVFGVAWSQDVTSLKQFALKMKTKLGAQQIEDEIRNAPMTPETQDLQDQLAGALKKD
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Belongs to the AIM11 family.
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D6VW54
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MLKVPLSDVLSQKMLFLKSFRYFHCTKYFSRDNASSTTDIFRNAMKRKRELANLKEQSHGNVARNAAFPKEYIKRPKQVPRNATNRKKILITWSTGTDRAKEAANSVVSEIFKKNHKGNIKVVDPTTHRIEASNIRYFAKGIDLDKVGLSIVNVEQIDNENQIPLVKIVESRVALKKYSDFLAKKKEKELMELGVLNKSYKNLVTDKKEDNLKHIKISWQIESDDLKRQKAHEIVSLLKKGNKVTLYLDDKNNINSNNWLENFEELDRSQKGEPPRLPESVFQKRAAVLETLKEIVSEYANDPVLLGNMNSKMIMKLIPKDVKPQNNDKRALKELRKKERQEKLQKRIQRKKMNEM
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Increases frequency of mitochondrial genome loss. Present with 319 molecules/cell in log phase SD medium. Belongs to the AIM23 family.
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C5DV23
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MLRLQLGKRIVRNAFSVVVIRGFCSSGPCRKDWMANNDILLNATAAMKRNKEKVQRGSLDSAHTNGSFRQVNMNQRSNHNKKPLKKPRSIVIKWSTGSDRAKEAANSTVSSIFKMNFEGTVQRINSETNKVEETNIREFVKGINLDEVGLSIVDVSQINENTSIPLVKLVEARVALKRYSDEMAKQKEKELIEMGVIKKSTKSSEPDKVESTVKRLKISWEIKPDDLCKQKAHEIVTQLKKGFKVFVYIDSKNSSGSRNWLDCFENSIPQEIKLSKREHEQRSFVVDKISEIVEEYSIQPNLDGTLGDKMIIKLAPKTLTGEKMDKKTLKEHKKKERQEKLQKRIEKKNQRGTGL
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Belongs to the AIM23 family.
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C5GW39
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MEAMSHSIRRSLQPFARSRRSWRSPARRAEQRWIHIQQLQSAEPGLVNGNYLPASTTANSASSPDAKFQVLGAPYSLLSVTLSASQNLYTRRGTLVGLSGKADNVISTLSLLEPARRALLRIPFLYQKISSTSPITALISTRSAITTFSVVEMNGSVDWMIAQEKALLAWTGHSLRIKPRLTRQLSLSHWGNSEVTGRGLLALVGTGQLYSVELKAGEQYISHPSNVVAYTITAPSPRPYRFKSTILPFQIPSLGIGKRLSDSNFIKNLSDTDTWKAALKLWHIIRTWSRRTIWGDRLFLQFDGPATILVQSRASRMADTLTTQQVNEIADAPPGVTQDAVDRAAAKLGEEETVPKAKDDLKPTTAISGQSVASVRRDGKVEFHQTGVGQ
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Belongs to the AIM24 family.
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C5FL48
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MRRLIPGSGFRPSNRLRWSSRYGLRRNIHIQAIPSSQLNSVTNESFHSASTTTNSAISPDAKFEVVGSPYSLLSVSLSASQNLYTRRGTLVGLSGKPENVVSTLRILEPFRRAALGIPFLYQKISSTSPVSALVSVKSPVTSFALLQLNGTVDWMLAQRNALLAWTGHSLTIKPRFNKQLSISHWGNSEVTGRGVIALVGKGQIYSITLKEGEQYIAHPSNVVAYTMMQTPPQPYRFKSTTIRFPVPNLGVGKRLFNTNFMSNLSKSDTWMAVMRIFHTFRTWTRRTIWGDRLFLQFQGPTTLLVQSRAARVNDILADHEVNEIADTTPGVTRAAVEATEVSPPEDVAHQTATKENHQRQSIATVHRDGKIDFKSTE
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Belongs to the AIM24 family.
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B8N219
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MSQPLRRGVRAVSWTRVLPPRARQGQTRCLQIRAAAAEQPSSANGNNLPVVGTPSSAESADARFDVIGAPYSLLSVSLSASQNLFTRRGTLVGLSGKADNVVSTLSVLEPFRRAVVGVPFLYQKVSSASPVTALVSVRSPTTSFAVVHLDGSVDWMVAQRRALLAWTGRSLSIKPTINTSLSVSHWGSSEVTGRGLLALVGAGQLYQVEVKAGEQYIVHPSNVVAYTMTNNPPRPYRFKSTTLKFQVPGLKGWPSFIQDSKFIRDMSGSDTWKTAMNIFHKIRTWSRMTIWGDRLFLQFDGPATILIQTRGPRINEVLTSHEVNEIASAPRGLTIGPAKPAEEKKPSADEEYRKAAEEAVNAAPAPTRTVEQLEQEIRGSAQSIATLTKEGKVIFEKPGQQN
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Belongs to the AIM24 family.
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Q0CSL5
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MSQPWRRGVRALSWTRVLPPRARQGLSASQTRCVQIRAAPAEQPASVNGDHLPVVATPNSAQSSDARFDVIGAPYSMLSVSLSASQNLYTRRGTLVGLSGKADNVSSASPVTALVSVRSPVTSFAVVHLNGSVDWMVAQRRALLAWTGRSLSIRPTINTSLSIAHWGSSEVTGRGLLALVGTGQLYSVELKAGEQYIVHPSNVVAYTMSSNPPRPYRFKSTTLKFQVPGLKSLPRFIQDSKFIQDMSDTDTWKGTMKLFHKIRTWSRMTIWGDRLFLQFDGPTTILLQTRGPRINEILTTHEVNEIADSPRGLTIGPRKPSEDKKTAEEALQPTPDAPSRSVDDLIQEVEGSAQRIATITKEGKVFFEKAGQKN
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Belongs to the AIM24 family.
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A0A179U6G7
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MEAMSHSIRRSLQPFARSRRSWRSPARRAEQRWIHIQQLQSAEPGLVNGNYLPASTTANSASSPDAKFRVLGAPYSILSVTLSASQNLYTRRGTLVGLSGKADNVISTLSLLEPARRALLRIPFLYQKISSTSPITALISTRSAITTFSVVEMNGSVDWMIAQEKALLAWTGHSLRIKPRLTRQLSLSHWGNSEVTGRGLLALVGTGQLYSVELKAGEQYISHPSNVVAYTITAPSPRPYRFKSTILPFQIPSLGIGKRLSDSNFIKNLSDTDTWKAALKLWHIIRTWSRRTIWGDRLFLQFDGPATILVQSRASRMADTLTTQQVNEIADAPPGVTQDAVDRAAAKLGEEETVPKAKDDLKPTTAISGQSVASVRRDGKVEFHQTGVGQ
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Belongs to the AIM24 family.
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Q59L33
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MSLNQYIRPVRTKLSHISCIRNISITQSSINTTIKNDESISKTTTIPENIQQAKELAGYRALEIPEFKTLGSAEGTTATATGSSSSSSSSILSINVPPSVPVYIRRGSLLSIYGIQEISSIDSVRSQLQFPNFWKRLIYGGYVSGYQKLISTTPFSLLISSKSRSSGSGGGSGSGSGFEKSFVNLVLDGTTDWAILDKSALQVYTGNSLSITMHKLPKFISKKLSRSLKKDKKSKTNTNKLETGLFSWKKLGYTLLSGRGKVGLVGNGSSSGYGSSIYNINLNQNEEILINKNNLLGITVNGPYDLQNCIVKYEFPIINNANPTNTNINIKEPVTIVKPKLIQPTTWNLIVLKLKNFNNGFKKFFQIINKYTLGLKTTSYNYLAGNQDFIKVIGPRNLLLQSNTNKSHRGFNNIIPRNKPQAKVWPTNQTTTKVDESSSFSTPKDYLNHVTIEPGKGAVFKSTLDFSETVESIENKNKNKNKSK
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Belongs to the AIM24 family.
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C4YPQ0
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MSLNQYIRPVRTKLSHISFIRNISITQSSINTTIKNDESISKTTTIPENIQQAKELAGYRALEIPEFKTLGSAEGTTATATGSSSILSINVPPSVPVYIRRGSLLSIYGIQEISSIDSVRSQLQFPNFWKRLIYGGYVSGYQKLISTTPFSLLISSKSRSSGSGSGSGFEKSFVNLVLDGTTDWAILDKSALQVYTGNSLSITMHKLPKFISKKLSRSLKKDKKSKTNTNKLETGLFSWKKLGYTLLSGRGKVGLVGNGSSSGYGSSIYNINLNQNEEILINKNNLLGITVNGPYDLQNCIVKYEFPIINNANPTNTNTNINIKEPVTIVKPKLIQPTTWNLIVLKLKNFNNGFKKIFQIINKYTLGLKTTSYNYLAGNQDFIKVIGPRNLLLQSNTNKSHRGFYNIIPRNKPQAKVWPTNQTTTKVDESSSFSTPKDYLNYVTIEPGKGAVFKSTLDFSETVESIENKNKNKNK
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Belongs to the AIM24 family.
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B9WD86
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MSSLNQYIRPVKSRLSYISFIRNISITQSSINSTIKDNESISKTTTIPENIQQAKELAGYRALEVPEFKVLGSTSNGGNSTSSSCSSSILSINVPPSVPIYIRRGSLLSIYGIQEISSIDSVRSQLQFPNFWQRLIYGGYISGYQKLISTTPFSLLISSKSRTIMNGGNSSTEKSFVNLILDGTTDWAILDKSALQVYTGNSLSITMHKLPKFISKKLSRSLKNNNNSSNKKLETGLFSWKKMGYTLLSGRGKIGLVGNGNNSGCSIYNINLNQDEEILINKNNLLAITVNGPYDLQNCIIKYQFPIINNSNNNNNNNNSNNMTKNIKESGNIVKPKLIEPTTWNLIILKIKNINNRIKKFFQFINKYTLNLKTTSYNYLSGNQEFIKIIGPRNLLLQSNINHNGFNFTTRRKQQQKSIWPTTTDTTNTTTTKVDNTSSTPKDYLNYVTIEPDKGAIFKSTSDFSETIETIEKKKKNKGKDINTTPI
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Belongs to the AIM24 family.
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Q6FJ45
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MLKSRFKVVGKEALMASLPLEPSVPMCIRKGCLVSVMAGGAHGSGKTASLVIGHKWVNFWTNLARFRSWNSSLYHVLTTSGKENRALVAPNISRGSPWLSALKLVVSILSKNSKGITITDPQRSIYPLELDGTQDWNVWGRDSLIAFEQNDSLDIKPASLSSSLKRDALFSHSHKYQVVTGRGSVLLGGYGDIYSIDLKNSTDDIVINAQNILAVSGKGQTETMNAIENNPFIISHTAASNIPEFTSNVQELAAFEDPKQQQSQTIVQKTVKEAARASKAVWHWISYVYKKTVIFSNNNGHNITSPAFVKIKGPRTIIIQTSHETTQPVSVSTVDILPRTVENAIPEVVETPKAKSDSYINYATVQPDGNVTFRSVSNFNETIAERY
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Belongs to the AIM24 family.
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C5M9N0
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MINTKIGRPCVRLHQLNFIRSITINQQPSSTISTEQLTKTTTIPSNIQQVEELTNSRTLEAPEFKTLGNSGSSTTSSSSSSILSINLPPSVPIYLKRGSLLSIYGIKQDITSINSVRSSLEFPLFWKKLIYGIDSNKGYQRLISTSPFSILVSSQSRRGGSIFSKNNGDKSFVNLILDGGTDWAILKNDSIQAYSGNSLNLNIYKLPNYISKKLSKKLGFGNKKFKTGLISWINRKIGYILISGRGNVGLIGNGNIYNLNLIKNEEILINKENLLGITVNGPYDLQNCIIKYQFPLKDQSIIDSNTSDVIIEKPKLYEPNSWGMIKYRFDQFNKSFKKIFQSIFKYSSDVKESGFNYLVGNQEFIKIIGPRNILIQSNVDNSFIIPSIKRSDKIVTPVKSNDNTEVKKSTTTGDYLNYVTIEPGKGAVFKSTPDFKDTVDQIDNKSK
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Belongs to the AIM24 family.
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C4Y7Q2
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MKHLTRAVRPLHVQAAPVAASAHPGALSRVPSAAAVDLPAPTPGDQVRLQALGSPPSVASVAVPPSLPVFVRRGSVLAVSGRIDRIVSAFVAPMWLRRLTLGNIVSRYQRLVATEPFAVLASASAPSLWPQLVRRATPRSFASLTLDGTADWAVLKRDALQVYAGPALTLSVHAAPQRISRRLAQSLNTSRIPTGLRRTGYTFVSGRGVVALAGHGSVYAARVAADEQLTVARSSIVAISVNGPHDLHNCVAQMPQTQASAAGSAGSATSAAGSNSRKWTDLKWKDVVPWVRGVWSKLVSAPRWGSGFVRVSGPRTVLLQSGGAQQMWEHTVRGPRSASAPKVSADYLNVVTFDQAHRPEIRSTSDFGEAVRAIEKTK
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Belongs to the AIM24 family.
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C5PFU3
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MEPMNYLVRRGFRPSAWKYGKWRPIGKTVSERRRISIQPVPSVESNTVNASYLPAASTPSSVTSPGLCIVSNDASFEVLGSPYSLLSVSLSASQNLYTRRGTLVGLTGKSENVVSTLRLLEPLRRAALRMPFLYQKISSASPVNALISVRSPITSFAVVQLDGTVDWMITQRDALLSWTGHALTVKPTLNRELSLVHWGSSKVTGRGLLAVVGKGQVYSINLRAGERYIAHPSNVVAYTINSHWPRPFRFKSTSLKFQIPKLGLGTLLMKSNFLRNLADSDTWKATMRIFHTVRTWARRTIWGDRLFLQFEGPATVLIQSRASRIAESLTAREVNEIASTQPGVTREATETVEARLEKQSPPPAKDDGMKTVGQSVASVRRDGKVEFEKVDGV
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Belongs to the AIM24 family.
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Q6BKX6
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MKANIAMASKQLQFIRSLIISQPPTIALPNQSSNISKIENIKGNDLPNQKTLNDPEFQSLGQPASVLAINSPPSVPIYIRKNSLLSIYGIDNSFVNSIKGSVEFINPLKRFIYGGYVSKYQKIISTVPFSLLVSSSSKNFRLRTNRQKSFATLLLDGTNDWAVLNNTALQAYTGGTLNVSMFRIPKNISKTLASLLKITNATETGLFRWNNLGYALLTGRGQVGLVGNGAIYNINLKENEEVLISRKNLLSISVNGPYDLQNCIVKYSFPVTKPETGTIGSTKEAPVQLNKDDVIPANNFNHYWNIIKGYSRHIINFFKRSQRLTYNFLVGNEDFVRVIGPRNLLLQSNSVGSHSTSSSELPKPNLSNIKANIEKKSSDFLNYVTIEPGRGAVFKSTPNFRESVQKIEKKSS
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Belongs to the AIM24 family.
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Q5B6V7
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MATGSYFPPPGAPSSISPRNSTPALSPLSPPLQQRSNALSNRLTSVLSVSYADSDIRDALETLSLRGVHNTAEVRRQLRLDVQKEVVDCNAEIVRDFGNVAEQLKRIGSVISSLKETCDEMRKHIVLAKQDTTPVLEEASALMIQKQEAETKQRLLDAFTKHFIVSEEELLALTSIEEPIDDEFFDVLARVKQVHRDCEALLGAEHERLGLELMEKSSRSLNSAYQKLYRWIQKEFKSLNLEDPQISGTIRQALRVLAERPSLFQTCLDFFAEARDYVLSDAFHYALTDAVSGGDSAVKPIEFSAHDPLRYIGDMLAWVHSTTVSEREALETLFVAEGDELAKGIQAGLNSEPWSRIDEDEEMTFDGQKALSDLVSRDLIGVARSLRQRVELVIQGHDDPVTCYKVINLLSFYQTIFSKLVGPNSNLAELLKALEKFTLNHFQTIMRDEVNNISTDHSALAPPDDLSAPQFLHDSLEVLTALMKTHEASLGTEDPSITSESEENEFTPVLHAALDPFFTLAKASADELPDPTARAIYLTNVHITTRSTISPYPFATSTHLPPLSATLSTLRVELLESQHRYLLDTSGLQVLLTALQPFSQSNESGTEKDLAAIADLPAFQAEALISTSQQLDDFLPSALMDATDNLKRVQSATFVKSVTEEAVEAFCRDFEFVEGMIIGADEARGVGQSDGAVNEEGEEGDGDGDGEVELELEVEQRGQGQSLRKLFPRTTGEIRVLLS
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Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events (By similarity). Belongs to the COG6 family. The predicted gene AN3723 has been split into 2 genes: AN10466 and AN10441.
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Q6CPA5
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MWRRSISILRPSPTTVIPSNVLSGSQLELKPLFDNHAETTREDGSNVTTTQFQLLGDNPTLASIQVSPSIPLYVRHNSIVSIHDSDRLSNVNVSYNKWFTFWPTLSLSRFDKLVGTNTFNCLVSSRKSSDTLSVLQLNGTQDWIVLNPKSVVSFEGNSSLSIQWFHKWLNYFRWISNKVTVLRSYGKLSGRGNVLLNGNGSVYKLELKSEDDQIILQKNRILAFNGLNKLDFKQAVTFEQTSKSLESDSQPETIHNNEDKIAFMKTVNTTLEFLKTRWHTMSNTDFVRVKGPRTVLVQTDAKSSAQTWPTSTLSLKPAKNYLSFAKIDNGSVNFKNTTSLLEKK
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Belongs to the AIM24 family.
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C4QXH2
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MLTQRVCRILNANVTVRNLSIVQASSVSSEKRKDSEQPKLLSSIDDIGVNQASKPVFQVIGSPATVLNVSIPPSYPLYVSKGSIISLNSKDKHSVLDSLVSQTRLINPIKRTLFGLINFRYEKIFSTIPFNALVSSSVSTFSWGSSSKIVRQRSFVSLDLDGRLDWAVFPPKAVQAYAGDNLTITNPFLPKSLTKFPRVYTLISGRGLLSLTGEGQIYKITLGNETILIRKENLLAISVNGNSEIPQSLKNVNLNKELKEGSREQISSRPVLKYFSQAKDVITSSYRYLTGNNQYIKVHGPRTLLLSTNSQLESFHYKNGQGSENYFSLAKSIGFANPEPQPKDYLKVVTIEKGEIKGYESKNSFLEEQKQQAQ
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Belongs to the AIM24 family.
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C5DE09
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MKAAALRLGHASVAKRSISLVRPVAATVVPAQMAQKPDAEPIFGQEDNSDIQDAQFRVLGQPPTLCSVHVPASVSLHVRRGCLVSLHGVGEQNAVAISQEWIGLAWNLAKHGSWRAALFHQLVAPRAFSALVAPNVNGGKIASWFGVSAQQFRTLCLLDLDGTQDWCVLGKHSLIAYEGNTSLRIQRSSVWPSWLHFNRGDSALPSTYQLIQGRGNALLSGAGSVYTIELPNENEELILKGEHLLAISGRTPRDIAEAVTEYSFPAVSVPAIPETAVSKGRTPMPTSSLSAFSTALASYSRNAVSWLRHAYTSYINGTTKYLRIRGPRFLLVQSAHNAFMPATSPSAVQPPSSPVSVKAPASTPNSKDYLSYVTVGKDASVSFQSTPDFNKKVAEIEALKHK
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Belongs to the AIM24 family.
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A5DXQ6
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MIRSRQKVLSLVTWTLKRSIVVNAVSASSVDPSFSTMANTTNVAANTNLNKTTTEPGNIRNAPQLSILQTLENAEFIALGTPPTLLTVHSPPSVPLFVRRGALTSIYGLKSTSNTTPTYGSSSSSSSSSSSSSSTATSFTSSLTSSTQPLIRNTLEFPLWWDRFRFNGGHILSYQKLISTVPFSTLISSSSSSLSSSSKYGDVKSFANLILDGSSDWAILNKTAIQAYTGNSLSISMHKLPKYISKSLAKFLNISRIETGLWSFWNSGYTLLSGRGHVGVVGSGGVYQLQLAEDEEILIRKSAILGVTVNGPFDLENCIIKNDVTTTLYLPQEGEQNHKVKVKLNVEERPQGKQVLVQPSAWDQIVLGSKLALNWTRLVWHYQKVFFNRISIILSRFLLGNAEFVKVVGPRNILIQASPHLKQTQKDTRRSFGGSNSEEITQLNEKLVFIEPQINPESGSKSKSNDYLSYVEIDPKKGAVFQNTPNFRDSI
|
Belongs to the AIM24 family.
|
A7TN35
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MNFMLRRNGGQFQKFGFFIRCNSTESFYSKAILGLKKDLKQAMLAKDDLKKTTIRNMLSTIKNKEIDAKDTKFDEFTLFGIYSKLINQRKDSISDYLKNNREDLAGKEEQELKLIQTYLDSLPIASPQEIDTKVEKFLNDLKEKEGTVPMKDVFSKVDWNTLTKEWKASQSMIKSSIVSKYKNIF
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Belongs to the AIM41 family.
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B3LJN9
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MFRQSIRPLVSNRLTFIRYNSSPAYTAAVSLLKGDLKKAMIAKDEMKKTAIRNMLSAIKNKEIALKGKSADEYSLYDMYSKLISQRKDSINEFLANKRDDLVAKEQGEMDIIKKYMDQLPVSSELDIDQNVKKLLDALKTKAGEKKVQIKEIMGEIDWKSLPTEWKTSPTAIKNSIVKQFKEIFK
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Belongs to the AIM41 family.
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C7GWG7
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MFRQSIRPLVSNRLTFIRYNSSPAYTAAVSLLKGDLKKAMIAKDEMKKTAIRNMLSAIKNKEIALKGKSADEYSLYDMYSKLISQRKDSINEFLANKRDDLVAKEQGEMDIIKKYMDQLPVSSELDIDQNVKKLLDALKTKAGEKKVQIKEIMGEIDWKSLPTEWKTSPTAIKNSIVKQFKEIFK
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Belongs to the AIM41 family.
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B5VS96
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MFRQSIRPLVSNRLTFIRYNSSPAYTAAVSLLKGDLKKAMIAKDEMKKTAIRNMLSAIKNKEIALKGKSADEYSLYDMYSKLISQRKDSINEFLANKRDDLVAKEQGEMDIIKKYMDQLPVSSELDIDQNVKKLLDALKTKAGEKKVQIKEIMGEIDWKSLPTEWKTSPTAIKNSIVKQFKEIFK
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Belongs to the AIM41 family.
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A6ZP58
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MFRQSIRPLVSNRLTFIRYNSSPAYTAAVSLLKGDLKKAMIAKDEMKKTAIRSMLSAIKNKEIALKGKSADEYSLYDMYSKLISQRKDSINEFLANKRDDLVAKEQGEMDIIKKYMDQLPVSSELDIDQNVKKLLDALKTKAGEKKVQIKEIMGEIDWKSLPTEWKTSPTAIKNSIVKQFKEIFK
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Belongs to the AIM41 family.
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C8ZGX0
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MFRQSIRPLVSNRLTFIRYNSSPAYTAAVSLLKGDLKKAMIAKDEMKKTAIRSMLSAIKNKEIALKGKSADEYSLYDMYSKLISQRKDSINEFLANKRDDLVAKEQGEMDIIKKYMDQLPVSSELDIDQNVKKLLDALKTKAGEKKVQIKEIMGEIDWKSLPTEWKTSPTAIKNSIVKQFKEIFK
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Belongs to the AIM41 family.
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