UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 2
35.2k
| Functional Description
stringlengths 5
30.7k
|
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Q9AY60
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MEAVVVDAGSKLLKAGIALPDQSPSLVMPSKMKLEVEDGQMGDGAVVEEVVQPVVRGFVKDWDAMEDLLNYVLYSNIGWEIGDEGQILFTEPLFTPKALREQLAQLMFEKFNVSGFYDSEQAVLSLYAVGRISGCTVDIGHGKIDIAPVCEGAVQHIASKRFDIGGTDLTNLFAEELKKSNSSVNIDISDVERLKEQYACCAEDQMAFEAIGSSCRPERHTLPDGQVITIEKERYIVGEALFQPHILGLEDYGIVHQLVTSVSNVTPEYHRQLLENTMLCGGTASMTGFEDRFQREANLSASAICPSLVKPPEYMPENLARYSAWLGGAILAKVVFPQNQHVTKGDYDETGPSIVHKKCF
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Essential protein required during embryogenesis and all plant development stages, probably through a chromatin-mediated regulation of gene expression. Belongs to the actin family. Plant ARP7 subfamily.
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Q8C404
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MGKLSPCTGRSRPGGPGPQLPLLLLLLQLLLLLLSPARASGATQPPHVVFVLADDLGWNDLGFHGSVIRTPHLDALAAGGVVLDNYYVQPLCTPSRSQLLTGRYQIHLGLQHYLIMTCQPSCVPLDEKLLPQLLKEAGYATHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYTHEACAPIESLNGTRCALDLRDGEEPAKEYNNIYSTNIFTKRATTVIANHPPEKPLFLYLAFQSVHDPLQVPEEYMEPYGFIQDKHRRIYAGMVSLMDEAVGNVTKALKSHGLWNNTVFIFSTDNGGQTRSGGNNWPLRGRKGTLWEGGIRGTGFVASPLLKQKGVKSRELMHITDWLPTLVDLAGGSTNGTKPLDGFNMWKTISEGHPSPRVELLHNIDQDFFDGLPCPGKNMTPAKDDSFPLEHSAFNTSIHAGIRYKNWKLLTGHPGCGYWFPPPSQSNVSEIPPVGPPTKTLWLFDINQDPEERHDVSREHPHIVQNLLSRLQYYHEHSVPSHFPPLDPRCDPKSTGVWSPWM
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Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation (By similarity). Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (By similarity). In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels (By similarity). Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate. Binds 1 Ca(2+) ion per subunit. Inhibited by ethanol (By similarity). Homodimer. The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. Belongs to the sulfatase family.
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Q32KK1
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MGELSGCTGGSRAGGPGPRLPLLLLLLLWPARASDAAPPPHVVFVLADDLGWNDLGFHGSVIRTPHLDALAAGGVVLDNYYVQPLCTPSRSQLLTGRYQIHMGLQHYLIMTCQPNCVPLDEKLLPQLLKDAGYATHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYTHEACAPIECLNGTRCALDLRDGEEPAKEYTDIYSTNIFTKRATTLIANHPPEKPLFLYLAFQSVHDPLQVPEEYMEPYDFIQDKHRRIYAGMVSLLDEAVGNVTKALKSRGLWNNTVLIFSTDNGGQTRSGGNNWPLRGRKGTLWEGGIRGAGFVASPLLKQKGVKSRELMHITDWLPTLVNLAGGSTHGTKPLDGFDVWETISEGSPSPRVELLLNIDPDFFDGLPCPGKNTTPEKNDSFPLEHSAFNTSIHAGIRYKNWKLLTGYPGCGYWFPPPSQSNISEVPSVDSPTKTLWLFDINRDPEERHDVSREHPHIVQNLLSRLQYYHEHSVPSYFPPLDPRCDPKGTGVWSPWM
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Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation (PubMed:24311516). In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels (PubMed:24311516). Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (By similarity). Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate. Binds 1 Ca(2+) ion per subunit. Inhibited by ethanol. Homodimer. Defects in Arsb are the cause of mucopolysaccharidosis type VI (MPS-VI) (PubMed:8575749). Belongs to the sulfatase family.
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P76708
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MLLAGAIFVLTIVLVIWQPKGLGIGWSATLGAVLALVTGVVHPGDIPVVWNIVWNATAAFIAVIIISLLLDESGFFEWAALHVSRWGNGRGRLLFTWIVLLGAAVAALFANDGAALILTPIVIAMLLALGFSKGTTLAFVMAAGFIADTASLPLIVSNLVNIVSADFFGLGFREYASVMVPVDIAAIVATLVMLHLYFRKDIPQNYDMALLKSPAEAIKDPATFKTGWVVLLLLLVGFFVLEPLGIPVSAIAAVGALILFVVAKRGHAINTGKVLRGAPWQIVIFSLGMYLVVYGLRNAGLTEYLSGVLNVLADNGLWAATLGTGFLTAFLSSIMNNMPTVLVGALSIDGSTASGVIKEAMVYANVIGCDLGPKITPIGSLATLLWLHVLSQKNMTISWGYYFRTGIIMTLPVLFVTLAALALRLSFTL
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Involved in arsenical resistance. Thought to form the channel of an arsenite pump (By similarity). Belongs to the ArsB family.
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Q5HF02
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MTTLATLIFLVTLLFVLWQPKGLDIGITALTGAFIAVITGVVSFSDVFEVTGIVWNATLTFVSVILISLILDKVGLFEWSAIHMLHASKGNGLKMFVYIILLGAIVAAFFANDGAALILTPIVLAMVKNIGFSKRAIFPFIIASGFIADTTSLPLIVSNLVNIISADYFHVGFVRYFSRMIIPNLFSLLASIIVLWLYFRKAIPKTFDDNNIKHPKDAINDLKLFKISWIVLVILLFGYLISEFTKIPVSIFTGIIAFIFLMLARKSNAVNIKQVIKGAPWNIVLFSIGMYIVVFGLRNAGITLILAKILEYISNYGLFSTILGMGFISAFLSSIMNNMPTVLIDAIAIGQSNVHGMLKEGLIYANVIGSDLGPKITPIGSLATLLWLHVLTQKDVKISWGTYFKTGIIITIPVLFITLIGLYLTLIIF
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Involved in arsenical resistance. Thought to form the channel of an arsenite pump. Belongs to the ArsB family.
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Q99T95
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MTTLATLIFLVTLLFVLWQPKGLDIGITALTGAFIAVITGVVSFSDVFEVTGIVWNATLTFVSVILISLILDKVGLFEWSAIHMLHASKGNGLKMFVYIILLGAIVAAFFANDGAALILTPIVLAMVKNIGFSKRAIFPFIIASGFIADTTSLPLIVSNLVNIISADYFHVGFVRYFSRMIIPNLFSLLASIIVLWLYFRKAIPKTFDDNNIKHPKDAINDLKLFKISWIVLVILLFGYLISEFTKIPVSIFTGIIAFIFLMLARKSNAVNIKQVIKGAPWNIVLFSIGMYIVVFGLRNAGITLILAKILEYISNYGLFSTILGMGFISAFLSSIMNNMPTVLIDAIAIGQSNVHGMLKEGLIYANVIGSDLGPKITPIGSLATLLWLHVLTQKDVKISWGTYFKTGIIITIPVLFITLIGLYLTLIIF
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Involved in arsenical resistance. Thought to form the channel of an arsenite pump. Belongs to the ArsB family.
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Q6GFT0
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MTTLATFIFLVTLLFVLWQPKGLDIGFTALAGAFIAVITGVVSFSDVFEVTGIVWNATLTFVSVILISLILDKVGLFEWSAIHMLHASKGSGLKMFVYIILLGAVVAAFFANDGAALILTPIVLAMVKNIGFSKRAIFPFIIASGFIADTTSLPLIVSNLVNIISADYFNISFSQYLSRMIIPNLFSLLASLLVLWLYFRKAIPKSFDANHIKKPIDAINDLKLFKISWIVLVILLFGYLISEFTKIPVSIFTGIIAFIFLILARKSNAVNIKQVIKGAPWNIVLFSIGMYIVVFGLRNAGITLILAKILEYISNYGLFSTILGMGFISAFLSSIMNNMPTVLIDAIAIGQSNVHGMLKEGLIYANVIGSDLGPKITPIGSLATLLWLHVLTQKDVKISWGTYFKTGIIITIPVLFFTLLGLYLTLILF
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Involved in arsenical resistance. Thought to form the channel of an arsenite pump. Belongs to the ArsB family.
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Q6G8F6
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MTTLATLIFLVTLLFVLWQPKGLDIGITALTGAFIAVITGVVSFSDVFEVTGIVWNATLTFVSVILISLILDKVGLFEWSAIHMLHASKGNGLKMFAYIILLGAIVAAFFANDGAALILTPIVLAMVKNIGFSKRAIFPFIIASGFIADTTSLPLIVSNLVNIISADYFHIGFIRYFSRMIIPNLFSLLASIIVLWLYFRKAIPKTFDDNNIKHPKDAINDLKLFKISWIVLVILLFGYLISEFTKIPVSIFTGIIAFIFLMLARKSNALNIKQVIKGAPWNIVLFSIGMYIVVFGLRNAGITLILAKILEYISNYGLFSTILGMGFISAFLSSIMNNMPTVLIDAIAIGQSNVHGMLKEGLIYANVIGSDLGPKITPIGSLATLLWLHVLTQKDVKISWGTYFKTGIIITIPVLFITLIGLYLTLIIF
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Involved in arsenical resistance. Thought to form the channel of an arsenite pump. Belongs to the ArsB family.
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P30329
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MTILAIVIFLLTLTFVIWQPKGLDIGITALIGAVVAIITGVVSLSDVLEVTGIVWNATLTFVAVILISLILDEIGFFEWSAIHMVKASNGNGLKMFVFIMLLGAIVAAFFANDGAALILTPIVLAMVRNLGFNQKVIFPFIIASGFIADTTSLPLIVSNLVNIVSADYFDIGFIEYFSRMIIPNIFSLIASILVLWLYFRKSIPKTFDTENLSDPKSAIKDSKLFKLSWIVLAVLLVGYLVSEFIQIPVSIIAGIIAFIFVILARKSKAVHTKQVIKGAPWNIVVFSIGMYLVVFGLKNVGITTILGDVLTNISNYGLFSSIMGMGFIAAFLSSIMNNMPTVLIDAIAIGQSSATGILKEGMVYANVIGSDLGPKITPIGSLATLLWLHVLTQKGVKISWGTYFKTGIIITIPVLFVTLLGLYLTLIIF
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Involved in arsenical resistance. Thought to form the channel of an arsenite pump. Belongs to the ArsB family.
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Q8NW09
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MTTLATLIFLVTLLFVLWQPKGLDIGITALTGAFIAVITGVVSFSDVFEVTGIVWNATLTFVSVILISLILDKVGLFEWSAIHMLHASKGNGLKMFVYIILLGAIVAAFFANDGAALILTPIVLAMVKNIGFSKRAIFPFIIASGFIADTTSLPLIVSNLVNIISADYFHIGFIRYFSRMIIPNLFSLLASIIVLWLYFRKAIPKTFDDNNIKHPKDAINDLKLFKISWIVLVILLFGYLISEFTKIPVSIFTGIIAFIFLMLARKSNALNIKQVIKGAPWNIVLFSIGMYIVVFGLRNAGITLILAKILEYISNYGLFSTILGMGFISAFLSSIMNNMPTVLIDAIAIGQSNVHGMLKEGLIYANVIGSDLGPKITPIGSLATLLWLHVLTQKDVKISWGTYFKTGIIITIPVLFITLIGLYLTLIIF
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Involved in arsenical resistance. Thought to form the channel of an arsenite pump. Belongs to the ArsB family.
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Q5HRI3
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MTTVLAIVIFFITLTLIIWQPKGLDIGISAIIGALLVIITGVVNFTDILEVIGIVWNATLTFVSVILISLILDEIGFFEWSAIHMVKASNGHGLKMFIYIMILGALIAAFFANDGAALILTPIVLAMIRNLGFNNKLVFPFIIACGFIADSTSLPLVVSNLVNIVSADYFGIKFVEYLMRMFIPNLFSLLASILVLWFYFRKSIPKTFDISSISEPKDAIRDTRLFKISWIILALLLIGYLVSEFIHIPVSFITGAIAVIFILLARQSNVVHTKQVIKGAPWNIVIFSIGMYLVIFGLKNVGMTLILADILSSIAQHGLFSSIMGMGFVSAFLSAIMNNMPTVLIDAIAIDQSHAISSIKEGMIYANVIGADLGPKITPIGSLATLLWLHVLVQKGVKISWGTYFKTGIVITIPVLFFTLLGLYLTLIIF
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Involved in arsenical resistance. Thought to form the channel of an arsenite pump. Belongs to the ArsB family.
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Q8CQF4
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MTILAITIFILTLIFVIWQPKGLDIGITALIGAVIAIITGVVSFSDVLEVTGIVWNATLTFVAVILISLILDEIGFFEWSAIHMVRASKGNGLKMFVYIMLLGAIVAAFFANDGAALILTPIVLAMVRSLGFDKKAVFPFIIASGFIADTTSLPLIVSNLVNIVSADYFDIGFVEYFSKMIIPNIFSLIASILVLWLYFRKSIPRKFDAVNIREPKEAIKDKKLFNISWIVLTVLLVGYLISEFINIPVSIIAGIIALIFVLLARKSKAVHTKQVIKGAPWNIVLFSIGMYLVVFGLKNVGITTLLSDVLTNISSYGLFSSIMGMGFISAFLSSIMNNMPTVLIDAIAIGQSQTTSILKEGMIYANVIGSDLGPKITPIGSLATLLWLHVLTQKGVKISWGQYFKIGIIITIPVLFITLLGLYLTLIIF
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Involved in arsenical resistance. Thought to form the channel of an arsenite pump. Belongs to the ArsB family.
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Q01255
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MTILAIVIFLLTLIFVIWQPKGLDIGITALIGAVVAIITGVVSFSDVLEVTGIVWNATLTFVAVILISLILDEIGFFEWSAIHMVKASNGNGLKMFVFIMLLGAIVAAFFANDGAALILTPIVLAMVRNLGFNKKVIFPFIIASGFIADTTSLPLIVSNLVNIVSADYFDIGFIEYFSRMIIPNIFSLIASILVLWLYFRKSIPKTFNTENLSDPKNVIKDPKLFKLSWIVLAILLVGYLVSEFIQIPVSIIAGIIALIFVILARKSKAVHTKQVIKGAPWNIVVFSIGMYLVVFGLKNVGITTILGDILTNISSYGLFSSIMGMGFIAAFLSSIMNNMPTVLIDAIAIGQSSATGILKEGMVYANVIGSDLGPKITPIGSLATLLWLHVLTQKGVKISWGTYFKTGIIITIPVLFVTLLGLYLTLIIF
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Involved in arsenical resistance. Thought to form the channel of an arsenite pump. Belongs to the ArsB family.
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P74985
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MLLAGSIFVLTLILAIWQPRGLSIGWSASICAALALVSGVIHVGDIPVVWNIVWNATATFIAVIIISLLLDESGFFEWAALHVSRWGNGRGRLLFTWIVLLGAAVAALFANDGAALILTPIVIAMLLALGFSKRTTLAFVMAAGFIADTASLPLIVSNLVNIVSADFFRLGFTEYASVMLPVDIAAIAATLGMLHLFFRRDIPATYDVSLLKMPASAIKDPATFRAGWIVLVLLLVGFFVLEPLGIPVSAIAAVGTVVLFAVAKKGHAINTGKVLRGAPWQIVVFSLGMYLVVYGLRNAGLTEYLSGVLNMLADKGLLAATFGTGFLTAFLSSVMNNMPTVLVGALSIDGSTASGVIKEAMIYANVIGCDLGPKITPIGSLATLLWLHVLSQKNMTISWGYYFRTGIIMTLPVLFVTLAALALRLSVTL
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Involved in arsenical resistance. Thought to form the channel of an arsenite pump (By similarity). Belongs to the ArsB family.
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Q74NT6
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MENKKTIYFLCTGNSCRSQMAEAWGKKYLGDKWNVLSAGIEAHGVNPNAIKAMKEVDIDITDQTSDIIDRDILDKADLVVTLCGHANDVCPTTPPHVKRVHWGFDDPAGQEWSVFQRVRDEIGARIKKYAETGE
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Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. [thioredoxin]-dithiol + arsenate + H(+) = [thioredoxin]-disulfide + arsenite + H2O Belongs to the low molecular weight phosphotyrosine protein phosphatase family. Thioredoxin-coupled ArsC subfamily.
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Q8NQC7
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MNNQPSVLFVCVGNGGKSQMAAALAKKHAGDALKVYSAGTKPGTKLNQQSLDSIAEVGADMSQGFPKGIDQELIKRVDRVVILGAEAQLEMPIDANGILQRWVTDEPSERGIEGMERMRLVRDDIDARVQNLVAELTQNA
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Involved in defense against toxic arsenate. Involved in the mycothiol/myoredoxin redox pathway which uses a mycothioltransferase mechanism; facilitates adduct formation between arsenate and mycothiol. arsenate + mycothiol = arseno-mycothiol + H2O By arsenite. Belongs to the low molecular weight phosphotyrosine protein phosphatase family.
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P08692
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MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK
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Involved in resistance to arsenate (PubMed:3021763, PubMed:8003492, PubMed:7577935). Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)] (PubMed:8003492, PubMed:7577935, PubMed:14592722). The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable). [glutaredoxin]-dithiol + arsenate + glutathione + H(+) = arsenite + glutathionyl-S-S-[glutaredoxin] + H2O Inhibited by the thiol reagents iodoacetate (IAA) and N-ethylmaleimide (NEM) (PubMed:7577935). Activity is rapidly inactivated by the histidine-modifying reagent diethylpyrocarbonate (DEPC) (PubMed:8969183). kcat is 0.53 sec(-1) with arsenate as substrate. kcat is 0.218 sec(-1) with Grx2 as substrate. Optimum pH is 6.3-6.8. Monomer in solution. Belongs to the ArsC family.
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Q5HRI4
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MQKKTIYFICTGNSCRSQMAEGFGKLILGDKWNVYSAGIETHGVNPHAIKAMKEVGIDISHHTSDLINNDILIASDIVVTLCSDADANCPVLPKNVTKEHWGFDDPAGKDWSEFQRVRDEIKAAIETFAHRV
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Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. [thioredoxin]-dithiol + arsenate + H(+) = [thioredoxin]-disulfide + arsenite + H2O Belongs to the low molecular weight phosphotyrosine protein phosphatase family. Thioredoxin-coupled ArsC subfamily.
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Q4LAB5
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MDKKTIYFICSGNSCRSQMAEGWGKEILGEDWNVYSAGIETHGVNPKAIEAMKEVDIDISNHTSDLIDSDILEQSDLVVTLCSDADDNCPILPPNVKKEHWGFDDPAGKEWPEFQRVRDEIGKRIQEFKETLV
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Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. [thioredoxin]-dithiol + arsenate + H(+) = [thioredoxin]-disulfide + arsenite + H2O Belongs to the low molecular weight phosphotyrosine protein phosphatase family. Thioredoxin-coupled ArsC subfamily.
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Q8TGM5
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MPPGIPRGAMCVQRFDDSRNSAIHITYRISLRSSSMREPRDPLLKVFNILKFPVTKILVFDKNLMNR
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Encoded on the antisense strand of the nuclear 35S rDNA. Product of a dubious gene prediction unlikely to encode a functional protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.
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D6VUK2
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MFSLSSLSSSGGHSEQKERERISYFDIRINSPYKDIILIQGSPLELSSIPLSGNLVISVKNEIVVKKISLRLVGRFKLEFLQVGRYKKNSSSLASLVKEKRKIFECYWDNLLVSSKGDVLVGGENAENQHNSSSGRSTSNQDMDTSGNAIFLSKRSLSSPVFNKIIRRKTHSSHRKILELPENGVTGTPFEGLRENARSRSSSSNTLNNNSHSYSNRDGSGSSYLFLMKRGNYELPFNTMLPPEVCETIEGLQSGSILYSFEAIIDGRQLWDTDLSVHTSPHGPIGSTSTSGNGMRTKNKIIIKKFKYLRILRTLSMDNLAMQEEISVGNTWRDKLQYETSIPSRAVPIGSTTPVKIKIFPFEKNIRLDRIEMALIQYYAMKDSSAQIYDDEIAVMKITHLADFGPLTDKLDVDCPFTIPDNLKQITQDCCLQDNLIRVMHKLQVRILLQRQVDGEYKNLEIKAQLPMLLFISPHLPMKGRLVLFDKHDGKIHFRPGELVPLFLTTYPAQGLTPGVELNSTTTAHLALPQPPPNYHESTNDHLMPALQPLGADSVVLTVPSYEQAQAQASASSYVTGSVPAYCDDD
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May regulate endocytosis by recruiting RSP5 ubiquitin ligase activity to specific plasma membrane proteins in response to extracellular stimuli. Interacts with RSP5. Ubiquitinated by RSP5. Present with 1970 molecules/cell in log phase SD medium. Belongs to the arrestin family.
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B8NLM9
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MGHEDAVYLAKLAEQAERYEEMVENMKVVASADVELTVEERNLLSVAYKNVIGARRASWRIVTSIEQKEESKGNESQVTLIKEYRQKIESELAKICDDILEVLDKHLIPSAQSGESKVFYHKMKGDYHRYLAEFAIGDRRKGAADASLEAYKAATEVAQTDLAPTHPIRLGLALNFSVFYYEILNSPDQACHLAKLAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSSEPSRC
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14-3-3 family protein that plays a role in the morphological differentiation and secondary metabolism biosynthesis (PubMed:29247055). Required for normal fungal morphogenesis in an environment-dependent manner, affecting the balance between production of conidiophores and the formation of sclerotia, resistant structures that are necessary for the dissemination and survival (PubMed:29247055). Acts as a positive regulator of conidiation and a negative regulator of sclerotial production (PubMed:29247055). Regulates also the production of secondary metabolites such as aflatoxin, but also the indole-tetramic acid mycotoxin cyclopiazonic acid (CPA) and ustiloxin, an inhibitor of microtubule assembly (PubMed:29247055). Diminishes colony growth and affects conidiation (PubMed:29247055). Decrease in the expression of transcription factors brlA and wetA, components of the central regulatory pathway essential for conidiophore formation (PubMed:29247055). Increases the expression of nsdC, encoding a transcription factor necessary for normal sclerotial production, ans subsequent production of sclerotia (PubMed:29247055). Increases also the production of aflatoxinvia the induction of aflatoxin cluster regulatory genes aflR, aflJ and ver1 (PubMed:29247055). Dicreases the expression of the polyketide synthase-nonribosomal peptide synthetase (PKS/NRPS) gene (AFLA_139490), essential in the synthesis of cyclopiazonic acid (CPA), and of ustD, involved in the production of ustiloxin (PubMed:29247055). Belongs to the 14-3-3 family.
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D4GUZ4
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MPGLLSDILAWVVIGTFVAGAVANGRDRELGRRVMTAAWVLFALFWLQLIPHFTLVHKSYIEGLLTIAAVPASLYAGWLLYNGRDTLFVLSRAVAAMGVVYLPFETIPAFTLLGATVPAPRGVLMETVAAQTRFLIESLGYTPQMIVGDQGYLNTFLWMQGSHRLEISVVLACTGLGSIAIFAGLIAAVDAPMGRKLRGLAIAVPIIYALNLLRTTFIAISVGKQYFHLFVDEVLFLFGSSDPYMVSFFISDRIISQALAVVALVGVTYLVVHEVPELLTVIEDVLYMVTGDEYDLRNELGLD
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Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the archaeosortase and its substrate, which is then transferred and covalently attached to the cell membrane (Probable). This sortase recognizes a tripartite structure consisting of a conserved Pro-Gly-Phe (PGF) motif, followed by a transmembrane alpha helix domain and a cluster of basic residues, usually at the C-terminus of target proteins (Probable). Confirmed substrates include the cell surface S-layer glycoprotein Csg and HVO_0405 (PubMed:23651326, PubMed:26712937, PubMed:28069824). ArtA is required for the C-terminal processing of Csg and for its lipidation and attachment to the archaeal plasma membrane (PubMed:23651326, PubMed:26712937). It is also required for the processing of HVO_0405, which contains an atypical central tripartite structure (PubMed:28069824). Deletion of the gene results in poor growth, especially under low-salt conditions, alterations in cell shape and in the S-layer, impaired motility and impaired conjugation. Belongs to the exosortase/archaeosortase family. Archaeosortase A subfamily.
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Q3IS61
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MSLLEAIAELHVIPYTDVLAWVVMAAFIAGVAADYRDNLLAARRLTAGAWWLFAVFWFVLIQHFAFVHRSVVQTVLILIAVPACLYVGWLVFAGRDSLLTLSRAVAFMTVIYLPFETSELARGLLIEAVAFQTATVIDALSLADGMEYMQDPDEGSTLMNTFWFPETGRASRVVFECTGIGAMSIFGGLIAAVNAPLRRKAVGIALSISIIWVLNIGRNVFIALANGYQWFAYSWLEGPIMALFGLTDPARVSFFVADRVLAQLLAVVALAGLAWFIARWVPELLDIAEELLSIVGIDVELHHPSVDRTDTDPAD
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Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the archaeosortase and its substrate, which is then transferred and covalently attached to the cell membrane. Belongs to the exosortase/archaeosortase family. Archaeosortase A subfamily.
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P81329
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MGNKNAIYILRFLIYFFIFYYILKMLEGNIMDLLTITLSKLLNLKFYKNEIIVGKNIIEISSPCTCSLEMALFLGYIFGTPDVPIKYKISYSVFGLSIITISNILRIILIINYSNMINYNVVHDVISFIIFPIALFLNWFWIYLLKMKKIIMFK
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Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the archaeosortase and its substrate, which is then transferred and covalently attached to the cell membrane. Belongs to the exosortase/archaeosortase family. Archaeosortase D subfamily.
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Q60336
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MGSLLMERNFMVEDTFTNGKLSKKEKILFLIKFYIIFLVVFFILSYFGKYLIGIVTYLSYIFTKIIISDARLADNFIYLPNNTVEVVEECTGSFLIAGLLALIIVYSKNIKEFIIGIFFVLLAFFVNIFRIVLICYLVNMHPESSYLYHEIAGYGVILTLVPVLVIGYLKIIEKYRHSSNKSHL
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Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the archaeosortase and its substrate, which is then transferred and covalently attached to the cell membrane. Belongs to the exosortase/archaeosortase family. Archaeosortase E subfamily.
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P77640
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MKKVLIAALIAGFSLSATAAETIRFATEASYPPFESIDANNQIVGFDVDLAQALCKEIDATCTFSNQAFDSLIPSLKFRRVEAVMAGMDITPEREKQVLFTTPYYDNSALFVGQQGKYTSVDQLKGKKVGVQNGTTHQKFIMDKHPEITTVPYDSYQNAKLDLQNGRIDGVFGDTAVVTEWLKDNPKLAAVGDKVTDKDYFGTGLGIAVRQGNTELQQKLNTALEKVKKDGTYETIYNKWFQK
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Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. The complex is composed of two ATP-binding proteins (ArtP), two transmembrane proteins (ArtM and ArtQ) and two solute-binding proteins (ArtJ and ArtI). Belongs to the bacterial solute-binding protein 3 family.
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P45091
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MKKTLLTAILLGASVAASAQELTFAMQPSYPPFETTNAKGEIIGFDVDVTNAICQEIQATCKFKSETFDALIPNLKAKRFDAAISAIDITDARAKQVLFSDAYYDSSASYVALKGKATLESAKNIGVQNGTTFQQYTVAETKQYSPKSYASLQNAILDLKSGRIDIIFGDTAVLADMISKEPEIQFIGEKVTNKKYFGNGLGIAMHKSNKDLAAQLNKGLAAIKANGEYQKIYDKWITK
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Part of the ABC transporter complex ArtPIQM involved in arginine transport. The complex is composed of two ATP-binding proteins (ArtP), two transmembrane proteins (ArtM and ArtQ) and a solute-binding protein (ArtI). Belongs to the bacterial solute-binding protein 3 family.
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Q9JS59
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MIKQIGRFFRAFIFIMPLSLTSCESKIDRNRIWIVGTNATYPPFEYVDAQGEVVGFDIDLAKAISEKLGKQLEVREFAFDALILNLKKHRIDAILAGMSITPSRQKEIALLPYYGDEVQELMVVSKRSLETPVLPLTQYSSVAVQTGTFQEHYLLSQPGICVRSFDSTLEVIMEVRYGKSPVAVLEPSVGRVVLKDFPNLVATRLELPPECWVLGCGLGVAKDRPEEIQTIQQAITDLKSEGVIQSLTKKWQLSEVAYE
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Probably part of an ABC transporter complex involved in arginine transport. Binds arginine. Interacts with host epithelial cells, suggesting a role in host-cell adhesion during infection. Was identified as a potential vaccine component. In vitro, induces antibodies capable of neutralizing the infectivity of C.pneumoniae. This protein, although well conserved among chlamydial species, shows species-specific immunogenicity. Belongs to the bacterial solute-binding protein 3 family. Truncated N-terminus.
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O84385
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MCIKRKKTWIAFLAVVCSFCLTGCLKEGGDSNSEKFIVGTNATYPPFEFVDKRGEVVGFDIDLAREISNKLGKTLDVREFSFDALILNLKQHRIDAVITGMSITPSRLKEILMIPYYGEEIKHLVLVFKGENKHPLPLTQYRSVAVQTGTYQEAYLQSLSEVHIRSFDSTLEVLMEVMHGKSPVAVLEPSIAQVVLKDFPALSTATIDLPEDQWVLGYGIGVASDRPALALKIEAAVQEIRKEGVLAELEQKWGLNN
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Probably part of an ABC transporter complex involved in arginine transport. Binds arginine (By similarity). Interacts with host epithelial cells, suggesting a role in host-cell adhesion during infection. Does not induce neutralizing antibodies. This protein, although well conserved among chlamydial species, shows species-specific immunogenicity. Belongs to the bacterial solute-binding protein 3 family.
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P77547
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MKKLVLAALLASFTFGASAAEKINFGVSATYPPFESIGANNEIVGFDIDLAKALCKQMQAECTFTNHAFDSLIPSLKFRKYDAVISGMDITPERSKQVSFTTPYYENSAVVIAKKDTYKTFADLKGKRIGMENGTTHQKYIQDQHPEVKTVSYDSYQNAFIDLKNGRIDGVFGDTAVVNEWLKTNPQLGVATEKVTDPQYFGTGLGIAVRPDNKALLEKLNNALAAIKADGTYQKISDQWFPQ
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Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Binds L-arginine with high affinity. The complex is composed of two ATP-binding proteins (ArtP), two transmembrane proteins (ArtM and ArtQ) and two solute-binding proteins (ArtJ and ArtI). Belongs to the bacterial solute-binding protein 3 family.
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P17720
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ATEGARNIGQSAPEGKVQMDCPSRHNFDPECEKAFVEHIHLELASSYHAWSMWAFYARDCKAAVGMTRLCEWASHVSAQRARRMAAYVLTRGGHVDYKEIPAPKKQGWDNFEDAFSHCVANKKRILTSLQSLYQCCQSKDAHCSNFIQTDMMDEVIAWNKFLSDCLSNLHCIGSQGMGPWVFDRWLARIVMSKFKHPKIPSLSTSDLESNIPNELFDAEGDMVRAIKKL
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Cyst. Artemin is elongation factor-associated and self-associating. Belongs to the ferritin family.
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P54537
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MIKVEKLSKSFGKHEVLKNISTTIAEGEVVAVIGPSGSGKSTFLRCLNLLEKPNGGTITIKDTEITKPKTNTLKVRENIGMVFQHFHLFPHKTVLENIMYAPVNVKKESKQAAQEKAEDLLRKVGLFEKRNDYPNRLSGGQKQRVAIARALAMNPDIMLFDEPTSALDPEMVKEVLQVMKELVETGMTMVIVTHEMGFAKEVADRVLFMDQGMIVEDGNPKEFFMSPKSKRAQDFLEKIL
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Part of a binding-protein-dependent transport system for arginine. Probably responsible for energy coupling to the transport system. Impaired growth on arginine as the nitrogen source. Belongs to the ABC transporter superfamily.
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P77311
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MFEYLPELMKGLHTSLTLTVASLIVALILALIFTIILTLKTPVLVWLVRGYITLFTGTPLLVQIFLIYYGPGQFPTLQEYPALWHLLSEPWLCALIALSLNSAAYTTQLFYGAIRAIPEGQWQSCSALGMSKKDTLAILLPYAFKRSLSSYSNEVVLVFKSTSLAYTITLMEVMGYSQLLYGRTYDVMVFGAAGIIYLVVNGLLTLMMRLIERKALAFERRN
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Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Probably responsible for the translocation of the substrate across the membrane (By similarity). The complex is composed of two ATP-binding proteins (ArtP), two transmembrane proteins (ArtM and ArtQ) and two solute-binding proteins (ArtJ and ArtI). Belongs to the binding-protein-dependent transport system permease family. HisMQ subfamily.
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P45089
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MFQEYLSVIVKGIPTSLLLTVVSLLIAFFLALFLTFLLSMENKWIKSAVNLYLTLFTGTPLLVQFFLIYAGPGQFQWIIDSPLWYVLSNAWFCAALALALNSAAYSTQLFHGAVKAIPKGQWESCGALGLNRIQTLKILIPYALKRALPSYSNEIILVFKGTALASTITIMDIMGYARQLYGTEYDALTIYGIAGGIYLIITGIATLLLRKLEKKVLAFERFEVSKA
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Part of the ABC transporter complex ArtPIQM involved in arginine transport. Probably responsible for the translocation of the substrate across the membrane (By similarity). The complex is composed of two ATP-binding proteins (ArtP), two transmembrane proteins (ArtM and ArtQ) and a solute-binding protein (ArtI). Belongs to the binding-protein-dependent transport system permease family. HisMQ subfamily.
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Q8IMC5
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MFWHLLCVPNDENASAPDDGNQSCQPSSKQDQYLSPNRNCQKNLLRLYPPPPSKPPPLVGAILQTRLLHQISPSAIADADADLNAVGELLYPNVLQRSATLPAKHNRLGVRSRVTFKVPSSNLPAQDSYSHQPRNQVAVAAKDGILVDVKAKESVKMTSEDLLQPGHVVKERWKVVRKIGGGGFGEIYEGQDLITREQVALKVESARQPKQVLKMEVAVLKKLQGKEHVCRFIGCGRNDRFNYVVMQLQGKNLAELRRAQPRGAFSLSTTLRLGLQILKAIESIHSVGFLHRDIKPSNFSVGRLPYNCRRVYMLDFGLARQYTTGTGEVRCPRAAAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVNGQLPWRKIKDKEQVGLTKEKYDHRILLKHLPSDLKQFLEHIQSLTYGDRPDYAMLIGLFERCMKRRGVKESDPYDWEKVDSTAIGNISATGNPSIPIKSDYMHGNITQMTVAASNASGTEYIRKRAEIETAHITATDPLNIKEKVDKNCNATSLAQPAKGSGEPMVQHGNAANNQNITSKGLQQQSTLTNSQVAIANIQSAPSMIEREDVQYTKLEEGAPTKFITMKPNGECDNVDIAAKCIFEQKHVEANDDIVGRASLSGVEQHYKSQIKKHNSPEIANKQIQRTGTVTNDKTSEVNRSTEEQKSTFGRLRVLTAPPMSVHDLPSGGGHSHQVSDLSGKQDPYAATSNAAPIGINSSSTKFGSQHGQIFGLAAMPPINRRSATSTNLRPSSSASQRINSGSTIGGAVGNGSNTARSSVAGDHSVTQFALIDDENVSALQQVTKGGALTLASQWKSQFDDSEDTTDNEWNREHQLQPNLEQLIKLDISLPLNEAKPFPQHGVAGTGKLINPPGEAKGRPKRYTLNITGIENYEALRISIPNCWSEPAMGNVLRKGLEPPAVQQAAFDDTVYRMDIARNVCVRETYSEITHLARPSTSSVLRNRLPSPFKKDSALQLNSTNDSLDKSRHRNSLPNVSVNDIFDDLQMKLNLDLGSAIQENNCCISGRLEIRVIPKDTSHPDDSVYYDAMGAVKNTPTANEGHDHSDQAVNNCDEMEATSAVIAFPNKSISKIMSPPGRDATEERTGASLCSLYSAGVNKLKLNGNTAPRTQFKKGSTDGFGENESEFDFPLLNPSKIPVRQSKCASWAGADFISASKPLESAEVPQEIPYHPQSDTTYSVIDSIPVRKTTYSIALECPPNISDLTPGLSYFYCNIVVPLRLFSILLTES
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Probable serine/threonine protein kinase. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Interacts with Mtor. Found in the cytoplasm during interphase. Localizes to the mitotic spindle in dividing cells. Detected in larval brain. Detected at low levels throughout development. Highest expression levels are seen in embryos. Embryonic lethal. Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family.
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Q6ZUL6
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MLMSWSPEECKGQGEPLDDRHPLCARLVEKPSRGSEEHLKSGPGPIVTRTASGPALAFWQAVLAGDVGCVSRILADSSTGLAPDSVFDTSDPERWRDFRFNIRALRLWSLTYEEELTTPLHVAASRGHTEVLRLLLRRRARPDSAPGGRTALHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPGTLECAELLLRFGARVDGRSEEEEETPLHVAARLGHVELADLLLRRGACPDARNAEGWTPLLAACDVRCQSITDAEATTARCLQLCSLLLSAGADADAADQDKQRPLHLACRRGHAAVVELLLSCGVSANTMDYGGHTPLHCALQGPAAALAQSPEHVVRALLNHGAVRVWPGALPKVLERWSTCPRTIEVLMNTYSVVQLPEEAVGLVTPETLQKHQRFYSSLFALVRQPRSLQHLSRCALRSHLEGSLPQALPRLPLPPRLLRYLQLDFEGVLY
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. In the ciliary body, it is detected in the cytoplasm and perinuclear region of the pigmented ciliary epithelial layer. In the retina, it is detected in the nuclei of retinal ganglion cells. Expressed in the eye. The highest expression is observed in the iris, with moderate levels in the trabecular meshwork (TM), the lamina, and the optic nerve; slightly lower levels in the ciliary body, retina, and choroid; and very low levels in the lens. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. The disease is caused by variants affecting the gene represented in this entry. Belongs to the ankyrin SOCS box (ASB) family.
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B2RUP6
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MLMSWSPEECRDQGEPQGDRYSLCAKLVEKPDRGSEEHLEPGLGPIIIRSASGPTLAFWQAVLVGDVGSVSRILSDSSTGLAPDSIFDTSDPERWRDYRFNIRALRLWSLTYEEELTTPLHVAASRGHTEVLELLLRRRAKPDSAPGGRTALHEACSAGHAACVRVLLVAGADPNTLDQDGKRPLHLCRGPGILECVELLLKFGAQVDGRTEDEEETPLHIAARLGHVELADLLLRWGACPDVRNSEGWTPLLAACDIRCQSPKDAEATTNRCFQLCRLLLSVGADADAANQDKQRPLHLACRHGHSAVVQLLLSCGVNANAMDYGGHTPLHCALLGPTTAVAHSPEHTVRDLLNHGAVRVWPGALPKVLDRWCMSPRTIEVLMNTYRVVQLPEEAKGLVPPEILQKYHGFYSSLFALVRQPRSLQHLCRCALRSHLEGCLPHALPRLPLPPRMLRFLQLDFEDLLY
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q3SZE4
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MEDGSVSYGFKNIFITMFATFFFFKLLIKVFLALLTHFYIVKGNRKEAARIAEEIFGEISDCWADRSPLHEAAAQGRLLALKTLIAQGVNVNLVTINRVSSLHEACLGGHVACAKALLENGAHVNGVTVHGATPLFNACCSGSAACVNVLLEFGAKAQLEVHLASPIHEAVKRGNRECMEILLANNVNIDQEVPHLGTPLYAACTYQRLDCVKKLLELGANVNHGQWLDTPLHAAAKQNSVEIIHLLIDYGANLKCKNAQGQSALDLAAPKSSVEQALLLREGPPALSQLCRLCVRKCLGRNCHKTIHKLYLPDPLEKFLLYQ
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q7Z667
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MEDGPVFYGFKNIFITMFATFFFFKLLIKVFLALLTHFYIVKGNRKEAARIAEEIYGGISDCWADRSPLHEAAAQGRLLALKTLIAQGVNVNLVTINRVSSLHEACLGGHVACAKALLENGAHVNGVTVHGATPLFNACCSGSAACVNVLLEFGAKAQLEVHLASPIHEAVKRGHRECMEILLANNVNIDHEVPQLGTPLYVACTYQRVDCVKKLLELGASVDHGQWLDTPLHAAARQSNVEVIHLLTDYGANLKRRNAQGKSALDLAAPKSSVEQALLLREGPPALSQLCRLCVRKCLGRACHQAIHKLHLPEPLERFLLYQ
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q9D0V1
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MEDAPAFYGFKNIFLTMFATFFFFKLLIKVFLALLTHFYIVKGNRKEAARIAEEIYGGLSDCWADRSPLHEAAAQGRLLALKTLIAQGINVNLVTINRVSSLHEACLGGHVACAKALLENGAHVNAQTVHGATPLFNACCSGSAACVNVLLEFGAKAQLEIYLASPIHEAVKRGHRECMEILLTKDVNIEQEVPQLGTPLYVACTYQRVDCVKKLLELGASVDHGQWLDTPLHAAVRQSSVEVINLLTVYGANLNLRNAQGKSALDLAVPKSSVRQALLLHEGPPALSQLCRLCVRKCLGRTCHHAIYALGLPESLEKFLLYQ
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q5RFS1
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MEDGPVFYGFKNIFITMFATFFFFKLLIKVFLALLTHFYIVKGNRKEAARIAEEIYGGISDCWADRSPLHEAAAQGRLLALKTLIAQGVNVNLVTINRVSSLHEACLGGHVACAKALLENGAHVNGVTVHGATPLFNACCSGSAACVNVLLEFGAKAQFEVHLASPIHEAVKRGHRECMEILLANNVNIDHEVPQLGTPLYVACTYQRVDCVKKLLELGASVDHGQWLDTPLHAAARQSNVEVIHLLTDYGANLKRRNAQGKSALDLAAPKSSVEQALLLCEGPPALSQLCRLCVRKCLGRACHQAIHKLHLPEPLERFLLYQ
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q8N8F5
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MNLMDITKIFSLLQPDKEEEDTDTEEKQALNQAVYDNDSYTLDQLLRQERYKRFINSRSGWGVPGTPLRLAASYGHLSCLQVLLAHGADVDSLDVKAQTPLFTAVSHGHLDCVRVLLEAGASPGGSIYNNCSPVLTAARDGAVAILQELLDHGAEANVKAKLPVWASNIASCSGPLYLAAVYGHLDCFRLLLLHGADPDYNCTDQGLLARVPRPRTLLEICLHHNCEPEYIQLLIDFGANIYLPSLSLDLTSQDDKGIALLLQARATPRSLLSQVRLVVRRALCQAGQPQAINQLDIPPMLISYLKHQL
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Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. Interacts with CUL5 and RNF7. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q9D738
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MNLMDIAKIFSLLQPEKEEEDTGTGEKQALNQAVYDNDSCTLDHLLHQERYKRFINSRSGWGIPGTPLRLAASYGHLNCVKVLLEHGADVDSLDVKAQTPLFTAVSHGHLECVRMLLEAGACPSGSIYNNCSPVLTASRDGAFAILQELLGHGAEANVKAKLPVWASNIASCSGPLYLAAVYGHLDCFRLLLLYGADPDYNCTDQGLLSRVPQPRTLLEICLHHNCEPEYIQLLIDFGANIYLPSLPVDPTSQDDKGIKLLLQARATPRSLLSQTRLVIRRSLCRANQSQATDQLDIPPVLISYLKHQ
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Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. Interacts with CUL5 and RNF7. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q9H8Z1
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MEPRAADGCFLGDVGFWVERTPVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIECVKLLLSYGAKVNPPLYTASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVNAAKLHETALHHAAKVKNVDLIEMLIEFGGNIYARDNRGKKPSDYTWSSSAPAKCFEYYEKTPLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYLSYN
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q8VBX0
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MEPRAGDGCFLGDVGFWVERTPVHEAAQRGESLQLQQLIDSGACVNQVTVDSITPLHAASLQGQAQCVQLLLAAGAQVDARNIDGSTPLCDACASGSIECVKLLLSYGAKVNPPLYTASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVNAAKLHETALHHAAKVKNVDLIEMLIEFGGNIYARDNRGKKPSDYTWSSSAPAKCFEYYEKTPLSLSQLCRVSLRKATGVRGLEKVAKLNIPPRLIDYLSYN
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q92816
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MSDANKAAIAAEKEALNLKLPPIVHLPENIGVDTPTQSKLLKYRRSKEQQQKINQLVIDGAKRNLDRTLGKRTPLLPPPDYPQTMTSEMKKKGFNYIYMKQCVESSPLVPIQQEWLDHMLRLIPESLKEGKEREELLESLINEVSSDFENSMKRYLVQSVLVKPPVKSLEDEGGPLPESPVGLDYSNPWHSSYVQARNQIFSNLHIIHPTMKMLLDLGYTTFADTVLLDFTGIRAKGPIDCESLKTDLSIQTRNAEEKIMNTWYPKVINLFTKKEALEGVKPEKLDAFYSCVSTLMSNQLKDLLRRTVEGFVKLFDPKDQQRLPIFKIELTFDDDKMEFYPTFQDLEDNVLSLVERIAEALQNVQTIPSWLSGTSTPVNLDTELPEHVLHWAVDTLKAAVHRNLEGARKHYETYVEKYNWLLDGTAVENIETFQTEDHTFDEYTEFIEKFLSLASEIMLLPQWIHYTMVRLDCEDLKTGLTNKAKAFANILLNDIASKYRKENECICSEFEAIKEHALKVPETTEEMMDLISYVEKARTVGIEELILRIQESKRQMSYFLDVFLFPQEDLALNATVLMWPRKINPIFDENDELIENAKHKKENELMAKREKLILEIEKESRRMEEFTEFAELERMQQYVTDVRQLQKRIQESEEAVQFINKEEELFKWELTKYPELDKLKVNIEPYQKFFNFVLKWQRSEKRWMDGGFLDLNGESMEADVEEFSREIFKTLKFFQTKLKKELQEKRKAARKRSLEEEKIEEEPKDNATITMCRMRARHWKQISEIVGYDLTPDSGTTLRKVLKLNLTPYLEQFEVISAGASKEFSLEKAMNTMIGTWEDIAFHISLYRDTGVCILSSVDEIQAILDDQIIKTQTMRGSPFIKPFEHEIKAWEDRLIRIQETIDEWLKVQAQWLYLEPIFCSEDIMQQMPEEGRQFQTVDRHWRDIMKFCAKDPKVLAATSLTGLLEKLQNCNELLEKIMKGLNAYLEKKRLFFPRFFFLSNDEMLEILSETKDPLRVQPHLKKCFEGIAKLEFLPNLDIKAMYSSEGERVELIALISTSAARGAVEKWLIQVEDLMLRSVHDVIAAARLAYPESARRDWVREWPGQVVLCISQMFWTSETQEVISGGTEGLKKYYKELQNQLNEIVELVRGKLSKQTRTTLGALVTIDVHARDVVMDMIKMGVSHDTDFLWLAQLRYYWENENARVRIINCNVKYAYEYLGNSPRLVITPLTDRCYRTLIGAFYLNLGGAPEGPAGTGKTETTKDLAKALAVQCVVFNCSDGLDYLAMGKFFKGLASSGAWACFDEFNRIELEVLSVVAQQILCIQRAIQQKLVVFVFEGTELKLNPNCFVAITMNPGYAGRSELPDNLKVLFRTVAMMVPNYALIAEISLYSYGFLNARPLSVKIVMTYRLCSEQLSSQFHYDYGMRAVKAVLVAAGNLKLKYPNENEDILLLRSIKDVNEPKFLSHDIPLFNGITSDLFPGIKLPEADYHEFLECAHEACNVHNLQPVKFFLEKIIQTYEMMIVRHGFMLVGEPFAAKTKVLHVLADTLTLMNEHGYGEEEKVIYRTVNPKSITMGQLFGQFDPVSHEWTDGIVANTFREFALSETPDRKWVVFDGPIDTLWIESMNTVLDDNKKLCLMSGEIIQMSPQMSLIFETMDLSQASPATVSRCGMIYLEPSQLGWEPLVSSWLNSLKGPLCEPEYQALLRGLFAWLIPPSLNQRVELFQLNYLYTTIVSKILKILITFRISNYFKYVPLKTQCTFIKFFLHQQACFIFSLIWSIGGSCDTDGRRVFDTFIRLIILGKDDENPVPDSVGKWECPFDEKGLVYDYMYELKNKGRWVHWNELIKNTNLGDKQIKIQDIIVPTMDTIRYTFLMDLSITYAKPLLFVGPTGTGKSVYVKDKLMNHLEKDQYFPFYINLSARTSANQVQNIIMARLDKRRKGVFGPPMGKKCIIFIDDMNMPALEKYGAQPPIELLRQFFDCGHWYDLKDTSKITLVDIELIAAMGPPGGGRNPVTPRCIRHFNICSINSFSDETMVRIFSSIVAFYLRTHEFPPEYFVIGNQIVNGTMEIYKQSVENLLPTPTKSHYTFNLRDFSRVIRGCLLIERDAVANKHTMIRLFVHEVLRVFYDRLINDDDRRWLFQLTKTVIKDHFKESFHSIFSHLRKQNAPVTEEDLRNLMFGDYMNPDLEGDDRVYIEIPNIHHFSDVVDQCLDEYNQTHKTRMNLVIFRYVLEHLSRICRVLKQSGGNALLVGLGGSGRQSLTRLATSMAKMHIFQPEISKSYGMNEWREDMKSFIAVPVTNRIVDNKSKILEKRLRYLNDHFTYNLYCNICRSLFEKDKLLFSFLLCANLLLARKEIEYQELMFLLTGGVSLKSAEKNPDPTWLQDKSWEEICRASEFPAFRGLRQHFCEHIYEWREIYDSKEPHNAKFPAPMDKNLNELQKIIILRCLRPDKITPAITNYVTDKLGKKFVEPPPFDLTKSYLDSNCTIPLIFVLSPGADPMASLLKFANDKSMSGNKFQAISLGQGQGPIAAKMIKAAIEEGTWVCLQNCHLAVSWMPMLEKICEDFTSETCNSSFRLWLTSYPSSKFPVTILQNGVKMTNEPPTGLRLNLLQSYLTDPVSDPEFFKGCRGKELAWEKLLFGVCFFHALVQERKKFGPLGWNIPYGFNESDLRISIRQLQLFINEYDTIPFEAISYLTGECNYGGRVTDDWDRRLLLTMLADFYNLYIVENPHYKFSPSGNYFAPPKGTYEDYIEFIKKLPFTQHPEIFGLHENVDISKDLQQTKTLFESLLLTQGGSKQTGASGSTDQILLEITKDILNKLPSDFDIEMALRKYPVRYEESMNTVLVQEMERFNNLIITIRNTLRDLEKAIKGVVVMDSALEALSGSLLVGKVPEIWAKRSYPSLKPLGSYITDFLARLNFLQDWYNSGKPCVFWLSGFFFTQAFLTGAMQNYARKYTTPIDLLGYEFEVIPSDTSDTSPEDGVYIHGLYLDGARWDRESGLLAEQYPKLLFDLMPIIWIKPTQKSRIIKSDAYVCPLYKTSERKGTLSTTGHSTNFVIAMLLKTDQPTRHWIKRGVALLCQLDD
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Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). Consists of at least two heavy chains and a number of intermediate and light chains. Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function (By similarity). Belongs to the dynein heavy chain family. Was originally derived from a readthrough transcript including ASB14 and DNAH12. DNHD2 was thought to be a distinct gene.
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Q8VHS7
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MSDPNKTAIAAEKEALNLKLPPIVQPPKNIGVDTPKQSELLKYRRSKEQQKKINQLVISGAKKSLDKTLDKRIPPLPEPDFPPTMTSEIKKRGLNYIFMKQCVENSPIVPIQSQWLDNMLMLVPEHLKEGEKSEELLGSLIDEVSMDYEKSMKRYLVQSVLVKPPVKWLEDEGGPLPESPEGLDYSNPWHSNFVQARSQILANLHIVHPTMKMLLELGYTAFAKIILLDLTGIRARGPIDCEALRNDLSIQARKSEEKIMNTWYPKVINLFTKKEALEGIKTEKLDSFYNCVSILMSNQLKDLLWRTVEEFIKLFDPRYLNRLPIFKMELTFDDDKMEFYPTFQDLEDVVLGLIERISETLQTVQTVPSWLSGTSSPVNLDTEIPEHVLQWALCTLRTAIQHNLEGAKAHHKTYVTKYNWLLDGTATKMIQRFQAENHTFDEYTEFIEKFFNLASEIMLLPQWAHYPMVRLDCEDLKIGLTNKARAFANILLNDIASKHRKENESICSEFEAIRDHALRVPETTEEMMELIAFVERARTVGILDLALRIQESKRQMSYFLDALLMSQEDLNLNATVLLWPTKITPVFDENDELIENAKHAKENELIAKREKLILEIEKESRRMEEFTEFAELDRMHQYVADVRQLQKRIQESEEAVQFINKEEELFKWELTKYPELEKLKVTIEPYQKFFNFVLKWQRTEKRWMDGGFLDLNGESMEADIDDFSREVFRTLKFFHAKQKKELQERRKAARKRSLMEEKPEEEPKENPTITMMRARHWKQMSEIVGYDLTPDSGTTLRKVLKLNLSPYLESFEVISAGASKEFSLERSMNAMIATWDDISFHISLYRDTGIGILSSVDEIQAILDDQIIKTQTMRGSPFIKPFENEIKAWEDRLIRIQETIDEWLKVQAQWLYLEPIFCSEDIMQQMPEEGRQFQTVDRHWKDIMKFCAKDPKVLAATSLTGLLEKLQNCNDLLEKIMKGLNAYLEKKRLFFPRFFFLSNDEMLEILSETKDPLRVQPHLKKCFEGIAKLEFLANLDIKAMYSSEGERVELIALISTTAARGAVEKWLIQVEDLMLRSIRDVIAASRLAYPESARKDWVREWPGQVVLCVSQMFWTSETQEIISGGTEGLKKYYKELQYQLNDIVELVRGKLSKQTRITLGALVTIDVHARDVVMDMIEMGVSHDTDFQWLAQLRYYWEYENARVRIINCNVKYAYEYLGNSPRLVITPLTDRCYRTLIGAFYLNLGGAPEGPAGTGKTETTKDLAKALAVQCVVFNCSDGLDYLAMGKFFKGLASSGAWACFDEFNRIELEVLSVVAQQILCIQRAIQQKLEAFVFEGTELRLNPNCFVAITMNPGYAGRSELPDNLKVLFRTVAMMVPNYALIAEISLYSYGFLNAKPLSVKIVMTYRLCSEQLSSQFHYDYGMRAVKAVLVAAGNLKLKYPNENEDILLLRSIKDVNEPKFLSHDIPLFNGITSDLFPGIKLPEADYKEFLECAHETCQTHNLQPVKFFLEKIIQTYEMMIVRHGFMLVGEPFAAKTEVLHVLADTLTLMNERNYGDEEKVMYRTVNPKSITMGQLFGQFDPVSHEWTDGIVANTFREFALAESPDRKWVVFDGPIDTLWIESMNTVLDDNKKLCLMSGEIIQMSPQMSLIFETMDLSQASPATVSRCGMIYLEPSQLGWEPLVASWLNSLKEPLSELEHQNLLKELFDWLVPPSLVFRRKKCKFLSLHDLSKYFKQVLIYYILVVSPKFSLKSNHYKIFFHQQASFIFSLIWSIGASCDTDGRLAFDAFLRTAVSGRNEEAPMPVSISKWECPFDEKGLVYDYMYELRNRGRWIHWNELIKSSDLEDKRAKIQDIIVPTMDTIRYTFLMDLSITSAKPLLFVGPTGTGKSVYVKDKLMNHLEKEKYFPFYVNFSARTSANQVQNIIMARLDKRRKGVFGPPMGKKCVIFIDDMNMPSLEKYGAQPPIELLRQFFDCGHWYDLKDTSKITLIDIELIAAMGPPGGGRNAVTPRFIRHFNICTINTFSDETMVRIFSSIMAFYLRTHAFSPEYFVLGNQIVSGTMEVYKQSMGNLLPTPAKSHYTFNLRDFSRVIRGCLLIEKDAIESKHTMIRLFVHEVLRVFYDRLINDEDRNWLFLLIKNVIKDHFKESFDTVFHHLRNGNAPVTEEDLRNLMFGDYMNPDLEGDDRVYIEIPDIHHFNEVVDQCLDEYNQTHKRRMNLVVFRYVLEHLSRICRILKQSGGNALLIGLGGSGRQSLTKLATSMAKMQIFQPEISKSYGMNEWREDIKGFLLLIIIWAVVESLSKILEKRLRYLNDHFTYNLYCNICRSLFEKDKLLFSFLLCANLLLAKKEIEYQELMFLLTGGVSLKSAEKNPDPDWLQDKSWEEICRASELPVFHGLREHFCNYIYLWEEIYDSKEPHNMKFPEPMDKTLNELQKIIILRCLRPDKITPAITNYVTDKLGKKFVEPPPFDLTKSYLDSNCTIPLVFVLSPGADPMASLLKFANDKSMSGNKFQAISLGQGQGPVASKMITAAIEEGTWVCLQNCHLAVSWMPTLEKICEDFSPETCNPTFRLWLTSYPSPKFPVTILQNGVKMTNEPPTGLRLNLLQSYLSDPISDTQFFKGCPGKELAWEKLLFGVCFFHALVQERKKFGPLGWNIPYGFNESDLRISVRQLQLFINEYDTIPFEAISYLTGECNYGGRVTDDWDRRLLLTMLADFYNSFIIENPHYKFSPSGNYYAPPKGTYDDYIEFIKKLPFTQEPEIFGLHENVDISKDLQQTKVLFESLLLTQGGAKQTGSSGSTDQVLLEITEDILTQLPNDFDIEAALKNYPVRYEESMNTVLVQEMERFNNLIRTIRNTLRDLKKAIKGLVVMDSALEALSGSLLIGKVPEMWAKRSYPSLKPLGSYITDFLARLKFLEDWFSSGKPSVFWISGFFFTQAFLTGAMQNFARKYTIPIDLLGYEFEVIPFDYSDTPPEDGVYIHGLYLDGARWDRFSGLLAEQYPKLLFDLMPIIWIKPNLKIEIVKIEAYICPLYKTSERKGTLSTTGHSTNFVIAMLLKTDQPTQHWIKRGVALLCQLDN
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Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity). Protein modification; protein ubiquitination. Consists of at least two heavy chains and a number of intermediate and light chains. Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function (By similarity). Belongs to the dynein heavy chain family. Was originally derived from a readthrough transcript including ASB14 and DNAH12.
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P0C927
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MDQQSSDEDADTDFDTQIIIQQSLLDAYKPELTGRTPEDERSQSFSSEDYKKIVEAIETVKYSSYPRPSKEDALASFAKYHPAFDEANGSGWLPLHKAAVQLNKNILEITLNASKPSAWEQTTRNGETPLFLAVSSSLLENAHFLLLNGCDPNAKNFEGNSPLLTAVLKDSYDMATLLINHGANVNLRCANERTALHEAAKLGRQDMVKLMLSSGANPDARSSYGFTPLALAAQGGHTETMQLLLQKGRADVHSQASDSSSVLLEAVRGGDPDSVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLVPVTDIAAIKRSGISPLHCAAAGAHPQCLDLLIRAGFDVNFMLDQRVRKHYDDQRKSALYFAVSNGDLSSVKLLLSAGALPNQDPVNCLQIALRMGNYELINLLLRHGANVNYFCRVNPLHFPSALQYTLKDEVMLRMLLNYGYDTERCFDCPHGERVHRCCTFEGWTSTVIKDTMFCEVITLSWLQHLSGKVVRVMLDYVDQVQICSKLKAVLEKQKLWPEIHVILTNPRSLQHLCRLKIRKCMGRLRLRCPVFMSFLPLPNLLKAYVLYKEYDLYGQGSSTGT
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q08DG3
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MDANDDPDEDHLTSYDVQLSIQESIEAGKTVFYPERFVPLSDQNRKLVEAIQQGHILELQEYVKYKYALDEADEKGWFPLHEAVVQPIQQILEVVLDASYKTLWEFKTSDGETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLLAIKRGSYDMVSALLKHNTSLDQPCVKRWSAMHEAAKQGHKDIIALLLNNGGNVHLKDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGSGNIPNRAGHLPIHRAAYEGHYLALKYLIPVTSKHAIQKSGLTPIHSAADGQNAQCLELLIENGFDVNSLLADHISESYDDERKTALYFAVCNNDILCTEILLAAGADPNLDPLNCLLVAVRANNHEIVRLLLAHGANVNCYFMHVNDTRFPSAIQYALNDEVMLRLLLNNGYQVEMCFECMHGDIFGNSFVWSEIEEEVLPGWTSCVIKDNPFCEFITVPWMKHLVGSVIRVLIDYMDYIPLCAKLKSALEVQREWPEIRQILENPCSLKHLCRLKIRRLMGLQRLCQPTLMEKLSLPPTIQRYILFKEYDLYGQELNLP
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q68D37
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MDTNDDPDEDHLTSYDIQLSIQESIEASKTALCPERFVPLSAQNRKLVEAIKQGHIPELQEYVKYKYAMDEADEKGWFPLHEAVVQPIQQILEIVLDASYKTLWEFKTCDGETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPVTSKNAIRKSGLTPIHSAADGQNAQCLELLIENGFDVNTLLADHISQSYDDERKTALYFGVSNNDVHCTEVLLAAGADPNLDPLNCLLVAVRANNYEIVRLLLSHGANVNCYFMHVNDTRFPSVIQYALNDEVMLRLLLNNGYQVEMCFDCMHGDIFGNSFVWSEIQEEVLPGWTSCVIKDNPFCEFITVPWMKHLVGRVTRVLIDYMDYVPLCAKLKSALEVQREWPEIRQILENPCSLKHLCRLKIRRLMGLQKLCQPASVEKLPLPPAIQRYILFKEYDLYGQELKLT
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q8CDP8
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MDINDDSNDDHLASYDIQLCIQESIEASQAIFHPKRLVQLSDQNRKLVEAIRQGRIFELQEYVQYKYALEEADEKGWFPLHEAVVQPIQQILETVLDASYKTLWEFKTCDGETPLTLAVKAGLVENVKTLLDKGVWPNTKNDKGETPLLIAIKRGSYDMVSALIKYNTSLDQPCVKRWSAMHEAAKQGRKDIITLLLNHRGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVFALADDGASVLFEAAGGGNPDCISLLLKYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPVTSKHAIQKSGLTPIHSAAEGQNAQCLELLIENGFDVNALLADHISQSYDDERKTALYFAVSNNDIHCTEVLLAAGADPNLDPLNCLLVAVRANRHEIVRLLLSYGANVNCYFMHVNDTRFPSAIQYALNDEIMLRLLLNNGYQVELCFDCMHGNIFGNSFVWSETEEEGLPGWTSCIIKDNPFCEFITVPWMKHLVGGIVRILIDYMDYVPLCAKLKSVLEVQREWPEIRQIIENPCSLKHLCRLKIRRVMGLQRLCQPASIQMLPLPAAMRRYLLFKEFDLYGQ
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q8WXK0
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MARETFPFTSSMLRSLRLQQEWLEWEDRRRAAAQQCRSRRCPSSPRARLTRPHRSCRDPAVHQALFSGNLQQVQALFQDEEAANMIVETVSNQLAWSAEQGFWVLTPKTKQTAPLAIATARGYTDCARHLIRQGAELDARVGGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLLEAGATVNLAAGESQETPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTACAGAEGPGSCRRHQAAARRLLEAGADARAAGRKRHTPLHNACANGCGGLAELLLRYGARAEVPNGAGHTPMDCALQAVQDSPNWEPEVLFAALLDYGAQPVRPEMLKHCANFPRALEVLLNAYPCVPSCETWVEAVLPELWKEHEAFYSSALCMVNQPRQLQHLARLAVRARLGSRCRQGATRLPLPPLLRDYLLLRVEGCIQ
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q8BYT0
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MAGESFPFTSSTLRALRLQREWLDWEDRRRAAAQQCRRHRDLPCPQAQLLRPRRSCRDPAVHNALFSGDLQQLQILFQDEDAANMIVETVSNQLAWSAEQGFWVLTPKTKQTAPLTIAVARGYTDCARHLILQGAELDARIGGRAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLLEAGASVNVASQESEVTPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAACAGAEGPGSSRQHEAAARQLLEAGADPQAAGRKRHTPLHNACANGCGGLAELLLRHGASPGVTNGAGHTPMDCALQAVQDAPNWEPEVLFAALLDYGAQPVHPEMLKHCANFPRALEVLLNAYPCVPSCDPWVEAVLPELWQEHEAFYSSALSMENQPRQLQHLARLAVRAQLGSHCRQAAAQLPLPPLLRDYLLLGVEGRIQ
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q32KY8
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MSKSSKLCCKTSCPRSNIFCSLVDKVFKRPSLQSLHQWGYHCYEPRVYRTLAKILRYVDLEGFDILLSDYIAFVEKSGCHLEVNFNLEFTEICVNTILYWVFARKGNPDFVELLLKKTKDYVQDRSFNLALIWRTFTPVYCPSPLSGITPLLYVAQTRQSNILKILLQYGILERENNPINIVLTILLYPSRVRIMVDHELVDIEEDAKTCLVLCSRVLSTISIREIEMQLSLGRRPIISNWLDYIPSTRYKDPCELLHLCRITIRAQLLTNNMLPNGIFSLLIPVCLQNYLNLES
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May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family.
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Q9LEU6
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MDNLSFHDGNIFNLLHTRSQDPSHEVDQRMQFHSSLVRRLSQEQELEGHQGCVNALAWNSNGSLLISGSDDLRINIWNYSSRKLLHSIDTGHTANIFCTKFVPETSDELVVSGAGDAEVRLFNTSRLSGRAEDDNAIIPSALYQCHTRRVKKLAVEPGNPNVVWSASEDGTLRQHDFRESTSCPPAGTAHQECRSVLLDLRSGAKRALADPPKQTLSLKSCDISATRPHLLLVGGSDAFARLYDRRMLPPLASSRKRMPPPPCVNYFCPMHLSERGRTNLHLTHVTFSPNGEEVLLSYSGEHVYLMNVNNGICSTGIMQYTPGDVDNLFSFSNNLHDVESPPQVSTTPQNGFHRSSNAATVKKCTELVEIAKWSLEEGTDVFYAIEAANEVLDAHSNDIESALRHECLCTRAALLLKRKWKNDAHMAVRDCHNARRIDASSFKAHYYMSEALQQLGKCKEALDFATAAQHMNPSDADIVAKVESIKRDLQAAGAEKNEETGAGTTRVLSLSDILYRSEANSDSSHDMSRSEREDSDYDEELELDIQTSLSDDEGRDTDSNSMRGSLNLRIHRVGDDKPMENTVDNASSGTASSSQNDRTSYQPEGAIDMKRRYVGHCNVGTDIKQASFLGQRGEYIASGSDDGRWFIWEKQTGRLMKVLVGDESVLNCIQCHPFDSVVATSGIDNTIKIWSPTASVPSIVAGGSAGPATANVVEVMESNQQKLSRNRENPLSVELMQRFRMQEFAEGNFHPFECTQS
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May function as a substrate adapter for CUL4-DDB1 E3 ubiquitin-protein ligase complex (Probable). Negative regulator of fatty acid biosynthetic process and accumulation (PubMed:28663238). Acts as an abscisic acid (ABA) negative regulator (PubMed:26147561). Involved in responses to salt (NaCl) and osmotic (e.g. in response to mannitol and PEG) stresses (PubMed:26147561). Protein modification; protein ubiquitination. Interacts with DDB1; the subcellular localization of this complex depends on farnesylation status (PubMed:26147561). Binds to HDA9 in the cytosol when farnesylated (PubMed:28663238). Excluded from the nucleus when farnesylated at Cys-754. Farnesylated at Cys-754 by FTB/ERA1; this modification triggers an exclusion from the nucleus. Production of 'obese' seeds characterized by increased weight, oil body density and higher fatty acid contents (PubMed:28663238). Increased sensitivity to abscisic acid (ABA) as well as salt (NaCl) and osmotic (e.g. in response to mannitol and PEG) stresses in term of seed germination and roots elongation (PubMed:26147561).
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A6ZQG3
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MTTLASSIEHKTKHLAAPFENDENTWMKKYCCQCKSCKMSVPVQPWLPRFFVFGILCPVFWLVNLLAWWFLQYWQPHELEFHDLQEDEYPGFYEYEAITKRTVIPLKEEVLQEIRVMQNFSDSNSEEYYESKDGMPSSFLNVNTEQVEDENDTLKKYRYAFLKKVAHDVLESHDLLRKTFRNWNLRSLLGLLIDSILIIFVVLLCKKSR
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Required for receptor inhibition of inappropriately expressed a-factor receptor (STE3) in MAT a cells. Inhibits signaling by relocalizing the G protein beta-gamma (STE4-STE18) subunit to intracellular membranes. May also be a mechanism for the down-regulation of the mating pheromone response after the zygotic fusion event, promoting the transition of the new diploid cell to vegetative growth (By similarity). Induced by alpha-pheromone. Repressed by the ALPHA2-MCM1 repressor (By similarity).
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D6VW18
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MTTLASSIEHKTKHLAAPFENDENPWMKKYCCQCKSCKMSVPVQPWLPRFFVFGILCPVFWLVNLLAWWFLQYWQPHELEFHDLQEDEYPGFYEYEAITKRTVIPIKEEVLQEIRVMQNFSDSNSEEYYESKDGMPSSFLNVNTEQVEDENDTLKKYRYAFLKKVAHDVLESHDLLRKTFRDWNLRSLLGLLIDSILIIFVVLLCKKSR
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Required for receptor inhibition of inappropriately expressed a-factor receptor (STE3) in MAT a cells. Inhibits signaling by relocalizing the G protein beta-gamma (STE4-STE18) subunit to intracellular membranes. May also be a mechanism for the down-regulation of the mating pheromone response after the zygotic fusion event, promoting the transition of the new diploid cell to vegetative growth. Induced by alpha-pheromone. Repressed by the ALPHA2-MCM1 repressor.
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Q32LE5
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MNPVVVVHGGGASNISKDRKERVRQGILRAATVGYNILKQGGSAVDAVEGAVTVLEDDPDFNAGCGSVLNENGEVEMDASIMNGKDLSAGAVSAVRCIANPIKLARLVMDKTPHCFLTDQGAARFAAANGIPTIPGQQLVTERSRKRLEKEKLEKDAQKPDCQKNLGTVGAVALDCQGNLAYATSTGGIVNKMPGRVGDTPCVGSGGYADNDIGAVSTTGHGESILKVNLARLALFHVEQGKSLEEAANASLGHMKSKVKGVGGIIMVNKAGEWAVKWTSTSMPWAAAKDGKLHSGIDFGDTSIIDLS
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Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. H2O + L-asparagine = L-aspartate + NH4(+) Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide. Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer. Midpiece of sperm tail. Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. Belongs to the Ntn-hydrolase family.
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Q5BKW9
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MLPVVVVHGGAGHIPKERTEESTIGVKEAARTGYAILQRGGSAVDAVVEAVALMETNPRFNAGRGSVLNIKGEVEMDALVMDGRTLDSGAVSAVRRIANPVQLARLVMEKTKHLCLTAEGASKFARSMGVPEVPEESLITDYAKMRWKKNLEPDANPVECQMGKMGTVGAVAVDMDGNIACATSTGGMINKMEGRVGDTPCVGCGGYADNKIGAVSPTGHGEAIMKVTLSRLVLFHMEQGKTPEEASDLALAYMKERVDGLGGVVVVDHNGTWAARFSSLQMSWAAAQQGKLHFGLFHGDHFTEPVEEHT
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Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. H2O + L-asparagine = L-aspartate + NH4(+) Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide. Heterodimer of an alpha and beta chain produced by autocleavage. Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. Abnormal and deformed fish at 6 dpf. Belongs to the Ntn-hydrolase family.
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Q9VXT7
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MPRPVLLIHGGAGDISDSRIAGKFAGIKQALRSAWGLLSPDNGSGGGSALDAVEAAVRSMELDENFNAGYGSCLNTSGQVELEASLMEGRDLRAGCITLLRDVMHPITVARRLMEKQRHTFLGGAAAQELALATGSERLQPGALVTEGARLTLKEFEDQVAQGKDPFFARTELTDDKPVPKTDPSGETVGAVAMDASGQIVVGTSTGGITGKWPGRIGDTPILGSGTYADNCRGGVSTTGHGETLMRYNLAQRILSAMEYQGLSAQAAADKECREMTKRLGGTGGAIVVGHSGDLGISFTSRRMAWGYVQDGTIFYGIEGQVVHQEPFTLST
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Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. H2O + L-asparagine = L-aspartate + NH4(+) Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide. Heterodimer of an alpha and beta chain produced by autocleavage. Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. Belongs to the Ntn-hydrolase family.
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Q29I93
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MPRPVLLIHGGAGDIPDSRIAGKFKGIKEALRCAWGSLVPASGAKGGALDAVETAVRSMELDENFNAGYGSCLNTDGQVEMEASLMEGQDLRAGCVTLLRDVMHPITVARRLMEKQRHTFIGGEAAQELALSTGSERLPANALVTEGARFTLQQFKEQLTQGKDPFFARTELAAEQKTDPSGETVGAVAMDHNGQIVVGTSTGGITGKWPGRIGDTPILGSGTYADNARGGVSTTGHGETIMRYNLAQRILAAIEHKGMSAQAAADQECREMTRRIGGTGGAIVVGHAGDLGISFTSQRMAWGYIQDDTIFYGIEGQVVHQEPLS
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Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. H2O + L-asparagine = L-aspartate + NH4(+) Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide. Heterodimer of an alpha and beta chain produced by autocleavage. Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. Belongs to the Ntn-hydrolase family.
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Q9H6F7
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MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTTITDLP
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Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. H2O + L-asparagine = L-aspartate + NH4(+) Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide. Glycine accelerates autocleavage into an alpha and beta chain. Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer. Midpiece of sperm tail. Expressed in brain, kidney, testis and tissues of the gastrointestinal tract. Present in sperm (at protein level). Over-expressed in uterine, mammary, prostatic and ovarian carcinoma. By 5-alpha-di-hydrotestosterone and progesterone. Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. Belongs to the Ntn-hydrolase family. Truncated N-terminus. Contaminating sequence.
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Q4R7U8
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MNPIVVVHGGGAGPISKDRKERMHQGIVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTDGEVEMDASIMDGKDLSVGAVSAVRCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTEKNKKRLEKEKHEKGAQKTDCEKNLGTVGAVALDFKGNVAYATSTGGIVNKMVGRVGDTPCVGAGGYADNDIGAISTTGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTAITDLP
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Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. H2O + L-asparagine = L-aspartate + NH4(+) Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide. Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer. Midpiece of sperm tail. Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. Belongs to the Ntn-hydrolase family.
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Q9CVX3
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MACARGTVAPPVRASIDVSLVVVVHGGGASNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASIMDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIPQVPVEKLITERTKKHLEKEKLEKGAQNADCPKNSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLALFHVEQGKTVEEAAQLALDYMKSKLKGLGGLILVNKTGDWVAKWTSASMPWAAVKNGKLQAGIDLCETRTRDLPC
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Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. H2O + L-asparagine = L-aspartate + NH4(+) Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide. Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer. Midpiece of sperm tail. In retina localizes in photoreceptor inner segment (PubMed:27106100). High expression in the heart and brain while low to minimal expression in the other tissues. In ocular tissues, high levels is observed in the optic nerve and retina while relatively low levels of expression are detected in the iris-ciliary body, lens or retinal pigment epithelium. Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. Belongs to the Ntn-hydrolase family.
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Q8CG44
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MATARPSSCGRDSVPATPRASIDVSLVVVVHGGGASNISPGRKELVSEGIAKAATEGYNILKAGGSAVDAVEGAVTMLENDPEFNAGYGSVLNADGDIEMDASIMDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGRGAEKFAADMGIPQTPAEKLITERTKKHLEKEKLEKGAQKADCPKNSGTVGAVALDCKGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLALFHVEQGKTVDEAATLALDYMKSKLKGLGGLILINKTGDWVAKWTSASMPWAAVKNGKLQAGIDLCETKTRNLPTC
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Has both L-asparaginase and beta-aspartyl peptidase activity. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine (By similarity). May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. H2O + L-asparagine = L-aspartate + NH4(+) Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide. Heterodimer of an alpha and beta chain produced by autocleavage. This heterodimer may then dimerize in turn, giving rise to a heterotetramer (By similarity). Midpiece of sperm tail. Present in testis, brain, liver, kidney, heart and skeletal muscle. In brain, specifically present in the astrocytic lineage. Present in sperm (at protein level). Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. In vasectomized rats, autoantibodies against Asrgl1 are present. Belongs to the Ntn-hydrolase family.
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Q6GM78
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MKPVIVVHGGAGKIVEELDATYRAGVKRAVLKGYDVLSQGGSALTAVEEAVIVLEDEQIFNAGHGSVLNEKGDIEMDAIIMDGKNLDSGAVSAIRNIANPIKLARLVMEKTDHMLLTCEGATLFAKAQGIPEVPNESLVTERSRKRWMKNLKENSNPVADQIGLGTVGAVAIDCEGNVACATSTGGLTNKMVGRVGDTACIGSGGYADNNVGAVSTTGHGESIMKVILARLILHHMEQGKSPEEAADAGLNYMKSRVGGIGGVIIVNSSGDWTAKFSTNQMSWAAVKDDQLHIGIYHGENNVTPLEKAL
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Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. H2O + L-asparagine = L-aspartate + NH4(+) Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide. Heterodimer of an alpha and beta chain produced by autocleavage. Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. Belongs to the Ntn-hydrolase family.
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I3L1X1
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MTKEYQDLQHLDNEESDHHQLRKGPPPPQPLLQRLCSGPRLLLLSLGLSLLLLVVVCVIGSQNSQLQEELRGLRETFSNFTASTEAQVKGLSTQGGNVGRKMKSLESQLEKQQKDLSEDHSSLLLHVKQFVSDLRSLSCQMAALQGNGSERTCCPVNWVEHERSCYWFSRSGKAWADADNYCRLEDAHLVVVTSWEEQKFVQHHIGPVNTWMGLHDQNGPWKWVDGTDYETGFKNWRPEQPDDWYGHGLGGGEDCAHFTDDGRWNDDVCQRPYRWVCETELDKASQEPPLL
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Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. Interacts with LASS2. (Microbial infection) Interacts with hepatitis E virus capsid protein ORF2. Expressed exclusively in hepatic parenchymal cells. Phosphorylated on a cytoplasmic Ser residue. Calcium is required for ligand binding. Hepatic asialoglycoprotein receptor subunit 1
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Q91Y84
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MTKDYQDFQHLDNDNDHHQLRRGPPPTPRLLQRLCSGSRLLLLSSSLSILLLVVVCVITSQNSQLREDLLALRQNFSNLTVSTEDQVKALSTQGSSVGRKMKLVESKLEKQQKDLTEDHSSLLLHVKQLVSDVRSLSCQMAAFRGNGSERTCCPINWVEYEGSCYWFSSSVRPWTEADKYCQLENAHLVVVTSRDEQNFLQRHMGPLNTWIGLTDQNGPWKWVDGTDYETGFQNWRPEQPDNWYGHGLGGGEDCAHFTTDGRWNDDVCRRPYRWVCETKLDKAN
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Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. Interacts with LASS2. Expressed exclusively in hepatic parenchymal cells. Phosphorylated on a cytoplasmic Ser residue. Calcium is required for ligand binding. Hepatic asialoglycoprotein receptor subunit 1
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Q5RBQ8
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MTKECQDLQHLDNEESDHHQLRKGPPPSQPLLQRLCSGPRLLLLSLGLSLLLLVVVCVIGSQNSQLQKELRGLRETFSNFTASTEAQVKGLSTQGGNVGRKMKSLESQLEKQQKDLSEDHSSLLLHVKQFVSDLRSLSCQMAALQGNGSERACCPVNWVEHERSCYWFSRSGKAWADADNYCRLEDAHLVVVTSWEEQKFVQHHTGPVNTWMGLHDQNGPWKWVDGTDYETGFKNWRPEQPDDWYGHGLGGGEDCAHFTDDGRWNDDVCQRPYRWVCETELDKASQEPPLL
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Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface (By similarity). Interacts with LASS2. Phosphorylated on a cytoplasmic Ser residue. Calcium is required for ligand binding.
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P02706
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MTKDYQDFQHLDNENDHHQLQRGPPPAPRLLQRLCSGFRLFLLSLGLSILLLVVVCVITSQNSQLREDLRVLRQNFSNFTVSTEDQVKALTTQGERVGRKMKLVESQLEKHQEDLREDHSRLLLHVKQLVSDVRSLSCQMAALRGNGSERICCPINWVEYEGSCYWFSSSVKPWTEADKYCQLENAHLVVVTSWEEQRFVQQHMGPLNTWIGLTDQNGPWKWVDGTDYETGFKNWRPGQPDDWYGHGLGGGEDCAHFTTDGHWNDDVCRRPYRWVCETELGKAN
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Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. Interacts with LASS2. Expressed exclusively in hepatic parenchymal cells. Phosphorylated on a cytoplasmic Ser residue. Calcium is required for ligand binding. Two types of rat hepatic lectin have been identified, RHL-1 and RHL-2/3, having a relative abundance of 4:1. Hepatic asialoglycoprotein receptor subunit 1
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Q03969
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MAKDFQDIQQLSSEENDHPFHQGEGPGTRRLNPRRGNPFLKGPPPAQPLAQRLCSMVCFSLLALSFNILLLVVICVTGSQSEGHGGAQLQAELRSLKEAFSNFSSSTLTEVQAISTHGGSVGDKITSLGAKLEKQQQDLKADHDALLFHLKHFPVDLRFVACQMELLHSNGSQRTCCPVNWVEHQGSCYWFSHSGKAWAEAEKYCQLENAHLVVINSWEEQKFIVQHTNPFNTWIGLTDSDGSWKWVDGTDYRHNYKNWAVTQPDNWHGHELGGSEDCVEVQPDGRWNDDFCLQVYRWVCEKRRNATGEVA
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Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. The functioning ligand-binding unit of this receptor is thought to be at least a dimer. Interacts with LASS2. (Microbial infection) Interacts with hepatitis E virus capsid protein ORF2. Expressed exclusively in hepatic parenchymal cells. Calcium is required for ligand binding. Hepatic asialoglycoprotein receptor subunit 2
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P24721
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MEKDCQDIQQLDSEENDHQLSGDDEHGSHVQDPRIENPHWKGQPLSRPFPQRLCSTFRLSLLALAFNILLLVVICVVSSQSIQLQEEFRTLKETFSNFSSSTLMEFGALDTLGGSTNAILTSWLAQLEEKQQQLKADHSTLLFHLKHFPMDLRTLTCQLAYFQSNGTECCPVNWVEFGGSCYWFSRDGLTWAEADQYCQLENAHLLVINSREEQDFVVKHRSQFHIWIGLTDRDGSWKWVDGTDYRSNYRNWAFTQPDNWQGHEQGGGEDCAEILSDGHWNDNFCQQVNRWVCEKRRNITH
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Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. Interacts with LASS2. Expressed exclusively in hepatic parenchymal cells. Calcium is required for ligand binding. Hepatic asialoglycoprotein receptor subunit 2
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Q5M8C9
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MEKDFQDIQQLDSEENDHQLIGDEEQGSHVQNLRTENPRWGGQPPSRPFPQRLCSKFRLSLLALAFNILLLVVICVVSSQSMQLQKEFWTLKETLSNFSTTTLMEFKALDSHGGSRNDNLTSWETILEKKQKDIKADHSTLLFHLKHFPLDLRTLTCQLAFFLSNGTECCPVNWVEFGGSCYWFSRDGLTWAEADQYCQMENAHLLVINSREEQEFVVKHRGAFHIWIGLTDKDGSWKWVDGTEYRSNFKNWAFTQPDNWQGHEEGGSEDCAEILSDGLWNDNFCQQVNRWACERKRDITY
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Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. Interacts with LASS2. Expressed exclusively in hepatic parenchymal cells. Calcium is required for ligand binding. Two types of rat hepatic lectin have been identified, RHL-1 and RHL-2/3, having a relative abundance of 4:1. RHL-2 and RHL-3 only differs in their carbohydrate structures. Hepatic asialoglycoprotein receptor subunit 2/3
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Q54WW4
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MNKKSVLVIHGGAGVISKSTISKEREEIFLNSLKNILLAGKIILKQGGTSLDVVQEAVRLLEEDPIYNAGKGSVFTELGTNEMDAAIMDGTNLKAGAVGGVSIIRNPIIAARAVMEHTNHCLLVGKGAEEFAKSKNLEIVEPSFFFTQNRYDQLLRAKDEKKLILDHDGENLLEKEKEKEKNNETSTTTTTISVGVDPIDPKYKMGTVGAVCLDSFGNLAAATSTGGMTNKMHGRVGDTPIIGAGVYANKNVAVSSTGTGEAFMRTVAAFDIAAMMEYGSLSLKDASNKVVMEKLITVGDGGVICVDKYGNVEMPFNTEGMYRGYVIIDNNCENDQNDIINVSIYK
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Has both L-asparaginase and beta-aspartyl peptidase activity. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine (By similarity). Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide. H2O + L-asparagine = L-aspartate + NH4(+) Heterodimer of an alpha and beta chain produced by autocleavage. Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity). Belongs to the Ntn-hydrolases family.
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Q09788
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MRTTFATVALAFLSTVGALPYAPNHRHHRRDDDGVLTVYETILETVYVTAVPGANSSSSYTSYSTGLASVTESSDDGASTALPTTSTESVVVTTSAPAASSSATSYPATFVSTPLYTMDNVTAPVWSNTSVPVSTPETSATSSSEFFTSYPATSSESSSSYPASSTEVASSYSASSTEVTSSYPASSEVATSTSSYVAPVSSSVASSSEISAGSATSYVPTSSSSIALSSVVASASVSAANKGVSTPAVSSAAASSSAVVSSVVSSATSVAASSTISSATSSSASASPTSSSVSGKRGLAWIPGTDLGYSDNFVNKGINWYYNWGSYSSGLSSSFEYVLNQHDANSLSSASSVFTGGATVIGFNEPDLSAAGNPIDAATAASYYLQYLTPLRESGAIGYLGSPAISNVGEDWLSEFMSACSDCKIDFIACHWYGIDFSNLQDYINSLANYGLPIWLTEFACTNWDDSNLPSLDEVKTLMTSALGFLDGHGSVERYSWFAPATELGAGVGNNNALISSSGGLSEVGEIYIS
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Covalently attached to the cell wall.
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P83147
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TEFATNDGGQR
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Degrades acharan sulfate and, to a lesser extent, heparin and heparan sulfate. Inhibited by Cu(2+) ion, nitrogen and lead. Activated by reducing agents, such as DL-dithiothreitol and 2-mercaptoethanol. Optimum pH is 7.2. Optimum temperature 45 degrees Celsius. Monomer. The N-terminus is blocked.
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A0A2U8U2L2
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MAAPSLESNWLVQIPNQSGSHVAQARKDSFAEHMSYNKTHIEAGRMVLAGPLVEALPQDGQPPVITGSIMVWKATAGEREMLDKWLSDNPFATSGVWDLTKMECTPFLCGVRKGL
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Part of the gene cluster that mediates the biosynthesis of xenovulene A, an unusual meroterpenoid that has potent inhibitory effects on the human gamma-aminobutyrate A (GABAA) benzodiazepine receptor (PubMed:29773797). The first step of xenovulene A biosynthesis is the biosynthesis of 3-methylorcinaldehyde performed by the non-reducing polyketide synthase aspks1 (PubMed:17912413, PubMed:29773797, PubMed:20552126). The salicylate hydroxylase asL1 then catalyzes the oxidative dearomatization of 3-methylorcinaldehyde to yield a dearomatized hydroxycyclohexadione (PubMed:29773797). The 2-oxoglutarate-dependent dioxygenase asL3 further catalyzes the oxidative ring expansion to provide the first tropolone metabolite (PubMed:29773797). The cytochrome P450 monooxygenase asR2 allows the synthesis of tropolone hemiacetal (PubMed:29773797). In parallel, a previously unrecognised class of terpene cyclase, asR6, produces alpha-humulene from farnesylpyrophosphate (FPP) (PubMed:29773797). The putative Diels-Alderase asR5 probably catalyzes the formation of the tropolone-humulene skeleton by linking humulene and the polyketide moiety (PubMed:29773797). Oxidative-ring contractions catalyzed by asL4 and asL6 then processively remove carbon atoms from the polyketide to yield xenovulene A (PubMed:29773797). Expression is significantly up-regulated under xenovulene A producing condition. Does not affect the production of xenovulene A. Xenovulene A is a natural product exhibiting little structural resemblance with classical benzodiazepines yet is able to displace high-affinity ligand binding to the benzodiazepine site of the gamma-aminobutyrate A (GABAA) receptor and could be potentially used as an anti-depressant with reduced addictive properties.
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A0A2U8U2L3
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MGSLTDNAAIPTVDISAFLDPNASQEARQDVVNAMSNACHVYGFFNLAGHGIPQETLREAFELNKMFFALPEESKKEVLISKSIGQSFRGYEPPGIQTHHKGLLPDIKETFMVGREVPLDDPDCGTFSTGPNLWPSSLPKEKFQDRIMAYQGSMLELVKNILAILAQGLPKEWGCSPTVFNSLLDKPSIPMRFLHYAPVPSQLEDVRQFGVADHTDFGCVSILLQEPGTSGLEVYYPPSDSWIPVPVIDDGFVINMGDMMQRYTGGYYRSARHRVLTNREKHRHSVAFFLNGNLGLKAKALDGSETETVVGDWIRGRLIDTMGQTGKLLQRESPKPVVLP
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2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of xenovulene A, an unusual meroterpenoid that has potent inhibitory effects on the human gamma-aminobutyrate A (GABAA) benzodiazepine receptor (PubMed:29773797). The first step of xenovulene A biosynthesis is the biosynthesis of 3-methylorcinaldehyde performed by the non-reducing polyketide synthase aspks1 (PubMed:17912413, PubMed:29773797, PubMed:20552126). The salicylate hydroxylase asL1 then catalyzes the oxidative dearomatization of 3-methylorcinaldehyde to yield a dearomatized hydroxycyclohexadione (PubMed:29773797). The 2-oxoglutarate-dependent dioxygenase asL3 further catalyzes the oxidative ring expansion to provide the first tropolone metabolite (PubMed:29773797). The cytochrome P450 monooxygenase asR2 allows the synthesis of tropolone hemiacetal (PubMed:29773797). In parallel, a previously unrecognised class of terpene cyclase, asR6, produces alpha-humulene from farnesylpyrophosphate (FPP) (PubMed:29773797). The putative Diels-Alderase asR5 probably catalyzes the formation of the tropolone-humulene skeleton by linking humulene and the polyketide moiety (PubMed:29773797). Oxidative-ring contractions catalyzed by asL4 and asL6 then processively remove carbon atoms from the polyketide to yield xenovulene A (PubMed:29773797). Binds 1 Fe(2+) ion per subunit. Secondary metabolite biosynthesis; terpenoid biosynthesis. Expression is significantly up-regulated under xenovulene A producing condition. Xenovulene A is a natural product exhibiting little structural resemblance with classical benzodiazepines yet is able to displace high-affinity ligand binding to the benzodiazepine site of the gamma-aminobutyrate A (GABAA) receptor and could be potentially used as an anti-depressant with reduced addictive properties. Belongs to the iron/ascorbate-dependent oxidoreductase family.
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A0A2U8U2L4
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MPQLKVLINGGGIAGNAIAFWLTKLGHDVTVLERFPALRTTGLQLDLRGHGIEVLKRMGLDDAMKAKVIKEDGAQFVDTNGKVVAYFPAVDTSKGGVQAFTSEYEIMRGDICRVFYAATKDRATYKFGTSVESFEDLGDSIKVQLTDHTVDHYDLLIGADGVTSSIRKMMLGPGVPDKFIQFQNLYASYFTIPAPIKPDEKYMANIFIAPGSKLLMTRRDNPERLQVYMGGKAPGARLENARRGDTAEEKLGIEEFMQGCGWRTSEMIDELRKADDFYLERLGMVKLDSWHRGRVALVGEAAWCSSVLTGMGTTSCLVGAYCLAGEIAKHCGRGDQGEAKDDPMMVQKNLANALAGYEEKFMPFMHQVQDGLSAKTGTRTYMPSSQWGVTILNWVIKIIALLRLNMAGDWVIREAVRNWKLPDYPELLKE
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Flavin-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of xenovulene A, an unusual meroterpenoid that has potent inhibitory effects on the human gamma-aminobutyrate A (GABAA) benzodiazepine receptor (PubMed:29773797). The first step of xenovulene A biosynthesis is the biosynthesis of 3-methylorcinaldehyde performed by the non-reducing polyketide synthase aspks1 (PubMed:17912413, PubMed:29773797, PubMed:20552126). The salicylate hydroxylase asL1 then catalyzes the oxidative dearomatization of 3-methylorcinaldehyde to yield a dearomatized hydroxycyclohexadione (PubMed:29773797). The 2-oxoglutarate-dependent dioxygenase asL3 further catalyzes the oxidative ring expansion to provide the first tropolone metabolite (PubMed:29773797). The cytochrome P450 monooxygenase asR2 allows the synthesis of tropolone hemiacetal (PubMed:29773797). In parallel, a previously unrecognised class of terpene cyclase, asR6, produces alpha-humulene from farnesylpyrophosphate (FPP) (PubMed:29773797). The putative Diels-Alderase asR5 probably catalyzes the formation of the tropolone-humulene skeleton by linking humulene and the polyketide moiety (PubMed:29773797). Oxidative-ring contractions catalyzed by asL4 and asL6 then processively remove carbon atoms from the polyketide to yield xenovulene A (PubMed:29773797). Binds 1 FAD per subunit. Secondary metabolite biosynthesis; terpenoid biosynthesis. Expression is significantly up-regulated under xenovulene A producing condition. Severely reduces, but does not abolish xenovulene A biosynthesis. Xenovulene A is a natural product exhibiting little structural resemblance with classical benzodiazepines yet is able to displace high-affinity ligand binding to the benzodiazepine site of the gamma-aminobutyrate A (GABAA) receptor and could be potentially used as an anti-depressant with reduced addictive properties. Belongs to the aromatic-ring hydroxylase family.
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A0A2U8U2K8
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MSAIQRLTGKTAVITGGATGIGFAAAKRFIEEGAFVFIFGRRQEKLDAATAALGPNSRAVQGSVTELADLDRLYEAVKAERGSLDIVMANAGAGMATPLGKITGEQCDIVFGTNLKGTIFTIQGALPLMAQAGGGSIILTGSSSGTTGAPPLSVYGASKAAIRNLARSWAGTLRDEGIRINVLSPASIATEIAKEALGEQGMKMFAQQNPLKRMGQPEEVGAVAAFLASSDSSFMTASEVSVDGGLAQI
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Oxidoreductase; part of the gene cluster that mediates the biosynthesis of xenovulene A, an unusual meroterpenoid that has potent inhibitory effects on the human gamma-aminobutyrate A (GABAA) benzodiazepine receptor (PubMed:29773797). The first step of xenovulene A biosynthesis is the biosynthesis of 3-methylorcinaldehyde performed by the non-reducing polyketide synthase aspks1 (PubMed:17912413, PubMed:29773797, PubMed:20552126). The salicylate hydroxylase asL1 then catalyzes the oxidative dearomatization of 3-methylorcinaldehyde to yield a dearomatized hydroxycyclohexadione (PubMed:29773797). The 2-oxoglutarate-dependent dioxygenase asL3 further catalyzes the oxidative ring expansion to provide the first tropolone metabolite (PubMed:29773797). The cytochrome P450 monooxygenase asR2 allows the synthesis of tropolone hemiacetal (PubMed:29773797). In parallel, a previously unrecognised class of terpene cyclase, asR6, produces alpha-humulene from farnesylpyrophosphate (FPP) (PubMed:29773797). The putative Diels-Alderase asR5 probably catalyzes the formation of the tropolone-humulene skeleton by linking humulene and the polyketide moiety (PubMed:29773797). Oxidative-ring contractions catalyzed by asL4 and asL6 then processively remove carbon atoms from the polyketide to yield xenovulene A (PubMed:29773797). Expression is significantly up-regulated under xenovulene A producing condition. Does not affect the production of xenovulene A. Xenovulene A is a natural product exhibiting little structural resemblance with classical benzodiazepines yet is able to displace high-affinity ligand binding to the benzodiazepine site of the gamma-aminobutyrate A (GABAA) receptor and could be potentially used as an anti-depressant with reduced addictive properties. Belongs to the short-chain dehydrogenases/reductases (SDR) family.
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A0A2U8U2L0
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MTVKILVSGAGVAGTALVNFLCRSKHEYDITVVERAPALRAAGSQLDLKSFGAPLMRKLGLIEKVREKSIHETAFTFVDSKGREWARFPVNEAGKGYEGITSEFEIMRADLVAVLYEASKEVSANPFMKGPQKLRYVFGKHGVHFTQGNSKVNVVFSDGSSDDYDLVVGADGQYSMTRRLLWEPEKGSGDTTLKYTGVTAGFFQMPKSEDEADSTLFKNCLQAGPRGLCLRCAHKDFTQAMLGIPTTDEHKQVFKKPLEQQKQMWEESVGSFKWQGQRVLAELRKSDDFYMTPVAQVKVDRWSKGRVVLVGDAGYCPSVMTGRGTTVSLVGAYVLAGELAKHGDNIDAALESYEKVLRPFITTAQEIPSMGMGMFQSKFGVGVFYVLLAIISKLKIDRLLQALMKEEKETWELPEYPELEFEA
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FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of xenovulene A, an unusual meroterpenoid that has potent inhibitory effects on the human gamma-aminobutyrate A (GABAA) benzodiazepine receptor (PubMed:29773797). The first step of xenovulene A biosynthesis is the biosynthesis of 3-methylorcinaldehyde performed by the non-reducing polyketide synthase aspks1 (PubMed:17912413, PubMed:29773797, PubMed:20552126). The salicylate hydroxylase asL1 then catalyzes the oxidative dearomatization of 3-methylorcinaldehyde to yield a dearomatized hydroxycyclohexadione (PubMed:29773797). The 2-oxoglutarate-dependent dioxygenase asL3 further catalyzes the oxidative ring expansion to provide the first tropolone metabolite (PubMed:29773797). The cytochrome P450 monooxygenase asR2 allows the synthesis of tropolone hemiacetal (PubMed:29773797). In parallel, a previously unrecognised class of terpene cyclase, asR6, produces alpha-humulene from farnesylpyrophosphate (FPP) (PubMed:29773797). The putative Diels-Alderase asR5 probably catalyzes the formation of the tropolone-humulene skeleton by linking humulene and the polyketide moiety (PubMed:29773797). Oxidative-ring contractions catalyzed by asL4 and asL6 then processively remove carbon atoms from the polyketide to yield xenovulene A (PubMed:29773797). Binds 1 FAD per subunit. Secondary metabolite biosynthesis; terpenoid biosynthesis. Expression is significantly up-regulated under xenovulene A producing condition. Severely reduces, but does not abolish xenovulene A biosynthesis. Xenovulene A is a natural product exhibiting little structural resemblance with classical benzodiazepines yet is able to displace high-affinity ligand binding to the benzodiazepine site of the gamma-aminobutyrate A (GABAA) receptor and could be potentially used as an anti-depressant with reduced addictive properties. Belongs to the aromatic-ring hydroxylase family.
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A0A2U8U2K9
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MFDTTKLQSSTQDGSTSSVTGEPIFGANDPNSELNPSSSHFNVRAWASNYAKVTLEGGSQFRRMGVCFQNLNAFGFITPADYQKDVANIWLALPGMLIRNRKRVNILHQFDGIIRPGEMCVVLGPPSSGCSTFLKTLSGDRDGFFIGEDSYFNYEGISDKELHTAHRGDAIYTAETDVHFPKLTVSQTLEFAAQARCPREIPQGIPRQQFCKQLKDVVMGMYGISHTADTKVGNDYIRGVSGGERKRVTIAEATLSNAPLQCWDNCTRGLDSANAIGFCKTLRLQSEFFGQSCAVSMYQAPQSAYDLFDKATVLYQGHQIYFGPADEAKAYFERLGFECPSRQTTPDFLTSMTFPEERITRAGFNPPRTPEEFAAAWRSSPEYKALQTDISEYKTKHPIDGPNAGVYRELKKSYQARGQRIKSPYTLTYMQQVQMCMRRAWNRLVSDPGPTIVVTMGNFVLALIMSSLFFNMQPDTDSFYGREVVLFMAVMFNAFASVLEVMTLYAQRPIVEKQARYAFYHPSAEAYSSVLMDLPIKVLACVSFNLVFYFMTNLNRTPGNFFFYLLASFFIVLSMSGIFRFIKIPSAAFSRTVQQAMIPASILMVFLITFAGFMVPINYMLPWCRWINYLNPVAYGFESLMINEYAGREFRCSNYIPFDGTPGDPNVACNVVGAVAGETFVSGDAHISEAYSYDAAHKWRNIGIVIAMTIFNYTMCFITSEYVSAKKSKGEILVFRRGFVPKNTHVNKITDDLEARSLPVTKIVESPEGSKEKVGGELQSGSTSIFHWRNVCYDIKIKGKPRRILDNVDGWVKPGTMTALMGVSGAGKTTLLDCLADRRTGIGIITGEMLVDGKIRDESFQRKTGYAQQQDLHLETATVRESLVFSALLRRPHHIPKAEKLAYVEEVIDLLEMGPYADAVVGVLGEGLNVEQRKRLTIAVELAAKPPLLLFVDEPTSGLDSQTSWAVVNLLEKLSKAGQSILCTLHQPSAMLFQRFDRLLLLADGGKTVYFGDIGENSSTLVEYFERKAKHPCPPNANPAEWMLEAIGAAPGTTSEVDWQHVWRTSPEFDRVQEELSRLREHGSQSNSHDSEKSETKAVTYHGEFAVPLWTQFVVVIERVFQQSWRTPAYIYSRFALCGVVSLFIGLVFLNSPLSVRGLQNQMFAVFQLFAIVGQLVSQQMPQFIIQRSLYEVRERPAKTYSWKVFMVSQILSDIPYYALASVMMWALWYFPIGLYKNAEVAGQETERGALMWLLFLAWLMWVSTFGHFCISFSETAEAGANAANFMYVLVNFFCGALITPNQMPRFWIFLYRASPLSYLVSSMLSAGIANVEVTCAANEYTIIDPPMGQTCYEYLRNEINTIGGYLLDNNATENCKFCKLKYSNVFLSEIEIEYGTRWRNFGIIWVYVIFNISAAITLYWVARMPKGHRKV
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ABC transporter; part of the gene cluster that mediates the biosynthesis of xenovulene A, an unusual meroterpenoid that has potent inhibitory effects on the human gamma-aminobutyrate A (GABAA) benzodiazepine receptor. Expression is significantly up-regulated under xenovulene A producing condition. Xenovulene A is a natural product exhibiting little structural resemblance with classical benzodiazepines yet is able to displace high-affinity ligand binding to the benzodiazepine site of the gamma-aminobutyrate A (GABAA) receptor and could be potentially used as an anti-depressant with reduced addictive properties. Belongs to the ABC transporter superfamily. ABCG family. PDR (TC 3.A.1.205) subfamily.
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Q2M8A6
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MEFSFSPKRLVVAVAAALPLMASAADTPSTATARKGFAGYDHPNQYLVKPATTIADNMMPVMQHPAQDKETQQKLAELEKKTGKKPNVVVFLLDDVGWMDVGFNGGGVAVGNPTPDIDAVASQGLILTSAYSQPSSSPTRATILTGQYSIHHGILMPPMYGQPGGLQGLTTLPQLLHDQGYVTQAIGKWHMGENKESQPQNVGFDDFRGFNSVSDMYTEWRDVHVNPEVALSPDRSEYIKQLPFSKDDVHAVRGGEQQAIADITPKYMEDLDQRWMDYGVKFLDKMAKSDKPFFLYYGTRGCHFDNYPNAKYAGSSPARTSYGDCMVEMNDVFANLYKTLEKNGQLDNTLIVFTSDNGPEAEVPPHGRTPFRGAKGSTWEGGVRVPTFVYWKGMIQPRKSDGIVDLADLFPTALDLAGHPGAKVANLVPKTTFIDGVDQTSFFLGTNGQSNRKAEHYFLNGKLAAVRMDEFKYHVLIQQPYAYTQSGYQGGFTGTVMQTAGSSVFNLYTDPQESDSIGVRHIPMGVPLQTEMHAYMEILKKYPPRAQIKSD
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No E.coli strains have been observed to have an arylsulfatase activity. A 'latent' activity has been observed by heterologous expression of a genomic region linked to tynA, but it does not map near aslA. Binds 1 Ca(2+) ion per subunit. The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. Belongs to the sulfatase family.
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Q2M8A5
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MLQQVPTRAFHVMAKPSGSDCNLNCDYCFYLEKQSLYREKPVTHMDDDTLEAYVRHYIAASEPQNEVAFTWQGGEPTLLGLAFYRRAVALQAKYGAGRKISNSFQTNGVLLDDEWCAFLAEHHFLVGLSLDGPPEIHNQYRVTKGGRPTHKLVMRALTLLQKHHVDYNVLVCVNRTSAQQPLQVYDFLCDAGVEFIQFIPVVERLADETTARDGLKLHAPGDIQGELTEWSVRPEEFGEFLVAIFDHWIKRDVGKIFVMNIEWAFANFVGAPGAVCHHQPTCGRSVIVEHNGDVYACDHYVYPQYRLGNMHQQTIAEMIDSPQQQAFGEDKFKQLPAQCRSCNVLKACWGGCPKHRFMLDASGKPGLNYLCAGYQRYFRHLPPYLKAMADLLAHGRPASDIMHAHLLVVSK
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Binds 3 [4Fe-4S] clusters (By similarity). The first cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity). Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family. Despite its homology to the anaerobic sulfatase-maturating enzymes, it is not involved in Cys-type sulfatase maturation in vivo.
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H8L902
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MMNSIENEEFIPILLGSDMNVYGMARSFNEAYGKICQAYASDQLAPTRYSKIVNVEVIPGFDKDPVFIETMLRLAKERYSDKSKKYLLIACGDGYAELISQHKQELSEYFICPYIDYSLFERLINKVSFYEVCEEYDLPYPKTLIVREEMLVNGHLEQELPFEFPVALKPANSVEYLSVQFEGRKKAFILETREEFDLILGRIYEAGYKSEMIVQDFIPGDDSNMRVLNAYVDEDHQVRMMCLGHPLLEDPTPASIGNYVVIMPDYNEKIYQTIKAFLEKIEYTGFANFDMKYDPRDGEYKLFEINLRQGRSSFFVTLNGLNLARFVTEDRVFNKPFVETTYGTNQSDKARLWMGVPKKIFLEYARENEDKKLAEQMIKENRYGTTVFYEKDRSIKRWLLMKYMFHNYIPRFKKYFHVKEG
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Catalyzes the addition of D-aspartate onto the lysine residue in the peptidoglycan precursor UDP-MurNAc-pentapeptide. The ligation occurs between the beta-carboxylate of D-Asp and the epsilon-amino group of L-Lys. Is highly specific for D-aspartate, as L-aspartate, D-glutamate, D-alanine, D-iso-asparagine and D-malate are not substrates. [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n) + n ATP + n D-aspartate = [beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-6-N-(beta-D-Asp)-L-Lys-D-Ala-D-Ala)]n + n ADP + n H(+) + n phosphate Binds 2 magnesium ions per subunit. Cell wall biogenesis; peptidoglycan biosynthesis. The substrate D-aspartate is provided by the coexpressed aspartate racemase, whose gene is adjacent to that of the D-aspartate ligase.
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Q10916
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MRIIYLISTVLLIYTNATVLRTKESIQNKVTYDKYGFQPLCISCTGLISVASFFLKFDVSEPVILEFATIVCKLFAKQPWAVCDGISSQFRDEFFYVFRRLANESPSQICGIILPDCADPTDPSESGWMVALPPKPKRTRISKKKVQKKPNMSMSQNLNVLQLTDLHVDFEYKYPSEANCDDPVCCRVSVSEPKKAAGYWGSVGKCDIPFWTVENMLSHINKTHMIDMVIMTGDYINHVDWEYSIEEHLSVLRKLHRLVQNTFPSTPIYWALGNHEGVPVNSFAPHSVDERFWPTWLYKEFQTMSGPWLSEGAKDSLLKRGSYSTQVMDGLKLITLNTGFCEVTNFFLYLNQSDPDSSMSWFVKELFESEKKGEQVYVLAHIPPGDSECLEGWAFNYYRVIQRFSSTIAAQFFGHDHLDYFTVFYEDMHNVSSKPISVGYASPSVTTFEYQNPAYRIYEIDPYNKFKIVDFTTYYADLEKATEDKKPVWEKLYSARQAHGMDDLSPLSWNKVIQKLFTSEKKREKFYQYAFRNFSPQCDSTCQMQLMCNLRMGHHNSTLYCPTF
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Sphingomyelin phosphodiesterase (sphingomyelinase) that converts sphingomyelin to ceramide (N-acyl-sphingoid base) and phosphocholine at acidic pH. Displays its enzymatic activity when secreted. May play distinct roles in signaling. a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine H2O + N-acyl-15-methylhexadecasphing-4-enine-1-phosphocholine = H(+) + N-acyl-15-methylhexadecasphing-4-enine + phosphocholine Binds 2 Zn(2+) per subunit. Lipid metabolism; sphingolipid metabolism. Preferentially expressed in embryos, lower expression in later development. There are two types of sphingomyelinases: asm (acid), and nsm (neutral). Only acid sphingomyelinases have been found in worms. Does not require zinc ions as a cofactor. Belongs to the acid sphingomyelinase family.
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Q23498
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MQQPLIILGIGIVLALVSNVESGVLRKPVDEHEYEKWTNARGNEAAVPPPKYKMLRYAKKAINEPENRKMSCLFCTFAVDGVQALIAQNSTDNEIAAFLVNLCDLFDVEQPHVCKNIIYAFKDEVVFVLERSVFTPEEICGAFIANCGHSDKPLTHMWNITIPGGKPPIKPWPKIPDNKPTFKVLHLSDIHIDHQYVVGTEAYCQLDSALGTYAMCCRDYSQDSQGAPTNLKDKPIYVPAGPWGMPYLCDLPYQTFESAMKHISKTFKDLDYIIITGDFEAHDSWDYTEDLTRENMNNMTNVFLEYFPGVPVYVSIGNHEGVPQDAMAPHTMPEYDTRGPQWLYKIMSEMWSHWIPQEALDTVQYRASYAVYPKPGLKLISLNTIYCSEFNFYLYVNEVDPDATLEWLIEELQDSENKGELVHIISHIPPGDNYCLKGWSWNFFEIVKRYENTIAQMFYGHTHYDQFMVYYDMDDPNRRPFHFNWISPSLTTYDWLNPAYRIYEIDGGYEGATYTVKDAKTYFANVTEANMKNKEPEWVLSYDTREHYQMADFSPQSWSDLSDKLWTNTTLFRDYVRLYYRNHYNNECYTDYKCRYTFVCDIKKGRSYDESFCDHLTK
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Sphingomyelin phosphodiesterase (sphingomyelinase) that converts sphingomyelin (N-acyl-sphingoid-1-phosphocholine) to ceramide (N-acyl-sphingoid base) and phosphocholine at acidic pH. Displays its enzymatic activity when secreted. May play distinct roles in signaling. a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine H2O + N-acyl-15-methylhexadecasphing-4-enine-1-phosphocholine = H(+) + N-acyl-15-methylhexadecasphing-4-enine + phosphocholine Binds 2 Zn(2+) per subunit. Lipid metabolism; sphingolipid metabolism. Only the secreted form is enzymatically active. Preferentially expressed in postembryonic development. Requires Zn(2+) to be fully active. There are two types of sphingomyelinases: asm (acid), and nsm (neutral). Only acid sphingomyelinases have been found in worms. Belongs to the acid sphingomyelinase family.
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Q3ZC91
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MARLGALVCCLLAAWHCRPGLGLPLAPAGTGPAVGQFWHVTDFHLDPTYHITGDHTKVCASSKGAEASDPGPFGDVMCDSPYRLIFSALDFIKNSGQKVSFMIWTGDSPPHVPVLELSTDKVINVTANITTTIQRLFPNLQVFPALGNHDYWPQDQLPVVNSKVYNAVANLWKPWLTEDAITTLRKGGFYTQKVSNNPKLRIISLNTNLYYGPNSVTLNQTDPANQFEWLENTLNISQQNKEKVYIIAHVPVGYLPYARGISAMRKYHNEKLIDIFRKYSDIIAGQFYGHTHRDSIMVLSDKKGKPVNSLFVAPAVTPVRSVLERLTNNPGVRLFQYDPRDYKLLDMLQYYLNLTDANLKGESNWKLEYNLTQAYDIQDLQPKSLYKLAKQFAIQESKQFIKYYKYFFVSYDSSVICQGKCKIFQICAIMNLDVISYTDCFRQYHMKHRL
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Has in vitro nucleotide phosphodiesterase activity with nucleoside triphosphates, such as ATP. Has in vitro activity with p-nitrophenyl-TMP. Has lower activity with nucleoside diphosphates, and no activity with nucleoside monophosphates. Has in vitro activity with CDP-choline, giving rise to CMP and phosphocholine. Has in vitro activity with CDP-ethanolamine. Does not have sphingomyelin phosphodiesterase activity. Binds 2 Zn(2+) per subunit. Monomer. N-glycosylated. Belongs to the acid sphingomyelinase family.
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Q8WV13
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MALVRALVCCLLTAWHCRSGLGLPVAPAGGRNPPPAIGQFWHVTDLHLDPTYHITDDHTKVCASSKGANASNPGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSPPHVPVPELSTDTVINVITNMTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVTSKVYNAVANLWKPWLDEEAISTLRKGGFYSQKVTTNPNLRIISLNTNLYYGPNIMTLNKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNITAMREYYNEKLIDIFQKYSDVIAGQFYGHTHRDSIMVLSDKKGSPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQYYLNLTEANLKGESIWKLEYILTQTYDIEDLQPESLYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAIMNLDNISYADCLKQLYIKHNY
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Has in vitro nucleotide phosphodiesterase activity with nucleoside triphosphates, such as ATP (PubMed:25288789, PubMed:26783088). Has in vitro activity with p-nitrophenyl-TMP (PubMed:25288789). Has lower activity with nucleoside diphosphates, and no activity with nucleoside monophosphates (PubMed:25288789, PubMed:26783088). Has in vitro activity with CDP-choline, giving rise to CMP and phosphocholine. Has in vitro activity with CDP-ethanolamine (PubMed:26783088). Does not have sphingomyelin phosphodiesterase activity (PubMed:25288789, PubMed:26783088). Binds 2 Zn(2+) per subunit. Requires micromolar levels of Zn(2+) for activity (PubMed:26783088). Inhibited by millimolar levels of Zn(2+) (PubMed:25288789, PubMed:26783088). Optimum pH is 4-6. Monomer. Detected in blood serum. Detected in macrophages (at protein level). Up-regulated in macrophages in response to cholesterol accumulation. Up-regulated by cAMP. N-glycosylated. Belongs to the acid sphingomyelinase family.
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Q3U8C2
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MALLGNFLCCLLVAWLCGPGLGVPLAPADRAPAVGQFWHVTDLHLDPTYHITDDRTKVCASSKGANASNPGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSPPHVPVPELSTGTVIKVITNMTMTVQNLFPNLQVFPALGNHDYWPQDQLPIVTSKVYSAVADLWKPWLGEEAISTLKKGGFYSQKVASNPGLRIISLNTNLYYGPNIMTLNKTDPANQFEWLENTLNSSLWNKEKVYIIAHVPVGYLPYATDTPAIRQYYNEKLLDIFRRYSSVIAGQFYGHTHRDSLMVLSDKNGNPLNSVFVAPAVTPVKGVLQKETNNPGVRLFQYKPGDYTLLDMVQYYLNLTEANLKGESNWTLEYVLTQAYSVADLQPKSLYALVQQFATKDSKQFLKYYHYYFVSYDSSATCDQHCKTLQVCAIMNLDSMSYDDCLKQHL
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Has in vitro nucleotide phosphodiesterase activity with nucleoside triphosphates, such as ATP (PubMed:26792860). Has in vitro activity with p-nitrophenyl-TMP. Has lower activity with nucleoside diphosphates, and no activity with nucleoside monophosphates. Has in vitro activity with CDP-choline, giving rise to CMP and phosphocholine. Has in vitro activity with CDP-ethanolamine. Does not have sphingomyelin phosphodiesterase activity (By similarity). Binds 2 Zn(2+) per subunit. Requires micromolar levels of Zn(2+) for activity. Inhibited by millimolar levels of Zn(2+). Detected in blood serum (at protein level). N-glycosylated. Belongs to the acid sphingomyelinase family.
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Q641Z7
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MALPGNFLCCLLVAWLCDPGLGVPLAPAYGAPAVGQFWHVTDLHLDPTYHITDDHTKVCASSKGANVSNPGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSPPHVPVRELSTGSVIEVITNMTVTVQNLFPNLQVFPALGNHDYWPQDQLPIATSKVYSAVSDLWKPWLDEEAISTLRKGGFYSQKVASNPDLRIISLNTNLYYGPNIMTLNKTDPANQFEWLENTLNSSLRNKEKVYVIAHVPVGYLPYATKTPAMRQYYNEKLVDIFRRYSSVIAGQFYGHTHRDSLMVLSDKNGNPINSVFVAPAVTPVKGVLEKETNNPGVRLFQYKPGDYTLLDMLQYYLNLTEANLKGESNWTLEYTLTQAYGVADLQPKSLHGLAQQLATIDSKQFLKYYHYFFVSYDSSAPCDQRCKTLQICAIMNLDLVSYEDCLKRHL
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Has in vitro nucleotide phosphodiesterase activity with nucleoside triphosphates, such as ATP. Has in vitro activity with p-nitrophenyl-TMP. Has lower activity with nucleoside diphosphates, and no activity with nucleoside monophosphates. Has in vitro activity with CDP-choline, giving rise to CMP and phosphocholine. Has in vitro activity with CDP-ethanolamine. Does not have sphingomyelin phosphodiesterase activity. Binds 2 Zn(2+) per subunit. Monomer. N-glycosylated. Belongs to the acid sphingomyelinase family.
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Q96CB7
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MRLLAWLIFLANWGGARAEPGKFWHIADLHLDPDYKVSKDPFQVCPSAGSQPVPDAGPWGDYLCDSPWALINSSIYAMKEIEPEPDFILWTGDDTPHVPDEKLGEAAVLEIVERLTKLIREVFPDTKVYAALGNHDFHPKNQFPAGSNNIYNQIAELWKPWLSNESIALFKKGAFYCEKLPGPSGAGRIVVLNTNLYYTSNALTADMADPGQQFQWLEDVLTDASKAGDMVYIVGHVPPGFFEKTQNKAWFREGFNEKYLKVVRKHHRVIAGQFFGHHHTDSFRMLYDDAGVPISAMFITPGVTPWKTTLPGVVNGANNPAIRVFEYDRATLSLKDMVTYFMNLSQANAQGTPRWELEYQLTEAYGVPDASAHSMHTVLDRIAGDQSTLQRYYVYNSVSYSAGVCDEACSMQHVCAMRQVDIDAYTTCLYASGTTPVPQLPLLLMALLGLCTLVL
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Lipid-modulating phosphodiesterase (PubMed:26095358). Active on the surface of macrophages and dendritic cells and strongly influences macrophage lipid composition and membrane fluidity. Acts as a negative regulator of Toll-like receptor signaling (By similarity). Has in vitro phosphodiesterase activity, but the physiological substrate is unknown (PubMed:26095358). Lacks activity with phosphocholine-containing lipids, but can cleave CDP-choline, and can release phosphate from ATP and ADP (in vitro) (By similarity). Binds 2 Zn(2+) ions per subunit. Interacts with TLR4, TLR7, TLR8 and TLR9. N-glycosylated. Belongs to the acid sphingomyelinase family.
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P58242
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MTLLGWLIFLAPWGVAGAQLGRFWHISDLHLDPNYTVSKDPLQVCPSAGSQPVLNAGPWGDYLCDSPWALINSSLYAMKEIEPKPDFILWTGDDTPHVPNESLGEAAVLAIVERLTNLIKEVFPDTKVYAALGNHDFHPKNQFPAQSNRIYNQVAELWRPWLSNESYALFKRGAFYSEKLPGPSRAGRVVVLNTNLYYSNNEQTAGMADPGEQFRWLGDVLSNASRDGEMVYVIGHVPPGFFEKTQNKAWFRESFNEEYLKVIQKHHRVIAGQFFGHHHTDSFRMFYDNTGAPINVMFLTPGVTPWKTTLPGVVDGANNPGIRIFEYDRATLNLKDLVTYFLNLRQANVQETPRWEQEYRLTEAYQVPDASVSSMHTALTRIASEPHILQRYYVYNSVSYNHLTCEDSCRIEHVCAIQHVAFNTYATCLHGLGAKLVPGFLLILTLLPSLHVLEVL
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Lipid-modulating phosphodiesterase. Active on the surface of macrophages and dendritic cells and strongly influences macrophage lipid composition and membrane fluidity (PubMed:26095358). Acts as a negative regulator of Toll-like receptor signaling (PubMed:26095358, PubMed:27687724). Has in vitro phosphodiesterase activity, but the physiological substrate is unknown (PubMed:26095358, PubMed:27687724). Lacks activity with phosphocholine-containing lipids, but can cleave CDP-choline, and can release phosphate from ATP and ADP (in vitro) (PubMed:27687724). Binds 2 Zn(2+) ions per subunit. Interacts with TLR4, TLR7, TLR8 and TLR9. Macrophages and dendritic cells. Strongly up-regulated by TLR stimuli and interferon gamma. N-glycosylated. Mice display higher inflammatory responses in models of TLR-dependent peritonitis. Macrophages show enhanced responsiveness to TLR stimulation and a significant change in membrane fluidity and the global cellular lipid composition. Belongs to the acid sphingomyelinase family.
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Q9UAY4
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MLLGLLVLSLAFQGTLAVTECEECKSIVDLLQFEWGEKKTEECVMEIAVFICETFHIEDNDVCNFIISDFSDEFMYVIKQILVTPHQLCGLLMKNDCGDFVDPLATIWNMTIPGNQPPFVPKQVVPPGNPTLRALHLTDLHVDMFYTVGLEADCGTPQCCRPQDMNVEIVENGDVKQPAGPWGSVGSCDTPYWLLTNMLQNIASTAGKLDYIMVSGDLVSHTVWAYTPETHSFMVKNLSDTIRSYFPKTPVYFAVGNHEGVPVDNIAPHFTPKKYHMDWLYKAMSNAWQGWIPADQEKSLEYNGCYMKKIYDGLRMISLNNVYGDRINFWLYINQTDPDGTLQWLINQLQDAENVGDKVHIVAHIPGSDGEALEGYALNYYKIINRYANTVVGQFFGHTHSEKFYMMYANPDDYKSTPTNVVYSAPSVTPYSDYFPAYRIYTIDGVHKGSTYQVIDYEEWFFNLTSNNANPTNVKWEVLYQSANMEYGLKGQIPTEYNQMIERMKTDDSLFNKYYENHNRRSIYDGRAPCNDQQCRNGYLCDARQFHQTQQLCTDLEGGIQKPEPKKNKYSARFATSNERRRGKEECKI
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Converts sphingomyelin to ceramide. a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine Binds 2 Zn(2+) per subunit. Lipid metabolism; sphingolipid metabolism. There are two types of sphingomyelinases: asm (acid), and nsm (neutral). Only acid sphingomyelinase has been found in worms. Belongs to the acid sphingomyelinase family.
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Q9HTD7
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MSPVASSRIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSGVPLSHYPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIRGDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLAPELLTEVNLGGTAIGTGINADPGYQKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIMPGKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHELVEHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENMIAPRLIPLRA
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L-aspartate = fumarate + NH4(+) Homotetramer. Belongs to the class-II fumarase/aspartase family. Aspartase subfamily.
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P07346
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MISVMSSAASFRTEKDLLGVLEVPAQAYYGIQTLRAVNNFRLSGVPISHYPKLVVGLAMVKQAAADANRELGQLSERKHAAISEACARLIRGDFHEEFVVDMIQGGAGTSTNMNANEVIANIALEAMGHQKGEYQYLHPNNDVNMAQSTNDAYPTAIRLGLLLGHDALLASLDSLIQAFAAKGAEFSHVLKMGRTQLQDAVPMTLGQEFRAFATTLGEDLARLKTLAPELLTEVNLGGTAIGTGINADPRYQALAVQRLATISGQPLVPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPARQPGSSIMPGKVNPVIPEAVNQVAFQVIGNDLALTMAAEGGQLQLNVMEPLIAFKIFDSIRLLQRAMDMLREHCIVGITANEARCRELVEHSIGLVTALNPYIGYENATRIARIALESGRGVLELVREEGLLDDAMLDDILRPENMIAPRLVPLKA
|
L-aspartate = fumarate + NH4(+) Homotetramer. Belongs to the class-II fumarase/aspartase family. Aspartase subfamily.
|
P33109
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MSNNIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNSKISDVPEFVRGMVMVKKAAAMANKELKTIPRKIADVIIQACDEVLDKGKCMDQFPVDVFQGGAGTSLNMNTNEVLANIGLELMGHQKGEYQYLNPNDHLNKCQSTNDAYPTGFRIAVYASNQKLIDAINQLREGFDRKAKEFETILKMGRTQLQDAVPMTLGQEFHAFSVLLNEETRNLHRTATLLLEVNLGATAIGTALNTPEGYQPLAVQKLAEVSGLPVVPAEDLIEATSDCGAYVMVHSALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDTCVTMAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCINGITANKEVCEHYVFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTEAELDDIFSVENLMHPAYKAKRYTDENEQ
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L-aspartate = fumarate + NH4(+) Homotetramer. Belongs to the class-II fumarase/aspartase family. Aspartase subfamily.
|
P78140
|
MSNNIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISDIPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVLNNGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYSSLIKLVDAINQLREGFERKAVEFQDILKMGRTQLQDAVPMTLGQEFRAFSILLKEEVKNIQRTAELLLEVNLGATAIGTGLNTPKEYSPLAVKKLAEVTGFPCVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDTTVTMAAEAGQLQLNVMEPVIGQAMFESVHILTNACYNLLEKCINGITANKEVCEGYVYNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTEAELDDIFSVQNLMHPAYKAKRYTDESEQ
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L-aspartate = fumarate + NH4(+) Homotetramer. Belongs to the class-II fumarase/aspartase family. Aspartase subfamily.
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Q3AV13
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MAASDVLVVAGTHGNELNAPWLLEQWNRQPDLINSAGLSIQRLVGNPQAKAAMRRYVDRDLNRSFRVDLLEQSGGDLEMRRARELLGRYGPRGDEPCSVVLDLHSTTAAMGCSLVLYGRRPADLALAALVQSALGLPIYLHESDSAQTGFLVERWPCGLVVEVGPVPQGVLEARIVRQTRLAIEACFEALASVRSGVVRLPRQVVVHRHLGSCDVPRGESDQPQALVHQRLQGRDWVPFKPLDAIFEAADGSTVETPQMEHQSIPVFINEAAYAEKHIAFSLTRREVWTMEPQWLDHLSELLS
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H2O + N-acyl-L-aspartate = a carboxylate + L-aspartate Binds 1 zinc ion per subunit. Belongs to the AspA/AstE family. Aspartoacylase subfamily.
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Subsets and Splits
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