UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 2 35.2k | Functional Description stringlengths 5 30.7k |
|---|---|---|
Q10468 | MRLDRRALYALVLLLACASLGLLYASTRDAPGLPNPLALWSPPQGPPRLDLLDLATEPRYAHIPVRIKEQVVGLLAQNNCSCESSGGRFALPFLRQVRAIDFTKAFDAEELRAVSISREQEYQAFLARSRSLADQLLIAPANSPLQYPLQGVEVQPLRSILVPGLSLQEASVQEIYQVNLIASLGTWDVAGEVTGVTLTGEGQSDLTLASPILDKLNRQLQLVTYSSRSYQANTADTVRFSTKGHEVAFTILIRHPPNPRLYPPSSLPQGAQYNISALVTVATKTFLRYDRLRALIASIRRFYPTVTIVIADDSDKPERISDPHVEHYFMPFGKGWFAGRNLAVSQVTTKYVLWVDDDFVFTARTRLEKLVDVLERTPLDLVGGAVREISGYATTYRQLLSVEPGAPGFGNCLRQKQGFHHELAGFPNCVVTDGVVNFFLARTDKVRQVGFDPRLNRVAHLEFFLDGLGSLRVGSCSDVVVDHASKVKLPWTSKDPGAELYARYRYPGSLDQSQVAKHRLLFFKHRLQCMTAE | Involved in the biosynthesis of gangliosides GM2, GD2, GT2 and GA2 from GM3, GD3, GT3 and GA3, respectively. ganglioside GM3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GM2 (d18:1(4E)) + H(+) + UDP ganglioside GD3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GD2 (d18:1(4E)) + H(+) + UDP ganglioside GM3 + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GM2 + H(+) + UDP ganglioside GD3 + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GD2 + H(+) + UDP ganglioside GD1a + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GalNAc-GD1a + H(+) + UDP ganglioside GT3 (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GT2 (d18:1(4E)) + H(+) + UDP a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = ganglioside GA2 (d18:1(4E)) + H(+) + UDP alpha-N-glycoloylneuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + UDP-N-acetyl-alpha-D-galactosamine = H(+) + N-acetyl-beta-D-galactosaminyl-(1->4)-[alpha-N-glycoloylneuraminosyl-(2->3)]-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + UDP Sphingolipid metabolism. Homodimer; disulfide-linked. Strongly expressed in brain, testis, spleen, and to a lesser extent in liver. Belongs to the glycosyltransferase 2 family. |
Q86Y40 | MGSAGFSVGKFHVEVASRGRECVSGTPECGNRLGSAGFGALCLELRGADPAWGPFAAHGRSRRQGSRFLWLLKILVIILVLGIVGFMFGSMFLQAVFSSPKPELPSPAPGVQKLKLLPEERLRNLFSYDGIWLFPKNQCKCEANKEQGGYNFQDAYGQSDLPAVKARRQAEFEHFQRREGLPRPLPLLVQPNLPFGYPVHGVEVMPLHTVPIPGLQFEGPDAPVYEVTLTASLGTLNTLADVPDSVVQGRGQKQLIISTSDRKLLKFILQHVTYTSTGYQHQKVDIVSLESRSSVAKFPVTIRHPVIPKLYDPGPERKLRNLVTIATKTFLRPHKLMIMLRSIREYYPDLTVIVADDSQKPLEIKDNHVEYYTMPFGKGWFAGRNLAISQVTTKYVLWVDDDFLFNEETKIEVLVDVLEKTELDVVGGSVLGNVFQFKLLLEQSENGACLHKRMGFFQPLDGFPSCVVTSGVVNFFLAHTERLQRVGFDPRLQRVAHSEFFIDGLGTLLVGSCPEVIIGHQSRSPVVDSELAALEKTYNTYRSNTLTRVQFKLALHYFKNHLQCAA | Involved in the synthesis of the Sd(a) antigen (Sia-alpha2,3-[GalNAc-beta1,4]Gal-beta1,4-GlcNAc), a carbohydrate determinant expressed on erythrocytes, the colonic mucosa and other tissues. Transfers a beta-1,4-linked GalNAc to the galactose residue of an alpha-2,3-sialylated chain. Protein modification; protein glycosylation. Widely expressed. Highly expressed in colon and to a lesser extent in kidney, stomach, ileum and rectum. The Sd(a) antigen on red blood cells defines the SID blood group system. There is considerable variability in the strength of antigen expression, ranging from ordinary Sd(a+) to strong Sd(a++) expression [MIM:615018]. Lack of Sd(a) antigen results in the Sd(a-) phenotype, due to genetic variants in B4GALNT2. The gene represented in this entry is involved in disease pathogenesis. Belongs to the glycosyltransferase 2 family. Beta-1,4 N-acetylgalactosaminyltransferase 2 |
Q09199 | MTSSVSFASFRFPWLLKTFVLMVGLATVAFMVRKVSLTTDFSTFKPKFPEPARVDPVLKLLPEEHLRKLFTYSDIWLFPKNQCDCNSGKLRMKYKFQDAYNQKDLPAVNARRQAEFEHFQRREGLPRPPPLLAPPNLPFGYPVHGVEVMPLHTILIPGLQYEGPDAPVYEVILKASLGTLNTLADVPDDEVQGRGQRQLTISTRHRKVLNFILQHVTYTSTEYYLHKVDTVSMEYESSVAKFPVTIKQQTVPKLYDPGPERKIRNLVTIATKTFLRPHKLKILLQSIRKYYPDITVIVADDSKEPLEINDDYVEYYTMPFGKGWFAGRNLAISQVTTKYVLWVDDDFLFSDKTKIEVLVDVLEKTELDVVGGSVQGNTYQFRLLYEQTKNGSCLHQRWGSFQALDGFPGCTLTSGVVNFFLAHTEQLRRVGFDPILQRVAHGEFFIDGLGRLLVGSCPGVIINHQVRTPPKDPKLAALEKTYDKYRANTNSVIQFKVALQYFKNHLYCST | Responsible for synthesis of murine T-lymphocyte CT antigen. Can transfer N-acetylgalactosamine moiety from UDP-GalNAc to the low molecular weight acceptor 3'-sialyl-N-acetyllactosamine, to form a non-reducing terminal tetrasaccharide Sda blood group structure. Protein modification; protein glycosylation. Belongs to the glycosyltransferase 2 family. |
Q8N7T6 | MGSPRAARPPLLLRPVKLLRRRFRLLLALAVVSVGLWTLYLELVASAQVGGNPLNRRYGSWRELAKALASRNIPAVDPHLQFYHPQRLSLEDHDIDQGVSSNSSYLKWNKPVPWLSEFRGRANLHVFEDWCGSSIQQLRRNLHFPLYPHIRTTLRKLAVSPKWTNYGLRIFGYLHPFTDGKIQFAIAADDNAEFWLSLDDQVSGLQLLASVGKTGKEWTAPGEFGKFRSQISKPVSLSASHRYYFEVLHKQNEEGTDHVEVAWRRNDPGAKFTIIDSLSLSLFTNETFLQMDEVGHIPQTAASHVDSSNALPRDEQPPADMLRPDPRDTLYRVPLIPKSHLRHVLPDCPYKPSYLVDGLPLQRYQGLRFVHLSFVYPNDYTRLSHMETHNKCFYQENAYYQDRFSFQEYIKIDQPEKQGLEQPGFEENLLEESQYGEVAEETPASNNQNARMLEGRQTPASTLEQDATDYRLRSLRKLLAQPREGLLAPFSKRNSTASFPGRTSHIPVQQPEKRKQKPSPEPSQDSPHSDKWPPGHPVKNLPQMRGPRPRPAGDSPRKTQWLNQVESYIAEQRRGDRMRPQAPGRGWHGEEEVVAAAGQEGQVEGEEEGEEEEEEEDMSEVFEYVPVFDPVVNWDQTFSARNLDFQALRTDWIDLSCNTSGNLLLPEQEALEVTRVFLKKLNQRSRGRYQLQRIVNVEKRQDQLRGGRYLLELELLEQGQRVVRLSEYVSARGWQGIDPAGGEEVEARNLQGLVWDPHNRRRQVLNTRAQEPKLCWPQGFSWSHRAVVHFVVPVKNQARWVQQFIKDMENLFQVTGDPHFNIVITDYSSEDMDVEMALKRSKLRSYQYVKLSGNFERSAGLQAGIDLVKDPHSIIFLCDLHIHFPAGVIDAIRKHCVEGKMAFAPMVMRLHCGATPQWPEGYWEVNGFGLLGIYKSDLDRIGGMNTKEFRDRWGGEDWELLDRILQAGLDVERLSLRNFFHHFHSKRGMWSRRQMKTL | Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked glycans and probably O-linked glycans. Mediates the N,N'-diacetyllactosediamine formation on gastric mucosa. an N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-alpha-D-galactosamine = an N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP Localizes to apical Golgi. Highly expressed in testis, colon and stomach. Weakly expressed in other tissues. Belongs to the chondroitin N-acetylgalactosaminyltransferase family. Truncated N-terminus. Probable intron retention. |
Q6L8S8 | MGSPRAALLMLLLRPIKLLRRRFRLLLLLAVVSVGLWTLYLELVASAQAGGNPLNHRYGSWRELAKALASRNIPAVDPNLQFYRPQRLSLKDQEIARSRSRNSSYLKWNKPVPWLSEFRGHANLHVFEDWCGSSIQQLRNNLHFPLYPHIRTTLRKLAVSPKWTNYGLRIFGYLHPFTDGKIQFAIAADDNAEFWLSRDDQVSGLQLLASVGKTGKEWTAPGEFGKFQSQISKPVSLSASLRYYFEVLHKQNDEGTDHVEVAWRRNDPGAKFTIIDSPFLSLFTNETILRMDEVGHIPQTAASHVGSSNTPPRDEQPPADMLRPDPRDTLFRVPLIAKSHLRHVLPDCPYKPSYLVDGLPLQRYQGLRFVHLSFVYPNDYTRLSHMETHNKCFYQESAYDQDRSSFQEYIKMDKPEKHGPEQPAGLEDGLLEESQYEDVPEEIPTSQDQNTGIQGRKQKTISTPGLGVTDYHLRKLLARSQSGPVAPLSKQNSTTAFPTRTSNIPVQRPEKSPVPSRDLSHSDQGARRNLPLIQRARPTGDRPGKTLEQSQWLNQVESFIAEQRRGDRIEPPTPSRGWRPEEDVVIAADQEGEVEEEEEGEDEEEDMSEVFEYVPMFDPVVNWGQTFSAQNLDFQALRTDWIDLNCNTSGNLLLPEQEALEVTRVFLRKLSQRTRGRYQLQRIVNVEKRQDRLRGGRYFLELELLDGQRLVRLSEYVSTRGWRGGDHPGREDTEARNLQGLVWSPRNRHRHVLNAQDPEPKLCWPQGFSWNHRAVVHFIVPVKNQARWVQQFIRDMESLSQVTGDAHFSIIITDYSSEDMDVEMALKRSRLRSYQYLKLSGNFERSAGLQAGIDLVKDPHSIIFLCDLHIHFPAGIIDTIRKHCVEGKMAFAPMVMRLHCGATPQWPEGYWEVNGFGLLGIYKSDLDKIGGMNTKEFRDRWGGEDWELLDRILQAGLEVERLSLRNFFHHFHSKRGMWNRRQMKMP | Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked glycans and probably O-linked glycans. Mediates the N,N'-diacetyllactosediamine formation on gastric mucosa (By similarity). an N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-alpha-D-galactosamine = an N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP Localizes to apical Golgi. Belongs to the chondroitin N-acetylgalactosaminyltransferase family. Beta1,4-N-acetylgalactosaminyltransferase III |
Q96LV2 | MPRLPVKKIRKQMKLLLLLLLLSCAAWLTYVHLGLVRQGRALRQRLGYGRDGEKLTSETDGRGVHAAPSTQRAEDSSESREEEQAPEGRDLDMLFPGGAGRLPLNFTHQTPPWREEYKGQVNLHVFEDWCGGAVGHLRRNLHFPLFPHTRTTVKKLAVSPKWKNYGLRIFGFIHPARDGDVQFSVASDDNSEFWLSLDESPAAAQLVAFVGKTGSEWTAPGEFTKFSSQVSKPRRLMASRRYYFELLHKQDDRGSDHVEVGWRAFLPGLKFEVISSAHISLYTDESALKMDHVAHVPQSPASHVGGRPPQEETSADMLRPDPRDTFFLTPRMESSSLENVLEPCAYAPTYVVKDFPIARYQGLQFVYLSFVYPNDYTRLTHMETDNKCFYRESPLYLERFGFYKYMKMDKEEGDEDEEDEVQRRAFLFLNPDDFLDDEDEGELLDSLEPTEAAPPRSGPQSPAPAAPAQPGATLAPPTPPRPRDGGTPRHSRALSWAARAARPLPLFLGRAPPPRPAVEQPPPKVYVTRVRPGQRASPRAPAPRAPWPPFPGVFLHPRPLPRVQLRAPPRPPRPHGRRTGGPQATQPRPPARAQATQGGREGQARTLGPAAPTVDSNLSSEARPVTSFLSLSQVSGPQLPGEGEEEEEGEDDGAPGDEAASEDSEEAAGPALGRWREDAIDWQRTFSVGAVDFELLRSDWNDLRCNVSGNLQLPEAEAVDVTAQYMERLNARHGGRFALLRIVNVEKRRDSARGSRFLLELELQERGGGRLRLSEYVFLRLPGARVGDADGESPEPAPAASVRPDGRPELCRPLRLAWRQDVMVHFIVPVKNQARWVAQFLADMAALHARTGDSRFSVVLVDFESEDMDVERALRAARLPRYQYLRRTGNFERSAGLQAGVDAVEDASSIVFLCDLHIHFPPNILDGIRKHCVEGRLAFAPVVMRLSCGSSPRDPHGYWEVNGFGLFGIYKSDFDRVGGMNTEEFRDQWGGEDWELLDRVLQAGLEVERLRLRNFYHHYHSKRGMWSVRSRKGSRTGAS | Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked glycans and probably O-linked glycans. an N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-alpha-D-galactosamine = an N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP Highly expressed in ovary, adult and fetal brain. Also expressed in fetal kidney and lung. Belongs to the chondroitin N-acetylgalactosaminyltransferase family. |
Q8CHV2 | MPWFPVKKVRKQMKLLLLLLLLTCAAWLTYVHRSLVRPGRALRQRLGYGRDGEKLTGVTDSRGVRVPSSTQRSEDSSESHEEEQAPEGRGPNMLFPGGPRKPPPLNLTHQTPPWREEFKGQVNLHVFEDWCGGAVGHLRRNLHFPLFPHTRTTVTKLAVSPKWKNYGLRIFGFIHPARDGDIQFSVASDDNSEFWLSLDESPAAAQLVAFVGKTGSEWTAPGEFTKFSSQVSKPRRLMASRRYYFELLHKQDDKGSDHVEVGWRAFLPGLKFEIIDSAHISLYTDESSLKMDHVAHVPQSPASHIGGFPPQGEPSADMLHPDPRDTFFLTPRMEPLSLENVLEPCAYAPTYILKDFPIARYQGLQFVYLSFIYPNDHTRLTHMETDNKCFYRESPLYLERFGFYKYMKMDKEEGEEDEEEEVQRRAFLFLNPDDFLDEEDEQDLLDSLEPTDASVQQSHRTPTPAASTGTTASPTPPTTSPLDEQTLRHSRALNWAPRPLPLFLGRAPPPRTVEKSPSKVYVTRVRPGQRASPRALRDSPWPPFPGVFLRPKPLPRVQLRVPPHPPRTQGYRTSGPKVTELKPPVRAQTSQGGREGQLHGQGLMVPTVDLNSSVETQPVTSFLSLSQVSRPQLPGEGEEGEEDGAPGDEATSEDSEEEEEPAAGRPLGRWREDAINWQRTFSVGAMDFELLRSDWNDLRCNVSGNLQLPEAEAVDVVAQYMERLNAKHGGRFSLLRIVNVEKRRDSARGSRFLLELELQERGGSRQRLSEYVFLRLPGARVGDEDGESPEPPPAASIHPDSRPELCRPLHLAWRQDVMVHFIVPVKNQARWVVQFLADMTALHVHTGDSYFNIILVDFESEDMDVERALRAAQLPRYQYLKRTGNFERSAGLQTGVDAVEDPSSIVFLCDLHIHFPPNILDSIRKHCVEGKLAFAPVVMRLGCGSSPWDPHGYWEVNGFGLFGIYKSDFDRVGGMNTEEFRDQWGGEDWELLDRVLQAGLEVERLRLRHFYHHYHSKRGMWATRSRKGARAQRS | Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked glycans and probably O-linked glycans. an N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-alpha-D-galactosamine = an N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP Belongs to the chondroitin N-acetylgalactosaminyltransferase family. Beta1,4-N-acetylgalactosaminyltransferase IV |
Q8MIG0 | MKFREPLLGGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLRRLPQLVGVHPPLQGSSHGAAAIGQPSGELRLRGVAPPPPLQNSSKPRSRAPSNLDAYSHPGPGPGPGSNLTSAPVPSTTTRSLTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGRYTPMDCISPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGESMFNRAKLLNVGFKEALKDYDYNCFVFSDVDLIPMNDHNTYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLSINGFPNNYWGWGGEDDDIYNRLAFRGMSVSRPNAVIGKCRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTYMVLEVQRYPLYTKITVDIGTPS | The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix. The secreted form is responsible for the synthesis of complex-type to N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids (PubMed:9405390). D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) + UDP Protein modification; protein glycosylation. Homodimer; and heterodimer with alpha-lactalbumin to form lactose synthase (PubMed:10393171, PubMed:11419947, PubMed:12051854, PubMed:12927542). Interacts (via N-terminal cytoplasmic domain) with UBE2Q1 (via N-terminus); the interaction is direct (By similarity). Found in trans cisternae of Golgi. B4GALT1 cell surface expression is regulated by UBE2Q1 (By similarity). Found in trans cisternae of Golgi. Soluble form found in body fluids. Detected in milk (at protein level). The soluble form derives from the membrane forms by proteolytic processing. Belongs to the glycosyltransferase 7 family. |
Q14523 | MRLREPLLSGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTPLQGGSNSAAAIGQSSGELRTGGARPPPPLGASSQPRPGGDSSPVVDSGPGPASNLTSVPVPHTTALSLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAIIIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYDYTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTINGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIAHTKETMLSDGLNSLTYQVLDVQRYPLYTQITVDIGTPS | The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix. D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) + UDP Protein modification; protein glycosylation. Homodimer; and heterodimer with alpha-lactalbumin to form lactose synthase. Interacts (via N-terminal cytoplasmic domain) with UBE2Q1 (via N-terminus); the interaction is direct (By similarity). Found in trans cisternae of Golgi but is mainly localized at the plasma membrane (PubMed:1714903). B4GALT1 cell surface expression is regulated by UBE2Q1 (By similarity). Found in trans cisternae of Golgi. Soluble form found in body fluids. Ubiquitously expressed, but at very low levels in fetal and adult brain. The soluble form derives from the membrane forms by proteolytic processing. The disease is caused by variants affecting the gene represented in this entry. Belongs to the glycosyltransferase 7 family. Beta-1,4-galactosyltransferase 1 |
P15535 | MRFREQFLGGSAAMPGATLQRACRLLVAVCALHLGVTLVYYLSGRDLSRLPQLVGVSSTLQGGTNGAAASKQPPGEQRPRGARPPPPLGVSPKPRPGLDSSPGAASGPGLKSNLSSLPVPTTTGLLSLPACPEESPLLVGPMLIDFNIAVDLELLAKKNPEIKTGGRYSPKDCVSPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGDTMFNRAKLLNIGFQEALKDYDYNCFVFSDVDLIPMDDRNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLAINGFPNNYWGWGGEDDDIFNRLVHKGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIAHTKETMRFDGLNSLTYKVLDVQRYPLYTQITVDIGTPR | The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix. The secreted form is responsible for the synthesis of complex-type to N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) + UDP Protein modification; protein glycosylation. Homodimer; and heterodimer with alpha-lactalbumin to form lactose synthase (By similarity). Interacts (via N-terminal cytoplasmic domain) with UBE2Q1 (via N-terminus); the interaction is direct (PubMed:18511602). Found in trans cisternae of Golgi. B4GALT1 cell surface expression is regulated by UBE2Q1 (PubMed:18511602). Found in trans cisternae of Golgi. Soluble form found in body fluids. In the brain, highest levels of expression are found at 11.5 dpc with decreased expression thereafter. The soluble form derives from the membrane forms by proteolytic processing. Belongs to the glycosyltransferase 7 family. b4GalT1 |
P80225 | PGATLQXAXXLLVAVXAXPPPPLGVXPKPXPG | This protein is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) + UDP Protein modification; protein glycosylation. Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid. The soluble form derives from the membrane form by proteolytic processing. Belongs to the glycosyltransferase 7 family. |
Q80WN9 | MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSIRSPAHALYPAASSSTNCSRPNATASSSGLPEVPSARPGPTAPVIPPCPDVPPGLVGRVVIEFTSPMPLERVQRENPGVLLGGRYTPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPMLRRQRLRYGIYVINQHGEETFNRAKLLNVGFLEALKEDATYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIAMDKFGFRLPYASYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPDVRIGRYRMIKHDRDKHNEPNPQRFSKIQNTKLSMKWDGIGSLRYRVLEVSRQPLFTNITVDIGRPMSWLNQG | Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose (By similarity). D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP Protein modification; protein glycosylation. Trans cisternae of Golgi stack. Belongs to the glycosyltransferase 7 family. |
Q9NSY7 | MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSARGPAHALHPAASSSSSSSNCSRPNATASSSGLPEVPSALPGPTAPTLPPCPDSPPGLVGRLLIEFTSPMPLERVQRENPGVLMGGRYTPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPILRRQRLRYGVYVINQHGEDTFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIAMDKFGFRLPYAGYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPDIRIGRYRMIKHDRDKHNEPNPQRFTKIQNTKLTMKRDGIGSVRYQVLEVSRQPLFTNITVDIGRPPSWPPRG | Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids (PubMed:9405390). Can produce lactose (PubMed:9405390). D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP Protein modification; protein glycosylation. Trans cisternae of Golgi stack. Weakly expressed in various tissues. Highest expression in prostate, testis, ovary, intestine, muscle, and in fetal brain. Belongs to the glycosyltransferase 7 family. Beta-1,4-galactosyltransferase 2 |
Q3TMP2 | MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSTRSPAHALYPAASSSTNCSRPNATAASSGLPEVPSARPGPTAPVIPPCPDVPPGLVGRVVIEFTSPMPLERVQRENPGVLLGGRYSPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPMLRRQRLRYGVYVINQHGEETFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIAMDKFGFRLPYASYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPDVRIGRYRMIKHDRDKHNEPNPQRFNKIQNTKMSMKWDGIGSVRYRVLEVSRQPLFTNITVDIGQPMSWLTQG | Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose (By similarity). D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP Protein modification; protein glycosylation. Trans cisternae of Golgi stack. Belongs to the glycosyltransferase 7 family. b4GalT2 |
Q5E9K4 | MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGREQEPAFDYSHPHDVYSNLSHMPGAPVAPGGLPAPQGLPYCPKRSPLLVGPISVSFSPVPSLAEIVERNPRVEPGGRYRPARCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYQLLSRELGPLYTNITADIGTDPRGPRTSSGPHYPPGSSQAFRQEMLQRRPPARPGPLPTANHTAPHGSH | Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) + UDP Protein modification; protein glycosylation. Trans cisternae of Golgi stack. Belongs to the glycosyltransferase 7 family. |
Q80WN8 | MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDQGPTFDYSHPRDVYSNLSHLPGAPVAAGASPAEALPFCPERSPFLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCEARSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGMFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYQLLAKELGPLYTNITADIGTDPRGPRAPSGPRYPPGSSQAFRQEMLQRRPPARPGPLPTANHTAPHGSH | Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) + UDP Protein modification; protein glycosylation. Trans cisternae of Golgi stack. Belongs to the glycosyltransferase 7 family. |
Q9H8T2 | MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDQGPTFDYSHPRDVYSNLSHLPGAPGGPPAPQGLPYCPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYQLLARELGPLYTNITADIGTDPRGPRAPSGPRYPPGSSQAFRQEMLQRRPPARPGPLSTANHTALRGSH | Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) + UDP Protein modification; protein glycosylation. Trans cisternae of Golgi stack. Found in various tissues. Highest expression in placenta, prostate, testis, ovary, intestine and muscle, and in fetal brain. Belongs to the glycosyltransferase 7 family. Beta-1,4-galactosyltransferase 3 |
Q9QY13 | MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDPGPTFDYSHPHDVYSNLSHLPAAPGAAGAPPAQALPYCPERSPFLVGPVSVSFSPVPSLAEIVERNPRVESGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYRLLARELGPLYTNITADIGTDPRGPRSPSGPRYPPGSSQAFRQEMLQRRPPARPGPLPTANHTAPRGSH | Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) + UDP Protein modification; protein glycosylation. Trans cisternae of Golgi stack. Belongs to the glycosyltransferase 7 family. b4GalT3 |
Q5NVN3 | MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDQGPTFDYSHPRDVYSNLSHLPGAPGGPPAPQGLPYCPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYQLLARELGPLYTNITADIGTDPRGPRAPSGPRYPPGSSQAFRQEMLQRRPPARPGPPPTANHTALRGSH | Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside nLc4Cer(d18:1(4E)) + H(+) + UDP beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) + UDP Protein modification; protein glycosylation. Trans cisternae of Golgi stack. Belongs to the glycosyltransferase 7 family. |
Q06DE4 | MATAIPQRQLFVAGEWRAPALGRRLPVVNPATESPIGEIPAGTAEDVDAAVAAAREALKRNRGRDWARAPGAVRAKYLRAIAAKIIERKSELARLETLDCGKPLDEAAWDMDDVAGCFEYFADLAESLDKRQNAPVSLPMENFKCYLRKEPIGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADVCKEVGLPSGVLNIVTGLGSEAGAPLSSHPGVDKVAFTGSYETGKKIMASAAPMVKPVSLELGGKSPIVVFDDVDVEKAVEWTLFGCFWTNGQICSATSRLILHKKIAKEFQERMVAWAKNIKVSDPLEEGCRLGPVVSEGQYEKIKQFVSTAKSQGATILTGGVRPKHLEKGFYIEPTIITDVDTSMQIWREEVFGPVLCVKEFSTEEEAIELANDTHYGLAGAVLSGDRERCQRLTEEIDAGIIWVNCSQPCFCQAPWGGNKRSGFGRELGEGGIDNYLSVKQVTEYASDEPWGWYKSPSKL | Dehydrogenase that can use N-acetyl-gamma-aminobutyraldehyde (NAGABald), gamma-guanidinobutyraldehyde (GGBald), betaine aldehyde (Bet-ald), gamma-aminobutyraldehyde (GAB-ald), acetaldehyde, 4-aminobutylaldehyde (AB-ald), 3-aminopropionaldehyde (AP-ald), 4-N-trimethylaminobutyraldehyde (TMAB-ald) and 3-N-trimethylaminopropionaldehyde (TMAP-ald) as substrates. Catalyzes the oxidation of GAB-ald more efficiently than Bet-ald. Mediates the conversion of GAB-ald into gamma-aminobutyric acid (GABA), and prevents the formation of 2-acetyl-1-pyrroline (2AP) which gives fragrant rice its aromatic properties. betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Optimum pH is 10. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Homodimer. Expressed constitutively in roots, embryos, seedlings, stems, leaves and flowers, with higher levels in young leaves, and lower levels in roots. Strongly expressed in inflorescence meristem during cell division. Following submergence treatment, transient decreased levels that recovers after re-aeration. Reduced crop productivity, but increased accumulation of gamma-4-aminobutyraldehyde (GAB-ald) and higher 2-acetyl-1-pyrroline (2AP) biosynthesis, which influences aroma. Present in a truncated form, mostly allele badh2.1, also called 'fgr' in fragrant rice varieties (e.g. basmati and jasmine rice). The loss of activity leads to accumulation of 2-acetyl-1-pyrroline (2AP) that confers the flavor of fragrant rice. Haplotype analysis suggests a single origin of the badh2.1 allele within the Japonica varietal group and demonstrates the introgression of this allele from Japonica to Indica (PubMed:17129318, PubMed:18599581, PubMed:18491070, PubMed:19371779, PubMed:19706531). Belongs to the aldehyde dehydrogenase family. |
O04895 | MAIRVPSRQLFIDGEWREPIKKNRIPIINPSTEEIIGDIPAATAEDVELAVAAARRALKRNKGEDWASASGAHRAKYLRAIAAKITEKKDYFAKLEAMDCGKPLDEAARDIDDVAGCFEYYADQAEALDAKQKAPIALPMDTFKCHVLKQPIGVVGLISPWNYPLLMATWKVAPALAAGCSAVLKPSELASVTCLELAEVCREVGLPPGVLNILTGLGPEAGGPLACHPDVDKVAFTGSTATGSKVMSSAAQLVKPVTLELGGKSPIVIFEDVDLDKAAEWTAFGCFWTNGQICSATSRLLVHESIAAEFLDRLVKWCKNIKISDPFEEGCRLGPVVSKSQYEKVLKFISTAKSEGATILCGGSRPEHLKKGYYVEPTIISDVSTSMQIWREEVFGPVLCQKTFGSEDEAIELANDTQYGLGAAVLSKDLDRCERITKALEVGAVWVNCSQPCFTQAPWGGTKRSGFGRELGEWGIENYLNIKQVTRDTSTDEPWGWYKSP | betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Homodimer. Belongs to the aldehyde dehydrogenase family. |
P42757 | MAFPIPARQLFIDGEWREPLLKNRIPIINPSTEEIIGDIPAATAEDVEVAVVAARKAFKRNKGRDWAALWSHRAKYLRAIAAKITEKKDHFVKLETLDSGKPRDEAVLDIDDVATCFEYFEYFAGQAEALDAKQKAPVTLPMERFKSHVLRQPIGVVGLISPWNYPLLMDTWKIAPALAAGCTTVLKPSELASVTCLEFGEVCNEVGLPPGVLNILTGLGPDAGAPIVSHPDIDKVAFTGSSATGSKIMASAAQLVKPVTLELGGKSPVIMFEDIDIETAVEWTLFGVFWTNGQICSATSRLLVHESIAAEFVDRMVKWTKNIKISDPFEEGCRLGPVISKGQYDKIMKFISTAKSEGATILCGGSRPEHLKKGYYIEPTIITDITTSMQIWKEEVFGPVICVKTFKTEDEAIELANDTEYGLAGAVFSKDLERCERVTKALEVGAVWVNCSQPCFVHAPWGGVKRSGFGRELGEWGIENYLNIKQVTSDISDEPWGWYKSP | betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Homodimer. Belongs to the aldehyde dehydrogenase family. |
P28237 | MSMPIPSRQLFIDGEWREPIKKNRIPIINPSNEEIIGDIPAGSSEDIEVAVAAARRALKRNKGREWAATSGAHRARYLRAIAAKVTERKDHFVKLETIDSGKPFDEAVLDIDDVATCFEYFAGQAEAMDAKQKAPVTLPMERFKSHVLRQPIGVVGLITPWNYPLLMATWKIAPALAAGCTAVLKPSELASITCLEFGEVCNEVGLPPGVLNIVTGLGPDAGAPLAAHPDVDKVAFTGSSATGSKVMASAAQLVKPVTLELGGKSPIIVFEDVDIDQVVEWTMFGCFWTNGQICSATSRLLVHESIAAEFIDRLVKWTKNIKISDPFEEGCRLGPVISKGQYDKIMKFISTAKSEGATILCGGSRPEHLKKGYFIEPTIISDISTSMQIWREEVFGPVLCVKTFSSEDEALELANDTEYGLASAVFSKDLERCERVSKLLESGAVWVNCSQPCFVHAPWGGIKRSGFGRELGEWGIENYLNIKQVTSDISNEPWGWYKSP | betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Homodimer. Belongs to the aldehyde dehydrogenase family. |
Q40024 | MAAPPAIPRRGLFIGGGWREPTLGRHIPVINPATEDTIGDIPAATAEDVELAVAAGGPVLARRREPWARASGATRAKYLNAIAAKITGKIAYLALLETVDSGKPKDEAVADMDDVAACFEYYAALAEALDGKQHAPISLPMEEFKTYVLKEPIGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASLTCLELGAICEEIGLPSGVLNIITGLGPDAGAPIASHPHVDKIAFTGSTATGKTIMTAAAQMVKPVSLELGGKSPLVTFDDVADIDKAVEWPMLGCFFNGGQVCSATSRLLLHEKIAEPFLDRLVEWAKNIKISDPLEEGCRLGSVISKGQYEQIKKFISTARSEGATILHGGDRPKHLGKGFFIEPTINTGVSTSMQIWREEVFGPVICVKVFKTESEAVELANDTHYGLAGGVISDDLERCERIAKVIHSGIVWKNCSQPTLVQAPWGGNKRSGFGRELGEWGLENYLSVKQVTRYCKDELYGWYQRPSKL | betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Homodimer. Belongs to the aldehyde dehydrogenase family. |
O59808 | MTIDLNVIQSDIISARRAPENSLFIDGKFVSPIEPAAKPIPLINPATEEIIGTCANASAKDVDSAVENAYNTFRSGIWAKWPGKQRGLVLRKIAKMMREKRELLAGIDTINCGKPTPYALFDIDSCADMFEYYAEVAETDNPTVKVPLPNNPGFCAFEKRFPRGVIGVITPWNFPLKMALWKLVPAIASGNCVVLKPSELAPWSCLEFALICKEAGLPDGVLNVIIGSGKESGAALSCHPKIAYLAFTGSLATGKKIMHAAAENIVPLTLELGGKSPLIICEDADLSLAIPSAAFAIFFNQGEACTAASRLIVHESVADEVLGGLVSEANKLIIGNGLDPQVTLGPVVSKTQFEKIVSYIQSAINEGCKCVVGGLPRSEQKGYFIPPTVFTNVQTHNKIWREEIFGPVLAVKTFHTNEEALELANDSEYGLGSGVFSTNPKTLEFFSNNIEAGMCSLNNYHVVTHELPWIGWKHSGLGVGLSKHGYNEYMRLKQITQYVG | betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Belongs to the aldehyde dehydrogenase family. |
Q8H1B4 | MAFPIPARQLFIDGEWREPIKKNRIPVINPSTEEIIGDIPAATAEDVEVAVVAARRAFRRNNWSATSGAHRATYLRAIAAKITEKKDHFVKLETIDSGKPFDEAVLDIDDVASCFEYFAGQAEALDGKQKAPVTLPMERFKSHVLRQPLGVVGLISPWNYPLLMATWKIAPALAAGCTAVLKPSELASVTCLEFGEVCNEVGLPPGVLNILTGLGPDAGAPLVSHPDVDKIAFTGSSATGSKVMASAAQLVKPVTLELGGKSPIVVFEDVDIDKVVEWTIFGCFWTNGQICSATSRLLVHESIAAEFVDKLVKWTKNIKISDPFEEGCRLGPVISKGQYDKIMKFISTAKSEGATILYGGSRPEHLKKGYYIEPTIVTDISTSMQIWKEEVFGPVLCVKTFSSEDEAIALANDTEYGLAAAVFSNDLERCERITKALEVGAVWVNCSQPCFVQAPWGGIKRSGFGRELGEWGIQNYLNIKQVTQDISDEPWGWYKSP | Dehydrogenase innvolved in glycine betaine biosynthesis (PubMed:2320587, PubMed:24884441, PubMed:22345508). Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of betaine aldehyde to glycine betaine (PubMed:24884441, PubMed:22345508). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively (PubMed:22345508). 4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) + NADH 3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH 4-(trimethylamino)butanal + H2O + NAD(+) = 4-(trimethylamino)butanoate + 2 H(+) + NADH betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Is reversibly and partially inactivated by betaine aldehyde in the absence of NAD(+) in a time- and concentration-dependent mode. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Forms homodimers. Induced by salt stress. The catalytic activity of the dimeric betaine aldehyde (BADH) from spinach does not require potassium ion as cofactor, contrary to the tetrameric BADH from Pseudomonas aeruginosa (AC Q9HTJ1), although both enzymes contain potassium-binding sites. Belongs to the aldehyde dehydrogenase family. |
O07458 | MMAKKRVATDNAADAKMELANRLFFRLYQCANMLHKTGTRAVEAEGLTTQQWAVLGALSRPTVANGMSVGDLARYLMVSRQNLTGLIGRMERDGHVAVVPDERDRRSRLVTMTKSGRHVWEVLAQPKIRAYYGEVLGDFSINDVTHTLHYLLKILDNMKRLDDGAAGETAATDLE | Transcriptional activator of genes for the anaerobic degradation of benzoate. |
Q6FH21 | MFQIPEFEPSEQEDSSSAERGLGPSPAGDGPSGSGKHHRQAPGLLWDASHQQEQPTSSSHHGGAGAVEIRSRHSSYPAGTEDDEGMGEEPSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFVDSFKKGLPRPKSAGTATQMRQSSSWTRVFQSWWDRNLGRGSSAPSQ | Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways. Forms heterodimers with the anti-apoptotic proteins, Bcl-X(L), Bcl-2 and Bcl-W. Also binds protein S100A10 (By similarity). The Ser-75/Ser-99 phosphorylated form binds 14-3-3 proteins (By similarity). Interacts with AKT1 and PIM3. Interacts (via BH3 domain) with NOL3 (via CARD domain); preventing the association of BAD with BCL2 (By similarity). Interacts with HIF3A (via C-terminus domain); the interaction reduces the binding between BAD and BAX (By similarity). Interacts with GIMAP3/IAN4 and GIMAP5/IAN5 (PubMed:16509771). Colocalizes with HIF3A in the cytoplasm (By similarity). Upon phosphorylation, locates to the cytoplasm. Expressed in a wide variety of tissues. Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. Phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-99 or Ser-75 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-118, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-99 is the major site of AKT/PKB phosphorylation, Ser-118 the major site of protein kinase A (CAPK) phosphorylation. Phosphorylation at Ser-99 by PKB/AKT1 is almost completely blocked by the apoptotic C-terminus cleavage product of PKN2 generated by caspases-3 activity during apoptosis. Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-99. Belongs to the Bcl-2 family. The protein name 'Bcl2 antagonist of cell death' may be misleading. The protein antagonises Bcl2-mediated repression of cell death, hence it promotes apoptosis. Bcl 2-associated death promoter entry |
Q61337 | MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASATDRGLGPSLTEDQPGPYLAPGLLGSNIHQQGRAATNSHHGGAGAMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSAGWTRIIQSWWDRNLGKGGSTPSQ | Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2. Appears to act as a link between growth factor receptor signaling and the apoptotic pathways. Forms heterodimers with the anti-apoptotic proteins, Bcl-X(L), Bcl-2 and Bcl-W. Also binds protein S100A10 (By similarity). The Ser-112/Ser-136 phosphorylated form binds 14-3-3 proteins. Interacts with AKT1 and PIM3 (By similarity). Interacts (via BH3 domain) with NOL3 (via CARD domain); preventing the association of BAD with BCL2 (By similarity). Interacts with HIF3A isoform 2 (via C-terminus domain); the interaction reduces the binding between BAD and BAX (PubMed:21546903). Interacts with GIMAP3/IAN4 and GIMAP5/IAN5 (PubMed:16509771). Colocalizes with HIF3A isoform 2 in the cytoplasm (PubMed:21546903). Upon phosphorylation, locates to the cytoplasm. Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. Phosphorylated on one or more of Ser-112, Ser-136, Ser-155 and Ser-170 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-136 or Ser-112 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-155, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-136 is the major site of AKT/PKB phosphorylation, Ser-155 the major site of protein kinase A (CAPK) phosphorylation. Methylation at Arg-131 and Arg-133 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-136. Belongs to the Bcl-2 family. The protein name 'Bcl2 antagonist of cell death' may be misleading. The protein antagonises Bcl2-mediated repression of cell death, hence it promotes apoptosis. |
Q9JHX1 | MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASTTDRGLGPSLTEDQPGPYLAPGLLGSIVQQQPGQAANNSHHGGAGTMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSASWTRIIQSWWDRNLGKGGSTPSQ | Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways. Forms heterodimers with the anti-apoptotic proteins, Bcl-X(L), Bcl-2 and Bcl-W. Also binds protein S100A10. The Ser-113/Ser-137 phosphorylated form binds 14-3-3 proteins. Interacts with AKT1 and PIM3 (By similarity). Interacts with HIF3A (via C-terminus domain); the interaction reduces the binding between BAD and BAX (By similarity). Interacts (via BH3 domain) with NOL3 (via CARD domain); preventing the association of BAD with BCL2 (PubMed:17998337). Interacts with GIMAP3/IAN4 and GIMAP5/IAN5 (By similarity). Colocalizes with HIF3A in the cytoplasm. Upon phosphorylation, locates to the cytoplasm. Expressed in all tissues tested, including brain, liver, spleen and heart. In the brain, restricted to epithelial cells of the choroid plexus. Isoform alpha is the more abundant form. Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family. Phosphorylated at one or more of Ser-113, Ser-137, Ser-156 and Ser-171 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-137 or Ser-113 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-156, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-137 is the major site of AKT/PKB phosphorylation, Ser-156 the major site of protein kinase A (CAPK) phosphorylation. Methylation at Arg-132 and Arg-134 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-137. Belongs to the Bcl-2 family. The protein name 'Bcl2 antagonist of cell death' may be misleading. The protein antagonises Bcl2-mediated repression of cell death, hence it promotes apoptosis. |
A7Z4X7 | MDHTYEVHQIKTYHQMWSNYCYIIADRSKKSAIAVDPSWEIDKITDKLHELDVDLSAILLTHSHYDHVNLAEPLQQIYHSDIYMSSAEIDFYQFRCRNLIALEDGQTFAAGGFIIRSILTPGHTAGGMCYLLSDHLFTGDTVFTEGCGICGDRGSSAEDMFHSIQRIKASIPPHVRVYPGHSFGEKPGQKMESLLKNNIYFQIEKKEHFVNFRNRKNQKGLFHFK | Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Binds 2 Zn(2+) ions per subunit. Antibiotic biosynthesis; bacillaene biosynthesis. Belongs to the metallo-beta-lactamase superfamily. |
A7Z4X8 | MITYLFPGQGSQKQGMGSSLFDEFKDLTEQADETLGYSMKRLCLENPYSNLHKTQFTQPALYVVNVLSYLKKIQDNDIKPDYVAGHSLGEYNALFAAGAFDFITGLQLVRKRGELMSMATDGKMAAVMGLTAAQVSDALQTHGLHTIDIANMNSPHQVVISGRKEDIERAKSVFEGLKDVTMFHPLNVSGAFHSRYMSEAKQEFEKFLQSFHFSAISIPVISNVHARPYEQDGIHSVLADQIDHSVRWNDSIRYLLDKGRMEFEEVGPGHVLTGLIHRIKNETEASPAM | Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the transfer of the malonyl-CoA group to the acyl-carrier-protein AcpK (Mal-AcpK) (By similarity). holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP] Antibiotic biosynthesis; bacillaene biosynthesis. Belongs to the FabD family. |
A7Z4X9 | MNQPIVFMFSGQGSQYYQMGKELFAHNAAFRQKMLDLDDFAVSRFGYSVLKEMYHTGNRLSDPFDRLLFSHPAIFMAEYALAYALEQRGIRPDYVIGASLGEYAAAAVSGVLSAEDALDCVLEQARIVTETCRNGSMLAILGDPALYQDDPLLGEHSELASVNYHSHFVISGEREHIKKIMDDLREKQIPHQLLPVSYGFHSALVDQAEQPYKRFLAQKSIRTPFIPYISSATGEAETDIQADFFWDIVRKPIRFREALQFADSRQKGLYIDAGPSGTLAAFAKQILPAGSAERIRAIMTPFHKEQTHLQQIEDSILSPPGRRL | Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Antibiotic biosynthesis; bacillaene biosynthesis. |
A7Z4Y0 | MISFVFPGQGSQRIGMGEDLFGRYPELTAKADHILGYSIQELCRDGERLNQTQFTQPALYVVNALSYLKKTEETGLKPDFTAGHSLGEYNALYASGAFDFEEGLQLVKKRGELMSRAKGGGMAAVIGLTHEQVTDVLRENHLDMIDIANMNTPQQIVISGYKEDIEKAASVFEAVNGVKMVHRLNVSGAFHSRYMLEAKEEFSRFIESFHFKPLSIPVISNVTARPYEQRELKETLTGQITGSVNWTDSIRFLMGRKNMSFEEIGPGKVLTGLIQRITAEAEPITDEIKVPAEAGKSSITAASLGNEEFKRDYQLKYAYLAGGMYRGISSKEMVVKLAEKGMMGFFGTGGLNIAHVEDAILSIQHELRDGGSFGINVVHNMKHTDSEEKMIDLLLKHGIQNLEASAFLTVTPALVRFRAKGLKRGAGGQIIARQRIIAKLSRPEVAEAFLSPAPDHILQKLAAENKITAEEASLMREIPVAHDICVEADSGGHTDGGVAYSLMPAIIRLRDDMMKKYRYGKTVRIGAAGGIGTPEAAMAAFMLGADFIVTGSINQCTVEAATSGLVKDLLQQMNVQDTAYAPAGDMFESGSKVQVLKKGLFFPTRASKLHELYQRHRSIEEIDEKTLRQIEEKYFKASVSSIYDKVKAHYSNEDISKAERNPKEKMALIFKWYFRQSSASAIKGDPDAKVDFQIHCGPALGAFNQWVKGTELESWKNRHADGIGMRLMEETASLLNQKLGSFLQTC | Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Probably has an acyl transferase activity and could also have a flavin mononucleotide-dependent oxidoreductase activity. holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP] Antibiotic biosynthesis; bacillaene biosynthesis. In the N-terminal section; belongs to the FabD family. |
P30846 | MTELPIDENTPRILIVEDEPKLGQLLIDYLRAASYAPTLISHGDQVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFSDIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRRCKPQRELQQQDAESPLIIDEGRFQASWRGKMLDLTPAEFRLLKTLSHEPGKVFSREQLLNHLYDDYRVVTDRTIDSHIKNLRRKLESLDAEQSFIRAVYGVGYRWEADACRIV | Member of the two-component regulatory system BaeS/BaeR which responds to envelope stress (PubMed:12354228). Activates expression of periplasmic chaperone spy in response to spheroplast formation, indole and P pili protein PapG overexpression (PubMed:12354228). Activates the mdtABCD (PubMed:12107133, PubMed:12107134) and probably the CRISPR-Cas casABCDE-ygbT-ygbF operon (PubMed:21255106). Phosphorylated by BaeS. Increased sensitivity to membrane stress caused by indole or by overexpression of P pili protein PapG; double baeR-cpxR mutants are more sensitive yet (PubMed:12354228). Loss of induction of the CRISPR-Cas casABCDE-ygbT-ygbF operon (PubMed:21255106). |
P76401 | MKFWRPGITGKLFLAIFATCIVLLISMHWAVRISFERGFIDYIKHGNEQRLQLLSDALGEQYAQHGNWRFLRNNDRFVFQILRSFEHDNSEDKPGPGMPPHGWRTQFWVVDQNNKVLVGPRAPIPPDGTRRPILVNGAEVGAVIASPVERLTRNTDINFDKQQRQTSWLIVALATLLAALATFLLARGLLAPVKRLVDGTHKLAAGDFTTRVTPTSEDELGKLAQDFNQLASTLEKNQQMRRDFMADISHELRTPLAVLRGELEAIQDGVRKFTPETVASLQAEVGTLTKLVDDLHQLSMSDEGALAYQKAPVDLIPLLEVAGGAFRERFASRGLKLQFSLPDSITVFGDRDRLMQLFNNLLENSLRYTDSGGSLQISAGQRDKTVRLTFADSAPGVSDDQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVELPLERDLQREV | Member of the two-component regulatory system BaeS/BaeR which responds to envelope stress (PubMed:12354228, PubMed:21317898). Activates expression of periplasmic chaperone spy in response to spheroplast formation, indole and P pili protein PapG overexpression (PubMed:12354228). Activates BaeR by phosphorylation which then activates the mdtABCD (PubMed:12107134) and probably the CRISPR-Cas casABCDE-ygbT-ygbF operons (PubMed:21255106). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. Autophosphorylated. Loss of induction of the CRISPR-Cas casABCDE-ygbT-ygbF operon (PubMed:21255106). |
A8XAC6 | MSTSVKHREFVGEPMGDKEVTCIAGIGPTYGTKLTDAGFDKAYVLFGQYLLLKKDEDLFVEWLKETAGVTANHAKSAFNCLNEWAEQFI | DNA-binding protein which plays an essential role in nuclear envelope formation. Required for normal chromosome segregation during mitosis. Associates with the nuclear lamina via its interaction with LEM domain containing proteins emr-1 and lem-2 (By similarity). Interacts with emr-1 and lem-2. Interacts with lem-4l, leading to decreased phosphorylation by VRK1 and promoting dephosphorylation by protein phosphatase 2A (PP2A) (By similarity). Phosphorylated by vrk-1. Phosphorylation by vrk-1 in mitosis is essential to achieve correct timing of recruitment of nuclear envelope components during nuclear envelope assembly. Dephosphorylated by protein phosphatase 2A (PP2A) following interaction with lem-4l during mitotic exit, leading to mitotic nuclear envelope reassembly (By similarity). Belongs to the BAF family. |
B7LW74 | MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGDTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTIADIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSATIQQINIVGNHAFTTNELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKLSGVQVTGNLAGHSAEIEELTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSMPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDSVLRREMRQMEGAWLGSDLVDQGKERLNRLGYFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQIGVQQDNWLGTGYAVGINGTKNDYQTYSELSVTNPYFTVDGVSLGGRIFYNDFQADDADLSDYTNKSYGTDVTLGFPINEYNSLRAGLGYVHNKLSNMQPQVAMDRYLESMGEYGKDSFAADDFTFNYGWTYNKLDRGYFPTDGSRVNLTGKVTIPGSDNEYYKLSLDTATYVPIDDDHKWVVLGRTRWGYGDGIGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYKKGAHSSNDEYDDYEECTESNGCQSDDAVGGNAMAVASFELITPTPFISEKYANSVRTSLFWDMGTVWDTNWQASRYPDYPDYSDPGNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
Q39TV7 | MARTDEIIARTAPGHLNDHNLIDREVESLCDGMVKYEKRPAKRHDGSVAEGIYNAWIILDNPKQYNSYTTDMVKAIILAFRRASVDRSVNAVVFTGVGDKAFCTGGNTKEYAEYYAGNPQEYRQYMRLFNDMVSAILGCDKAVISRVNGMRIGGGQEIGMACDFSIAQDLANFGQAGPKHGSAAIGGATDFLPLMVGCEQAMVSGTLCEPFSAHKAARLGIICDVVPALKVGGKFVANPTVVTDRYLDEYGRVVHGEFKAGAAFKEGQGQIKEGEIDLSLLDEKVESLCTKLLETFPECMTKSLEELRKPKLHAWNLNKENSRAWLALNMMNEARTGFRAFNEGTKETGREIDFVKLRQGLAKGTPWTEELIESLMPTAQK | Involved in the central benzoyl-CoA catabolism. Catalyzes the addition of one molecule of water to the double bond and the hydrolytic cleavage of C-C bond in the alicyclic ring, 6-oxocyclohex-1-ene-1-carbonyl-CoA (6-OCH-CoA) to yield 3-hydroxypimelyl-CoA. 6-oxocyclohex-1-ene-1-carbonyl-CoA + 2 H2O = 3-hydroxy-6-carboxyhexanoyl-CoA + H(+) Aromatic compound metabolism; benzoyl-CoA degradation. Homohexamer. By benzoate. Belongs to the enoyl-CoA hydratase/isomerase family. |
P44935 | MKKLLIASLLFGTTTTVFAAPFVAKDIRVDGVQGDLEQQIRASLPVRAGQRVTDNDVANIVRSLFVSGRFDDVKAHQEGDVLVVSVVAKSIISDVKIKGNSIIPTEALKQNLDANGFKVGDVLIREKLNEFAKSVKEHYASVGRYNATVEPIVNTLPNNRAEILIQINEDDKAKLASLTFKGNESVSSSTLQEQMELQPDSWWKLWGNKFEGAQFEKDLQSIRDYYLNNGYAKAQITKTDVQLNDEKTKVNVTIDVNEGLQYDLRSARIIGNLGGMSAELEPLLSALHLNDTFRRSDIADVENAIKAKLGERGYGSATVNSVPDFDDANKTLAITLVVDAGRRLTVRQLRFEGNTVSADSTLRQEMRQQEGTWYNSQLVELGKIRLDRTGFFETVENRIDPINGSNDEVDVVYKVKERNTGSINFGIGYGTESGISYQASVKQDNFLGTGAAVSIAGTKNDYGTSVNLGYTEPYFTKDGVSLGGNVFFENYDNSKSDTSSNYKRTTYGSNVTLGFPVNENNSYYVGLGHTYNKISNFALEYNRNLYIQSMKFKGNGIKTNDFDFSFGWNYNSLNRGYFPTKGVKASLGGRVTIPGSDNKYYKLSADVQGFYPLDRDHLWVVSAKASAGYANGFGNKRLPFYQTYTAGGIGSLRGFAYGSIGPNAIYAEHGNGNGTFKKISSDVIGGNAITTASAELIVPTPFVSDKSQNTVRTSLFVDAASVWNTKWKSDKSGLDNNVLKSLPDYGKSSRIRASTGVGFQWQSPIGPLVFSYAKPIKKYENDDVEQFQFSIGGSF | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Part of the Bam complex. Belongs to the BamA family. |
O25369 | MKKLILSSLVFACINTSVEALENDGSKPNDLTSPKEASQESQKNEAPKNEVQRNEAQKETPQSNQTPKEMKVKSISYVGLSYMSDMLANEIVKIRVGDIVDSKKIDTAVLALFNQGYFKDVYATFEGGILEFHFDEKARIAGVEIKGYGTEKEKDGLKSQMGIKKGDTFDEQKLEHAKTALKTALEGQGYYGSVVEVRTEKVSEGALLIVFDVNRGDSIYIKQSIYEGSAKLKRRMIESLSANKQRDFMGWMWGLNDGKLRLDQLEYDSMRIQDVYMRRGYLDAHISSPFLKTDFSTHDAKLHYKVKEGIQYRISDILIEIDNPVVPLKTLEKALKVKRKDVFNIEHLRADAQILKTEIADKGYAFAVVKPDLDKDEKNGLVKVIYRIEVGDMVYINDVIISGNQRTSDRIIRRELLLGPKDKYNLTKLRNSENSLRRLGFFSKVKIEEKRVNSSLMDLLVSVEEGRTGQLQFGLGYGSYGGLMLNGSVSERNLFGTGQSMSLYANIATGGGRSYPGMPKGAGRMFAGNLSLTNPRIFDSWYSSTINLYADYRISYQYIQQGGGFGVNVGRMLGNRTHVSLGYNLNVTKLLGFSSPLYNRYYSSVNEVVSPRQCSTPASVIINRLSGGKTPLQPESCSSPGAITTSPEIRGIWDRDYHTPITSSFTLDVSYDNTDDYYFPRNGVIFSSYATMSGLPSSGTLNSWNGLGGNVRNTKVYGKFAAYHHLQKYLLIDLIARFKTQGGYIFRYNTDDYLPLNSTFYMGGVTTVRGFRNGSVTPKDEFGLWLGGDGIFTASTELSYGVLKAAKMRLAWFFDFGFLTFKTPTRGSFFYNAPVTTANFKDYGVIGAGFERATWRASTGLQIEWISPMGPLVLIFPIAFFNQWGDGNGKKCKGLCFNPNMDDYTQHFEFSMGTRF | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Part of the Bam complex. Belongs to the BamA family. |
B5Y1J4 | MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRPGDTVTDDDISNTIRALFATGNFEDVRVLRDGDTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTIADIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAKIQQINIVGNHAFSTDELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKISGVQVTGDLAGHSAEIEALTKVEPGELYNGAKVTKMENDIKKLLGRYGYAYPRVQSQPEINDSDKTVKLHVNVDAGNRYYVRKIRFEGNDTSKDAVLRREMRQMEGAWLGSDLVDQGKDRLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYAVGINGTKNDYQTYTELSVTNPYFTVDGVSLGGRIFYNDFDANDADLSDYTNKSYGTDVTLGFPVNEYNTLRAGVGYVHNSLSNMQPQVAMWRYLNSMGQYPDNTNDRNSFSANDFTFNYGWTYNKLDRGFFPTEGSRVNLNGKVTIPGSDNEYYKATLDTATYVPIDNDHQWVVLGRTRFGYGDGIGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYFPSSSRHDGDSGYTNDCKSTESAPCKSDDAVGGNAMAVASLELITPTPFISDKYANSVRTSVFWDMGTVWDTHWDSNAYGGYPDYSDPSNIRMSAGIAVQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
A6T4X9 | MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRPGDTVTDDDISNTIRALFATGNFEDVRVLRDGDTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTIADIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAKIQQINIVGNHAFSTDELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKFSGVQVTGNLAGHSAEIEALTKVEPGELYNGAKVTRMENDIKKLLGRYGYAYPRVQSQPEINDSDKTVKLHVNVDAGNRYYVRKIRFEGNDTSKDAVLRREMRQMEGAWLGSDLVDQGKDRLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYAVGINGTKNDYQTYTELSVTNPYFTVDGVSLGGRVFYNDFDANDADLSDYTNKSYGTDITLGFPVNEYNTLRAGVGYVHNSLSNMQPQVAMWRYLNSMGQYPDNTNDRNSFSANDFTFNYGWTYNKLDRGFFPTEGSRVNLNGKVTIPGSDNEYYKATLDTATYVPIDNDHQWVVLGRTRFGYGDGIGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYFPASSRHDDDDSYDNECKSTESAPCKSDDAVGGNAMAVASLELITPTPFISDKYANSVRTSVFWDMGTVWDTHWDSSAYAGYPDYSDPSNIRMSAGIAVQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
Q9K1H0 | MKLKQIASALMMLGISPLALADFTIQDIRVEGLQRTEPSTVFNYLPVKVGDTYNDTHGSAIIKSLYATGFFDDVRVETADGQLLLTVIERPTIGSLNITGAKMLQNDAIKKNLESFGLAQSQYFNQATLNQAVAGLKEEYLGRGKLNIQITPKVTKLARNRVDIDITIDEGKSAKITDIEFEGNQVYSDRKLMRQMSLTEGGIWTWLTRSNQFNEQKFAQDMEKVTDFYQNNGYFDFRILDTDIQTNEDKTKQTIKITVHEGGRFRWGKVSIEGDTNEVPKAELEKLLTMKPGKWYERQQMTAVLGEIQNRMGSAGYAYSEISVQPLPNAETKTVDFVLHIEPGRKIYVNEIHITGNNKTRDEVVRRELRQMESAPYDTSKLQRSKERVELLGYFDNVQFDAVPLAGTPDKVDLNMSLTERSTGSLDLSAGWVQDTGLVMSAGVSQDNLFGTGKSAALRASRSKTTLNGSLSFTDPYFTADGVSLGYDVYGKAFDPRKASTSIKQYKTTTAGAGIRMSVPVTEYDRVNFGLVAEHLTVNTYNKAPKHYADFIKKYGKTDGTDGSFKGWLYKGTVGWGRNKTDSALWPTRGYLTGVNAEIALPGSKLQYYSATHNQTWFFPLSKTFTLMLGGEVGIAGGYGRTKEIPFFENFYGGGLGSVRGYESGTLGPKVYDEYGEKISYGGNKKANVSAELLFPMPGAKDARTVRLSLFADAGSVWDGKTYDDNSSSATGGRVQNIYGAGNTHKSTFTNELRYSAGGAVTWLSPLGPMKFSYAYPLKKKPEDEIQRFQFQLGTTF | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Part of the Bam complex. Present in outer membrane vesicle formulations which are used as vaccines in human. Belongs to the BamA family. |
C6V5K2 | MVWLLFLSSFCFADEVVEIRISGNKRVSETTVRGLLHVEVGQDVASDELNAVFKRLTASRLFSSVELDLTAGILEVKLQENPILRNVVVKGNKLLSRAAIDKILVYKKDAIFDVHEFENSITALKSYYRDSVVEKTAISYRIVPIDENNVDVEVTVKEAKPTVIRAIEFEGNTTYSDRVLKHVIRSREKSILRLFGTAHYYSREKLEFDKDLLADFYQGKGYFDYALEGLEERENEDGVVLVFKLKEGARYSFGRVSVVSEKGEIEISDLKEKVRIREGAVFNIGAVRENALTLLSVLNERGHMFVNVVPEYHPDANGRVDLTYHVVSTKKYRIRKINISGNTRTKDTVIRREMLLSENDLYQPSKVADSRRRILNLGFFDEVYIEEHKIDGQNLILEVRVKERPTGTLNLSGGYGSDVGFFGNFSFVENNLFGTSDRLVVELQKASLGSNYSMEFQRKRIFDTFITAGASVFYKNRNEKANGLYKFSSVGGDGSVSYSLRDDLRLHLGYSLSFDKIFDVEGDAPESVKSSAGTKILSAVSYSLFLNKLDNYFVPRYGYGVRFGNKFAGIGGDVKFLRSDFKAGGFVSVFDQSAVLSLIVRAGNIFGYSGQGVDVANRFFLNEMRGFDNLGIGPRDVETDDALGGNFFILGTAEVQVPMRLPVELDLKAAFFYEVGTLTGVDVTTEKVYDSHALRSSVGAGLVWNSPFGVLRVDVAKALVEGKGDKVKTVKFGIVSPF | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Part of the Bam complex. Belongs to the BamA family. |
Q6D8D5 | MAIKKLLIASLLFSSATVYGADGFVVKDIHFEGLQRVAVGAALLSMPVRVGDTIGDDDIGNTIRALFATGNFEDVRVLRDGETLIVQVKERPTIASVTFSGNKSVKDDMLKENLEASGVRVGEALDRTALTSIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFTEGVSAKIQQINIVGNKAFSSDELISRFQLRDEVPWWNVVGDRKYQKQKLSGDLETLRSFYLDRGYARFNIDSTQVSLTPDKKGIYITINMTEGEQYKLSGVAVKGNLAGHSAEIEGLTKVEPGELYNGTKVTRMEEDIKKLLGRYGYAYPRVVTQPEINDADKTVRLNINVDAGNRFYVRHVRFDGNDTSKDTVLRREMRQMEGAWLGNDLVEQGKERLNRLGYFESVEVETQRVPGVADQVDVTYKVKERNTGTFNFGVGFGTESGVSFQAGVQQDNWLGTGNSVGISGTKNDYQTYVELSLTDPYFTVDGVSLGGRVFYNKFEASDADLSDYTNVSYGVGSTLGFPINENNSLRVGLDYVHNDLSDMRPQVSMWRYLDSVGVNPSVVGENVKSSADFKANDFFLNTGWSYNNLDRGYFPTKGTRASANAKIAVPGSDNEYYKLTFDSASYYPLTESGKWVVMGRTRAGFADGIGSKEVPFYDNFYAGGSSTVRGFQSNTIGPKAAYYKCPANLVGSGFNSYSGCPIDSTNMDDAVGGNAMAVLSAELIVPTPFISDKYANSVRTSFFVDGGTVWDTNWENTAETLKAGVPDYGKATNFRVSSGIALQWMSPLGPLVFSYAQPVKKYDGDKSEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
C6DAJ1 | MAIKKLLIASLLFSSATVYGADGFVVKDIHFEGLQRVAVGAALLSMPVRVGDTIGDDDIGNTIRALFATGNFEDVRVLRDGGTLIVQVKERPTIASVTFSGNKSVKDDMLKENLEASGVRVGEALDRTALTSIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFTEGVSAKIQQINIVGNKAFSSDELISRFQLRDEVPWWNVVGDRKYQKQKLSGDLETLRSFYLDRGYARFNIDSTQVSLTPDKKGIYITINMTEGEQYKLSGVTVKGNLAGHSAEIEGLTKIEPGELYNGTKVTRMEEDIKKLLGRYGYAYPRVVTQPEINDADKTVRLNINVDAGNRFYVRHIRFDGNDTSKDAVLRREMRQMEGAWLGNDLVEQGKERLNRLGFFESVDVETQRVPGVADQVDVTYKVKERNTGTFNFGVGFGTESGVSFQAGVQQDNWLGTGNSVGISGTKNDYQTYVELSLTDPYFTVDGVSLGGRIFYNKFEASDADLSDYTNVSYGVGSTLGFPINENNSLRVGLDYVHNDLSDMRPQVAMWRYLDSVGVNPAVVQEGNKSSADFKANDFFLNTGWSYNNLDRGYFPTKGTRASANAKIAVPGSDNEYYKLTFDSASYYPLTDSGKWVVMGRTRAGFADGLGGKEVPFYDNFYAGGSSTVRGFQSNTIGPKAAYYKCAVGATSYSNCPIDSTNLDDAVGGNAMAVLSAELIVPTPFISDKYASSVRTSFFVDGGTVWDTNWENTPATIAAGVPDYSKASNFRVSSGIALQWMSPLGPLVFSYAQPVKKYDGDKSEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
Q7N8N9 | MAMKKLLIASLLFGSATAYGADGFVVQDIHFEGLQRVAVGAALLNMPVRVGDTVSDEDIGRTIHALFATGNFEDVRVLRDSNTLIVQVKERPTIASITFSGNKSVKDDMLKQNLEASHVRIGEALDRTMLSNIERGLEDFYYSVGKYNASVKAVVTPLPRNRVDLKLVFAEGVSAKIQQINIVGNKSFSSDELLNRFQLRDDVPWWNLTADQKYQKQKLTGDLEALRSFYLDRGYARFNIDSTQVSLTPDKKGIYVTINITEGDQYKISGIDLNGNMAGYQSEITKLAAIEPGSLYNGTQVTKMENDIKNLLGRYGYAYPRVMTQPEINDQGKTVKLHVNIDAGNRFYVRKIRFSGNDTTKDSVLRREMRQMERAWLGSDLIELGKERLNRLGYFETVDVETQRVPGSPDQVDVVYKVKERNTGSLNFGVGFGTESGVSFQIGAQQDNWLGTGNSVGVNASKNDYSTYAELSFTDPYFTVNGVSLGGRVFYNDFRADDAELSGYTNQSYGIDGFLGFPINENNSLRFGLNYVHNSLSDMLPQAAMWRYLNSMGEKPDYKSKAEFKADDFALNVGWTYNNLDRGFFPTSGVKSTLNGKVTIPGSDNEFYKVTFDTSAYYPINDDRTWVILGRSRLGYGDGLGGKELPFYENFYAGGSSTVRGFRSNNIGPKAIYMNGKDDPKKDSPSRDAVGGNAMAVASLELITPTPFLDSKYSNSVRTSFFIDSGTVWDTYWNDSAAMKGSGIPDYGKPGNIRVSAGIALQWVSPLGPLVFSYAKPIKDYEGDRSEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
Q9S341 | MAMKKLLIASLLFGSAAAYGADGFVVQDIHFEGLQRVAVGAALLNMPVRVGDTVSDEDIGRTIHALFATGNFEDVRVLRDGNTLIVQVKERPTIASITFSGNKSVKDDMLKQNLEASHVRVGEALDRTMLSNIERGLEDFYYSVGKYNASVKAVVTPLPRNRVDLKLVFAEGVSAKIQQINIVGNKSFSSDELLNRFQLRDDVPWWNLTADQKYQKQKLTGDLEALRSFYLDRGYARFNIDSTQVSLTPDKKGIYVTINMTEGDQYKISGIDLNGNMAGYQSEITKLAAIEPGSLYNGTQVTKMENDIKNLLGRYGYAYPRVMTQPEINDQDKTVKLHVNIDAGNRFYVRKIRFSGNDTTKDSVLRREMRQMERAWLGSDLVELGKERLNRLGYFETVDVETQRIPGSPDQVDVVYKVKERNTGSLNFGVGFGTESGVSFQIGAQQDNWLGTGNAVGINASKNDYSTYAELSFTDPYFTINGVSLGGRVFYNDFRADDAELSGYTNQSYGISGFLGFPINENNSLNFGLNYIHNSLSDMLPQVAMWRYLRSMGEKPDLESKAEFKADDFALTMGWTYNNLDRGFFPTSGVKSTLNGKVTIPGSDNEFYKVTLDTSAYYPINDDRTWVILGRSRLGYGDGLGGKELPFYENFYAGGSSTVRGFRSNNIGPKAIYLYKDGSPKKESPSRDAVGGNAMAVASLELITPTPFLDSKYSNSVRTSFFIDSGTVWDTDWNDSAVMKSKGIPDYSKPGNIRVSAGIALQWMSPLGPLVFSYAKPIKDYEGDRSEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
B5F8T8 | MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGNTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTLSDIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAKIQQINIVGNHAFSTEELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKLSGVQVSGNLAGHSAEIEKLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSQPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDSVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYSVGINGTKNDYQTYSELSVTNPYFTVDGVSLGGRIFYNDFEADDADLSDYTNKSYGTDVTLGFPINEYNTLRAGLGYVHNKLSNMQPQIAMDRYLESMGDPDASDFAADDFTFNYGWTYNKLDRGYFPTDGSRVNLTGKVTIPGSDNEYYKVSLDTATYVPIDNDHKWVVLGRTRWGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYKNGARTSGGDNDEYEDCTQESGCKSDDAVGGNAMAVASLEFITPTPFISEKYANSVRTSFFWDMGTVWDTNWDPSSAPSDVPDYSDPGNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
A9MPI4 | MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGDTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTLSDIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAKIQQINIVGNHAFSTEELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKLSGVEVSGNLAGHSAEIENLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSQPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDSVLRREMRQMEGAWLGSDLVDQGKERLNRLGYFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYSVGINGTKNDYQTYSELSVTNPYFTVDGVSLGGRIFYNDFQADDADLSDYTNKSYGSDVTLGFPINEYNTLRAGVGYVHNSLSNMEPQVAMWRYLYSMGEHPNTDDQNNSFKTDDFTFNYGWTYNKLDRGFFPTEGTRINLNGKVTIPGSDNEYYKATLDTATYVPIDDDHKWVILGRTRFGYGDGFGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYFPHAASNYDPDDDYECATQDGAKDMCKSDDAVGGNAMAVASLEFITPTPFISEKYANSVRTSFFWDMGTVWDTNWDSSQYSGYPDYSDPSNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
Q57T31 | MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGNTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTLSDIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAKIQQINIVGNHAFSTEELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKLSGVQVSGNLAGHSAEIEKLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSQPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDSVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYSVGINGTKNDYQTYSELSVTNPYFTVDGVSLGGRIFYNDFQADDADLSDYTNKSYGTDVTLGFPINEYNTLRAGLGYVHNKLSNMQPQIAMDRYLESMGQSADTSSFAADDFTFNYGWTYNKLDRGYFPTDGSRVNLTGKVTIPGSDNEYYKVSLDTATYVPIDNDHKWVVLGRTRWGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYGYGAHTDPNDNNDDYEACTQSSGCKSDDAVGGNAMAVASLEFMTPTPFISEKYANSVRTSFFWDMGTVWDTNWDPSSAPSDVPDYSDPGNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
B5FJ24 | MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGNTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTLSDIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAKIQQINIVGNHAFSTEELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKLSGVQVSGNLAGHSAEIEKLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSQPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDSVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYSVGINGTKNDYQTYSELSVTNPYFTVDGVSLGGRIFYNDFQADDADLSDYTNKSYGTDVTLGFPINEYNTLRAGLGYVHNKLSNMQPQIAMDRYLESMGQSADTSSFAADDFTFNYGWTYNKLDRGYFPTDGSRVNLTGKVTIPGSDNEYYKVSLDTATYVPIDNDHKWVVLGRTRWGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYKNGAHTSWDDNDDYEDCTQESGCKSDDAVGGNAMAVASLEFITPTPFISEKYANSVRTSFFWDMGTVWDTNWDPSSAPSDVPDYSDPGNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
B5R3J0 | MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGNTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTLSDIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAKIQQINIVGNHAFSTEELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKLSGVQVSGNLAGHSAEIEKLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSQPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDSVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYSVGINGTKNDYQTYSELSVTNPYFTVDGVSLGGRIFYNDFQADDADLSDYTNKSYGTDVTLGFPINEYNTLRAGLGYVHNKLSNMQPQIAMDRYLESMGQSADTSSFAADDFTFNYGWTYNKLDRGYFPTDGSRVNLTGKVTIPGSDNEYYKVSLDTATYVPIDNDHKWVVLGRTRWGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYKNGAHTSWDDNDDYEDCTQESGCKSDDAVGGNAMAVASLEFITPTPFISEKYANSVRTSFFWDMGTVWDTNWDPSSAPSDVPDYSDPGNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
B5RHG2 | MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGNTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTLSDIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAKIQQINIVGNHAFSTEELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKLSGVQVSGNLAGHSAEIEKLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSQPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDSVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYSVGINGTKNDYQTYSELSVTNPYFTVDGVSLGGRIFYNDFQADDADLSDYTNKSYGTDVTLGFPINEYNTLRAGLGYVHNSLSNMEPQVAMWRYLASMGQYPSTNDQDNSFSTDDFTFNYGWTYNKLDRGYFPTEGTRINLTGKVTIPGSDNEYYKATLDTATYVPIDNDHKWVILGRTRFGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYYPYNPKNYDADEDYDCATQDGAKDMCKSDDAVGGNAMAVASLEFITPTPFISEKYANSVRTSFFWDMGTVWDTNWDSSQYSGYPDYSDPSNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
B4TK52 | MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGNTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTLSDIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAKIQQINIVGNHAFSTEELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKLSGVQVSGNLAGHSAEIENLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSQPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDSVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSLDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYSVGINGTKNDYQTYSELSVTNPYFTVDGVSLGGRIFYNDFEADDADLSDYTNKSYGTDVTLGFPINEYNTLRAGLGYVHNKLSNMQPQIAMDRYLESMGDPDASDFAADDFTFNYGWTYNKLDRGYFPTDGSRVNLTGKVTIPGSDNEYYKVSLDTATYVPIDNDHKWVVLGRTRWGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYKNGAHTSWDDNDDYEDCTQESGCKSDDAVGGNAMAVASLEFITPTPFISEKYANSVRTSFFWDMGTVWDTNWDPSSAPSDVPDYSDPGNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
B4SV06 | MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGNTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTLSDIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAKIQQINIVGNHAFSTEELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKLSGVQVSGNLAGHSAEIEKLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSQPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDSVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYSVGINGTKNDYQTYSELSVTNPYFTVDGVSLGGRIFYNDFQADDADLSDYTNKSYGTDVTLGFPINEYNTLRAGLGYVHNSLSNMEPQVAMWRYLASMGQYPSTNDQDNSFSTDDFTFNYGWTYNKLDRGYFPTEGTRINLTGKVTIPGSDNEYYKATLDTATYVPIDNDHKWVILGRTRFGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYYPYNPKNYDADEDYDCATQDGAKDMCKSDDAVGGNAMAVASLEFITPTPFISEKYANSVRTSFFWDMGTVWDTNWDSSQYSGYPDYSDPSNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamA family. |
Q74W47 | MITMRCKMLTAAAVMLAMLTAGCSTLEKVVYRPDINQGNYLSPIDASKIHKGMTQQQVAYTLGTPMLQDPFGTQTWFYVFRQQPGHEKITQQTLTLTFDSSGVLTDIKNEPALTGS | Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Belongs to the BamE family. |
Q9I061 | MAKTWIYAASAAAIGGALIGGWLLDPAPPEASPQARQSPAAQAAAAPTAALAAPAADATRMLAPTPVTTPAPRERVTLWQGELRSREGAQGIPEYLAQVEPALLDTLALGQVLEMSLPGRERPLQARLASTHNSAGLPVWRGGLVDGDEAESLTVVRGSLETHINVATLDGSYSIIVDNRSGKTRVIDENDIAARSDPHGDHVDAPLAELPPMPPPAQG | Inhibitor of the metalloendopeptidase Mep72. Forms a protein-protein complex with the protease, which is the product of its coregulated adjacent gene, and probably prevents premature protease activity until the protein has been secreted. Constitutes an operon together with PA2783. Its expression is up-regulated in biofilms, while it is poorly expressed in planktonic cells. |
A0A218KSA8 | MEVHWVCMSAATLLVCYIFGSKFVRNLNGWYYDVKLRRKEHPLPPGDMGWPLIGDLLSFIKDFSSGHPDSFINNLVLKYGRSGIYKTHLFGNPSIIVCEPQMCRRVLTDDVNFKLGYPKSIKELARCRPMIDVSNAEHRLFRRLITSPIVGHKALAMYLERLEEIVINSLEELSSMKHPVELLKEMKKVSFKAIVHVFMGSSNQDIIKKIGSSFTDLYNGMFSIPINVPGFTFHKALEARKKLAKIVQPVVDERRLMIENGPQEGSQRKDLIDILLEVKDENGRKLEDEDISDLLIGLLFAGHESTATSLMWSITYLTQHPHILKKAKEEQEEITRTRFSSQKQLSLKEIKQMVYLSQVIDETLRCANIAFATFREATADVNINGYIIPKGWRVLIWARAIHMDSEYYPNPEEFNPSRWDDYNAKAGTFLPFGAGSRLCPGADLAKLEISIFLHYFLRNYRLERINPECHVTSLPVSKPTDNCLAKVIKVSCA | Involved in the biosynthesis of Glycyrrhetinic acid (GA), a natural product which exhibits anti-inflammatory activity (PubMed:31138208). Catalyzes 2 successive oxidations of beta-amyrin, producing a precursor of the triterpene sweetener glycyrrhizin (PubMed:18779566). Unable to use 11-deoxoglycyrrhetinic acid or ent-kaurenoic acid as substrates (PubMed:18779566). beta-amyrin + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = 11-oxo-beta-amyrin + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase] beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] = 11alpha-hydroxy-beta-amyrin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] 11alpha-hydroxy-beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] = 11-oxo-beta-amyrin + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] Expressed in roots and stolons. Not detected in leaves and stems. Saccharomyces cerevisiae expressing Glycyrrhiza uralensis CYP88D6 and CYP72A154, combined with the expression of Arabidopsis thaliana beta-amyrin synthase (beta-AS) and NADPH-cytochrome P450 reductase 1 (ATR1), accumulates glycyrrhetinic acid (GA) and, to lower levels, beta-amyrin; these GA production was increased in the presence of G.uralensis cytochrome b5 (GuCYB5). The CYP88D subfamily seems to be restricted to the Fabaceae. Belongs to the cytochrome P450 family. |
H9NAL5 | MWRLKLGEGNGDDPYLFSSNNFVGRQTWEFDPKAGTLEERAAVEEARRSFLVNRSRVKACSDLLWRMQFLKEAKFEQVIPPVKIEDAKDITYENATDSLRRGVSFFSALQASDGHWPGEIAGPLFFLPPLVFCLYITGHLEEIFDEEHRKEMLRHVYCHQNEDGGWGLHVESKSIMFCTVLNYICLRMLGEGPNGGRDNACKRARQWILDRGGVTYIPSWGKIWLSILGIYDWSGTNPMPPEIWLLPSFVPIHLAKTLCYCRMVYMPMSYLYGKRFVGPITPLILQLREELHLQPYEAINWNKTRRLYAKEDMYFPHPLVQDLIWDTLHIFVEPLLTHWPLNKLVREKALRLAMKHIHYEDENSHYITIGCVEKVLCMLACWIDDPNGDYFKKHLARIPDYMWVAEDGMKMQSFGSQQWDTGFAVQAIIASDLSSETGDVLKRGHDYIKKSQIRENPSGDFKSMYRHISKGAWTLSDRDHGWQVSDCTAEALKCCLLLSMMPAEVVGHKMDPEQLYDSVNLLLSLQSANGGVTAWEPVRAYAWTELLNPTEFLANLVAEREYVECTSSVVQALVLFQQLYPDHKTKKISRAIEKAVQFLENEQKPDGSWYGNWGVCFIYATWFALGGLAAAGKTYKTSQAMRKGVEFLLTTQKDDGGWGESYLSCPEQRYIPLEGNRSNLVQTAWAIMGLIHAGQAERDPIPLHRAAKLIINSQMENGDFPQQEIVGVFMRNCLLHYATFRNTFPLWALAEYRKAAFVTHKH | Component of the oleanane-type triterpene saponins biosynthetic pathway (PubMed:26333142, PubMed:29603041). Oxidosqualene cyclase converting oxidosqualene into beta-amyrin, generating five rings and eight asymmetric centers in a single transformation (PubMed:26333142, PubMed:29603041). (S)-2,3-epoxysqualene = beta-amyrin Secondary metabolite biosynthesis; terpenoid biosynthesis. Belongs to the terpene cyclase/mutase family. |
A0A0N7AWI6 | MWKLKIAEGNKNDPYLYSTNNFVGRQTWEFDPDYVASPGELEEVEQVRRQFWDNRYQVKPSGDLLWRMQFLREKNFRQTIPQVKVGDDEAVTYEAATTTLRRAVHFFSALQASDGHWPAENSGPLFFLPPLVMCVYITGHLDTVFPAEHRKEILRYIYCHQNEDGGWGLHIEGHSTMFCTTLSYICMRILGEGPDGGVNNACARGRKWILDHGSVTAIPSWGKTWLSILGVYEWIGSNPMPPEFWILPSFLPMHPAKMWCYCRMVYMPMSYLYGKRFVGPITPLILQLREELYGQPYNEINWRKTRRVCAKEDIYYPHPLIQDLLWDSLYVLTEPLLTRWPFNKLREKALQTTMKHIHYEDENSRYITIGCVEKVLCMLVCWVEDPNGDYFRKHLARIPDYIWVAEDGMKMQSFGSQEWDTGFSIQALLDSDLTHEIGPTLMKGHDFIKKSQVKDNPSGDFKSMYRHISKGSWTFSDQDHGWQVSDCTAEGLKCCLIFSTMPEEIVGKKIKPERLYDSVNVLLSLQRKNGGLSAWEPAGAQEWLELLNPTEFFADIVIEHEYVECTSSAIQALVLFKKLYPGHRKKEIDNFITNAVRYLEDTQMPDGSWYGNWGVCFTYGSWFALGGLAAAGKTYYNCAAVRKAVEFLLKSQMDDGGWGESYLSCPKKVYVPLEGNRSNLVHTGWALMGLIHSEQAERDPTPLHRAAKLLINSQMEDGDFPQQEISGVFMKNCMLHYAAYRNIYPLWALAEYRRRVPLPSLGT | Component of the oleanane-type triterpene saponins biosynthetic pathway (PubMed:15821288, PubMed:29378087). Oxidosqualene cyclase converting oxidosqualene into beta-amyrin, generating five rings and eight asymmetric centers in a single transformation (PubMed:9746369). (S)-2,3-epoxysqualene = beta-amyrin Secondary metabolite biosynthesis; terpenoid biosynthesis. Monomer. Mostly expressed in roots, and, to a lower extent, in stems and leaves. Progressive decrease in roots from the leaf opened stage to the green fruit, red fruit and root growth stages, respectively. Induced methyl jasmonate (MeJA) in adventitious roots (PubMed:15356323, PubMed:15538577). Accumulates upon Cle-mediated signaling, an elicitor derived from fungal cell walls of C.lagenarium, thus inducing the accumulation of saponins. Triggered by ethylene (ACC), rose bengal (RB), nitric oxide (NO) and hydrogen peroxide (H(2)O(2)) (PubMed:15821288). Accumulates under heavy metal stress in the presence of NiCl(2) and CdCl(2) (PubMed:23232757). Influenced in roots and leaves by relative humidity, and in roots by soil water potential (PubMed:30577538). Belongs to the terpene cyclase/mutase family. |
O82146 | MWRLMTAKGGNDPYLYSTNNFIGRQTWEFDPDYGTPAERAEVEEARLHFWNNRYQVKPSSDVLWRMQFLKEKNFKQIIPQVKVEDGEEITYEAATTTLRRAVHYFSALQADDGHWPAENAGPLFFLPPLVMCLYITGHLNTVFPAEHRIEILRYIYCHQNDDGGWGLHIEGHSTMFCTALSYICMRILGEGRDGGENNACARARKWILDHGSVTAIPSWGKTWLSILGLFDWSGSNPMPPEFWILPPFLPMHPAKMWCYCRMVYMPMSYLYGKRFVGPITPLILQLREELYAQAYDEINWRKVRHNCAKEDLYYPHPLIQDLMWDSLYIFTEPFLTRWPFNKLREKALQTTMKHIHYEDENSRYITIGCVEKVLCMLACWVEDPNGDYFKQHLARIPDYIWVAEDGMKMQSFGSQEWDTGFAIQALLASDLIDEIRPTLMKGHDFIKKSQVKENPSGDFKSMHRHISKGSWTFSDQDHGWQVSDCTAEALKCCLLFSRMPTEIVGDKMEDNQLFDAVNMLLSLQSKNGGLAAWEPAGSSEWLELLNPTEFFEDIVIEHEYVECTSSAIQAMVMFKKLYPGHRKKEIEVSITNAVQYLEDIQMPDGSWYGNWGVCFTYGTWFAMGGLTAAGKTYNNCQTLHKAVDFLIKSQRSDGGWGESYLSCPNKEYTPLEGNRSNLVHTSWAMMGLIHSRQAERDPTPLHRAAKLLINSQMESGDFPQQEITGVFMKNCMLHYAASRNIYPLWALAEYRKNVRLPSKSV | Component of the oleanane-type triterpene saponins (e.g. ginsenosides or panaxosides) biosynthetic pathway (PubMed:29378087). Oxidosqualene cyclase converting oxidosqualene into beta-amyrin, generating five rings and eight asymmetric centers in a single transformation (By similarity). (S)-2,3-epoxysqualene = beta-amyrin Secondary metabolite biosynthesis; terpenoid biosynthesis. Monomer. Belongs to the terpene cyclase/mutase family. |
Q8W3Z1 | MWRLKIADGGSDPYIYSTNNFVGRQTWEFDPQAGSPQERAEVEEARRNFYDNRYQVKPSGDLLWRMQFLKEKNFKQTIPPVKVEDGEEITYEKSTAALRRAVHFYSALQASDGHWPAENAGPLFFLPPLVMCMYITGHLNTVFPAEHQKEILRYIYYHQNEDGGWGLHIEGHSTMFCTALSYICMRILGEGPDGGQDNACARARKWILDHGGVTHMPSWGKTWLSILGIFEWIGSNPMPPEFWILPSFLPMHPAKMWCYCRMVYMPMSYLYGKRFVGPITPLILQLREELYTQPYHQVNWKKVRHLCAKEDIYYPHPLIQDLLWDSLYIFTEPLLTRWPFNKLVREKALQVTMKHIHYEDENSRYITIGCVEKVLCMLACWVEDPNGDYFKKHIARIPDYIWVAEDGIKMQSFGSQEWDTGFAIQALLASNLTDEIGPTLARGHDFIKKSQVKDNPSGDFESMHRHISKGSWTFSDQDHGWQVSDCTAEGLKCCLLFSIMPPEIVGEKMEPEQLYDSVNVLLSLQSKNGGLAAWEPAGAQEWLELLNSTEFFADIVIEHEYIECTASAMQTLVLFKKLYPGHRKKEIENFIKNAAQFLQVIQMPDGSWYGNWGVCFTYGTWFALGGLAAVGKTYNNCLAVRRAVDFLLRAQRDNGGWGESYLSCPKKEYVPLEGNKSNLVHTAWAMMGLIHAGQAERDPTPLHRAAKLIINSQLEDGDFPQQEITGVFMKNCMLHYAAYKNIYPLWALAEYRKHVPLPLGKNLNQVVNCIGQSLYKKYK | Oxidosqualene cyclase converting oxidosqualene into beta-amyrin, generating five rings and eight asymmetric centers in a single transformation. (S)-2,3-epoxysqualene = beta-amyrin Belongs to the terpene cyclase/mutase family. |
Q9MB42 | MWRLKIAEGGKDPYIYSTNNFVGRQTWEYDPDGGTPEERAQVDAARLHFYNNRFQVKPCGDLLWRFQILRENNFKQTIASVKIGDGEEITYEKATTAVRRAAHHLSALQTSDGHWPAQIAGPLFFLPPLVFCMYITGHLDSVFPEEYRKEILRYIYYHQNEDGGWGLHIEGHSTMFCTALNYICMRILGEGPDGGQDNACARARKWIHDHGGVTHIPSWGKTWLSILGVFDWCGSNPMPPEFWILPSFLPMHPAKMWCYCRLVYMPMSYLYGKRFVGPITPLILQLREELFTEPYEKVNWKKARHQCAKEDLYYPHPLLQDLIWDSLYLFTEPLLTRWPFNKLVREKALQVTMKHIHYEDETSRYITIGCVEKVLCMLACWVEDPNGDAFKKHLARVPDYLWVSEDGMTMQSFGSQEWDAGFAVQALLATNLVEEIAPTLAKGHDFIKKSQVRDNPSGDFKSMYRHISKGSWTFSDQDHGWQVSDCTAEGLKCCLLLSMLPPEIVGEKMEPERLYDSVNVLLSLQSKKGGLSAWEPAGAQEWLELLNPTEFFADIVVEHEYVECTGSAIQALVLFKKLYPGHRKKEIENFIANAVRFLEDTQTADGSWYGNWGVCFTYGSWFALGGLAAAGKTFANCAAIRKAVKFLLTTQREDGGWGESYLSSPKKIYVPLEGSRSNVVHTAWALMGLIHAGQAERDPAPLHRAAKLIINSQLEEGDWPQQEITGVFMKNCMLHYPMYRDIYPMWALAEYRRRVPLPSTPVCLT | Oxidosqualene cyclase converting oxidosqualene into beta-amyrin, generating five rings and eight asymmetric centers in a single transformation. Required for the production of soyasaponins and glycyrrhizin. (S)-2,3-epoxysqualene = beta-amyrin Highly expressed in thickened roots and root nodules. Detected in roots, hypocotyls and cotyledons of young seedlings. Peak of expression 2 days after germination. High levels of expression when aerial parts are growing. Up-regulated by methyl jasmonate (MeJA) and down-regulated by gibberellin A3 (GA3). Belongs to the terpene cyclase/mutase family. |
Q9LRH8 | MWRLKIAEGGNDPYLFSTNNFVGRQTWEYDPEAGSEEERAQVEEARRNFYNNRFEVKPCGDLLWRFQVLRENNFKQTIGGVKIEDEEEITYEKTTTTLRRGTHHLATLQTSDGHWPAQIAGPLFFMPPLVFCVYITGHLDSVFPPEHRKEILRYIYCHQNEDGGWGLHIEGHSTMFCTALNYICMRILGEGPDGGEDNACVRARNWIRQHGGVTHIPSWGKTWLSILGVFDWLGSNPMPPEFWILPSFLPMHPAKMWCYCRLVYMPMSYLYGKRFVGPITPLILQLREELHTEPYEKINWTKTRHLCAKEDIYYPHPLIQDLIWDSLYIFTEPLLTRWPFNKLVRKRALEVTMKHIHYEDENSRYLTIGCVEKVLCMLACWVEDPNGDAFKKHIARVPDYLWISEDGMTMQSFGSQEWDAGFAVQALLATNLIEEIKPALAKGHDFIKKSQVTENPSGDFKSMHRHISKGSWTFSDQDHGWQVSDCTAEGLKCCLLLSLLPPEIVGEKMEPERLFDSVNLLLSLQSKKGGLAAWEPAGAQEWLELLNPTEFFADIVVEHEYVECTGSAIQALVLFKKLYPGHRKKEIENFIFNAVRFLEDTQTEDGSWYGNWGVCFTYGSWFALGGLAAAGKTYTNCAAIRKGVKFLLTTQREDGGWGESYLSSPKKIYVPLEGNRSNVVHTAWALMGLIHAGQSERDPTPLHRAAKLLINSQLEQGDWPQQEITGVFMKNCMLHYPMYRDIYPLWALAEYRRRVPLP | Oxidosqualene cyclase converting oxidosqualene into beta-amyrin, generating five rings and eight asymmetric centers in a single transformation. (S)-2,3-epoxysqualene = beta-amyrin Belongs to the terpene cyclase/mutase family. |
E7DN63 | MWKLKIAEGQNGPYLYSTNNYVGRQTWEFDPNGGTIEERAKIEEARQQFWNNRYKVKPSSDLLWRIQFLGEKNFKQKIPAVKVEEGEEISHEVATIALHRAVNFFSALQATDGHWPAENAGPLFFLPPLVMCMYITGHLNTVFPAEHRKEILRYIYCHQNEDGGWGLHIEGHSTMFCTALSYICMRILGEGPDGGVNNACARARKWILDHGSVTAIPSWGKTWLSILGVFEWIGTNPMPPEFWILPSFLPVHPAKMWCYCRMVYMPMSYLYGKRFVGPITPLILQLREELYDRPYDEINWKKVRHVCAKEDLYYPHPLVQDLMWDSLYICTEPLLTRWPFNKLRNKALEVTMKHIHYEDENSRYITIGCVEKVLCMLACWVEDPNGDYFKKHLARIPDYLWVAEDGMKMQSFGSQEWDTGFAIQALLASEMNDEIADTLRKGHDFIKQSQVTNNPSGDFKGMYRHISKGSWTFSDQDHGWQVSDCTAEALKCCLLLSTMPRELVGQAMEPGRLYDSVNVVLSLQSKNGGLAAWEPAGASEYLELLNPTEFFADIVIEHEYVECTASSIQALVLFKKLYPGHRTKEINIFIDNAVKYLEDVQMPDGSWYGNWGVCFTYGSWFALGGLVAAGKSYNNSAAVRKGVEFLLRTQRSDGGWGESYRSCPDKVYRELETNDSNLVQTAWALMGLIHSGQADRDPKPLHRAAKLLINSQMEDGDFPQQEITGVFMKNCMLHYAAYRNIYPLWGLAEYRKNVLLPLENN | Oxidosqualene cyclase converting oxidosqualene into beta-amyrin, generating five rings and eight asymmetric centers in a single transformation. (S)-2,3-epoxysqualene = beta-amyrin Expressed in the leaves and in the epidermal cells but not in the inner tissues of the fruit. Belongs to the terpene cyclase/mutase family. |
Q9FYZ9 | MKVMKKLLCMNIAGDGETSYANNSGLQKVMMSKSLHVLDETLKDIIGDHVGFPKCFKMMDMGCSSGPNALLVMSGIINTIEDLYTEKNINELPEFEVFLNDLPDNDFNNLFKLLSHENGNCFVYGLPGSFYGRLLPKKSLHFAYSSYSIHWLSQVPEGLEDNNRQNIYMATESPPEVYKAYAKQYERDFSTFLKLRGEEIVPGGRMVLTFNGRSVEDPSSKDDLAIFTLLAKTLVDMVAEGLVKMDDLYSFNIPIYSPCTREVEAAILSEGSFTLDRLEVFRVCWDASDYTDDDDQQDPSIFGKQRSGKFVADCVRAITEPMLASHFGSTIMDLLFGKYAKKIVEHLSVENSSYFSIVVSLSRR | Converts benzoic acid into the volatile ester methyl benzoates. This scent, mostly produced in a rhythmical, diurnal manner, attracts the pollinators. benzoate + S-adenosyl-L-methionine = methyl benzoate + S-adenosyl-L-homocysteine Expressed only in the upper and lower petal lobes (PubMed:10852939, PubMed:14630969). Not found in the corolla tubes, anthers, pistils, sepals and ovaries (PubMed:10852939). Expressed in mature flowers with a peak 6 to 7 days postanthesis. Fades out in flower petals after pollination, thus resulting in a decrease in methylbenzoate emission (PubMed:14630969). Strongly repressed by ethylene (PubMed:14630969). The N-terminus is blocked. Belongs to the methyltransferase superfamily. Type-7 methyltransferase family. |
Q7XDM6 | MALNLAQSAAAAACFATAGDARRAASVVAMPSSSSSATTSLRMKRQAACEPVACRAVARHVAAAAASSRRNGVPVFVMMPLDTVSKCGSALNRRKAVAASLAALKSAGVEGIMVDVWWGIVESEGPGRYNFDGYVELMEMARKTGLKVQAVMSFHQCGGNVGDSVNIPLPRWVVEEMEKDNDLAYTDQWGRRNFEYISLGCDAMPVFKGRTPVECYTDFMRAFRDHFASFLGDTIVEIQVGMGPAGELRYPSYPESNGTWRFPGIGAFQCNDRYMRSSLKAAAEARGKPEWGHGGPTDAGGYNNWPEDTVFFRGDCGGWSTEYGEFFLSWYSQMLLEHGERVLSGATSVFGDGAGAKISVKVAGIHWHYGTRSHAPELTAGYYNTRHRDGYLPIARMLARHGAVLNFTCVEMRDHEQPQEAQCMPEALVRQVAAAARAAGVGLAGENALPRYDGTAHDQVVAAAADRAAEDRMVAFTYLRMGPDLFHPDNWRRFVAFVRRMSESGSPREAAESAAHGVAQATGSLVHEAAVALRS | Possesses beta-amylase activity in vitro (PubMed:21512221). May be involved in cold resistance by mediating the accumulation of maltose upon freezing stress, thus contributing to the protection of membranes (Probable). Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains. Optimum pH is 5.5-6.0. Optimum temperature is 35 degrees Celsius. Belongs to the glycosyl hydrolase 14 family. |
A3ADZ2 | MMSLNLAHQTGAAAAVAPAAPRTAVVAAAAGTVSAPAVAPAAAPSLQLQTQTVDPAAPAQGPDLPMAFQALVESLPEEQHPDVGGEERRKVGVPVYVMMPLDTVRKDGNGLNRRKAVEASLKALKSAGAEGIMVDVWWGIAECEGPGRYNFTGYMELMEMAKKNGLKVQAVMSFHQCGGNVGDSVTIPLPKWVLEEMDKDQDLAYTDRSGRRNYEYLSLGADAMPVLKGRTPVQCYGDFMRAFRDHFAAFMGNTIVEIQVGMGPAGELRYPSYPESNGTWRFPGIGEFQCYDRYMLSSLKAAAEAVGKPEWGNAGPGDSGGYNDWPEDSPFFRREGGWNTPYGEFFMSWYSQMLLEHGERILSAASGVYTGTPGVKISVKVAGIHWHYGTRSHAAELTAGYYNTRHHDGYQPIARMLARHGAVLNFTCVEMRNHEQPQDAQCRPEELVQQVAAAARESGVGLAGENALPRYDETAHDQIVTTAAEKAEEERMVAFTYLRMGPDLFQPDNWRRFAAFVKRMTESGVRDVCREQVEREAQGVAHATGSLVHEAAVALSN | Possesses beta-amylase activity in vitro (PubMed:21512221). May be involved in cold resistance by mediating the accumulation of maltose upon freezing stress, thus contributing to the protection of membranes (Probable). Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains. Optimum pH is 5.5-6.0. Optimum temperature is 35 degrees Celsius. Belongs to the glycosyl hydrolase 14 family. Truncated N-terminus. |
Q9VBV0 | MLNARDVCPEGNDDQQLDHNFKQMEEHLALMVEGNENEDPRKATCEYEDTNEDGATCTSGVLSEIQENFGRLRLCDVTAPLLEFHGLDCLQQIQKRSRHFAFDGSPAKKSRSGGVLVTGPKQKQLQKENVWNRKSKGSASADNIEKLPITIEKLHMIGLHGDCLEHNAVLRLMNLFRSLHDHLTADLGFSRQNSMPSDYLFDMPVKSTMPKSLNVRYQLQVLCTKVERFLVQQRRTLEANRHFDFEKYDECDKLLKGFASYLDNFKLLLKPKMRNRNGNSGSNADKFHTQRMERLLIGLRDWIKAAHLSVHVFNWEMDLEHRYSGAMTESHKSLNERAILLSGAELRAAEARGISAEDLFIAQRYKLGGPIYCVLEQHEFLSALIANPETYFPPSVVAICGPQKLGAVSMEQPSASEEEFEETEEVPSSPPRHTGRVPRFRS | Required to initiate both male and female gametogenesis. May regulate cystoblast cell divisions. In cystoblasts and/or very early cystocytes in ovary and testis. Flies exhibit abnormal cysts, they contain an excess number of cells that cannot differentiate into gametes. |
Q9NWP2 | MLPAAPGKGLGSPDPAPCGPAPPGNTKDIIMIYEEDAEEWALYLTEVFLHVVKREAILLYRLENFSFRHLELLNLTSYKCKLLILSNSLLRDLTPKKCQFLEKILHSPKSVVTLLCGVKSSDQLYELLNISQSRWEISTEQEPEDYISVIQSIIFKDSEDYFEVNIPTDLRAKHSGEISERKEIEELSEASRNTIPLAVVLPTEIPCENPGEIFIILRDEVIGDTVEVEFTSSNKRIRTRPALWNKKVWCMKALEFPAGSVHVNVYCDGIVKATTKIKYYPTAKAKECLFRMADSGESLCQNSIEELDGVLTSIFKHEIPYYEFQSLQTEICSQNKYTHFKELPTLLHCAAKFGLKNLAIHLLQCSGATWASKMKNMEGSDPAHIAERHGHKELKKIFEDFSIQEIDINNEQENDYEEDIASFSTYIPSTQNPAFHHESRKTYGQSADGAEANEMEGEGKQNGSGMETKHSPLEVGSESSEDQYDDLYVFIPGADPENNSQEPLMSSRPPLPPPRPVANAFQLERPHFTLPGTMVEGQMERSQNWGHPGVRQETGDEPKGEKEKKEEEKEQEEEEDPYTFAEIDDSEYDMILANLSIKKKTGSRSFIINRPPAPTPRPTSIPPKEETTPYIAQVFQQKTARRQSDDDKFCGLPKKQDRARIESPAFSTLRGCLTDGQEELILLQEKVKNGKMSMDEALEKFKHWQMGKSGLEMIQQEKLRQLRDCIIGKRPEEENVYNKLTIVHHPGGKETAHNENKFYNVHFSNKLPARPQVEKEFGFCCKKDH | Involved in B-cell receptor (BCR)-induced Ca(2+) mobilization from intracellular stores. Promotes Lyn-mediated phosphorylation of IP3 receptors 1 and 2. Interacts with LYN, ITPR1 and ITPR2. Expressed in B-cell but not T-cell or myeloid cell lines. Highest expression in CD19(+) B-cells, with very low expression in other cell populations. Phosphorylated on tyrosines upon BCR activation. Disease susceptibility may be associated with variants affecting the gene represented in this entry. |
Q8BRY8 | MLPVASGTRGSTQDLFQVGLAPPGNAKDILLLYEEDAEEWALYLREIFMRVVEREAILLYPLHSFSSSHLEMLNFYAYKCKLLIISNSLLKDLTPKKCQFLEKILHSTGNVVTLLCGMESSDPFYQLLSIPRKRWEISTEQDPDGYISVIRQILDQGPEDYLEVSIPTDSRAKYPEDTSGQKGTDVLASLRPSVPRVLVLPGEIPCEKPGEIFILLKDELIGEILEVEFISTNKRLRARPARWNKSVWHMKAADFPAGSVTVNIHCDGIIKATTEIKYCSAAKATESPFRVSDPGKSLCQKSIEELDNVLASIFKREIPYYEFKHLQAETYPQKERTHTTELPTLLHCAAKFGLKNLALHLLQCSGATRAARMKATDGSDLLHIAERHGHEELKEVFEDFLSQNTGRNSKQENDYEEDVISFSTYSPSMPSPASLHELRKTHRRNTDRSEEPERSVEMKEEEAGAEARRSLSEGERESSENQYDDLYVFIPGFDTEGNSEEPLPHCRPPLLPPRPGTAASQLERPHFTSQGKVLEDQMERSQNWNDLNARPETREESSREEKKEEAQEEEEEEENPYAFAETEDNEYDLILASKSVKKRTGNRSFIINRPPAPTPRPTHIPPKEETTPYIAQVFQQKAARRQSDGDKFYSLPKKPDKTRMEGPTFPSTRDYLTTGQEELILLQERVKNGKMSVDEALEKFKHWQMGKSGLEMIQQEKLRQLRDNIIGKRPEDENAYDKLTIVHHPSGNTAHNENMLYNSPFNSKFPARIQVEKEFGFCCKKDH | Involved in B-cell receptor (BCR)-induced Ca(2+) mobilization from intracellular stores. Promotes Lyn-mediated phosphorylation of IP3 receptors 1 and 2 (By similarity). Interacts with LYN, ITPR1 and ITPR2. Specifically expressed in spleen. Highly expressed in immature B-cells and recirculating B-cells, and at low levels in pro-B and pre-B cells. Phosphorylated on tyrosines upon BCR activation. Truncated C-terminus. |
Q0VCW3 | MMSEQDLADVVQIAVEELSPGHPVVLENHVVTDEDEPALKRQRLEINCQDPSIKSFLYSINQTICLRLDSIEAKLQALEATCKSLEEKLDLVTNKQHSPIQVPMVAGSPLGATQTCNKVRCVVPQTTVILNSDRQNAVVAKMEDPLSGRAPEPLENVISNAVPGRRQNTIVVKVPGQEDSHNEDGESGSEASDSVSNCGQSGSQNIGNNVTLITLNSEEDYPNGTWLGDENNPEMRVRCAIIPSDMLHISTNCRTAEKMALTLLDYLFHREVQAVSNLSGQGKHGKKQLDPLTIYGIRCHLFYKFGITESDWYRIKQSIDSKCRTAWRRKQRGQSLAVKSFSRRTPSSSSYGASETMMSTPPPSSELQQPPPQALHYALANAQQVQIHQIGEDGQVQVGHLHIAQVPQGEQVQITQDSEGNLQIHHVGQDGQVLQGAQLIAVASSDPAATGVDGSPLQGSDIQVQYVQLAPVTDHTAAAQAADALQPTLQPEMQLEHGAIQIQ | Controls V(D)J recombination during T-cell development by repressing T-cell receptor (TCR) beta enhancer function. Binds to scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Represses cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 activation, which causes cell cycle arrest (By similarity). Interacts with TP53 (By similarity). Interacts with CUX1/CDP (By similarity). Interacts with HDAC1 (By similarity). Part of a corepressor complex containing BANP, HDAC1, SIN3A, SIN3B, RBL1 and RBL2 (By similarity). Belongs to the BANP/SMAR1 family. |
Q502P7 | MMSEQGLVEIVQIAVADLNHEGHQTDVLENNEDSDQPGRKRARIEISQETSIKSMLISISQAICQRLDSMEAKLQVLEVTCRGLVEKLDTVMGKNQSTTQVPMVSGSPFGATQTCDKVRCVVPQTNVIVSGDRAKTEETSPRTSDSLENLLSNTVGRGRQKTIVLKVPVQEEIQDDQESGSETSDSVSNSGQPQNNNNVTLITLNSEEDYPTGTWLGDENNPEMRVRCPVSPADMLHISTNCRTAEKMALTLLDYLFHREVQAVSNLSGQGKHGKKQLDPLMIYGIRCHLFFKFAITESDWYRIKQSIDSKCRTAWRRKQRGQSLAVKSFSRRTPASQSSSDGVSAAETSAIETSTQQALHYALAGATQQVQIHRIGEDGQVQVIPQGHLHIAQVPQGEQVQITQDSEGNLQIHQVHVGQDGQVNVLRGPQLIAVASTDGTGGVDASPLQANDIQVQYVQLGTVTDHTGAVQAEALTPALQAEMDVKEAIQLQQAENGEVVQIQMPGT | DNA-binding protein which may repress cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 activation, which causes cell cycle arrest (By similarity). Belongs to the BANP/SMAR1 family. |
Q9NWY1 | MMSEHDLADVVQIAVEDLSPDHPVVLENHVVTDEDEPALKRQRLEINCQDPSIKTICLRLDSIEAKLQALEATCKSLEEKLDLVTNKQHSPIQVPMVAGSPLGATQTCNKVRCVVPQTTVILNNDRQNAIVAKMEDPLSNRAPDSLENVISNAVPGRRQNTIVVKVPGQEDSHHEDGESGSEASDSVSSCGQAGSQSIGSNVTLITLNSEEDYPNGTWLGDENNPEMRVRCAIIPSDMLHISTNCRTAEKMALTLLDYLFHREVQAVSNLSGQGKHGKKQLDPLTIYGIRCHLFYKFGITESDWYRIKQSIDSKCRTAWRRKQRGQSLAVKSFSRRTPNSSSYCPSEPMMSTPPPASELPQPQPQPQALHYALANAQQVQIHQIGEDGQVQVGHLHIAQVPQGEQVQITQDSEGNLQIHHVGQDGQLLEATRIPCLLAPSVFKASSGQVLQGAQLIAVASSDPAAAGVDGSPLQGSDIQVQYVQLAPVSDHTAGAQTAEALQPTLQPEMQLEHGAIQIQ | Controls V(D)J recombination during T-cell development by repressing T-cell receptor (TCR) beta enhancer function. Binds to scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Represses cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 activation, which causes cell cycle arrest (By similarity). Interacts with TP53 (By similarity). Interacts with CUX1/CDP (By similarity). Interacts with HDAC1 (PubMed:16166625). Part of a corepressor complex containing BANP, HDAC1, SIN3A, SIN3B, RBL1 and RBL2 (PubMed:16166625). Down-regulated in breast cancer cell lines. Belongs to the BANP/SMAR1 family. Extended N-terminus. |
Q9ES51 | MMSEQDLADVVQIAVEDLSPDHPVVLENHVVTDDDEPALKRQRLEINCQDPSIKSFLYSINQTICLRLDSIEAKLQALEATCKSLEEKLDLVTNKQHSPIQVPMVAGSPLGATQTCNKVRCVVPQTTVILNNDRQNAIVAKMEDPLSNRAPDSLENIISNAVPGRRQNTIVVKVPGQDDSHNEDGESGSEASDSVSNCGQPGSQNIGSNVTLITLNSEEDYPNGTWLGDENNPEMRVRCAIIPSDMLHISTNCRTAEKMALTLLDYLFHREVQAVSNLSGQGKHGKKQLDPLTIYGIRCHLFYKFGITESDWYRIKQSIDSKCRTAWRRKQRGQSLAVKSFSRRTPSSSSYSASETMMGTPPPTSELQQSQPQALHYALANAQQVQIHQIGEDGQVQVIPQGHLHIAQVPQGEQVQITQDSEGNLQIHHVGQDGQSWGLCQNPIPVSGDSVAQANPSQLWPLGGDTLDLPAGNEMIQVLQGAQLIAVASSDPAATGVDGSPLQGSDIQVQYVQLAPVSDHTAAAQTAEALQPTLQPDMQLEHGAIQIQ | Controls V(D)J recombination during T-cell development by repressing T-cell receptor (TCR) beta enhancer function. Binds to scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Represses cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 activation, which causes cell cycle arrest and inhibits tumor growth (PubMed:12494467). Interacts with TP53 (PubMed:12494467). Interacts with CUX1/CDP (PubMed:15371550). Interacts with HDAC1 (PubMed:16166625). Part of a corepressor complex containing BANP, HDAC1, SIN3A, SIN3B, RBL1 and RBL2 (PubMed:16166625). Highly expressed in heart, spleen, and thymus. Isoform 1 is highly expressed in kidney, brain and testis. Isoform 3 is highly expressed in kidney and lung. Belongs to the BANP/SMAR1 family. Interaction with TP35 was reported to promotes TP53 'Ser-15' phosphorylation and nuclear accumulation causing cell cycle arrest and inhibition of tumor growth (PubMed:15701641). However, the publication has been retracted due to image duplication and manipulation. Interaction with TP35 has been confirmed by other studies (PubMed:12494467). The nuclear locatization has been confirmed by other studies (PubMed:10940556, PubMed:12494467, PubMed:15371550, PubMed:16166625). |
A0A1S4DN73 | MFPLIILISFSFTFLSASATSGAGEGVANLSTCLINHNVHNFSMYPTSRNYFNLLDFSLQNLRFAASNMPKPTVIILPNSKEELVSTILCCRQTSYEIRVRCGGHSYEGTSSVSFDGSPFVIIDLMKLDDVSVDLDSETAWAQGGATIGQIYYAIAKASDVHAFSAGSGPTVGSGGHISGGGFGLLSRKFGVAADSVVDALLIDADGRLLDRKAMGEDVFWAIRGGGGGNWGIIYAWKIRLVKVPKIVTTFKISKPGSKQYVAPLLYKWQIVAPNLADDFTLGVQMIPIDLPADMKYGNPTPIEICPQFNGLYLGPKTEAVSILNEAFPELNVKNDDAKEMTWIESALFFSDLDNIFGNSSDDISHLKERYLGVKICFKGKSDYVKTPFSMDGIMTALVEHEKNPNAFLVFDPYGGAMDKISAQAIAFPHRKGNLFAIQYYAQWNEEDDAKSNEHIEWIRGFYNKMAPFVSSSPRGAYVNYLDMDLGMNMDDDYLLRNASSRYSSSVDAVERARAWGEKYFLNNYDRLVKAKTKIDPLNVFRHEQSIPPTLGSTQEHNYSSE | Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:21343426). Catalyzes a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of alkaloids (PubMed:21343426). Alkaloid biosynthesis; nicotine biosynthesis. Mostly expressed in roots. By jasmonic acid (MeJA). Strongly reduced nicotine biosynthesis but accumulation of dihydromethanicotine (PubMed:21343426). Inhibition of jasmonate-elicited formation of anatabine and other pyridine alkaloids (PubMed:21343426). Belongs to the oxygen-dependent FAD-linked oxidoreductase family. |
A0A1S3ZQ17 | MFPIIILISFSFTFLFASVTSGAGGVTNLSTCLINHNVHNFSIYPTKNDQSSSNYFNLLDFSLQNLRFAASYMPKPTVIILPNSKEELVSTILCCRQTSYEIRVRCGGHSYEGTSYVSFDGSPFVIVDLMKLDDVSVDLDSETAWAQGGATIGQIYYAISRVSDVHAFSAGSGPTVGSGGHISGGGFGLMSRKFGLAADSVVDALLIDAEGRLLDRKAMGEDVFWAIRGGGGGNWGIIYAWKIRLLKVPKIVTTCMIYRPGSKQYVAQLLQKWQIVTPNLADDFTLGVLMRPIDLRADMNYGNTTPIETFPQFNALYLGPKTEAVSILNEAFPELDAKNDDAKEMTWIESALFFSELDNVFGNSSDDISRLKERYMDAKTFFKGKSDFVKTPFSMDAMMTALVELEKNPKSFLVFDPYGGVMDKISDQAIAFPHRKGNLFAVQYYAFWNEEDDAKSNEYIEWTRGFYNKMAPFVSSSPRGAYINYLDMDLGVNMDDDYLLRNASSRSSSSSVDAVERARAWGEMYFLHNYDRLVKAKTQIDPLNVFRHEQSIPPMLGSTQEHSSE | Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (By similarity). Catalyzes a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of alkaloids (By similarity). Alkaloid biosynthesis; nicotine biosynthesis. Belongs to the oxygen-dependent FAD-linked oxidoreductase family. |
F1T162 | MKRNISMFLQLLLIILMMISFLFTSLLVPSVSATTLNTISTCLINYKVSNFSVYPTRNHAGNSYYNLLDFSIQNLRFAACSKPKPTVIIVPESKEQLVSSVLCCRQGSYEIRVRCGGHSYEGTSSVSFDGSPFVVIDLMKLDGVSVDVDSETAWVQGGATLGQTYYAISRASNVHGFSAGSCPTVGVGGHISGGGYGFLSRKYGLAADNVVDALLVDAEGRLLDRKAMGEEIFWAIRGGGGGIWGIIYAWKIRLLKVPKTVTSFIIPRPGSKRYVSQLVHKWQLVAPKLEDEFYLSISMSSPSKGNIPIEINAQFSGFYLGTKTEAISILNEAFSELGVLEGDCKEMSWIESTLFFSELDDVANSSDVSRLKERYFENKSYFKAKSDYVKTPISVGGIMTALNVLEKEPNGHVILDPYGGAMQRISEEAIAFPHRKGNLFGIQYLVVWKEKDNNNIVKSNIGYIEWIREFYNTMAPHVSSSPRAAYVNYMDLDLGVMDDYLLPCTSTTASANHAVERARVWGEKYFLNNYDRLVKAKTKIDPLNVFRHQQGIPPLFASMQEYTYSSK | Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (By similarity). Catalyzes a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of alkaloids (By similarity). Alkaloid biosynthesis; nicotine biosynthesis. Mostly expressed in roots at low levels. By jasmonic acid (MeJA). Belongs to the oxygen-dependent FAD-linked oxidoreductase family. |
A0A1S4CPU8 | MKRNISMSLQRLLIILMMISFLFTSLLVPSVSATNLNTISTCLINYKVSNFSVYPTRNHAGNRYYNLLDFSIQNLRFAASSKPKPTVIIVPESKEQLVSSVLCCRQGSYEIRVRCGGHSYEGTSYVSFDGSPFVVIDLMKLDDVSVDLDSETAWVQGGATLGQTYYAISRASDVHGFSAGSCPTVGVGGHISGGGFGFLSRKYGLAADNVVDALLVDAEGRLLDRKAMGEEVFWAIRGGGGGIWGIIYAWKIRLLKVPKTVTSFIVPRPGSKRYVSQLVHKWQLVAPKLDDDFYLSISMSSASKGNIPIEINAQFSGFYLGTKTEAISILNEAFPELGVVESDCKEMSWIESTLFFSELDNVANTSDVSRLKERYFENKSYFKAKSDHVKTPISVGGIMTALDVLEKEPNGHVIFDPYGAAMQRISEEAIAFPHRKGNLFRIQYLVVWKEKDNNNIAKSNGYIEWIREFYNTMAPHVSSSPRAAYVNYMDLDLGVMDDYLMLNTSITASADHAVERARVWGEKYFLNNYDRLVKAKTKIDPLNVFRHQQGIPPMFASMPEHTYSSK | Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (By similarity). Catalyzes a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of alkaloids (By similarity). Alkaloid biosynthesis; nicotine biosynthesis. Belongs to the oxygen-dependent FAD-linked oxidoreductase family. |
Q2NKS9 | MSGPNGDLGTPVEAGAEGEEDGFGEAEYAAINSMLDQINSCLDHLEEKNDHLHARLQELLESNRQTRLEFQQQLGETPSDASP | Belongs to the UPF0184 (EST00098) family. |
Q6SXP0 | MSGPNGDPNISVDDGIIEDEDEFSEEEYAAIDSMLDQINSCLDDIEDRNDALNGKLHELLESNRQARKDFRQQLNDEEASPPPAEDPASRDTQTED | Belongs to the UPF0184 (EST00098) family. |
P0C8Y3 | MSGPNGDPDISAEGIIEDEDEFNEEEYAAIDSMLDQINSCLDDIEERNDALNGKLQELLESNRAARRDFRQQITDHADLPPPANDDDEDEQSRDAQKKD | Belongs to the UPF0184 (EST00098) family. |
Q9Y3F7 | MSGPNGDLGMPVEAGAEGEEDGFGEAEYAAINSMLDQINSCLDHLEEKNDHLHARLQELLESNRQTRLEFQQQLGEAPSDASP | Belongs to the UPF0184 (EST00098) family. |
P58686 | MSGPNGDLGMPVDAGTEGENDSFGEAEYAAINSMLDQINSCLDHLEEKNDHLHARLQELLESNRQTRLEFQQQLGEAPGDASP | Belongs to the UPF0184 (EST00098) family. |
B5FY93 | MAGPNGDPHVLGGGTGDEGDEGGDTFEEEEYAAINSMLDQINSCLDHLEEKNDHLHICLKELLESNRQTRLEFQQQSKQLNTGADVQGSQPPA | Belongs to the UPF0184 (EST00098) family. |
O73881 | MSGPNGDPNISVEDGLINDDDDFGSEEYEAINSMLDQINSYLDDLEERNDSLNGKLHELMESNRQARLEFRAQLSNHTPQEDSADGESKEELGGDAGWENDKKIDEGS | Belongs to the UPF0184 (EST00098) family. |
Q8L3U3 | MNNNWLGFSLSPYEQNHHRKDVYSSTTTTVVDVAGEYCYDPTAASDESSAIQTSFPSPFGVVVDAFTRDNNSHSRDWDINGCACNNIHNDEQDGPKLENFLGRTTTIYNTNENVGDGSGSGCYGGGDGGGGSLGLSMIKTWLRNQPVDNVDNQENGNAAKGLSLSMNSSTSCDNNNDSNNNVVAQGKTIDDSVEATPKKTIESFGQRTSIYRGVTRHRWTGRYEAHLWDNSCKREGQTRKGRQVYLGGYDKEEKAARAYDLAALKYWGTTTTTNFPMSEYEKEVEEMKHMTRQEYVASLRRKSSGFSRGASIYRGVTRHHQHGRWQARIGRVAGNKDLYLGTFGTQEEAAEAYDIAAIKFRGLTAVTNFDMNRYNVKAILESPSLPIGSAAKRLKEANRPVPSMMMISNNVSESENSASGWQNAAVQHHQGVDLSLLHQHQERYNGYYYNGGNLSSESARACFKQEDDQHHFLSNTQSLMTNIDHQSSVSDDSVTVCGNVVGYGGYQGFAAPVNCDAYAASEFDYNARNHYYFAQQQQTQQSPGGDFPAAMTNNVGSNMYYHGEGGGEVAPTFTVWNDN | Transcription factor that promotes cell proliferation, differentiation and morphogenesis, especially during embryogenesis. Mostly expressed in developing seeds. Expressed in embryo throughout embryogenesis. Also present in free nuclear endosperm, but disappears once endosperm cellularization begins. |
Q8LSN2 | MNNNWLGFSLSPYEQNHHRKDVCSSTTTTAVDVAGEYCYDPTAASDESSAIQTSFPSPFGVVLDAFTRDNNSHSRDWDINGSACNNIHNDEQDGPKLENFLGRTTTIYNTNENVGDIDGSGCYGGGDGGGGSLGLSMIKTWLRNQPVDNVDNQENGNGAKGLSLSMNSSTSCDNNNYSSNNLVAQGKTIDDSVEATPKKTIESFGQRTSIYRGVTRHRWTGRYEAHLWDNSCKREGQTRKGRQVYLGGYDKEEKAARAYDLAALKYWGTTTTTNFPMSEYEKEIEEMKHMTRQEYVASLRRKSSGFSRGASIYRGVTRHHQHGRWQARIGRVAGNKDLYLGTFGTQEEAAEAYDIAAIKFRGLTAVTNFDMNRYNVKAILESPSLPIGSAAKRLKEANRPVPSMMMISNNVSESENNASGWQNAAVQHHQGVDLSLLQQHQERYNGYYYNGGNLSSESARACFKQEDDQHHFLSNTQSLMTNIDHQSSVSDDSVTVCGNVVGYGGYQGFAAPVNCDAYAASEFDYNARNHYYFAQQQQTQHSPGGDFPAAMTNNVGSNMYYHGEGGGEVAPTFTVWNDN | Transcription factor that promotes cell proliferation, differentiation and morphogenesis, especially during embryogenesis. Mostly expressed in developing seeds. Expressed in embryo throughout embryogenesis. Also present in free nuclear endosperm, but disappears once endosperm cellularization begins. |
Q9R9H8 | MEYAAIHHQPFSTDAYSYDGRTVHIKIRTKKGDADHIRFIWGDPYEYNDGKWSANEQPMRKIAATEMHDYWFAEVVPPFRRLQYAFVVTDDHEDIFFGSSGVCPYNEKTLETIHYYFKFPFVHEADTFQAPEWVKSTVWYQIFPERFANGREDLSPKNALPWGSKDPGVNDFFGGDLQGIVDKLDYLEDLGVNGIYLTPIFSAPSNHKYDTLDYFSIDPHFGDPEIFRTLVSQLHQRGMRIMLDAVFNHIGSASPQWQDVVKNGDQSRYKDWFHIHSFPVTDDNYDRFAFTADMPKLNTANPEVQKYLLDIALYWIREFDIDGWRLDVANEVDHVFWKTFRQAVSTEKPDVYILGEIWHSAEPWLRGDEFHAAMNYPFTEPMIEYFADQTISASRMAHRVNAHLMNGMKQANEVMFNLLDSHDTKRLLTRCRNDEKKARALLAFMFAQTGSPCIYYGTEIGLDGENDPLCRKCMVWEKEKQNQDMLQFMKRLIALRKQENTLLTEGHLEWNLLDDKNDFISFSRTLDEKILIYFFNQGNVVQHISLRELNIDRNNKICDAWTEQPLHYHDVIAVQPGEFLILSAAAPV | Hydrolyzes beta-cyclodextrin to maltose and glucose, soluble starch to maltose and glucose, and pullulan to panose with trace amounts of maltose and glucose. It is also able to hydrolyze acarbose. Can also exhibit a transglycosylation activity transferring glucose or maltose to another moiety of sugars by forming alpha-(1,6)- and alpha-(1,3)-glycosidic linkages upon the hydrolysis of substrate at concentrations of 5% or higher. Binds 1 Ca(2+) ion per subunit. Optimum pH is 7.0. Stable at pH 6.0 and about 80% of the enzyme activity remained between pH 7.0 and pH 8.0. Optimum temperature is 40-45 degrees Celsius. Monomer or homodimer; in equilibrium. Belongs to the glycosyl hydrolase 13 family. BbmA subfamily. |
Q795G7 | MEYAAIHHQPFSTDAYSYDGRTVHIKIRTKKGDADHIRFIWGDPYEYNDGKWSANEQPMRKIAATEMHDYWFAEVVPPFRRLQYAFVVTDDHEDIFFGSSGVCPYNEKTLETIHYYFKFPFVHEADTFQAPEWVKSTVWYQIFPERFANGREDLSPKNALPWGSKDPDVNDFFGGDLQGIVDKLDYLEDLGVNGIYLTPIFSAPSNHKYDTLDYFSIDPHFGDPELFRTLVSQLHQRGMRIMLDAVFNHIGSASPQWQDVVKNGDQSRYKDWFHIHSFPVTDDNYDRFAFTADMPKLNTANPEVQKYLLDIALYWIREFDIDGWRLDVANEVDHVFWKTFRQAVSTEKPDVYILGEIWHSAEPWLRGDEFHAAMNYPFTEPMIEYFADQTISASRMAHRVNAHLMNGMKQANEVMFNLLDSHDTKRLLTRCRNDEKKARALLAFMFAQTGSPCIYYGTEIGLNGENDPLCRKCMVWEKEKQNQDMLQFMKRLIALRKQENTLLTEGHLEWNLLDDKNDFISFSRTLDEKILIYFFNQGNVVQHVSLRELNIDRNKKICDAWTEQPLQHHDVIAVQPGEFLILSAAAPV | Hydrolyzes beta-cyclodextrin to maltose and glucose, soluble starch to maltose and glucose, and pullulan to panose with trace amounts of maltose and glucose. It is also able to hydrolyze acarbose. Can also exhibit a transglycosylation activity transferring glucose or maltose to another moiety of sugars by forming alpha-(1,6)- and alpha-(1,3)-glycosidic linkages upon the hydrolysis of substrate at concentrations of 5% or higher (By similarity). Binds 1 Ca(2+) ion per subunit. Monomer or homodimer; in equilibrium. Belongs to the glycosyl hydrolase 13 family. BbmA subfamily. |
Q9LF42 | MNSMNNWLGFSLSPHDQNHHRTDVDSSTTRTAVDVAGGYCFDLAAPSDESSAVQTSFLSPFGVTLEAFTRDNNSHSRDWDINGGACNNINNNEQNGPKLENFLGRTTTIYNTNETVVDGNGDCGGGDGGGGGSLGLSMIKTWLSNHSVANANHQDNGNGARGLSLSMNSSTSDSNNYNNNDDVVQEKTIVDVVETTPKKTIESFGQRTSIYRGVTRHRWTGRYEAHLWDNSCKREGQTRKGRQVYLGGYDKEEKAARAYDLAALKYWGTTTTTNFPLSEYEKEVEEMKHMTRQEYVASLRRKSSGFSRGASIYRGVTRHHQHGRWQARIGRVAGNKDLYLGTFGTQEEAAEAYDIAAIKFRGLSAVTNFDMNRYNVKAILESPSLPIGSSAKRLKDVNNPVPAMMISNNVSESANNVSGWQNTAFQHHQGMDLSLLQQQQERYVGYYNGGNLSTESTRVCFKQEEEQQHFLRNSPSHMTNVDHHSSTSDDSVTVCGNVVSYGGYQGFAIPVGTSVNYDPFTAAEIAYNARNHYYYAQHQQQQQIQQSPGGDFPVAISNNHSSNMYFHGEGGGEGAPTFSVWNDT | Transcription factor that, in opposition to HDG1, promotes cell proliferation and morphogenesis via transcriptionnal activation of meristem and cell proliferation genes, but prevents differentiation, especially during embryogenesis (PubMed:12172019, PubMed:25564655). Binds to the promoter and triggers the expression of epidermally expressed genes such as GSO1, GSO2, ACR4 and WER, and of HD-ZIP homeobox genes including PDF2, HDG1, HDG5, HDG7, HDG8, HDG11, ANL2, PDF2 and ATML1 (PubMed:25564655). Interacts with HDG1, HDG2, HDG3, HDG10, ANL2, ATML1, PDF2, HDG11 and HDG12. Mostly expressed in developing seeds. Also expressed in roots, seedlings, and siliques, and, at low levels, in leaves. Expressed in embryo during embryogenesis, first throughoutthe embryo, but later basally localized at the heart stage (PubMed:12172019, PubMed:25564655). Also present in free nuclear endosperm, but disappears once endosperm cellularization begins (PubMed:12172019). Observed in the stem cell niche and the provascular tissue of mature roots (PubMed:25564655). Was named 'Baby boom' because overexpressing transgenic plants exhibit several spontaneous somatic embryos. Belongs to the AP2/ERF transcription factor family. AP2 subfamily. |
A8Y5S8 | MPKKKGKGKGKGKGKGKGKKDGKHDSKADRESEIEKLKSNASLWEAKFTVTDISRLEYREAARALAKANEELENQQYRAEKDTKDIIAFLKRTDFEKTATIAALEEELKRERAKSAQEKDLLVAEYMQKIDALEEMFRQRSGDFQRMQGELKTIKHYRKIKANLEEDLISIREKMYVDGRAHQESLARTEYKFYMARIRIEKEAEQKISQLAEQAHYEAVDQLGAASQTVITENIRLNEGLDYHVKEAEQLKRINVALTEKNSSLALFKETNELMKKEADSHVQSQHSEISELTAKLSTLEQALGIMSREFEQERVEMERSAGVNNTELEELEMLLAAREKELSKVKQLAQSIIEQRRELELFFHEALNHARKEIKAQQQHYRQEALKSYRWRMNEAHAGRLEFPRIRTFSNAPNSTNDVQTELEDSDKWNNLRSSNVDISDLTWEQKERLLNLLFAKLNGIKTRKAAHPPALSASSSEKIQVSSDAGSTVESPSMTFITQMTMANMTSDPFVLPALKST | Basal body protein required in multiciliate cells to align and maintain cilia orientation in response to flow. May act by mediating a maturation step that stabilizes and aligns cilia orientation. Not required to respond to planar cell polarity (PCP) or flow-based orientation cues (By similarity). Localizes to a polar structure adjacent to the basal body. Belongs to the BBOF1 family. Extended N-terminus. |
Q9H5P8 | MPSKGKDKKKGKSKGKDTKKLIKTDESVVDRAKANASLWEARLEVTELSRIKYRDTSRILAKSNEDLKKKQCKMEKDIMSVLSYLKKQDQEKDNMIEKLKQQLNETKEKAQEEKDKLEQKYTRQINELEGQFHQKAKEIGMIHTELKAVRQFQKRKIQVERELDDLKENLRNTERIHQETLRRLESRFFEEKHRLEQEAEKKIIMLAERAHHEAIVQLNDAGRNVFKENDYLQKALAYHLKETDALQKNSQKLQESHTLLLHQKEINDLLVKEKIMQLVQQRSQIQTLQKKVVNLETALSYMTKEFESEVLKLQQHAMIENQAGQVEIDKLQHLLQMKDREMNRVKKLAKNILDERTEVERFFLDALHQVKQQILISRKHYKQIAQAAFNLKMRAACTGRTEYPKIRTFDGREHSTNSVNQDLLEAEKWTHIEGNVDIGDLTWEQKEKVLRLLFAKMNGCPSRKYNQSSRPPVPDYVVSDSGETKEFGDESKLQDKIFITQQIAISDSSGEVVLPTIPKEPQESDTGTF | Basal body protein required in multiciliate cells to align and maintain cilia orientation in response to flow. May act by mediating a maturation step that stabilizes and aligns cilia orientation. Not required to respond to planar cell polarity (PCP) or flow-based orientation cues (By similarity). Localizes to a polar structure adjacent to the basal body. Belongs to the BBOF1 family. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. |
Q4R8W1 | MPSKGKDKKKGKSRGKDTKKLIKTDESVVDRAKANASLWEARLEITELSRIEYRDTSRTLAKSNEDLKKKQCKMEKDIMSVLSYLKKQDQEKDNMIEKLKQQLNETKEKAQEEKDKLEQKYTRQIDELEGQFHQKAKEIGMIHTELKAVRQFQRRKIQVERELDDLKENLRNTERIHQETLRRLESRFFEEKHRLKQEAEKKIIMLAERAHHEAVVQLNDAGRNVFKENVYLQKALAYHLKEAGGLQKNSQKLQESHALLLHQKEINDLLIKEKIMQLVQQRSQIQTLQKKVVNLETALGYMTKEFESEVLKLQQHAMIENQAGQVEIDKLQHLLQMKDREMNRVKKLAKNILDERTEVERFFLDALHQVKQQILISRKHYKQIAQAAFNLKMRAACAGRTEYPKIRTFDGREHSTNSVNQDLLEAEKWTHIEGNVDIGDLTWEQKEKVLRLLFAKMNGCPSRKYNQSSKPPVPDYVVSDSGETKEFGDESKLQDKIFITQQIPISDSSGKVVLPTIPKGPQESDTGTF | Basal body protein required in multiciliate cells to align and maintain cilia orientation in response to flow. May act by mediating a maturation step that stabilizes and aligns cilia orientation. Not required to respond to planar cell polarity (PCP) or flow-based orientation cues (By similarity). Localizes to a polar structure adjacent to the basal body. Belongs to the BBOF1 family. Truncated N-terminus. |
Q9CUZ3 | MPAKDKRKDKRKDKRKGKNKGKEPKKIIKSDEPAIERAKANASLWEARLEVTELSRIEYRDTSRRLAKNNEDLKKQQYNMEKDIMSVLSYLKKQDQEKDNMIEKLKQQLAKTKEKAQEEKEKLEQKYALQVSELEGQFHQKAKEIGMIQTELKTIKQFQKRKIQVEKELDDLKENLRNSEKNYQETLRRLESRFFEEKHRLEQEAEKRIIMLAERAHHEAVVQLNTAGRNVFKENVYLHKALAYHLKEAEILQQNSKKIEENHSCLLQQKEINDLLVKEKIMQLTQQKSQIQTLQKKVVSLENALTYMTTEFEAEVLKLQQKAIIENQAGLVEIDKLQQLLQMKDREMNRVKRLAKNILDERTEVEQFFLDALYEVKQQILASRKHYKQIAQAAFNLKMRAACAGKTEYPRIRTFDGKEQSTNSVNQDLLEAEKWPTTQKNVDIRDLTWEQKEKVLRLLFAKMNGFAARKYSQSSKPPVPDHIIYGSGEMKETGDENNLLDQTFITQQAPVSDSNRMVSPDVIPQGLQDSDIA | Basal body protein required in multiciliate cells to align and maintain cilia orientation in response to flow. May act by mediating a maturation step that stabilizes and aligns cilia orientation. Not required to respond to planar cell polarity (PCP) or flow-based orientation cues (By similarity). Localizes to a polar structure adjacent to the basal body. Belongs to the BBOF1 family. |
Q6PFF9 | MTVPNVLAKALYDNVAESPDELSFRKGDIMTVLERDTQGLDGWWLCSLHGRQGIVPGNRLKILVGMYDKKPVGPGPGPPATPPQPQPSLPQGVHAPVPPASQYSPMLPTAYQPQSDNVYLVPTPSKTQQGLYQAPGPNPQFQSPPAKQTSTFSKQTPHHSFPSPATDLYQVPPGPGSPAQDIYQVPPSAGIGHDIYQVPPSLDTRGWEGTKPPAKVVVPTRVGQGYVYEAAQTEQDEYDTPRHLLAPGPQDIYDVPPVRGLLPNQYGQEVYDTPPMAVKGPNGRDPLLDVYDVPPSVEKGLLSSSHHSVYDVPPSVSKDVPDGPLLREETYDVPPAFAKPKPFDPTRHPLILAAPPPDSPAAEDVYDVPPPAPDLYDVPPGLRRPGPGTLYDVPRERVLPPEVADGSVVDDGVYAVPPPAEREAPTDGKRLSASSTGSTRSSQSASSLEVVVPGREPLELEVAVESLARLQQGVSTTVAHLLDLVGSASGPGGWRGTSEPQEPPAQDLKAAVAAVHGAVHELLEFARGAVSNATHTSDRTLHAKLSRQLQKMEDVYQTLVVHGQVLDSGRGSPGFTPEDLDRLVACSRAVPEDAKQLASFLHGNASLLFRRTKAPGPGPEGSSSLHPNPTDKASSIQSRPLPSPPKFTSQDSPDGQYENSEGGWMEDYDYVHLQGKEEFEKTQKELLERGNIMRQGKGQLELQQLKQFERLEQEVSRPIDHDLANWTPAQPLVPGRTGGLGPSDRQLLLFYLEQCEANLTTLTDAVDAFFTAVATNQPPKIFVAHSKFVILSAHKLVFIGDTLSRQAKAADVRSQVTHYSNLLCDLLRGIVATTKAAALQYPSPSAAQDMVDRVKELGHSTQQFRRVLGQLAAA | Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion (By similarity). Implicated in induction of cell migration and cell branching (PubMed:25499443). Involved in the BCAR3-mediated inhibition of TGFB signaling (PubMed:25499443). Forms complexes in vivo with PTK2/FAK1, adapter protein CRKL and LYN kinase. Can heterodimerize with NEDD9. Component of a complex comprised of SH2D3C, BCAR1/CAS, and CRK (By similarity). Within the complex, interacts with SH2D3C (via C-terminus), and CRK (By similarity). Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the complex is dependent on intergrin mediated-tyrosine phosphorylation of PTPRA (PubMed:22801373). Interacts with BCAR3 (via Ras-GEF domain); the interaction regulates adhesion-dependent serine phosphorylation (PubMed:10896938, PubMed:22801373). Interacts with SMAD2 and SMAD3 (PubMed:25499443). Interacts with NPHP1 (PubMed:10739664). Interacts with PTK2B/PYK2 (By similarity). Interacts (via C-terminus) with SH2D3C/CHAT isoform 2 (via C-terminus) (PubMed:10692442, PubMed:12486027, PubMed:17174122). Interacts with activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1 (By similarity). Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas (By similarity). Interacts with TNK2 via SH3 domains. Unphosphorylated form localizes in the cytoplasm (PubMed:22801373). Localizes to focal adhesion sites following integrin engagement (PubMed:22801373). Expressed in olfactory sensory neurons (at protein level) (PubMed:20881139). Expressed abundantly in the liver, lung, brain, and at lower levels in the heart (at protein level) (PubMed:19365570). Contains a central domain (substrate domain) containing multiple potential SH2-binding sites and a C-terminal domain containing a divergent helix-loop-helix (HLH) motif. The SH2-binding sites putatively bind CRK, NCK and ABL SH2 domains. The HLH motif is absolutely required for the induction of pseudohyphal growth in yeast and mediates heterodimerization with NEDD9. A serine-rich region promotes activation of the serum response element (SRE). The SH3 domain is necessary for the localization of the protein to focal adhesions and interacts with one proline-rich region of PTK2/FAK1. PTK2/FAK1 activation mediates phosphorylation at the YDYVHL motif; phosphorylation is most likely catalyzed by SRC family members. SRC-family kinases are recruited to the phosphorylated sites and can phosphorylate other tyrosine residues. Tyrosine phosphorylation is triggered by integrin mediated adhesion of cells to the extracellular matrix (By similarity). Dephosphorylated by PTPN14 at Tyr-132. Phosphorylated by SRC kinase in a EDN1- and PTK2B-mediated manner; phosphorylation strengthens its interaction with BCAR3 as part of the PTK2B/BCAR1/BCAR3/RAP1 signaling pathway. Belongs to the CAS family. |
Q63766 | MKYLVSVGAGPARRAGGLEDVSWGPRVSRRPQSYRAARHVNESLPRSAFRVPAAHGASVTPSAALGSGLPETQPEAVCRGTEKPRFAEGCKPAASRDKNVLAKALYDNVAESPDELSFRKGDIMTVLERDTQGLDGWWLCSLHGRQGIVPGNRLKILVGMYDKKPAAPGPGPPATPPQPQPSLPQGVHTPVPPASQYSPMLPTAYQPQPDNVYLVPTPSKTQQGLYQAPGPNPQFQSPPAKQTSTFSKQTPHHSFPSPATDLYQVPPGPGSPAQDIYQVPPSAGTGHDIYQVPPSLDTRSWEGTKPPAKVVVPTRVGQGYVYEASQAEQDEYDTPRHLLAPGSQDIYDVPPVRGLLPNQYGQEVYDTPPMAVKGPNGRDPLLDVYDVPPSVEKGLPPSNHHSVYDVPPSVSKDVPDGPLLREETYDVPPAFAKPKPFDPTRHPLILAAPPPDSPPAEDVYDVPPPAPDLYDVPPGLRRPGPGTLYDVPRERVLPPEVADGSVIDDGVYAVPPPAEREAPTDGKRLSASSTGSTRSSQSASSLEVVVPGREPLELEVAVETLARLQQGVSTTVAHLLDLVGSASGPGGWRSTSEPQEPPVQDLKAAVAAVHGAVHELLEFARSAVSSATHTSDRTLHAKLSRQLQKMEDVYQTLVVHGQVLDSGRGGPGFTLDDLDRLVACSRAVPEDAKQLASFLHGNASLLFRRTKAPGPGPEGSSSLHLNPTDKASSIQSRPLPSPPKFTSQDSPDGQYENSEGGWMEDYDYVHLQGKEEFEKTQKELLEKGNIVRQGKGQLELQQLKQFERLEQEVSRPIDHDLANWTPAQPLVPGRTGGLGPSDRQLLLFYLEQCEANLTTLTDAVDAFFTAVATNQPPKIFVAHSKFVILSAHKLVFIGDTLSRQAKAADVRSKVTHYSNLLCDLLRGIVATTKAAALQYPSPSAAQDMVDRVKELGHSTQQFRRVLGQLAAA | Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion (By similarity). Implicated in induction of cell migration and cell branching (By similarity). Involved in the BCAR3-mediated inhibition of TGFB signaling (By similarity). Forms complexes in vivo with PTK2/FAK1, adapter protein CRKL and LYN kinase. Can heterodimerize with NEDD9. Component of a complex comprised of SH2D3C, BCAR1/CAS, and CRK (By similarity). Within the complex, interacts with SH2D3C (via C-terminus), and CRK (By similarity). Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the complex is dependent on intergrin mediated-tyrosine phosphorylation of PTPRA (By similarity). Interacts with BCAR3 (via Ras-GEF domain); the interaction regulates adhesion-dependent serine phosphorylation (By similarity). Interacts with SMAD2 and SMAD3 (By similarity). Interacts with NPHP1 (By similarity). Interacts with PTK2B/PYK2 (By similarity). Interacts (via C-terminus) with SH2D3C/CHAT isoform 2 (via C-terminus) (By similarity). Interacts with activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1 (By similarity). Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas (By similarity). Interacts with TNK2 via SH3 domains. Interacts with PTK2B/PYK2 (By similarity). Unphosphorylated form localizes in the cytoplasm (By similarity). Localizes to focal adhesion sites following integrin engagement (By similarity). Widely expressed. Higher expression in lung, intestine and testis. Contains a central domain (substrate domain) containing multiple potential SH2-binding sites and a C-terminal domain containing a divergent helix-loop-helix (HLH) motif. The SH2-binding sites putatively bind CRK, NCK and ABL SH2 domains. The HLH motif is absolutely required for the induction of pseudohyphal growth in yeast and mediates heterodimerization with NEDD9. A serine-rich region promotes activation of the serum response element (SRE). The SH3 domain is necessary for the localization of the protein to focal adhesions and interacts with one proline-rich region of PTK2/FAK1. PTK2/FAK1 activation mediates phosphorylation at the YDYVHL motif; phosphorylation is most likely catalyzed by SRC family members. SRC-family kinases are recruited to the phosphorylated sites and can phosphorylate other tyrosine residues. Tyrosine phosphorylation is triggered by integrin mediated adhesion of cells to the extracellular matrix. Phosphorylated by SRC kinase in a EDN1- and PTK2B-mediated manner; phosphorylation strengthens its interaction with BCAR3 as part of the PTK2B/BCAR1/BCAR3/RAP1 signaling pathway. Dephosphorylated by PTPN14 at Tyr-226. Belongs to the CAS family. |
Q2KJF5 | MAAGKFASLPRNMPVNHQFPLASSMDLLSSKSPLVERRADAYQDVSIHGTLPRKKKGPPPIRSCDNFSHVGTLPHSRSPRHHSPLIQDVIQEQPLQDWKGEAFTFRDQHLLDPTLEYVKFSKERHVMDRTPERLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLMQRDGDFLVRDSLSSPGDFVLTCQWKNLPQHFKIRRTVVRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPVNRTVPLRCLEERYGASSPDRAHEGSLTEGRPDAAKRLSLTVGGTQAREQGLPRGNLLRNKEKSGSQPACLDHMQDRRALSLKAHQSESYLPIGGKLTPQSPSVGTSPCPNSPVFRTGSEPTLSPAVVRRVSSDARPGEALRGSDSQLCPKPPPKPCKAPLLKAPPSPSIWLNSEANYCELNPALAASYDGASRLPFCAQDSYVELLTAKQNGGLGTRNSDTSYLILDDDDRTRPWKPPPAPGDTVGEDQDTFVMPLLETTSSFKPNDFESKLLPPENKPLETSMLKRAKELFTNSDPKVIAQHLLSVDCKVARILEVSEEMRKNMGVNSGLELITLPYGHQLRLDIIERHNTMAIGIAVDILGCTGSLEDRAATLNKIIQVAVELKDSMGDLYSFSAIMKALEMPQITRLEKTWTALRHQYTQTAILYEKQLKPFSKVLHEGRESTCVPPNNVSVPLLMPLVTLMEREAVTFEGTDMWEKNDESCEIMLNHLATARLMAEAADSYRMNAERILAGFQPDEEMSEVFKTEFQMRLLWGSKGAQVNQTERYEKFNQILTALSRKLEPPPVKQMEF | Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (By similarity). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis (By similarity). Promotes insulin-mediated membrane ruffling (By similarity). In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1. Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity. May inhibit TGFB-SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (By similarity). Regulates EGF-induced DNA synthesis (By similarity). Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling. Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA. Positively regulates integrin-induced tyrosine phosphorylation of BCAR1. Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (By similarity). However, in a contrasting study, lacks GEF activity towards RAP1 (By similarity). Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the complex is dependent on integrin mediated-tyrosine phosphorylation of PTPRA (By similarity). Within the complex, interacts (via SH2 domain) with PTPRA (when phosphorylated on 'Tyr-797') (By similarity). Interacts (via Ras-GEF domain) with BCAR1 (By similarity). Interacts with (via Ras-GEF domain) NEDD9 (By similarity). Interacts with PTK2/FAK1 (By similarity). Interacts with PTPN1. Interacts (via SH2 domain) with EGFR (when tyrosine-phosphorylated) (By similarity). Localization to focal adhesions depends on interaction with PTPRA. The SH2 domain mediates interaction with tyrosine-phosphorylated proteins (By similarity). However, not involved in the binding to phosphorylated BCAR1 (By similarity). Required for cell cycle progression in response to INS/insulin (By similarity). Required for regulation of EGF-induced DNA synthesis (By similarity). The Ras-GEF domain appears to adopt a closed conformation rendering it incapable of carrying out canonical exchange factor function, this closed conformation is probably required for interaction with BCAR1. Phosphorylated on tyrosine residues. The guanine nucleotide exchange factor (GEF) activity is controversial. One study showed GEF activity towards RALA, RAP1A and RRAS (By similarity). However, in another study, a construct containing only the Ras-GEF domain lacks GEF activity towards RAP1 (By similarity). |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.