ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q54PI5 | MTNLDNNNLNEEIKNKLEKQQNQKEQKLIIVIMGVSGSGKTTIGNAIASSLGCGFNDADEFHSEENKEKMRSGIPLNDDDRKPWLSSINKRMIEFLNNENDGANDHVFTCSALKSTYRDQISNNINKDNLLFILLQGSKQLLSERLQNRKNHFFNPNLLDSQLSILELPTQSELSNHHYAFIDISNSVDEIVEEIFNYLK | Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Mass (Da): 22831
Sequence Length: 200
Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 2.7.1.12
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P46859 | MSTTNHDHHIYVLMGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDDDRKPWLQALNDAAFAMQRTNKVSLIVCSALKKHYRDLLREGNPNLSFIYLKGDFDVIESRLKARKGHFFKTQMLVTQFETLQEPGADETDVLVVDIDQPLEGVVASTIEVIKKGK | Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Mass (Da): 19543
Sequence Length: 175
Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 2.7.1.12
|
Q5T6J7 | MAAPGALLVMGVSGSGKSTVGALLASELGWKFYDADDYHPEENRRKMGKGIPLNDQDRIPWLCNLHDILLRDVASGQRVVLACSALKKTYRDILTQGKDGVALKCEESGKEAKQAEMQLLVVHLSGSFEVISGRLLKREGHFMPPELLQSQFETLEPPAAPENFIQISVDKNVSEIIATIMETLKMK | Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Mass (Da): 20578
Sequence Length: 187
Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 2.7.1.12
|
Q8R0J8 | MEAPGVLLVMGVSGSGKSTVGALLASKLGWKFYDADDYHSEENRIKMAKGVPLSDQDRIPWLCTLHDILLRDVALGQPVVLACSALKKTYRDILIRGGSDAPLKSDDSAKEPLAGGKLLVVYLCGSFDIIYGRLLQRKGHFMPPELLQSQFSILEPPSAPENFIQVSVDKSLPEITAAVMEALK | Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Mass (Da): 19981
Sequence Length: 184
Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 2.7.1.12
|
Q10242 | MTVTPINPTNQPYKYVFVVIGPAGSGKTTMAKAVSEKLGFEYIEGDDLHPKANIEKMSQGHPLNDNDRWGWLHNCGGACAMELDKESIKGVVLTCSALKRSYRDILRSSLEHRPAILRFIYLAASRETLIKRTTSRKNHYMKADMVESQLAILEAPTADEKDVITISVENGKEQSEEECLDIVHKMVNENKQP | Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Mass (Da): 21648
Sequence Length: 193
Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
EC: 2.7.1.12
|
Q03786 | MTEKHKTMGKFKVIVLAGTAGTGKSTIAGELIHEFKDIYPDLKFIEGDDLHPPANVEKMTRGIPLNDDDRWDWLKKVAVESTKAAASTKEHLSIVACSSLKKKYRDLIRHTCPESEFHFIFLYASKIEVLKRLKTRKGHFMKADMMESQFRDLELPDINDETDCDIVPLDFKTFYQIEKDVIQVVKSKVLNIE | Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Mass (Da): 22175
Sequence Length: 193
Pathway: Carbohydrate acid metabolism; D-gluconate degradation.
Subcellular Location: Cytoplasm
EC: 2.7.1.12
|
Q9VQ93 | MNRSDGLVRRSVKPRENGGAEGGLNANTPDDNQDALDNLKDQEDNIDDGDSKETRLTLMEEVLLLGLKDKEGYTSFWNDCISSGLRGCILIELGLRGRVMIEKSGMRRRGLCTRKLILKSDQQTGDVLLDEALKHIKETDPPETVQSWIEYLSGETWNPLKLRYQLKNVRERLAKNLVEKGVLTTEKQNFLLFDMTTHPLSDNVVKCRLVKKIQDSVLSKWVNDPQRMDKRMLALIFLAHASDVIENAFAPLNDDDYEVAMKRVRELLDLDFEAESAKPNANEILWAVFMAFTK | Function: Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi . Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus (By... |
Q9H4A6 | MTSLTQRSSGLVQRRTEASRNAADKERAAGGGAGSSEDDAQSRRDEQDDDDKGDSKETRLTLMEEVLLLGLKDREGYTSFWNDCISSGLRGCMLIELALRGRLQLEACGMRRKSLLTRKVICKSDAPTGDVLLDEALKHVKETQPPETVQNWIELLSGETWNPLKLHYQLRNVRERLAKNLVEKGVLTTEKQNFLLFDMTTHPLTNNNIKQRLIKKVQEAVLDKWVNDPHRMDRRLLALIYLAHASDVLENAFAPLLDEQYDLATKRVRQLLDLDPEVECLKANTNEVLWAVVAAFTK | Function: Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May... |
O22893 | MAPGLTQTADAMSTVTITKPSLPSVQDSDRAYVTFLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAMLPDVPEEHRRILVDQGCIVREIEPVYPPENQTQFAMAYYVINYSKLRIWKFVEYSKMIYLDGDIQVYENIDHLFDLPDGYLYAVMDCFCEKTWSHTPQYKIRYCQQCPDKVQWPKAELGEPPALYFNAGMFLYEPNLETYEDLLRTLKITPPTPFAEQDFLNMYFKKIYKPIPLVYNLVLAMLWRHPENVELGKVKVVHYCAAGSKPWRYTGKEANMEREDIKMLVKKWWDIYDDESLDYKKPVTVVDTEVDLV... | Function: Galactinol synthase involved in the biosynthesis of raffinose family oligosaccharides (RFOs) that function as osmoprotectants. Promotes plant stress tolerance such as heat, chilling, salinity and methylviologen (MV), a superoxide radical generating drug, by mediating raffinose accumulation, an osmoprotective ... |
Q947G8 | MAPEFESGTKMATTIQKSSCAYVTFLAGNGDYVKGVVGLAKGLIKAKSMYPLVVAILPDVPEEHRMILTRHGCIVKEIEPLAPSLQSLDKYARSYYVLNYSKLRIWEFVEYSKMVYLDGDMQVFENIDHLFELPDKYLYAVADCICDMYGEPCDEVLPWPKELGPRPSVYFNAGMFVFQPNPSVYVRLLNTLKVTPPTQFAEQDFLNMYFKDVYKPIPYTYNMLLAMLWRHPEKIEVNKAKAVHYCSPGAKPWKYTGKEEHMDREDIKMLVKKWWDIYNDTTLDHKAQGSTVEANRLRGAAFSDTNISALYITSPSAA | Function: Galactinol synthase involved in the biosynthesis of raffinose family oligosaccharides (RFOs) that function as osmoprotectants. May promote plant stress tolerance.
Catalytic Activity: myo-inositol + UDP-alpha-D-galactose = alpha-D-galactosyl-(1->3)-1D-myo-inositol + H(+) + UDP
Sequence Mass (Da): 36402
Sequenc... |
Q9FXB2 | MAPEINTKLTVPVHSATGGEKRAYVTFLAGTGDYVKGVVGLAKGLRKAKSKYPLVVAVLPDVPEDHRKQLVDQGCVVKEIEPVYPPENQTEFAMAYYVINYSKLRIWEFVEYNKMIYLDGDIQVFDNIDHLFDLPNGQFYAVMDCFCEKTWSHSPQYKIGYCQQCPDKVTWPEAKLGPKPPLYFNAGMFVYEPNLSTYHNLLETVKIVPPTLFAEQDFLNMYFKDIYKPIPPVYNLVLAMLWRHPENIELDQVKVVHYCAAGAKPWRFTGEEENMDREDIKMLVKKWWDIYNDESLDYKNVVIGDSHKKQQTLQQFIEAL... | Function: Galactinol synthase involved in the biosynthesis of raffinose family oligosaccharides (RFOs) that function as osmoprotectants. Promotes stress tolerance of factors such as drought, chilling, salinity and methylviologen (MV), a superoxide radical generating drug, by mediating an increase in levels of the endog... |
O22693 | MAPEISVNPMYLSEKAHQAPPRRAYVTFLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAMLPDVPEEHREILRSQGCVVREIEPVYPPDNQVEFAMAYYVLNYSKLRIWNFEEYSKMIYLDADIQVFDNIDHLFDLSDAYFYAVMDCFCEKTWSHSLQYSIGYCQQCPEKVTWPEDMESPPPPLYFNAGMFVFEPSPLTYESLLQTLEITPPSPFAEQDFLNMFFEKVYKPIPLVYNLVLAMLWRHPENVELEKVKVVHYCAAGSKPWRYTGEEANMDREDIKMLVDKWWDVYNDESLDFKSKIPADAEETVTKSSILASV... | Function: Galactinol synthase involved in the biosynthesis of raffinose family oligosaccharides (RFOs) that function as osmoprotectants. May promote plant stress tolerance (By similarity).
Catalytic Activity: myo-inositol + UDP-alpha-D-galactose = alpha-D-galactosyl-(1->3)-1D-myo-inositol + H(+) + UDP
Sequence Mass (Da... |
Q9UJ42 | MTALSSENCSFQYQLRQTNQPLDVNYLLFLIILGKILLNILTLGMRRKNTCQNFMEYFCISLAFVDLLLLVNISIILYFRDFVLLSIRFTKYHICLFTQIISFTYGFLHYPVFLTACIDYCLNFSKTTKLSFKCQKLFYFFTVILIWISVLAYVLGDPAIYQSLKAQNAYSRHCPFYVSIQSYWLSFFMVMILFVAFITCWEEVTTLVQAIRITSYMNETILYFPFSSHSSYTVRSKKIFLSKLIVCFLSTWLPFVLLQVIIVLLKVQIPAYIEMNIPWLYFVNSFLIATVYWFNCHKLNLKDIGLPLDPFVNWKCCFIP... | Function: Orphan receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39787
Sequence Length: 338
Subcellular Location: Cell membrane
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Q90X46 | MNGSKNGTAVANSTNGLDDNGLMVLESVSIIIIAILACLGNLVIVVTLYKKPYLLTPSNKFVFSLTSSNLLLSVLMLPFVVASSVRRDWMFGVVWCNFTALLHLLVSSSSMLTLGAIAIDRYYAVLYPMIYPMKITGNRAVLAIVYIWLHSLVGCLPPLFGWSSFEFDRFKWTCTVSWHKEISYTAFWVTWCCLLPLVAMLVCYGVIFRVARIKARKVYCGSVVVSQEESSSQNNGRKNSNTSTSSSGSRKSLIYSGSQCKAFITILVVLGTFLTTWGPYVVVISTEALLGKNSVSPQVETLVSWLSFTSAVCHPLIYGL... | Function: Key negative regulator of Shh signaling during neural tube development. Recruited to primary cilia and acts as a regulator of the PKA-dependent basal repression machinery in Shh signaling by increasing cAMP levels, leading to promote the PKA-dependent processing of gli3 into gli3r and repress the Shh signalin... |
Q8N6U8 | MSLNSSLSCRKELSNLTEEEGGEGGVIITQFIAIIVITIFVCLGNLVIVVTLYKKSYLLTLSNKFVFSLTLSNFLLSVLVLPFVVTSSIRREWIFGVVWCNFSALLYLLISSASMLTLGVIAIDRYYAVLYPMVYPMKITGNRAVMALVYIWLHSLIGCLPPLFGWSSVEFDEFKWMCVAAWHREPGYTAFWQIWCALFPFLVMLVCYGFIFRVARVKARKVHCGTVVIVEEDAQRTGRKNSSTSTSSSGSRRNAFQGVVYSANQCKALITILVVLGAFMVTWGPYMVVIASEALWGKSSVSPSLETWATWLSFASAVCH... | Function: Key negative regulator of Shh signaling, which promotes the processing of GLI3 into GLI3R during neural tube development. Recruited by TULP3 and the IFT-A complex to primary cilia and acts as a regulator of the PKA-dependent basal repression machinery in Shh signaling by increasing cAMP levels, leading to pro... |
B2RPY5 | MDFVQHALLTASRGALTMSLNSSLSYRKELSNLTATEGGEGGAVSEFIAIIIITVLVCLGNLVIVVTLYKKSYLLTLSNKFVFSLTLSNFLLSVLVLPFVVTSSIRREWIFGVVWCNFSALLYLLISSASMLTLGVIAIDRYYAVLYPMVYPMKITGNRAVMALVYIWLHSLIGCLPPLFGWSSVEFDEFKWMCVAAWHQEPGYTIFWQIWCALFPFLIMLVCYGFIFRVARVKARKVHCGTVVTVEEDSQRSGRKNSSTSTSSSGSRRNALQGVVYSANQCKALITILVVIGAFMVTWGPYMVVITSEALWGKNCVSPT... | Function: Key negative regulator of Shh signaling, which promotes the processing of GLI3 into GLI3R during neural tube development. Recruited by TULP3 and the IFT-A complex to primary cilia and acts as a regulator of the PKA-dependent basal repression machinery in Shh signaling by increasing cAMP levels, leading to pro... |
Q16538 | MARGGAGAEEASLRSNALSWLACGLLALLANAWIILSISAKQQKHKPLELLLCFLAGTHILMAAVPLTTFAVVQLRRQASSDYDWNESICKVFVSTYYTLALATCFTVASLSYHRMWMVRWPVNYRLSNAKKQALHAVMGIWMVSFILSTLPSIGWHNNGERYYARGCQFIVSKIGLGFGVCFSLLLLGGIVMGLVCVAITFYQTLWARPRRARQARRVGGGGGTKAGGPGALGTRPAFEVPAIVVEDARGKRRSSLDGSESAKTSLQVTNLVSAIVFLYDSLTGVPILVVSFFSLKSDSAPPWMVLAVLWCSMAQTLLL... | Function: Orphan receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63930
Sequence Length: 588
Subcellular Location: Cell membrane
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P28995 | MLSMIVLLFLLWGAPSHAYFSYYTAQRFTDFTLCMLTDRGVIANLLRYDEHTALYNCSASKTCWYCTFLDEQIITFGTDCDDTYAVPVAEVLEQAHGPYSALFDDMPPFIYYGREFGIVVLDVFMFYPVLVLFFLSVLPYATLILEMCVSILFIIYGIYSGAYLAMGIFAATLAIHSIVVLRQLLWLCLAWRYRCTLHASFISAEGKVYPVDPGLPVAAVGNRLLVPGRPTIDYAVAYGSKVNLVRLGAAEVWEP | Function: Major envelope protein present in abundant amounts in the virion envelope.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28673
Sequence Length: 255
Subcellular Location: Virion membrane
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Q04569 | MRCSHKLGRFLTPHSCFWWLFLLCTGLSWSFADGNGDSSTYQYIYNLTICELNGTDWLSSHFGWAVETFVLYPVATHILSLGFLTTSHFFDALGLGAVSTAGFVGGRYVLCSVYGACAFAAFVCFVIRAAKNCMACRYARTRFTNFIVDDRGRVHRWKSPIVVEKLGKAEVDGNLVTIKHVVLEGVKAQPLTRTSAEQWEA | Function: Major envelope protein present in abundant amounts in the virion envelope. Mediates virion sialic acid-dependent attachment the sialoadhesin receptor SIGLEC1. This attachment induces virion internalization into alveolar macrophages predominantly through clathrin-dependent endocytosis.
PTM: N-glycosylated.
Loc... |
P08148 | MSVDSSSTHRRRCVAARLVRLAAAGAAVTVAVGTAAAWAHAGALQHRCVHDAMQARVRQSVADHHKAPGAVSAVGLPYVTLDAAHTAAAADPRPGSARSVVRDVNWGALRIAVSTEDLTDPAYHCARVGQHVKDHAGAIVTCTAEDILTNEKRDILVKHLIPQAVQLHTERLKVQQVQGKWKVTDMVGDICGDFKVPQAHITEGFSNTDFVMYVASVPSEEGVLAWATTCQTFSDGHPAVGVINIPAANIASRYDQLVTRVVTHEMAHALGFSGPFFEDARIVANVPNVRGKNFDVPVINSSTAVAKAREQYGCDTLEYL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Has an integral role during the infection of macrophages in the mammalian host.
Catalytic Activity: Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.
PTM: The phosphatidylinosi... |
Q8MNZ1 | MSVDSSSSSTHRRRCVAARLVRLAAAGAAVTVAVGTAAAWAHAGALQHRCIHDAMQARVRQSVARHHTAPGAVSAVGLPYVTLDAAHTAAAADPRPGSAPTVVRAANWSTLRVAVSTEDLTDPAYHCARVGQRVNNHAGAIVTCTAEDILTDEKRDILRKYLIPQALQLHTERLKARQVQGKWKVTGMVDEICGDFKVPQAHITEGFSNTDFVMYVASVPSEEGVLAWATTCQVFSDGHPAVGVINIPAANIASRYDQLVTRVVTHEMAHALGFSEEFFTAARIVAHVSNVRHKTLKVPVVNSSTAVAKAREQYGCGTLE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Has an integral role during the infection of macrophages in the mammalian host.
Catalytic Activity: Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.
Location Topology: Single-... |
Q9FJB4 | MANNEDSNSNGLDSFDAVKQRFKDRSKKVVQTRELLSKQAVQTREILSKQAVKIAKQAEEHERFINKVTHLVGVLGFGGFCFLLGARPQDIPLVYCFFYVIFVPLRWIYYRFKKWHYYLLDFCYYANTIFLVDLLLYPKNEKLFMVCFSFAEGPLAWAIIVWRCSLVFSSPDKIVSVLIHLLPGLVFFTIRWWNPATFAAMHPVGTDRRVSWPYVEDKAYLFTWLFLVPLVVYTLWQVLYFLIVNVLRRQRLLRDPEVMTSYRELSKKAEKANNKLWQLSGLLGDQNRIWMYILFQAIFTVATMALTVPIFLSYRLHVIF... | Function: Glycerophosphocholine acyltransferase (GPCAT) that utilizes acyl-CoA to acylate glycero-3-phosphocholine (GPC), forming lysophosphatidylcholine (LPC) . Shows broad acyl specificities with a preference for 16:0-CoA, polyunsaturated acyl-CoA, and the hydroxylated ricinoleoyl-CoA . Catalyzes also the acylation o... |
F1QCC6 | MDLTAVALLVSLVSVSLSAENAGGKARSCTDVRQFYSGKGFTLNGVPQSEISGEHLRICPQGYTCCTSAMEETLSNLSRREFEGLVREAGRSIQALLNAQYRTFDTYFLELLNGSERWLEEAFVAALGELYRLNAGVFRDLYAELHRYYSGASLNLEEALDEFWMKLLERLLKASDPETASLLSDDFLDCASKQTETLRPFGDAPRELKAKLVRAFIAARAFVQGLNAAGEIVRKVSQVPLSPECNRAIMKLVYCPHCRGLGSVKPCINYCKNVMKGCLANQADLDTEWQSLIETMLQVASSFGAEPSMDTVIYSIPVRI... | Function: Cell surface proteoglycan that bears heparan sulfate.
PTM: O-glycosylated with heparan sulfate side chains.
Location Topology: Lipid-anchor
Sequence Mass (Da): 61296
Sequence Length: 554
Subcellular Location: Cell membrane
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P35052 | MELRARGWWLLCAAAALVACARGDPASKSRSCGEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANRSHAELETALRDSSRVLQAMLATQLRSFDDHFQHLLNDSERTLQATFPGAFGELYTQNARAFRDLYSELRLYYRGANLHLEETLAEFWARLLERLFKQLHPQLLLPDDYLDCLGKQAEALRPFGEAPRELRLRATRAFVAARSFVQGLGVASDVVRKVAQVPLGPECSRAVMKLVYCAHCLGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGTSGVESVIGSVHTW... | Function: Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan ... |
Q8FPR0 | MIERVWQLVSVAVMGAGSWGTTLAKVFADAGNTVQLWARRESLAETIRTSRENPDYLPGITLPDSVIVTSDAQAALDGCSIVVLGIPSQALRTTLVEWRDLISPDATLVSLAKGIEKDTHLRMSQVIAEVTGADPSRIAVLSGPNLAREIAEGQPAATVIACEDENRAKLVQAAVAAPYFRPYTNTDVIGTELGGACKNVIALACGIAHGFGLGENSNASLITRGLAEIARLGEAMGADPRTFAGLAGMGDLVATCSSPLSRNRTFGDRLGRGESLEQAREATHGQVAEGVISSQSIHDLAVGLGVEMPITQAVYAVCHQ... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 35576
Sequence Length: 339
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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B6IYY5 | MEPFKHPIAILGAGSWGTALALVLARKGQKVRLWSYESDHVDEMQAEGVNNRYLPNYPFPETLKAYCDLKASLEGVTDILIVVPSFAFHEVITRMKPLIDAKTRIAWGTKGLAKGSRLLHEVVATELGQVPMAVISGPSLATEVAANLPTAVSLASNNSQFSKDLIERLHGQRFRVYKNDDMIGVELCGSVKNILAIATGISDGLKLGSNARAALITRGLTEMGRLVSVFGGKQETLTGLAGLGDLVLTCTDNQSRNRRFGLALGEGVDKKEAQQAIGQAIEGLYNTDQVHALAQKHAIEMPLTFQVHRILHEDLDPQQA... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 36067
Sequence Length: 332
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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Q0KET4 | MKLTFLGAGAWGTALASHAAAANDVVLWGRDPAQLAAIAATRENAAYLPGVTLSERLAVQADFEQAVAHAADDADGIVVVATPVAGLREMTRRLAARGARPVSMLWLCKGFESGTHLLPHQMVRAELDAAGRTEGFAYGVLTGPSFAREVALGLPCALTVAGNEPSLAERAQAAFHHHAMRIYGSDDLTGVEVGGAVKNVLAIATGASDGLGLGLNARAALVTRGLAEMTRLGLALGGRVETFMGLAGVGDLILTATGDLSRNRKVGQQLAAGQSLEQILAGLGHVAEGVRCAQAVAELASAYGVEMPIARAVCAVLFDG... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 34688
Sequence Length: 338
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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B1XS88 | MKVTLLGAGAWGMAMAAQATRHLQEGDVCLWSRSKEQLLDIQESGENRAYLSGIKLPEGLKLEGDFSAAVKRLSIDDLLVIATPMSGLSETIAQVLRVAEHPLNIIWLCKGLEPNTALLPHQVVERESKIHSHGITHSYGALSGPSFAREVGVGMPCALTVASKSPKLCEVVQAAFHHGNMRVYSSDDLIGVELGGAIKNVLAIAAGIGDGLDLGLNARAAVLTRGLAEMMRLVKAAGGKSETCMGLTGVGDLILTATGDLSRNRRVGLELAAGKSLPEILASLGHVAEGVLCAQAVGDLAKRLGIEMPITAMMDEVLSG... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 35785
Sequence Length: 340
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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C3K747 | MTEQRPIAVLGGGSFGTAVANLLAENGHAVRQWMRDPEQAEAIRVHRENPRYLKGIKIHPAVEPVTDLLETLTACDLCFVALPSSALRSVLAPHAERLAGKLLVSLTKGIEAQTFKLMSEILEEIAPQARIGVLSGPNLAREVAEHALTATVVASEDEELCERVQAVLHGRTFRVYASSDRFGVELGGALKNVYAIIAGMAVALGMGENTKSMLITRALAEMTRFAVNQGANPMTFLGLAGVGDLIVTCSSPKSRNYQVGFALGQGLSLEDAVTRLGEVAEGVNTLKVLKAKAQEVGVYMPLVAGLHAILFEGRTLNQVI... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 36499
Sequence Length: 341
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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Q883Y4 | MTTQQPVAVLGGGSFGTAIANLLAENGHQVRQWMRDPEQAEAIRVNRENPRYLKGIKVRPEVEPVTDLTAALEVSELIFVALPSSALRSVLSPHIERLSGKMLVSLTKGIEAQSFKLMSQILEEIVPQARIGVLSGPNLAREIAEHALTATVVASEDEDLCQQVQAALHGRTFRVYASNDRFGVELGGALKNVYAIIAGMAVALDMGENTKSMLITRALAEMTRFAVSQGANPMTFLGLAGVGDLIVTCSSPKSRNYQVGFALGQGLSLEEAVTRLGEVAEGVNTLKVLKVKAQEVQVYMPLVAGLHAILFEGRTLSQVI... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 36680
Sequence Length: 341
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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Q8DH49 | MSPRVLILGLGHWGQTLAYLFEQRGCTVSSWGRSQGALSAALFQDIHLLVSALPIKAVREVAAQVTRLHPPLGIILVSATKGLESETFATAADIWQTYCPHHDLVVLSGPNLASEIQQGLPAAAVVGGNLAATKQVQDCLGSPTFRLYSNEDRRGVEMGGIFKNVIAIACGVNDGLGLGVNARSALITRGLVEMVRVGTHWGGQVETFYGLSGLGDLLATCTSALSRNYQVGWHLAQGKSLSQALALTKGTAEGVNTARVLCTYAQQHQLDIPITAMVNAVLCGSLTPQAALHCLLERPFKPEVIPGQ | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 32598
Sequence Length: 308
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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B8GR94 | MSQPPVAVLGAGSWGTALAMHLARQGHRVRLWGRDPEAMAAMAEANCNTRYLPDAPFPPGLEPTADLDAALRESSCWLVVVPSQAFREMLQKLAPYRDDARVLVWATKGLEEHSGQWLHQVVAEEMGVNFPCAVISGPSFAKEVARGLPTALTVASTTPGVAERVAEWFHGERMRVYLSDDVLGVQLGGAFKNVLAIAAGISDGLGFGANARAALITRGLAELMRLGDAAGARRETLMGLSGLGDLVLTCTDDQSRNRRLGLALGRGESLDAALAAIGQAVEGARTARMAVSKAAELGVDMPICHQVHRVLYVGHSAIEA... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 35363
Sequence Length: 333
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
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P61748 | MNDKIAIIGAGSWGTAVACSLGKNGHRVVLWSHTAGVADSINTEHINVKYLPKHKLPKTVSASTDMEEVCKDASFIFLASPSLYLTSAVEELLKFAPFSHDDGEMPYPTIAVLTKGFIPDENGEPQFIIDVLEKMLPDFYKNHLVYVAGPSHGEEVAEGKLTGLIAASQNPMCSIRCREILRSRSLLVYSSLDIIGVQVCAAAKNVVAVAFGVLDALTVTSDIFGDNTESLLLAAGLNEIQTIGRAMGATHPETFTSISGVGDLDVTCRSKYGRNRRFGNEIITKKILLSFENLDDLIKNIDKIGYLPEGVVACKYLNIL... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 38855
Sequence Length: 357
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
|
O83973 | MASIAILGGGAWGTALAASLTVNGHTVMLWARRRQTCDAINARNENVQYLPGITLPAALCASPDMAYVCAGADLIVLAVPSCYLAEVAALMNTTPRFQRLRTAAVGQEYPLIGILTKGFIPDQEGMPHLITDALGALLPSGAHGQLVYISGPSHAQEVAQGKVTGLIAASQNPMAAIRVRELLRSKRVQVYSSLDVVGVQVCAAVKNVIAIAFGLLDAMAEHSEAFGDNTESMLLAAGLNEIQTIGKQLGSTHPETFTSLAGIGDLDVTCRSAYGRNRRFGRDIVHKGILDSFSGIQDLVSRLPEVGYLAEGVVACMHVQ... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 37879
Sequence Length: 356
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
|
B3E9A1 | MKIGVIGAGSWGTALANVVAANGHDTTLWAYEPELVTGMAATRVNHLFLPGIELHPGLNYTGALAEAVSGAELVLLVTPTQVMRNLLADLAGSIAPTAILASASKGIELGTLCTVSQICCQVLGDAVRERFVALSGPTFAKEVALGLPSLIVAGSANDAAAHTVQAAFSNPVFRVYTSDDAIGVELGGAVKNVIAIAAGISDGLGFGHNTRAALITRGLAEMKRLGRAMGAQDATFAGLAGMGDLVLTCTGDLSRNRTVGVKLGQGLTLEVIMAEMRMVAEGVKSAESVNALAQKLGVEMPITQKVYEILYGNKPARQAV... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 34376
Sequence Length: 333
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
|
Q83G27 | MQLSGYPMRQASCDMKEGGLRNKVAVIGSGSWGTAIANLLCKAGNETILWGRDENVIDEINNARVNSKYLPGVELFLRATCDLDYAVADASHVYIALPSFALSKVLPKLSLDKFSIVISLIKCLEPDTGRRMSEVISEALDLGHNRLAVISGPNLALEVANDEPSVSVVASANIATANIVAGTLKCPGFYCIPSSDIKGVEICAASKNLVALISGIARGMDLGDNTRAALITLGFRELLRLVLENGGTEETVFGVAGLGDVVATCNSHLSRNNKAGVLLAKGAPLDEVKQTAEGVVAISGVLALAERSGVYMPIAQALSQ... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 35581
Sequence Length: 339
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
|
A5CVT6 | MSNNLSIIGAGAWGSALSIALYDNFDTIYLHTHTQADIKKLKSKHSALSIPYPYNVKIAYDLYKLQDSKNIIITTPSYAFSEILEKIKPFINHTHKIAWGTKGFDTTKRCFLYESFKRLFPNRNGCVISGPSFAFEVALNKPTALVVASIDENTRNHFAKLIQTNTLRTYTNADIIGVEVGGSVKNILAIAAGIASGLKYGFNTQAALIARGLSEMSRLGKSLGAKNSTFIGLSGLGDLVLTCSDNLSRNRRFGQELVNNHNIKNALINVGGTVEGLNTLDLILSIANKKQVEMPICEQVYQITQGKITPAEAVNYLMSR... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 35924
Sequence Length: 327
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
|
A5F502 | MSETQNHNSYGKPVEMTVIGAGSYGTSLAISLARNGANIVLWGHDAEHMARLDADRANHEFLPGIAFPDTLIVETDLQKAVQASRDLLVVVPSHVFGIVLKSLQPHLRADSRICWATKGLEPETGRLLQDVAHDVLGDSYPLAVLSGPTFAKELAMGMPTAISVASPDAQFVRDLQEKIHCSKTFRVYANSDFIGMQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGAQPETFMGMAGLGDLVLTCTDNQSRNRRFGLALGQGKDVDTAQTDIGQVVEGYRNTKEVWMLAKRMGVEMPIVEQIYQ... | Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Mass (Da): 37110
Sequence Length: 344
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Subcellular Location: Cytoplasm
EC: 1.1.1.94
|
Q9PAM6 | MPLNEPSSNAFPRTVLFDLDGTLLDSAPDMLATANAMLAARGRAPITLAQLRPVISIGTFRILAVAFPELDAAAIQGLIPEFLQRYEALIGSVSKPFDGVEMMLDALECAGTVWGIVTNKPEFLARLILPLLGWTSRCAVLIGGDTLAERKPHPLPLLTAAERIGVMPTDCVYVGDDVSDIQAARAAGMPSMVALWGYRSHEDNPMTWQADTLVEQPHLLSRPDVWPST | Function: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress.
Catalytic Activity: 2-phosphoglycolate + H2O = glycol... |
Q75BG9 | MKERSILRTLFLWRLINALSIRSFFQADEYWQSLEPAHVKAFGYGGLTWEWQHGLRSYAFPMLFEMSYYVAWILGVATRMALQGLAHATALCGAVVPSGAAGVAAMKAVWELPEAAQELVEYYGVLYGPRVVMAAVAACGEFYSVLLVRKLYLRVADKGDDQKGDAAPVSRLALMLTMTNFFNCFFATRTFINSFEMTLTAVALYHWDWSGGLDVGSLGFSASLAVAAFACLQRPTNVLIWAVLGLFLVLNLVRSRRWQLLLTLVAKVAAAGALAVCANIAIDYYFYGGVLLPLLRFIEFNVTTPLAAFYGRAPWHFHLL... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67312
Sequence Length: 595
Pathway: Glycolipid biosynthesis; glyc... |
Q4WPG0 | MSSSRRRKSFTSSSSSSSPSFHSPPPTSRLRPRSPPSSNTKTSPTSTTPLATNILLSLIAFRLVNAFTVRTFFQPDEFFQSLEPAWQIAFGENQGAWITWEWRHQLRSSIHPLLFAAVYSAADVVAQLLRLSLASRADLLVAAPKTAQAVIAGLGDFYTWKLARYVYGARSYEAWATLALTVVSPWQWFCSTRTLSNCLETTITIVALYLWPWSWSFETPVRKKATRAASRERAQRGPEGSDSLQRLRQCLSLAAVACILRPTNILIWMGLASVAWFRTSWDRRAILVREVLLCGCAVLGLSCVVDRLFYGSWTFPPLRF... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87863
Sequence Length: 771
Pathway: Glycolipid biosynthesis; glyc... |
Q2UH15 | MSTSSRRRRSPLELSSSRSSSSSSSSYASWASTTSPSTSTSTPPSLSRTTTVSTSHVFLFLLAFRLLNALSLRTFFQPDEFFQSLEPAWQTAFGETHGANGDTICGLPSILCYLLQFILSPTLPRALFVSPPHSAILSAIGDLYTWKLARYVYGRRSHEAWAALALTVLSPWQWFCSTRTLSNCLETTITIVALNLWPWEWSSESTPTVQPRRNTRSTTRDTGLDNTGDGAVVVRLRKCLTLAALACILRPTNILIWMGLAGVAWFRSAWRERTILCREVLLCGVSVLTGSVVLDRLYYGLWTFPPLKFLYFNIAQSLAV... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81947
Sequence Length: 728
Pathway: Glycolipid biosynthesis; glyc... |
Q5AK24 | MTKSTVLSSYKLFAFIFIFRLANSFAIETFFQADEFFQALEPAHHFVYGYGYLTWEWKQQLRSAIHPLIYVLGYKLVGDNTTLVCISPKVINALIAAIGEYNLYKFIIVYDSEKLAWITLMLSLFNPFNWYVITRSFSNNLEMVFTVLALRFWPWNKKINGRWYISLGFGFVSCIIRPTNILIWIPLGIWLLISIRITLKWVALSFLEVVLILLINTALDYYFYQKLTFPLYNFLEFNVFKNLSIFYGTAPWHFYIFQAIPLMLMLYLPLMIYGLKKNILLLTGLFYIIGFSLIQHKEFRFIYPIHPILLYFTARGYVKF... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57060
Sequence Length: 482
Pathway: Glycolipid biosynthesis; glyc... |
Q6BH65 | MAYNNSVRKRKKDIQDANGFHRDQTIDKKSRATNKLEESLPTFKVFIVLFFIRLLNSLTIKTFFQADEYYQCLEPAYNFVFGSGYITWEWEEGIRSSIHPLIYALGYKMVSYVHFDDKPIILIPKVIGALIASIGEVYLYKFSKKFTKNEKLARLTLILSLLSPFNWYIITRSFSNSFEMVLTTIAFTYWPWDNVISYKDISMSCIIAFISCIVRPTNGIIWLYLGINFMIKNYKLEKQSGKLMKLILILSIELILILLVNTGLDYIFYGKTTFPLYNFVEFNVIRNLSIFYGVAPWHFYLFQGVPIILMTYLPWLLHSA... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64581
Sequence Length: 549
Pathway: Glycolipid biosynthesis; glyc... |
Q5BCB9 | MPMSARSRRSNPRLPPSPSSSSSSDAVRASPHSSPPSRLRPPSANPDVSSNILLFLIGFRLVNALTVRTFFQPDEFFQSLEPAWKIAFGTNQGPWITWEWEHQLRSSLHPLIFAAVYTVADLVARTLGLTPTSRAELLIAGPGITQAVIAAVGDFYTWKLARYIYGDRSHESWATVRIRSNAIEADADQLQLALTVVSLASVALYRSAWGERQTLAREALICGSSVLAVSTVVDRFFYGFWTFPPLRFLYFNVAQSLAAFYGRNDWSYYASQGYPLLLTTALPFTLVGLYRTLKTPPKLEKQKGSILVQLASISLAMPAT... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75503
Sequence Length: 663
Pathway: Glycolipid biosynthesis; glyc... |
Q4IB63 | MSSATVSRKSLDEARNQRNRSFFLRDIIVIRLINAWWIATFFQPDEFFQSLEPAWNLAFGSQSGAWLTWEWQHQLRTSLHPALFAGVYLVADFISSHILPVGILRATILVAVPQALQAVIAGLGDWYTWQLAVSIYGANSNVSFFALFLQIFNPWQWYCSTRTFSNSLEMTLTVMAMYYWPWELLGVAQTTKENPKPAPILKSLWSLRASLCLAALAVVLRPTNILIWATIVLFTITRISLQGPSPLTLSTVVTLIREAIWCGSLILAISAASDRWYFGFWTFPAYNFLYFNLSKSLAVFYGRSPWHYYFLQGLPLICTT... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69884
Sequence Length: 613
Pathway: Glycolipid biosynthesis; glyc... |
Q9USN0 | MRIWFWLAILVFRWWNALWVKTFFQPDEFYQSLEVAHHFIFRYGFLTWEWTSAIRSALHPLIFAALYRVLQVLKLDSSYFVFTNAPKLLQGTFAAILDYGTYKFALVRYGSKTANWTLACSLVSIMNAYVGVRTFSNSLETTLTSIGFYYFSYYLKYENSSPEQRKKAYSSLLGFISVAAFACFIRPTNILVWIFPLLFWNKNPQTPIKDLLSFSNVFNRFRFLYALGYGRLFGIFVLCVSLFLVNIIADRILYGRFVFPIISFFQFNVTSGLSSLYGLNAWHYYLSQALPLICGGFLPFVLLTMDLQTAGTILCVFFPY... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59222
Sequence Length: 506
Pathway: Glycolipid biosynthesis; glyc... |
P86935 | MPWWLISLTFIYRLFLCATIRTVEAPDEWWQSTEVAYNMVFGKGHLPWEWRYGLRSVLFPAVVALPFYLLKLLGRDTTWAVWFAPRVLQALVLTLIDVSVFCMGATLDELLAKRELELAEETRQSKTKGFSYFCEVSVSRSRRGICNSISYTALLLSLSNWYMAYCGVRLYGNVIEALLVLLTLQQRRYVPFLLLTGLASAIRVTSAVVLSPLVFRHLANATREHGFIRGLFRIVLTGLIVLVAVLGGVMVLDYCFYGRWVLTPLAFFRFNVLHNLSRFFGEHPWYFYVGPVLVGIVGPHVLFTIAAPLVLWRDTASRAV... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64182
Sequence Length: 558
Pathway: Glycolipid biosynthesis; glycosylph... |
Q6CAB8 | MMQHKEIKHPYQGIKYTVLVVIAAFRVANALTTKTFFQPDEYWQSLEPAHRLAYGYGYLTWEWHEGLRSSLPPLVGAGIYKALQLLGLDDPRIVRIAPKIVMALFASAGDVYTWKLSARLQGPAEAPWALFVSLLSAFNWFFLTRTFSNSAEMVLTAVALNYWSFNGKEVNFKRLSVALFIGAISCVLRPTNAILWAVLGLHLVLTTTAKMRVLWLAVRNVALVFAATYYIDYLYYGEPVFPLLNFLKFNLLQSLAHFYGTSPTLYYFYEALPLLTVGWLPLTLWGLWINRSQVLVKAALAVVVAFSLIRHKEVRFIYPL... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58336
Sequence Length: 510
Pathway: Glycolipid biosynthesis; glyc... |
A1WWH7 | MPKLVLLRHGQSIWNLENRFTGWYDVDLSDQGINEAREAGVALREAGIAPQVAYTSVLKRAIRTLWLSLAELDRMWIPEIKDWRLNERHYGALTGLNKAETAEQYGDEQVHIWRRSYDTPPPALDAEDERHPRHDPRYAGLDPQQLPGTESLKLTLERVLPCWEGEIAPALRQHDCVLIAAHGNSLRALVKHLDGLADDAIMKVEIPTGRPLVYELAEDLSVQRSYYVQD | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 26219
Sequence Length: 230
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
|
C4K389 | MTIKKLILVRHGESEWNKENRFTGWADVDLSEKGRVEAQQAGNLLKKKGFSFDFAYTSVLRRATNTLSLILDVLQQQNLPIEKSWRLNERHYGALQGLNKSETAAKFGSEQVKQWRRGFSTLPPALNLNDPRAPANDSLYATLNKNDLPLTESLATTVDRVVPYWDEVVKPRIIDGKRVIIVAHGNSIRALVKYVDHLSEEEIMEINIPTAVPLVYEFNSSLQPINHYYLGNAEEITQKVAAVAAQGKA | Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 28055
Sequence Length: 249
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.11
|
G5EFZ1 | MFVALGAQIYRQYFGRRGMAMANNSSVANKVCLIVIDGWGVSEDPYGNAILNAQTPVMDKLCSGNWAQIEAHGLHVGLPEGLMGNSEVGHLNIGAGRVIYQDIVRINLAVKNNKFVTNESLVDACDRAKNGNGRLHLAGLVSDGGVHSHIDHMFALVKAIKELGVPELYLHFYGDGRDTSPNSGVGFLEQTLEFLEKTTGYGKLATVVGRYYAMDRDNRWERINVAYEAMIGGVGETSDEAGVVEVVRKRYAADETDEFLKPIILQGEKGRVQNDDTIIFFDYRADRMREISAAMGMDRYKDCNSKLAHPSNLQVYGMTQ... | Cofactor: Binds 2 manganese or magnesium ions per subunit (By similarity). Cobalt and nickel are less efficient .
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 59225
Sequence Length: 539
Pat... |
A9WJ95 | MTRPRPVVLIIMDGWGIAPPGPGNAADLADTPHVDAWMANCPFTTLGASGLDVGLPEGQIGNSEVGHLNIGAGFVVYQELTRISKAIADGDFFTNPVLLQAIEHVKQRNSALHLMGLFGPGGVHAHEDHLHALLELAHRHHLQRVYLHLFLDGRDVLPRSALGFLDTLEGVIARLGVGTIATVSGRYYAMDRDKRWERTGRAYAALVDGVGEKAPSARAAIEASYARDVSDEFVLPTVIVTASGEPTATVRDGDAVIFTNFRPDRGRQLTRAFVDPDLNERIRQHYERQKAEGQPLPATIWQRERQLRDLCFVTMTQYEE... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 58598
Sequence Length: 540
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceral... |
Q7NSR8 | MKSIKPVLLLILDGFGHRTEGDDNAILHARMPVWSRLREQYAYGTINASENFVGLPSGQFGNSEVGHLNIGAGRIVQQDISRIDCDIEDGRFSSNDTLQQAMSKAQGSALHILGLLSDGGVHSHENHIHALIRAAQAAGVPKIYVHAFLDGRDTPPRSAETYLKRLDAALAECPNARLVSVTGRYWAMDRDKRWERVEPAYRLLVDGEGLFHAETGLDALKAAYERDENDEFVKATGIGAPVKMQDGDALIFMNFRADRARQLTSALTDPAFDGFKARQPKFGYYATLTSYGEAYSALPVAYAPQKIHNGMGEYLSSKGL... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 55525
Sequence Length: 507
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceral... |
Q9L214 | MSTPEPVLAGPGILLVLDGWGSADAADDNALSLARTPVLDELVAQHPSTLAEASGEAVGLLPGTVGNSEIGHMVIGAGRPLPYDSLLVQQAIDSGALRSHPRLDAVLNEVAATSGALHLIGLCSDGQIHAHVEHLSELLAAAATHQVERVFIHAITDGRDVADHTGEAYLTRVAELAAAAGTGQIATVIGRGYAMDKAGDLDLTERAVALVADGRGSPADSAHSAVHSSERGDEWVPASVLTEAGDARVADGDAVLWFNFRSDRIQQFADRLHEHLTASGRTVNMVSLAQYDTRTAIPALVKRADASGGLADELQEAGLR... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 53353
Sequence Length: 511
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceral... |
Q67SW0 | MSAYRRPVALIVLDGWGLNPDPRANAVAMARHPNFDRLMARYPHTTLTASGEAVGLLPGQMGDSNVGHLNLGAGRIVYQTLVRIWRSIQDGSFYTLPVWRPVLDRAKQPGKALHLMGLVSDGGVHSHIDHLLALIDLAKRENVERVYVHAFLDGRDVPPQSALPYLERVEAKLKETGIGAIATISGRYYAMDRDKRWDRTEKAFLAITQGIGHTAGSVAEAVERAYARGETDEFVQPTVIEGVDGRVREGDGVIFFNFRPDRARQLVRALHETAFDGFKRPEGYRPVELVTMTQYDQTFTDIPVAFGPQFVDVPMGQVVA... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 56812
Sequence Length: 517
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceral... |
Q3A1E5 | MTVEIRRPVALVILDGWGINPVCEHNAVCQADTPRLRALLESWPHARIGASGRDVGLPDGQMGNSEVGHLNIGAGRTVYQDLTRISLSIEEDTFFENTELRKVMQQVVESQGKLHLMGLLSDGGVHSHMEHLYALVEMARRAGVEQVCIHAFMDGRDTPPQSGAGYLAQLEDKLQDIGLGRVATVIGRYWAMDRDNRWERVEKAYRAMTEGVGTSFESSAAAIADAYAQGQTDEFVEPRFVGGEKPCTVDDGDGMIFFNFRADRAREITRTFTSSDFSGFSREKTPRLAGYVCLTEYDASFGLPMAFPPETYPELLGEVV... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 55889
Sequence Length: 514
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceral... |
Q2JSV1 | MDAQSVAPVVLVILDGWGYREAPEGNAVLAARTPVVDSLWATYPHTLLQASGRAVGLPSGQMGNSEVGHLTLGAGRVVPQELVRISDAIETGSLFHEPLLVEVCHRLKEQGGRFHFIGLCSEGGVHSHIDHLYGLLKLAAQAGIPAYVHAITDGRDTLPRDGARVLAALEKELQWLGSGVIATLSGRYYAMDRDRRWERTQKAYEILTEDGPGCGRSAAEVMEDFYAQDITDEFIPPTRLAPGAVQSGDAVIFFNFRPDRARQLTQAFVCPDFSGFQRRLIPDLTFITMTQYDPTLPVQVLFKPQNLDHLLGQVVSEAGL... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 57879
Sequence Length: 530
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceral... |
P74507 | MAEAPIAPVVLVILDGWGYRPDTRANAIAQANTPIMDSLIAAYPNTLVNTSGKDVGLPKGQMGNSEVGHLNLGAGRVVPQELVRISDAIEDGTFFDNQALIEVCQRVRDRRGKLHLIGLCSDGGVHSHIDHLLGLIDLAKLQGISQLCIHAITDGRDTPTNEGAHFVQQIQAHLEKIGLGRIVSVSGRYYALDRDRRWDRVEKAYRVMTEDGVGDGRSAAQVIKDYYASDITDEFIPPTRIGAGAIASGDGVIFYNFRPDRARQLCYALVNPSFDGFPRERIQPLDFVTFTQYDPALPVVVAFEPQNLNNILGEIISRQG... | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 57982
Sequence Length: 532
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceral... |
Q8L2S1 | GEAVGLPAQQMGNSEVGHLNLGAGRVVHQSLTYINRKIKDGSFFKNKCFLKVIQHVKTNKSKLHLLGLVSDGGVHSHLDHF | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Mass (Da): 8858
Sequence Length: 81
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceralde... |
B4XF06 | MASPSHPSRDCSQVIDHSHVPEFEVATWIKITLILVYLVIFVVGILGNSVTIRVTQVLQKKGYLQKEVTDHMVSLACSDILVFLIGMPMEFYSIIWNPLTTPSYTVSCKVHTFLFEACSYATLLHVLTLSFERYIAICHPFRYKAMSGPCQVKLLIGFVWVTSALVALPLLFAMGVEYPLVNVPSHRGLICNRSRTRHQEQPESSNMSICTNLSSRWTVFQSSIFSAFVVYLVVLVSVAFMCWSMMQVLRRSKQGTLAAQGQQLQLRKLESQESRSARRQTIIFLELIVVTLAVCWMPNQVRRIMAAAKPKHDWTKSYFR... | Function: Zn(2+) acts as an agonist. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated mainly through G(q)-alpha and G(12)/G(13) proteins. Involved in regulation of body weight, gastrointestinal mobility, hormone... |
O43194 | MASPSLPGSDCSQIIDHSHVPEFEVATWIKITLILVYLIIFVMGLLGNSATIRVTQVLQKKGYLQKEVTDHMVSLACSDILVFLIGMPMEFYSIIWNPLTTSSYTLSCKLHTFLFEACSYATLLHVLTLSFERYIAICHPFRYKAVSGPCQVKLLIGFVWVTSALVALPLLFAMGTEYPLVNVPSHRGLTCNRSSTRHHEQPETSNMSICTNLSSRWTVFQSSIFGAFVVYLVVLLSVAFMCWNMMQVLMKSQKGSLAGGTRPPQLRKSESEESRTARRQTIIFLRLIVVTLAVCWMPNQIRRIMAAAKPKHDWTRSYFR... | Function: Zn(2+) acts as an agonist. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated mainly through G(q)-alpha and G(12)/G(13) proteins. Involved in regulation of body weight, gastrointestinal mobility, hormone... |
Q5U431 | MASSSGSNHICSRVIDHSHVPEFEVATWIKITLILVYLIIFVVGILGNSVTIRVTQVLQKKGYLQKEVTDHMVSLACSDILVFLIGMPMEFYSIIWNPLTTPSYALSCKLHTFLFETCSYATLLHVLTLSFERYIAICHPFKYKAVSGPRQVKLLIGFVWVTSALVALPLLFAMGIEYPLVNVPTHKGLNCNLSRTRHHDEPGNSNMSICTNLSNRWEVFQSSIFGAFAVYLVVLASVAFMCWNMMKVLMKSKQGTLAGTGPQLQLRKSESEESRTARRQTIIFLRLIVVTLAVCWMPNQIRRIMAAAKPKHDWTRTYFR... | Function: Zn(2+) acts as an agonist (By similarity). This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated mainly through G(q)-alpha and G(12)/G(13) proteins. Involved in regulation of body weight, gastrointestinal m... |
P35413 | MMWGAGSSMAWFSAGSGSVNVSSVDPVEEPTGPATLLPSPRAWDVVLCISGTLVSCENALVVAIIVGTPAFRAPMFLLVGSLAVADLLAGLGLVLHFAADFCIGSPEMSLMLVGVLAMAFTASIGSLLAITVDRYLSLYNALTYYSETTVTRTYVMLALVWVGALGLGLVPVLAWNCRDGLTTCGVVYPLSKNHLVVLAIAFFMVFGIMLQLYAQICRIVCRHAQQIALQRHLLPASHYVATRKGIATLAVVLGAFAACWLPFTVYCLLGDADSPRLYTYLTLLPATYNSMINPVIYAFRNQDVQKVLWAICCCCSTSKI... | Function: Orphan receptor with constitutive G(s) signaling activity that activate cyclic AMP. Has a potential role in modulating a number of brain functions, including behavioral responses to stress, amyloid-beta peptide generation in neurons (By similarity) and neurite outgrowth (By similarity). Maintains also meiotic... |
O15529 | MDTGPDQSYFSGNHWFVFSVYLLTFLVGLPLNLLALVVFVGKLRCRPVAVDVLLLNLTASDLLLLLFLPFRMVEAANGMHWPLPFILCPLSGFIFFTTIYLTALFLAAVSIERFLSVAHPLWYKTRPRLGQAGLVSVACWLLASAHCSVVYVIEFSGDISHSQGTNGTCYLEFRKDQLAILLPVRLEMAVVLFVVPLIITSYCYSRLVWILGRGGSHRRQRRVAGLVAATLLNFLVCFGPYNVSHVVGYICGESPVWRIYVTLLSTLNSCVDPFVYYFSSSGFQADFHELLRRLCGLWGQWQQESSMELKEQKGGEEQRA... | Function: G protein-coupled receptor that is activated by short chain fatty acids (SCFAs), such as propionate. Hence may play a role in the regulation of whole-body energy homeostasis and/or in intestinal immunity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38665
Sequence Length: 346
Subcellular... |
Q9Y5Y3 | MACNSTSLEAYTYLLLNTSNASDSGSTQLPAPLRISLAIVMLLMTVVGFLGNTVVCIIVYQRPAMRSAINLLLATLAFSDIMLSLCCMPFTAVTLITVRWHFGDHFCRLSATLYWFFVLEGVAILLIISVDRFLIIVQRQDKLNPRRAKVIIAVSWVLSFCIAGPSLTGWTLVEVPARAPQCVLGYTELPADRAYVVTLVVAVFFAPFGVMLCAYMCILNTVRKNAVRVHNQSDSLDLRQLTRAGLRRLQRQQQVSVDLSFKTKAFTTILILFVGFSLCWLPHSVYSLLSVFSQRFYCGSSFYATSTCVLWLSYLKSVFN... | Function: Orphan receptor. May play a role in brain function.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41967
Sequence Length: 372
Subcellular Location: Cell membrane
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Q9EQQ4 | MACNSTPMGTYEHLLLNVSNTLDPGDTPLSAPLRISLAIMMLLMIVVGFLGNTVVCIIVYQRPAMRSAINLLLATLAFSDIMLSLCCMPFTAITLITVRWHFGDHFCRLSATLYWFFVLEGVAILLIISVDRFLIIVQRQDKLNPRRAKMIIAASWVLSFCISAPSFTGWTFMEVPARAPQCVLGYTEFPAERAYVVTLVVAVFFAPFGVMLCSYLCILNTVRKNAVRVHNQSDSLDLRQLTGAGLRRLRRQQQQASLDLSFKTKAFTTILILFVGFSLCWLPHSVYSLLSAFSRRFYYSASFYTTSTCVLWLSYLKSVF... | Function: Orphan receptor. May play a role in brain function.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42358
Sequence Length: 373
Subcellular Location: Cell membrane
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P46093 | MGNHTWEGCHVDSRVDHLFPPSLYIFVIGVGLPTNCLALWAAYRQVQQRNELGVYLMNLSIADLLYICTLPLWVDYFLHHDNWIHGPGSCKLFGFIFYTNIYISIAFLCCISVDRYLAVAHPLRFARLRRVKTAVAVSSVVWATELGANSAPLFHDELFRDRYNHTFCFEKFPMEGWVAWMNLYRVFVGFLFPWALMLLSYRGILRAVRGSVSTERQEKAKIKRLALSLIAIVLVCFAPYHVLLLSRSAIYLGRPWDCGFEERVFSAYHSSLAFTSLNCVADPILYCLVNEGARSDVAKALHNLLRFLASDKPQEMANAS... | Function: Proton-sensing G-protein coupled receptor couples to multiple intracellular signaling pathways, including GNAS/cAMP, GNAQ/phospholipase C (PLC), and GNA12/GNA13/Rho pathways . Acidosis-induced GPR4 activation increases paracellular gap formation and permeability of vascular endothelial cells through the GNA12... |
P0C5J4 | MNESRWTEWRILNMSSSIVNVSEHHSCPLGFGHYSVEDVCIFETVVIVLLTFLIISGNLTVIFVFHCAPLLHHYTTSYFIQTMAYADLLVGVTCLVPTLSLLHYSTGVHESLTCQVFGYIISVLKSVSMACLACISVDRYLAITKPLSYNQLVTPCRLRICIIMIWIYSCLIFLPSFFGWGKPGYHGDIFEWCATSWLTSAYFTCFIVCLLYAPAALVVCFTYFHIFKICRQHTKEINDRRARFPSHEVEASREAGHSPDRRYAMVLFRITSVFYMLWLPYIIYFLLESSRVLDNPTLSFLTTWLAISNSFCNCVIYSLS... | Function: G- protein coupled receptor activated by antipsychotics reserpine leading to an increase in intracellular cAMP and its internalization (By similarity). May play a role in locomotor activity through modulation of dopamine, NMDA and ADORA2A-induced locomotor activity. These behavioral changes are accompanied by... |
Q6BD04 | MYSSEELWNSTEQVWINGSGTNFSLGRHEDDEEEEGDKHPFFTDAWLVPLFFSLIMLVGLVGNSLVIYVISKHRQMRTATNFYIANLAATDIIFLVCCVPFTATLYPLPGWIFGNFMCKFVAFLQQVTVQATCITLTAMSGDRCYVTVYPLKSLRHRTPKVAMIVSICIWIGSFVLSTPILMYQRIEEGYWYGPRQYCMERFPSKTHERAFILYQFIAAYLLPVLTISFCYTLMVKRVGQPTVEPVDNNYQVNLLSERTISIRSKVSKMVVVIVLLFAICWGPIQIFVLFQSFYPNYQPNYATYKIKTWANCMSYANSSV... | Function: Receptor speculated to be essential for sexual development. May regulate gonadotropin-releasing hormone (GnRH) secretion. The receptor expression could be a 'stop signal' for GnRH1, GnRH2, and GnRH3 neuronal migration, leading to suppression of cell growth and modulation of GnRH secretion, which is important ... |
Q9Y2T6 | MSQQNTSGDCLFDGVNELMKTLQFAVHIPTFVLGLLLNLLAIHGFSTFLKNRWPDYAATSIYMINLAVFDLLLVLSLPFKMVLSQVQSPFPSLCTLVECLYFVSMYGSVFTICFISMDRFLAIRYPLLVSHLRSPRKIFGICCTIWVLVWTGSIPIYSFHGKVEKYMCFHNMSDDTWSAKVFFPLEVFGFLLPMGIMGFCCSRSIHILLGRRDHTQDWVQQKACIYSIAASLAVFVVSFLPVHLGFFLQFLVRNSFIVECRAKQSISFFLQLSMCFSNVNCCLDVFCYYFVIKEFRMNIRAHRPSRVQLVLQDTTISRG | Function: May be involved in hyperalgesia associated with inflammatory and neuropathic pain (By similarity). Receptor for L-alpha-lysophosphatidylinositol (LPI). LPI induces Ca(2+) release from intracellular stores via the heterotrimeric G protein GNA13 and RHOA. Putative cannabinoid receptor. May play a role in bone p... |
P41264 | CIQLGTEQTCKSVDSNDCLVTTSVKVCLIGTVSKFQPSDTLLFLGPLEQGGLIFKQWCTTTCQFGDPGDIMSTPVGMKCPELSGSFRKKCAFATTPVCQFDGNTISGYKRMIATKDSFQSFNVTEPHISASSLEWIDPDSSLRDHINVIVGRDLSFQDLSETPCQVDLTTTSIDGAWGSGVGFNLICSVSLTECSTFLTSIKACDSAMCYGSTTANLLRGQNTVHIVGKGGHSGSKFMCCHDTKCSSTGLIAAAPHLDRVTGYNQADSDKIFDDG | Function: Forms homotetramers with glycoprotein N at the surface of the virion. Attaches the virion to host cell receptors including integrin ITGAV/ITGB3. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Class II fusion protein that promotes fusion of viral membrane w... |
Q9H772 | MFWKLSLSLFLVAVLVKVAEARKNRPAGAIPSPYKDGSSNNSERWQHQIKEVLASSQEALVVTERKYLKSDWCKTQPLRQTVSEEGCRSRTILNRFCYGQCNSFYIPRHVKKEEESFQSCAFCKPQRVTSVLVELECPGLDPPFRLKKIQKVKQCRCMSVNLSDSDKQ | Function: Cytokine that inhibits the activity of BMP2 and BMP4 in a dose-dependent manner, and thereby modulates signaling by BMP family members. Contributes to the regulation of embryonic morphogenesis via BMP family members. Antagonizes BMP4-induced suppression of progesterone production in granulosa cells.
PTM: N-gl... |
O88273 | MFWKLSLTLLLVAVLVKVAETRKNRPAGAIPSPYKDGSSNNSERWHHQIKEVLASSQEALVVTERKYLKSDWCKTQPLRQTVSEEGCRSRTILNRFCYGQCNSFYIPRHVKKEEDSFQSCAFCKPQRVTSVIVELECPGLDPPFRIKKIQKVKHCRCMSVNLSDSDKQ | Function: Cytokine that inhibits the activity of BMP2 and BMP4 in a dose-dependent manner, and thereby modulates signaling by BMP family members. Contributes to the regulation of embryonic morphogenesis via BMP family members. Antagonizes BMP4-induced suppression of progesterone production in granulosa cells.
PTM: N-gl... |
A5HEG9 | MTAEGEAKNPSAGGGGDNPQHQQAAPAPAPAQGEVAQEAAVQGTGQEQERDKADREVQGGAGEKDDGACRDLVLVEDPEVLAVEDPEEAAATAALQEEMKALVASIPDGAGAAFTAMQLQELEQQSRVYQYMAARVPVPTHLVFPVWKSVTGASSEGAQKYPTLMGLATLCLDFGKNPEPEPGRCRRTDGKKWRCWRNTIPNEKYCERHMHRGRKRPVQVFLEDDEPDSASGSKPAAPGKATEGAKKADDKSPSSKKLAVAAPAAVQST | Function: Involved in the regulation of cell proliferation in developing shoots and leaves . Does not possess transactivation activity .
Sequence Mass (Da): 28541
Sequence Length: 269
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Subcellular Location... |
Q6EPP9 | MDEEKEADSPQPPSKLPRLSGADPNAGVVTMAAPPPPVGLGLGLGLGGDSRGERDVEASAAAAHKATALTFMQQQELEHQVLIYRYFAAGAPVPVHLVLPIWKSVASSSFGPHRFPSLAVMGLGNLCFDYRSSMEPDPGRCRRTDGKKWRCSRDVVPGHKYCERHVHRGRGRSRKPVEASAAATPANNGGGGGIVFSPTSVLLAHGTARAT | Function: Transcription activator that plays a regulatory role in gibberellin-induced stem elongation.
Sequence Mass (Da): 22310
Sequence Length: 211
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Subcellular Location: Nucleus
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Q6AWX7 | MLAEGRQVYLPPPPPSKLPRLSGTDPTDGVVTMAAPSPLVLGLGLGLGGSGSDSSGSDAEASAATVREARPPSALTFMQRQELEQQVLIYRYFAAGAPVPVHLVLPIWKSIAAASSFGPQSFPSLTGLGSLCFDYRSSMEPEPGRCRRTDGKKWRCSRDVVPGHKYCERHVHRGRGRSRKPMEASAAVAPTYLPVRPALHTVATLATSAPSLSHLGFSSASKVLLAHTTTGTTRAT | Function: Transcription activator that plays a regulatory role in gibberellin-induced stem elongation.
Sequence Mass (Da): 24971
Sequence Length: 236
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Subcellular Location: Nucleus
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O81001 | MDLGVRVSGHETVSSPGQTELGSGFSNKQERSGFDGEDCWRSSKLSRTSTDGFSSSPASAKTLSFHQGIPLLRSTTINDPRKGQEHMLSFSSASGKSDVSPYLQYCRNSGYGLGGMMNTSNMHGNLLTGVKGPFSLTQWAELEQQALIYKYITANVPVPSSLLLSLKKSFFPYGSLPPNSFGWGSFHLGFSGGNMDPEPGRCRRTDGKKWRCSRDAVPDQKYCERHINRGRHRSRKPVEGQNGHNTNAAAAASAAAASTAAAVSKAAAGTSAVAMRGSDNNNSLAAAVGTQHHTNNQSTDSLANRVQNSRGASVFPATMN... | Function: Transcription activator that plays a role in the regulation of cell expansion in leaf and cotyledons tissues. Component of a network formed by miR396, the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function, at least partially through the control of cell proliferation. micr... |
A0A060D764 | MAMPYASLSPAGAADHRSSTATASLVPFCRSTPLSAGGGLGEEDAQASARWPAARPVVPFTPAQYQELEQQALIYKYLVAGVPVPPDLVVPIRRGLDSLATRFYGQPTLGYGPYLGRKLDPEPGRCRRTDGKKWRCSKEAAPDSKYCERHMHRGRNRSRKPVETQLAPQSQPPAAAAVSAAPPLAAAAAATTNGSGFQNHSLYPAIAGSTGGGGGVGGSGNISSPFSSSMGGSSQLHMDSAASYSYAALGGGTAKDLRYNAYGIRSLADEHNQLIAEAIDSSIESQWRLPSSSFPLSSYPHLGALGDLGGQNSTVSSLPK... | Function: Transcription activator that plays a role in the regulation of cell expansion in developing leaves . Component of a network formed by the microRNA396 (miRNA396), the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function and the transition between cell division and cell expans... |
A2XA73 | MMMMSGRPSGGAGGGRYPFTASQWQELEHQALIYKYMASGTPIPSDLILPLRRSFLLDSALATSPSLAFPPQPSLGWGCFGMGFGRKAEDPEPGRCRRTDGKKWRCSKEAYPDSKYCEKHMHRGKNRSRKPVEMSLATPPPPSSSATSAASNSSAGVAPTTTTTSSPAPSYSRPAPHDAAPYQALYGGPYAAATARTPAAAAYHAQVSPFHLHIDTTHPHPPPSYYSMDHKEYAYGHATKEVHGEHAFFSDGTEREHHHAAAGHGQWQFKQLGMEPKQSTTPLFPGAGYGHTAASPYAIDLSKEDDDEKERRQQQQQQQQ... | Function: Transcription activator that plays a regulatory role in gibberellin-induced stem elongation.
Sequence Mass (Da): 43446
Sequence Length: 396
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Subcellular Location: Nucleus
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P31421 | MESLLGFLALLLLWGAVAEGPAKKVLTLEGDLVLGGLFPVHQKGGPAEECGPVNEHRGIQRLEAMLFALDRINRDPHLLPGVRLGAHILDSCSKDTHALEQALDFVRASLSRGADGSRHICPDGSYATHSDAPTAVTGVIGGSYSDVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFFQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFELEARARNICVATSEKVGRAMSRAAFEGVVRALLQKPSARVAVLFTRSEDARELLAATQRLNASFTWVASDGWGALESVVAGSERAAEGAITIELA... | Function: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity. May mediate suppression of neurotransmission or... |
P31423 | MSGKGGWAWWWARLPLCLLLSLYAPWVPSSLGKPKGHPHMNSIRIDGDITLGGLFPVHGRGSEGKACGELKKEKGIHRLEAMLFALDRINNDPDLLPNITLGARILDTCSRDTHALEQSLTFVQALIEKDGTEVRCGSGGPPIITKPERVVGVIGASGSSVSIMVANILRLFKIPQISYASTAPDLSDNSRYDFFSRVVPSDTYQAQAMVDIVRALKWNYVSTLASEGSYGESGVEAFIQKSRENGGVCIAQSVKIPREPKTGEFDKIIKRLLETSNARGIIIFANEDDIRRVLEAARRANQTGHFFWMGSDSWGSKSAP... | Function: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity.
Location Topology: Multi-pass membrane protein
... |
O15303 | MARPRRAREPLLVALLPLAWLAQAGLARAAGSVRLAGGLTLGGLFPVHARGAAGRACGQLKKEQGVHRLEAMLYALDRVNADPELLPGVRLGARLLDTCSRDTYALEQALSFVQALIRGRGDGDEVGVRCPGGVPPLRPAPPERVVAVVGASASSVSIMVANVLRLFAIPQISYASTAPELSDSTRYDFFSRVVPPDSYQAQAMVDIVRALGWNYVSTLASEGNYGESGVEAFVQISREAGGVCIAQSIKIPREPKPGEFSKVIRRLMETPNARGIIIFANEDDIRRVLEAARQANLTGHFLWVGSDSWGAKTSPILSLE... | Function: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity (By similarity). Sign... |
Q12849 | MAGTRWVLGALLRGCGCNCSSCRRTGAACLPFYSAAGSIPSGVSGRRRLLLLLGAAAAAASQTRGLQTGPVPPGRLAGPPAVATSAAAAAAASYSALRASLLPQSLAAAAAVPTRSYSQESKTTYLEDLPPPPEYELAPSKLEEEVDDVFLIRAQGLPWSCTMEDVLNFFSDCRIRNGENGIHFLLNRDGKRRGDALIEMESEQDVQKALEKHRMYMGQRYVEVYEINNEDVDALMKSLQVKSSPVVNDGVVRLRGLPYSCNEKDIVDFFAGLNIVDITFVMDYRGRRKTGEAYVQFEEPEMANQALLKHREEIGNRYIE... | Function: Regulator of post-transcriptional mitochondrial gene expression, required for assembly of the mitochondrial ribosome and for recruitment of mRNA and lncRNA. Binds RNAs containing the 14 base G-rich element. Preferentially binds RNAs transcribed from three contiguous genes on the light strand of mtDNA, the ND6... |
Q8C5Q4 | MAGTRWVLGALLRGCGCNCSSCRRTGAACLPFYSAAGTFPSGVSGRRRLLLLLGAAAAAASQTRGLQLGPAAAGRLAGPIPARPSAAAAAAASYSALRAPLFPRSLAAAAGPARGYSQESKTTYLEDLPPLPEYELSPSKLGDEVDDVYLIRAQGLPWSCTVEDVLNFFSDCRIRNSENGIHFLLNRDGKRRGDALIEMESEQDVQKALEKHRMYMGQRYVEVYEINNEDVDALMKSLQVKPSPVLSDGVVRLRGLPYSCNEKDIVDFFAGLNIVDITFVMDYRGRRKTGEAYVQFEEPEMANQALLKHREEIGNRYIEI... | Function: Regulator of post-transcriptional mitochondrial gene expression, required for assembly of the mitochondrial ribosome and for recruitment of mRNA and lncRNA. Binds RNAs containing the 14 base G-rich element. Preferentially binds RNAs transcribed from three contiguous genes on the light strand of mtDNA, the ND6... |
P14686 | MTFISQVNKWFVNANVNSAAKLRLFCIPYAGGGASAFYEWSHFFPKEIEVCSIQLPGRENRGAEVPLTNLQQIVEIVAEEIQPLINIPFAFLGHSMGALISFELARTIRQKSNVNPVHLFVSGRHAPQIPCAKQDYHLLPDEQFIQELRSLNGTPEIVLQDAEMMSILLPRLRADFSVCGSYQYKNDEPFECPITAFGGKNDNGVTYQSLEAWREQTKREFSVCMYPGDHFFLYESKYEMIEFMCKQLRLVLAPKI | Function: Probable thioesterase involved in the biosynthesis of gramicidin S.
Sequence Mass (Da): 29224
Sequence Length: 256
Pathway: Antibiotic biosynthesis; gramicidin S biosynthesis.
EC: 3.1.2.-
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Q9RWW0 | MTLSETHPTARSEALFVRARAVTPGGVNSPVRAFRSVGGVPRFIASAQGAYLTDADGARYLDYIGSWGPMILGHNHPAVRDAVAQALASGTSFGAPNEREVELAELIVELTGAERVRFVSSGTEATMSALRLARGYTGRKFIVKFRGNYHGHADGLLVEAGSGLLTNAEGDLGAAAPSSAGVPEEYAGLTLVLDYNDPEALDALMAQRGDEIAAVIFEPVVGNAGVLIPTSDFLAALHRVRDFGAVLIADEVMTGFRLSLNGATGLLSLDPDLRCWGKIVGGGLPVGAYGGRADIMDFVSPQGPVYQAGTLSGNPLAMAA... | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 46305
Sequence Length: 444
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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Q6AQ32 | MESLKSKKLFAEAKKVIPGGVNSPVRACLSVGCDPLFIERAEGSYIYDADGQKYLDFVNSWGPMIMGHAHPDIIKAIQDAAVYGTSYGAPTSSEVDLASMVVEAVPSIEKVRFVSSGTEATMSAVRLARGYTGKNVIVKFDGCYHGHADSFLVKAGSGVLTLGIPGSPGVPEDIVKNTISIPYNSVEALETTLRDADLNIACVIVEPVAGNMGCVPPAPGFLQKLREITAEEGIVLIFDEVITGFRLSYGGAQQYYGVTPDLTCLGKIIGGGLPVGAYGGKADIMNSVAPDGPVYQAGTLSGNPLAMAAGKAALKLLQQD... | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 45562
Sequence Length: 430
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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Q6L2G9 | MKGDDLFSEALKLFPSGVNSPVRFYRPVPVMFERGRGSRIYDVNGKEYIDYSLGFGPMILGHADPDVASAIKRQADNGILFGSITENEVRLGNIIKNHVKSIEKMRFTNSGTEATMHAIRLARGYTKRKYILKMEGGFHGAHDYALIKSGSGTMTFGVPSSNGVPEEITKTVLVGKYNDENSIESLFNEYGNDIAAVITEPILGNIGVINPEPGFLEFLREITNKYNSLLIFDEVITGFRFAFSGYQDIINIKPDITTMGKIIGGGAPIGLFGSSSEIMDLISPSGNVYESGTFSGNPLSMAAGIAAMEKLQGMDYSRIN... | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 46628
Sequence Length: 420
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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Q12EF7 | MEPQNIKPHTPELSRNTALFERAKKLIPGGVNSPVRAFKAVGGTPRFVQRAQGAYFWDADDQRYIDYIGSWGPMILGHGHPAVLASVQKALLDGFSYGAPTEREVELAEELVRLVPSLEMVRLVSSGTEAAMSAIRLARGATGRSKIIKFEGCYHGHADALLVKAGSGLATFGNPTSAGVPPEVVQHTLVLEYNHLAQLEEAFALHGSAIACLMIEPIAGNMNFVRASIPFMQRCRELCTQYGALLVFDEVMTGFRVALGGAQSVYAKSIPGFKPDMTVLGKVIGGGMPLAAFGGTRAVMEQLAPLGPVYQAGTLSGNPV... | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 46774
Sequence Length: 442
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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B4S3Q6 | MPQLTRSAELFEKAKQFIPGGVNSPVRAFKSVGGTPIYMAKGQGAYMTDVDGNTYLDYVGSWGPFILGSMHPRITAALEHTLTKIGTSFGTPIEMEIEIAELLCQIVPSIEMVRMVNSGTEATMSAVRLARGYTSRDKIIKFEGCYHGHGDSFLIKAGSGALTLGAPDSPGVTKGTANDTLNAKYNDIESVRLLVNENKGNIAAIIIEPVAGNTGVIPAKPGFLQALRDLCTEEGIVLIFDEVMCGFRVALGGAQERYGVTPDLTTMGKIIGGGLPVGAFGGKREIMERIAPLGDVYQAGTLSGNPLALTAGLETLKILR... | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 46492
Sequence Length: 431
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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Q06774 | MSVSDELFAEALKVMPGGVSSPVRAYRSVGGTPRFVKRALGSHIVDVDDKRYVDLVCSWGPMIAGHAHPEVVAAVLQAVADSTSFGAPSEVELRLAQAVVARMGGAIDKVRFTCSGTEAVMTAARLARGITKRPLLVKFVGCYHGHSDSFLVSAGSGVASLGLPDSPGVPKEVAGDTVALPYGRIDMVEELFAERGDQVAAIVTEGVPANMGVIVPPEGFNRRLHDIAHAHGALLIQDEVLTGFRLSPTGAWGLQGAKEGWTPDLFTFGKVIGGGMPLAAVGGSAQLMDYLAPEGPVYQAGTLSGNPAACAAGLATLALM... | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 45932
Sequence Length: 441
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
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Q8D3C8 | MIKNSITNKLYVEAKKIIPGGVNSPARSFYFVKEIPVIAKRSKGPYIFDVDNNKYIDYICSWGASILGHNNYYITSKIIEYSKKGLNFGLLTEIEIKIARLISKYIPSIEMIRMVNSGTEATMSAIRLARSYTKKNKIIKFDGCYHGHADFLLANSNLDPYDLFSSNPISSGIPKNILKDTLICPYNDYESIEKIFDLYPNKIACIIVEPIAGNMGCVLPEKNFLYKLRMLCNKFNSLLIMDEIITGFRISLGGAQSYYNIYPDITCLGKIIGGGLPIGAFGGKKRIMNHVSPSGSVYQAGTFSGNPISMISGYACLKLL... | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 48949
Sequence Length: 435
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
|
B2SKS0 | MNHSRSHALFAQAQTVLPGGVNSPVRAFKSVGGEPFFVARADGSYLFDVDGNRYIDYVGSWGPMIAGHNHPAVREAVERAIRDGLSFGAPCAAEVTMAETITGLVPSCEMVRMVNSGTEATLSAVRLARGATGRNRIIKFEGCYHGHGDSFLVKAGSGMLTLGVPTSPGVPAGLSELTATLSFNDFEGATALFDEIGPEVAAVIIEPVVGNANCIPPQAGYLQHLRTLCTRHGALLIFDEVMTGFRVALGGAQAHYGVTPDLSTFGKIIGGGMPVGAYGGRRDLMEQIAPAGPIYQAGTLSGNPVAMAAGLAMLELVQEP... | Catalytic Activity: (S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Sequence Mass (Da): 44904
Sequence Length: 429
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
Subcellular Location: Cytoplasm
EC: 5.4.3.8
|
Q09768 | MGLLVLGTPLDWPESKKYCDYVRENGIMQFLHMYDTYISKKQDVLLWGDEIECIVVSMDDKSKKARVSLRQEDILNALGKYEETFRHVDFGPVYAALRNETCPKKIDAILSEVAKNPADYVERIGGNSNKDTIEITSSTKPHAQNAVPTFHPEYGRYMLESTPGAPYGSTLKDFTFVEYNMRLRRKIIENHLLPNELPLTITNFFRLGTPGFTDPEVEANGAISRSFFLPDDVINTHVRFPTLTANIRQRRGRKVAMNVPIFFDKNTIKPFHDPTVPWDRNLFPEDANARDGAALDNHIYMDSMGFGMGCCCLQITFQAK... | Function: Catalyzes the ATP-dependent ligation of L-glutamate and L-cysteine and participates in the first and rate-limiting step in glutathione biosynthesis.
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 76523
Sequence Length: 669
Pathway:... |
Q8EBF9 | MKPFNELVQHFSDAQGRAALLGMLRGIEREALRIDESGYLALDGHPLELGSALTHSRITTDYSEALLEFITPVNHQVESLLQGLTETHAYSVRHLHGQRLWPVSMPCYVKDEANIPIARYGTSNTGKMKTLYRKGLTYRYGALMQIISGVHFNFSVSQELWQSLYELSDKSLSFDDFISESYFGLIRNYRRLVWVLPYLFGASPALCNSFIKGQKTDLRFEKSGRGTLYLPYATSLRMSDLGYTNKEQADLNISYNSLPEYLAGIRAAIKMPSANFANIGVKVDGEYRQLNANVLQIENEFYSPIRAKRVTKSGEKPSEA... | Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 58378
Sequence Length: 523
Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
|
O22493 | MALMSQAGSSHCIYSEKVRCISGHRSIINNMDMFRMREICFGVDISSRNASRRVQGNYLNHIGVGSRRGDLTIVAASPPTEDAVVAAEPLTKEDLVGYLASGCKSKEKWRIGTEHEKFGFEFGTLRPMKYDQIADLLNGIAERFDWEKVMEGDKIIGLKQGKQSISLEPGGQFELSGAPLETLHQTCAEVNSHLYQVKAVAEEMGIGFLGTGFQPKWGLKDIPIMPKGRYEIIRNYMPKVGSLGLDMMFRTCTVQVNLDFSSEADMIRKFRAGLALQPIATALFANSPFTEGKPNGYLSKRSHIWTDTDNNRAGMLPFVF... | PTM: The Cys-187-Cys-407 disulfide bridge is known to modulate the enzyme activity according to the redox status. The oxidized form constitutes the active enzyme (By similarity).
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 59057
Sequence ... |
Q1W2L8 | MALMSQAGSSHCIYSEKMKCISGHSSITSNMEMLKMKDICFGNISSRNSSKPMQGIYLDRVGVERRRGRLAIVAASPPTEDAVVAAEPLTKEDLVAYLASGCKSKEKWRIGTEHEKFGFEFGTLRPMKYEQIAELLNGIAERFDWEKVMEGDNIIGLKQGKQSISLEPGGQFELSGAPLETLHQTCAEVNSHLYQVKAVAEEMGIGFLGTGFQPKWGLKDIPVMPKGRYEIMRNYMPKVGSLGLDMMFRTCTVQVNLDFSSEADMIRKFRAGLALQPIATALFANSPFTEGKPNGYLSMRSHIWTDTDNNRAGMLPFVFD... | PTM: The Cys-186-Cys-406 disulfide bridge is known to modulate the enzyme activity according to the redox status. The oxidized form constitutes the active enzyme (By similarity).
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Mass (Da): 58962
Sequence ... |
P41921 | MLSATKQTFRSLQIRTMSTNTKHYDYLVIGGGSGGVASARRAASYGAKTLLVEAKALGGTCVNVGCVPKKVMWYASDLATRVSHANEYGLYQNLPLDKEHLTFNWPEFKQKRDAYVHRLNGIYQKNLEKEKVDVVFGWARFNKDGNVEVQKRDNTTEVYSANHILVATGGKAIFPENIPGFELGTDSDGFFRLEEQPKKVVVVGAGYIGIELAGVFHGLGSETHLVIRGETVLRKFDECIQNTITDHYVKEGINVHKLSKIVKVEKNVETDKLKIHMNDSKSIDDVDELIWTIGRKSHLGMGSENVGIKLNSHDQIIADE... | Cofactor: Binds 1 FAD per subunit.
Function: Maintains high levels of reduced glutathione in the cytosol.
Catalytic Activity: 2 glutathione + NADP(+) = glutathione disulfide + H(+) + NADPH
Sequence Mass (Da): 53441
Sequence Length: 483
Subcellular Location: Cytoplasm
EC: 1.8.1.7
|
P75796 | MPHSDELDAGNVLAVENLNIAFMQDQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLQRRSREVIELSEQNAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQNASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGTVEQIFHAPQHPYTRALLAAVPQLGAMKGLDYPRRFPLISLEHPAKQAPPIEQKTVVDGEPVLRVRNLV... | Function: Part of the ABC transporter complex GsiABCD involved in glutathione import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + glutathione(out) + H2O = ADP + glutathione(in) + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 69114
Sequence Len... |
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