ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P53241 | MTISNKSWRSYFPHLRKLPEDDQYLYSDDTNSSIIAEEELHHSVDKSSKTDVTAETTAVEPHPHNLRHDLPYEVRDEAGRKWWKYFDEFEYRVNKEYKKSRKWYEFLYPNHTTQTKAERRLLYKLDIIIALYFFMLCWSKSVDLNNYTNAYVSNMKEDLNMKGNDYVYTSTIANVGAIVFQLPFMYLLPRFPSHIILPVMDLGWTWFTFACYRANSLAELRAYRFILSAFGAAYYPVSQYILGCWYAPDEINSRVCLFFCGQQLGSVTSGLLQSRIFKSLNGVHGLAGWRWMFLIDAIAISLPTAIIGFFVIPGVPSKCY... | Function: Involved in uptake of biotin with the concomitant entry of protons.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69083
Sequence Length: 593
Subcellular Location: Cell membrane
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Q56632 | MKDMSLVNSKVLLVGSARGIGFSVLEHLLQAGAQVMAADCEWQLLLEQSESLLGRYPDQLTLKKLDLAEPEAVREQVNQWAEQVAGFDHLVCCAGILHVAPLHEMPMEQVSSIFTVNAFGVLACMQGVASSMKARQQGSMVIIGSNAANTPRMSIGAYGASKAALHMLVKCIGMELAPYGIRCNLVSPGSTRTAMQQQLWTEQYGEAQVIAGDAAQFRLGIPLNKIAEPADIAQAVLFLLSDNAGHITLHDLRVDGGATLDH | Function: Involved in an early step of the biosynthesis of the catechol siderophore vibriobactin. Vibriobactin is a chelating compound involved in transporting iron from the bacterial environment into the cell cytoplasm.
Catalytic Activity: (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + NAD(+) = 2,3-dihydroxybenzoate + H(... |
O07898 | MVMKREVVGYTTMSEHLIDTQLTRSPFFFASANQSMLGCGVAHAFQQAIPFAELANQAKQLLQQAKRDECDNPLLFGIVPFDPKTPTRFMIPRTLYVSSSPRLNRPAHLTRQVAKLISSPSGEQYKQGVSHLLNMFHHSGLSKVVLSRAIEIATEQEIALPTLLRSLLAINHHGYTFAASLDEQRKLIGASPELLVAKRGNYLISNPLAGSRPRSQDAQENAQRRASLLNTAKDLHEHGLVVEEVERIMSRYCRNLYTPMVPSVIETETMLHLSTLLEGQVSDPEVCALQVAADLHPTPAVCGFPRESAYQAIRELEEFD... | Catalytic Activity: chorismate = isochorismate
Sequence Mass (Da): 43594
Sequence Length: 395
Pathway: Siderophore biosynthesis; vibriobactin biosynthesis.
EC: 5.4.4.2
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W7DQ33 | MVRITALMSGSILLFALQALAMPVETTSVEPAAEKRGLKLAFKRGEEVEPAEEKRGLKLAFKRGEEVEPAEEKRGLKLAFKRGEEVEPAEEKRGLKLAFKRGEEVEPAEEKRGLKLAFKRGEEVEPAEEKRGLKLAFKRGEEVEPAEEKRGLKLAF | Function: Ribosomally synthesized cyclic peptide victorin precursor, part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats . The vicA1 translated product contains a 7-fold repeated peptide embedding the hexapeptide Gly-Leu-Lys-Leu-A... |
A2SY66 | ISPSLLYLFSLATLLAVVTGTGTPSQEVHPSHYATTFNKSLFPKDFLFGIGSSAYQVEGASNIDGRGPSIWDTFTKQHPEKIWDHSSGNIGADFYHRYKSDIKIVKEIGLDSYRFSISWSRIFPKGKGEVNPLGVKFYNNVINEILANGLIPFVTLFHWDLPQSLEDEYKGFLSSKVVKDFENYADFVFKTYGDRVKHWVTLNEPFSYALYGYNGGTFAPGRCSKYAGNCEYGDSSTEPYIVAHNLILSHAAAAKLYKTKYQAHQKGNIGATLVTHYFEPHSNSAADRVAASRALDFFFGWFAHPLTYGHYPQSMISSLG... | Function: Hydrolyzes the disaccharide glycosides vicianin, pNP beta-primeveroside, 2-phenylethyl beta-primeveroside and furcatin.
Catalytic Activity: (R)-vicianin + H2O = mandelonitrile + vicianose
Sequence Mass (Da): 57620
Sequence Length: 509
EC: 3.2.1.119
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W7E8S5 | MKLFLLFTLTLVNIFSVSLQEPIQNQPAGNNTITSPHRNVWRALSEAEFSGVSAVLVHQLNLTTSRGGNRIIQIDYLYPNKSDVLLFLDHNGEEPKRYARATVQFGSPEVPYLQEYRIGPLPATNTTAVEPLRFPFNGKVQGKTKITSLDADGIDAFLPQLSSVVEDITRKLWNTTLAEGGVSFNLGKASFNSDSTQTIWLGFLNNATTGFDSSTLLPLGVSMQLDITSRDYNDWFVLYWFYNNKLYTPTSFNETVYSSDFQPPLANIDGPWTSTNKQEPTFLLDDLPPPKAISRGKNRYNLDTEENYVQWMDFSFYFSS... | Cofactor: Binds 1 copper ion per subunit.
Function: Copper amine oxidase, part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats . Within the pathway, vicK1 catalyzes the oxidative deamination of the N-terminal glycyl moiety of the h... |
W7E3A0 | MLRYLLIPILYLQVVLGVLSEVLPSLKPSVVPKNTSLLSGRGVFRQLIDHTHPEVGTFSQKYWFNTTYWGGPGSPIIFYTPGQHPATNRLYYLTDTTLPGLIAKEVRGAVVLVEHRYFGESQPFDNLSTSNLQYLALDQVLADFVHFARTVELPFDLSGNSHPLRTPWIWVGNSYSATLVAWTERLFPNTFWAYYASGAAVNSMQDFWQFNYPTQQGMPQSCRSNLEAIISHVDNVFLSGSPEQKQELKIRFGLQDLSLLEDTAYALSQPIIGWTLIQPSDTHTQFSEMCNAIENANFSSSRRDFGSKTNFQTVLDNYAD... | Function: Serine protease, part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats . Within the pathway, vicPa and vicPb are probably involved in the processing of the vicA1 and vicA2 precursors (Probable). The pathway starts with the... |
W7DWT4 | MEKPTRQTPFYTQHRAELLVLSSQIAAALLHALARVVEVGSGLKERVHPFTVLQIRLFITVLGCTAYLWRARIDFLGPTGLRPLLALRAAGGVFGACGFYLSISYLSLSEATVLNFIAPLGAIMLTTYWEGRTFAFLDLIACITALAGVVLVLQPIPIYKAVAQAEISSSISTDPYAHLKGVVSGITGVAGGIVAFSAMNRLGKNVQPAVTINYFGVSICIVTTAFSTIMPEVVWPTRIESWCLLAIIGILGLVMEYLLTAGLGSDDPRVTIMIYSQVLWALFLDWAIWRSHVNVLTVLGSMVVVASLAVPYLFRESSHP... | Function: Probable transporter; part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37974
Sequence Length: 349
Subcellular Location: Membrane
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P08670 | MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYR... | Function: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.
PTM: Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as... |
Q9MZA9 | MSTRSVSSSSYRRMFGGPGTASRPSSTRSYVTTSTRTYSLGSALRPTTSRTLYTSSPGGVYATRSSAVRLRSGVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGHLYEEEM | Function: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.
PTM: One of the most prominent phosphoproteins in various cells of mesenchymal origi... |
A0A0D1E6R6 | MRGILVALTAALIFCSLTPAQPVLHIQETNRAKNRANRKLVARQPEYKAVETLEKNVNIAIAVGTALVTLVSAGVGGMLLSDHLACKSVAKQEEIMQKSWDSMHPDGFTPAGDQMRPVSFDCSTQERGLKPLQSYTNGAEMY | Function: During infection, may play a role in establishing and maintaining biotrophy; the formation of a tight interaction zone between the host and the pathogen.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 15458
Sequence Length: 142
Subcellular Location: Membrane
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A0A0D1CVX2 | MAAGKRRVASLVLLMIIWWSIVSAAESQCEERNDYSRKRPSHKPFTSHQNKQDRSCSSPLPSESCSTSAITPSDSAVRDTSLSRRGLPGMPGDIEWMGFYGSLLAVPTMLSILGIITNYNLGKSYYNSELNAQYYKQSREMLRAHTAKLIQDQEKKFANAGVSWNGMVYGKDGQVNPGAKLPEWNGRVLGGTVANPKSQPVPGSGGAVQGAAAGVGGGTTAGVAAGAGAASAGTGPAQVGGATAGGAGAEAQTGTGAIATGTGTGGAGDAGGSAPVSSGAEQGDAEAGDEARGSEERGDDGTEDRRGGQSEGDDDSDSDG... | Function: During infection, may play a role in establishing and maintaining biotrophy; the formation of a tight interaction zone between the host and the pathogen.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 33723
Sequence Length: 335
Subcellular Location: Membrane
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Q17162 | MPVFHTKTIEGILEPVAQQVSRLVILHEEAEDGNAVLDLTLPVGAVSRAVDNLIKVGYDTCHSSDDRILQADMPPALQRVEASSRLLEDACHMLRADPYSSVARKKLIEGARGILQGTSALLLSFDESEVRKIIRGCRKVLDYLAVAEVIESMDDLAQFVKDISPWLTRVSRNIDAREKELTHQVHREILLRCMDTVKTLSPIMICAMKIFIQITEESQRGQQEAAENRNYLAQRMTDEMNEIIRVLQLTTYDEDEWDSDNVTVMRKALSAAQSLLTSALDWLADSRGRAGATGEKAIRRIVDYSERIAARALPEDARLI... | Function: Involved in cell adhesion. May be involved in the attachment of the actin-based microfilaments to the plasma membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 110188
Sequence Length: 993
Subcellular Location: Cytoplasm
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O46037 | MPVFHTKTIESILDPVAQQVSRLVILHEEAEDGNAMPDLSRPVQVVSAAVANLVKVGRDTINSSDDKILRQDMPSALHRVEGASQLLEEASDMLRSDPYSGPARKKLIEGSRGILQGTSSLLLCFDESEVRKIIQECKRVLDYLAVAEVINTMEQLVQFLKDLSPCLSKVHREVGAREKELTHQVHSEILVRCLEQVKTLAPILICSMKVYIHIVEQQGRGAEEAAENRNYLAARMSDELQEIIRVLQLTTYDEDTSELDNLTVLKKLSNAISNKMEQANEWLSNPYALRGGVGEKALRQVIDNATEISERCLPQDSYPI... | Function: Involved in cell adhesion. May be involved in the attachment of the actin-based microfilaments to the plasma membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 106302
Sequence Length: 961
Subcellular Location: Cytoplasm
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Q38008 | MLYNIMLEVAKGDYITILFALILFDFITGFLKAWKWKVTDSWTGLKGVIKHTLTFIFYYFVAVFLTYIHAMAVGQILLVIINLYYALSIMENLAVMGVFIPKFMTARVQEELQKYTAQLDAGKDLLEEFKGEKK | Function: Produces a lesion in the cytoplasmic membrane allowing the phage lysosyme to attack the peptidoglycan.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15510
Sequence Length: 134
Subcellular Location: Host membrane
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Q9ZXD8 | MWMNFESLQIARAYLFGEVKYLDLMLVLNIIDIITGVIKAWKFKELRSRSAWFGYVRKMLSFLVVIVANAIDTIMDLNGVLTFATVLFYIANEGLSITENLAQIGVKIPAVITDRLHVIESDNDQKTEKDDQAAG | Function: Produces a lesion in the cytoplasmic membrane allowing the phage lysosyme to attack the peptidoglycan.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15274
Sequence Length: 135
Subcellular Location: Host membrane
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P85420 | TPEQQRYVDLFIVVDHGMFMKYNGNSDKIRRRIHQMVNIMKEAYSTMYIDILLTGVEIWSNKDLINVQPAAPQTLDSFGEWRKTDLLNRKSHDNAQLLTSTDFNGPTIGLAYVGSMCDPKRSTGVIQDHSEQDLMVAITMAHELGHNLGISHDTGSCSCGGYSCIMSPVLSHEPSKYFSDCSYIQCWDFIMKENPQCILNKR | Cofactor: Binds 1 zinc ion per subunit.
Function: Snake venom zinc metalloproteinase that acts on fibrinogen, fibrin, fibronectin (FN1), type I collagen, type IV collagen, integrin alpha-7/beta-1 (ITGA7/ITGB1) and integrin alpha-1/beta-1 (ITGA1/ITGB1). Binds to fibronectin (FN1), fibrinogen and, weakly, to type I colla... |
C0HJU2 | YIELAVVADHGMFTKYNSNVNTIRTWVHEMVNSLNGFFRSMXVDDASLVNLEVWSKTLTSFGEWRDLLPRISHDHAQLLTTIVFDQQTIGIAYTAGMCDPSQSVAVVMDHVAVTMAHELGHNLGMDHDDTCTCGAKSCIMASTISKGLSFEFSDCSQNQYQTYVTKHNPQCILNK | Cofactor: Binds 1 zinc ion per subunit.
Function: Non-hemorrhagic snake venom zinc metalloprotease that hydrolyzes the Aalpha-chain of fibrinogen, more slowly the Bbeta-chain and shows no effect on the gamma chain. Has no coagulant activity on bovine plasma and fibrinogen.
Sequence Mass (Da): 19538
Sequence Length: 175... |
P60244 | PAPQTSIELFLIVDHSMYAKYNSNSSKITTTLKARVNIMNAIYSSLNLVITLSGIEMWSAADLITVQSSSRNTLKLFASWRETDLLKRTSNDNAQLLTATNFNGNTVGLAYLKTMCNSKYSVGLIQDHSAIPLLMAVTMAHELGHNLGMNHDGAGCSCATCIMAPVLSSGPAKSFSDCSKHDYQSFLTIHKPQCLLN | Cofactor: Binds 1 zinc ion per subunit.
Function: This protein is an alkaline zinc metalloprotease from snake venom that possesses weak hemorrhagic activity.
Sequence Mass (Da): 21437
Sequence Length: 197
Subcellular Location: Secreted
EC: 3.4.24.-
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P0C6R9 | IISPPVCGNELLEVGEECDCGTPENCQNXCCDAATCKLKSGSQCGHXDCCEQCKFTKSGTECRASMSECDPAEHCTGQSXXCXXDVFHKNGQPCLDNYGYCYNGNCPIMYHAQCYALFGADVYEAEDSCFKDNQKGNYYGYCRKENXXXXXCXXXDVKCGRLYCKDNSPKQNNPCKMFYSNDDEHKGNVLPGTKCE | Cofactor: Binds 1 zinc ion per subunit.
Function: hemorrhagic protease that acts as a potent inhibitor of collagen-induced adhesion by blockage of alpha-2/beta-1 (ITGA2/ITGB1) integrin. Cleaves at Leu-|-Met bonds .
PTM: The N-terminus of alternagin is blocked.
Sequence Mass (Da): 21731
Sequence Length: 196
Subcellular ... |
P0DM46 | TVTPEQDRYLQVKKY | Cofactor: Binds 1 zinc ion per subunit.
Function: Snake venom metalloproteinase that impairs hemostasis in the envenomed animal.
PTM: Contains 16 disulfide bonds.
Sequence Mass (Da): 1868
Sequence Length: 15
Subcellular Location: Secreted
EC: 3.4.24.-
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P0DJE2 | KSAAXVTLDLFGDWRAKRHDNAQLLTGINLNGQTLGIAFMSKXSVGLIQDYXKSYLLVASVMAHELGHNLGMEHDDGNCICPAKCIDNKPLRTDIVSPAVCGNYFVELTPGSQCADGVCCDQCRKAGVTVAPDLCFDYNQLGTEDKFTHSPDDPDYGMVDLGTKCADGKVCNSNRQCVDVNTAY | Cofactor: Binds 1 zinc ion per subunit.
Function: Snake venom zinc metalloprotease that has fibrinogenolytic and hemorrhagic activities in mouse and rats. Hydrolyzes the Aalpha-chain (FGA) and more slowly the Bbeta-chain of fibrinogen (FGB), without affecting the gamma-chain. Its hemorrhagic activity results of its inv... |
Q0NZY0 | DIVSPPVCGNYFVEVGEECDCGRPGKCQNPCCNATTCKLTPGSQCADGLCCDQCRFKGAGTECRAARSECDIAESCTGQSPECPTDDFQRNGQPCLNNQGYCYNGNCPILDHQCHNLFGAGATVAPDACFNFNRRGQGIYYCRKQNGVTIPCARKDIKCGRLFCVQ | Cofactor: Binds 1 zinc ion per subunit.
Function: The hemorrhagic metalloproteinase-disintegrin-like bothrojarin-1 is a potent inhibitor of collagen-induced platelet aggregation by blockage of alpha-2/beta-1 (ITGA2/ITGB1) integrin. It does not present any fibrinogen-clotting activity (By similarity).
Sequence Mass (Da)... |
Q0NZX7 | IVSPPVCGNYFVEVGEECDCGLPRNCQNQCCNATTCKLIPGAQCEDGECCERCQFKGAGNVCRPRRSKCDIAESCTGQSPDCPTDRFRRNGVSCLNN | Cofactor: Binds 1 zinc ion per subunit.
Function: The hemorrhagic metalloproteinase-disintegrin-like bothrojarin-1 is a potent inhibitor of collagen-induced platelet aggregation by blockage of alpha-2/beta-1 (ITGA2/ITGB1) integrin. It does not present any fibrinogen-clotting activity (By similarity).
Sequence Mass (Da)... |
P84035 | SHDNAQLLTAIKAYIATMCDPKMAVIMAHEIGHGGYYGYCRKIPCAPEDVKDDDIGMVLPGTK | Cofactor: Binds 1 zinc ion per subunit.
Function: Snake venom zinc metalloproteinase that catalyzes the conversion of prothrombin (F2) to alpha-thrombin through formation of a thrombin intermediate, without requiring additional cofactors. Also inhibits collagen-dependent platelet aggregation in vitro, an effect that do... |
P0C7B1 | SISACNGLKGHFLIEPLKLSDSEKTDLLNRSHDNAQLSPINLVVAVIMAHEMGHGMVLPGTK | Cofactor: Binds 1 zinc ion per subunit.
Function: Snake venom Zinc metalloproteinase that inhibits ADP-induced platelet aggregation and inhibits the alpha-5/beta-1 (ITGA5/ITGB1) integrin, a fibronectin receptor. Has caseinolytic activity. Induces the detachment of cells that are bound to fibronectin.
PTM: The N-terminu... |
O93523 | MIEVLLVTICLAAFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSKDYSETHYSPDGREITTYPAVEDHCYYHGRIENDADSTASISACNGLKGHFKLQRETYFIEPLKLSNSEAHAVFKYENVEKEDEAPKMCGVTQNWKSYEPIKKASQLVVTAEQQKYNPFRYVELFIVVDQGMVTKNNGDLDKIKARMYELANIVNEILRYLYMHAALVGLEIWSNGDKITVKPDVDYTLNSFAEWRKTDLLTRKKHDNAQLLTAIDFNGPTIGYAYIGSMCHPKRSVAIVED... | Cofactor: Binds 1 zinc ion per subunit.
Function: Has caseinolytic activity. Causes hemorrhage on rabbit skin and causes myonecrosis in mouse tibialis anterior muscle.
Catalytic Activity: Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 in insulin B chain.
Sequence Mass (... |
P22028 | IISPPVCGNELLEEGEECDCGTPEN | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloproteinase that binds to von Willebrand factor (VWF) and induces its interaction with GPIb (GP1BA), resulting in platelet aggregation.
Sequence Mass (Da): 2648
Sequence Length: 25
Subcellular Location: Secreted
EC: 3.4.24.-
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Q9PRP9 | SRKQKFDKKFIKLVIVVDHSMVXKXNNDLIAI | Cofactor: Binds 1 zinc ion per subunit.
Function: Calcium-dependent prothrombin (F2) activator. This protein may activate prothrombin via recognition by the regulatory subunit of the calcium ion bound conformation of its gamma-carboxyglutamic acid (GLA) domain, and the subsequent conversion of prothrombin to active thr... |
P0C7N3 | AMVTKNNGDLDKSGTECRLYCKDNSPGQNNSCKMFYSNEDEHKGMVLPGTK | Cofactor: Binds 1 zinc ion per subunit.
Function: Snake venom zinc metalloproteinase-disintegrin-like that blocks the interaction between platelets and collagen fibers through its binding to collagen fibers, resulting in the blockade of collagen-mediated platelet functions such as adhesion, release reaction, thromboxan... |
P86536 | VATSEQFNKTFIELVIVVD | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalytic subunit of coagulation factor X-activating enzyme, a zinc-protease enzyme that acts in hemostasis. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond at position 234 and is also able to activate coagulation factor IX (F9) and protein C (PROC) by... |
Q7LZ61 | MMQVLLVTISLAVFPYQGSSIILESGNVNDYEVVYPQKVTALPKGAVQQPEQKYEDTMQYEFEVNGEPVVLHLEKNKILFSEDYSETHYYPDGREITTNPPVEDHCYYHGRIQNDAHSSASISACNGLKGHFKLRGEMYFIEPLKLSNSEAHAVYKYENIEKEDEIPKMCGVTQTNWESDKPIKKASQLVSTSAQFNKIFIELVIIVDHSMAKKCNSTATNTKIYEIVNSANEIFNPLNIHVTLIGVEFWCDRDLINVTSSADETLNSFGEWRASDLMTRKSHDNALLFTDMRFDLNTLGITFLAGMCQAYRSVEIVQEQ... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds.
PTM: N-g... |
B5AJT4 | QYSESQESGHNRNAPDKELTTEEFQLIFHQSQTVDIEYDFINITTEMIETERKVSFTIDGKEYHLSLTPAASQSVLPYGTKIKSAIWWTDNDTHIHEEDYSDERWDSRAIYENLEIMATILVRTENGTSYYDGVFGEGIAMKVVRSLPGRLMNIYGANYHFVYDSNGSVYDVVLNGQDEPAVPADMAVNNFYPKLLVLVDYSLFKIFNENFEETVKYLTIFWNAVNLRFRPVQHPKVNIIITGIVIAKNEAAFQHVYRARYSKNSKLVHTGRVIDNGRYFFGTNFDPYYDNYDASFTMASMDDPTGKGGATVIGGICSSS... | Cofactor: Binds 1 zinc ion per subunit.
Function: The recombinant protein has gelatinase activity. In vivo, injection of this recombinant into fifth instar L.oleracea (host) larvae results in partial insect mortality associated with the molt to sixth instar, with surviving insects showing retarded development and growt... |
Q9XWU8 | MAKKQKKSTEKSERTVEFKEPPKPANSEERLKPAGRGMKPSPSQNTLNRMERETIVFWRRPHIVIPYALMEIAHLAVELFFKILAHKTVLLLTAISIGLAVYGYHAPGAHQEHVQTIEKHILWWSWWVLLGVLSSIGLGSGLHTFLIYLGPHIAAVTMAAYECQSLDFPQPPYPESIQCPSTKSSIAVTFWQIVAKVRVESLLWGAGTALGELPPYFMARAARISGQEPDDEEYREFLELMNADKESDADQKLSIVERAKSWVEHNIHRLGFPGILLFASIPNPLFDLAGITCGHFLVPFWSFFGATLIGKALVKMHVQM... | Function: Involved in autophagy . Thought to act in autophagasome and omegasome formation .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51868
Sequence Length: 458
Subcellular Location: Membrane
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Q54NL4 | MGKSNTIVLSNEKDIQLRIQQLEERKEKRKNVKLLFSPIKTTKYFLYILKDTLVSGIRYFQTRPFLLFFIALFASLTFIAVYVPGEHQKYMGKYSDLISDCIWWVGLGVLSSIGLGTGLHTFVLYLGPHIAKVTLAATEWNSVNFNVYGANSFIQPATAMIGGVSFWMILQKVQWAALFWGAGTAIGELPPYFVARTARLKGLKLEQEKKLKEQQEKPIDEKDQPKKGLLERLSEKVPALIGNLGFFGILAFASIPNPLFDLAGITCGHFLVPFWKFFGATFIGKAVVKAHIQACFVILAFNMETLTMVISFIEDKIPFL... | Function: Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes (By similarity). Required for autophagosome formation: participates in early stages of autophagosome biogenesis at the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets of the ER as lipids are extracted (By... |
Q96GC9 | MAENGKNCDQRRVAMNKEHHNGNFTDPSSVNEKKRREREERQNIVLWRQPLITLQYFSLEILVILKEWTSKLWHRQSIVVSFLLLLAVLIATYYVEGVHQQYVQRIEKQFLLYAYWIGLGILSSVGLGTGLHTFLLYLGPHIASVTLAAYECNSVNFPEPPYPDQIICPDEEGTEGTISLWSIISKVRIEACMWGIGTAIGELPPYFMARAARLSGAEPDDEEYQEFEEMLEHAESAQDFASRAKLAVQKLVQKVGFFGILACASIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAIIKMHIQKIFVIITFSKHIVEQM... | Function: Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes . Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine . Required for autophagosome formation: participates in early stages of autophagos... |
Q91ZQ0 | MAENGTNCDQRRGAMSKEQHNGSFTDPSSVNEKKRRDREERQNIVLWRQPLITLQYFSLETLVVLKEWTSKLWHRQSMVVSFFLLLAALVATYYVEGAHQQYVQRIEKQFLLYAYWIGLGILSSVGLGTGLHTFLLYLGPHIASVTLAAYECNSVNFPEPPYPDQIICPDEEGTEGAISLWSIISKVRIEACMWGIGTAIGELPPYFMARAARLSGAEPDDEEYQEFEEMLEHAETAQDFASRAKLAVQKLVQKVGFFGILACASIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAIIKMHIQKIFVIVTFSKHIVEQM... | Function: Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes (By similarity). Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine (By similarity). Required for autophagosome formation: participates... |
Q68EQ9 | MAENGTDCEQRRVGMAKEQNNGSFQDPSFLSDRKSRDREERQSIVLWRKPLITLQYFILEVLITLKDWSIRLWHRRMMVVSVLLLLAVLSVVYYIEGTHQQYVQYVEKKCLWCAYWVGLGILSSVGLGTGLHTFLLYLGPHIASVTIAAYECNSVNFPEPPYPDEIICPDEEGTEGAISLWTIISKVRLEACMWGAGTAIGELPPYFMARAARLSGVETDDEEYAEFEEMLEHAQTAQDFATRAKLAVQNLVQKVGFLGILACASIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAIIKMHIQKLFVIITFSKHIVEQM... | Function: Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes. Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine. Required for autophagosome formation: participates in early stages of autophagosom... |
U6BLN5 | MFVHLLVLLFAAVEAIPTGRFEVVYPSMVTFRSGIKRIRFRALDEDIELRLEPAGDVIADDFTVINGENGEVDHSVNIQSLKRKLYKDAKVGAALHIDEDGSLIINGIVNSKLRIEPDTSKKASRNGIIAHRVIEVIEDEQLFHDVIILPPGLTRTFNYSEPLPDDKCVKIEYVFVTESSFTKSFQISSMETYLANMMNMVKIMFDSLDLGIEVAIIGIIKLTKENEAKLAPYIPLCSREMDSRETLDDMAEFYCNSADKLIQNADIVTLITTRPLGTFDENGYFFNIHLGIAFLDNICVYCYKYAIVKEDTGIYQLANT... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
PTM: Contains several disulfide bonds.
Sequence Mass (Da): 44399
Sequence Length: 393
Subcellular Location: Secreted
EC: 3.4.24.-
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P86392 | MISYLASIFLLATVSAVPSGRVEVVFPSVETSRSGVKTVKFTALDQDVELKLRSAGEILGKRFAIQDVDVESLRRKIYRDSVNGAALLIDEDGPLTIEGIVNSKLRIQPFESGRITKDGIIAHQIVEVIDDKKSYDRVAVIPENVKRNAENVSRMARDDDCIVVEYYIVTDSAFTKRFKSNSALTNYVTVMFTGVQNLMDTLELGIGVRLLGVTTFTEKTEPSFIKDNLIPGPPAAFDPDVLISAMSKYYCNHQTGLAKDTDLIFLITARGMGDPREDGTVDINTAGIANSAGVCKPCFKSGIATDDSDYNERVDTLAHE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a metalloprotease. Penetrates intact tissue and specifically cleaves the vesicle-associated membrane protein 2 (VAMP2) (part of the SNARE complex) involved in pancreatic secretion, thus disrupting the normal vesicular traffic.
PTM: Contains 4 disulfide bonds.
Se... |
Q86K84 | MKLNISELKCQQHDKLVTIYCCACDAYFCKKCDKEKHSQDDNQEDSLHIRGLVNKDVIIGRDEEDDDDEDDEYDNKIQDILKKSNNLKKSNSIGGNIVENIELKSPMKTDSPYFIRDKNSIQSDIDSKITEKIDLDNLIHEEDDPFTIGINSNNSNSNNLIDVNDLHTPSTPSPLPSPSLSRSSSTNIKPQQQTSPSPSRSSESNSTTNNNNNKNEKKKLKNSSNSELNRKKIYKKEKIIGDSDEEEHILNNGNKNKNNKSKSVYDYDDDDDNDDDNNNNNNNNNNNNNNNNNENDDNSNSKSEGGVFYSSSSETEKEIE... | Function: Mediates the transfer of lipids between membranes at organelle contact sites.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71928
Sequence Length: 653
Subcellular Location: Membrane
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Q9VAG4 | MDLQLDSESYWNRSSRAAFSFDDEDEVDLAPDLVSNGILADDTISEASFNNSVALNLSIKSILSEEALKLVLQEQALDDRVLPKGVSPEEELKLLRRQLQSTLYSPNLEATAQKLLQGKTAPLEMFKSLHEKQQLLDTLMAQGGGHAVITVLLFLKRTLNTTQFHGILRERPKALEQYLSYLKESGDLAGHIELLQLFGRHQEAALKQFQAALASGDTSTRKKHLQLLVDAYATAGVGVIPLYEQVFHAALKMQQLMEKDSALGKLLRDQPTPVEVLYACCQVNSNWKEQDMLKPVSPQRFAADQQISPAQYEWTALNER... | Function: Essential for phagosome maturation and the innate immune response to bacteria. During phagosome maturation it is required for the fusion of late endosomes/lysosomes and phagosomes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 50412
Sequence Length: 447
Subcellular Location: Late endosome... |
P27392 | MDKKKLLYWVGGGLVLILIWLWFRNRPAAQVASNWEGPPYMTYNQPQAGSVTLPVAGYTSPSPTLPNRNRSCGCNPAVSAAMAQGADLASKLTDSITSQLNDYASSLNDYLASQAGV | Function: Protein of the infection vertex complex, which increases the vertex stability. Anchors the vertex structure to the viral membrane. Essential for viral infectivity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12551
Sequence Length: 117
Subcellular Location: Virion membrane
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Q77DJ5 | MEASYERGRPRAARQHSRDGHDHHVRARSSSRENYRGEYRQSRSASQVRVPTVFHKKRVEPLTVPPAPKDICPTLKKGFLCDSSFCKKDHQLESLTDRELLLLIARKTCGSVEQQLNITAPKDSRLANPTADDFQQEEGPKITLLTLIKTAEHWARQDIRTIEDSKLRALLTLCAVMTRKFSKSQLSLLCETHLRREGLGQDQAEPVLEVYQRLHSDKGGSFEAALWQQWDRQSLIMFITAFLNIALQLPCESSAVVVSGLRTLVPQSDNEEASTNPGTCSWSDEGTP | Function: Multifunctional protein that acts as a viral transcriptional activator. Promotes read-through of an RNA hairpin in the NP open reading frame to enhance viral transcription. Mechanistically, nonphosphorylated VP30 hexamers form a ternary complex with the viral leader RNA. Clamps the RNA template and the comple... |
P35258 | MQQPRGRSRTRNHQVTPTIYHETQLPSKPHYTNYHPRARSMSSTRSSAESSPTNHIPRARPPSTFNLSKPPPPPKDMCRNMKIGLPCADPTCNRDHDLDNLTNRELLLLMARKMLPNTDKTFRSPQDCGSPSLSKGLSKDKQEQTKDVLTLENLGHILSYLHRSEIGKLDETSLRAALSLTCAGIRKTNRSLINTMTELHMNHENLPQDQNGVIKQTYTGIHLDKGGQFEAALWQGWDKRSISLFVQAALYVMNNIPCESSISVQASYDHFILPQSQGKGQ | Function: Acts as a transcription anti-termination factor immediately after transcription initiation, but does not affect transcription elongation. This function has been found to be dependent on the formation of an RNA secondary structure at the transcription start site of the first gene (By similarity).
PTM: Phosphor... |
Q3T4M7 | MGEFGKTLITIVTAIIGVAIIAVIVSQRSNTAGVIQSATSGFSNILKSALAPII | Function: Component of the phage injection machinery. Required for DNA injection in the membrane transformation event. Involved in the formation of the membrane tail tube to connect the virus interior with the host cytosol. Essential for viral infectivity.
Location Topology: Single-pass membrane protein
Sequence Mass (... |
Q45UF8 | MSLRSLLITTEAVGETTQTSDHQTSFSTRTYNEINDRPSLRIEKDGEKAYCFKNLDPVRYDTRMGEYPFDYGGQSTENNQLQFDLFTKDLKADTDIDLSDDVKDDLKRQIMEYYQQGYRAIFLVRPQNQEQHYIASYSSTNLNFTSQPSIGVNLSILNKIQENKLYIYSTQPHIPSVGCEMIAKIFRTDIDNENSLINYSAPVTVTISVTKATFGDTFVCNHPNMNYQDLIPTMTKNSIYHDVKRITKIHEYINSKKKKKNSTSKIGGIQIAESKDGFWKILTKNYQIKLKFGVEGYGVMGGTFGNWLIDSGFKTVETNY... | Function: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer caps... |
Q01290 | MAPKQDTPFRSADMSMVQLYISNEIGREVCNALGELGLVHFRDLNSELSAFQRAFTQDIRRLDNVERQLRYFHSQMEKAGIPLRKFDPDVDILTPPTTTEIDELAERAQTLEQRVSSLNESYETLKKREVELTEWRWVLREAGGFFDRAHGNVEEIRASTDNDDAPLLQDVEQHNTAADVERSFSGMNIGFVAGVIGRDRVDAFERILWRTLRGNLYMNQAEIPEPLIDPTINEPVLKNVFVIFAHGKEILAKIRRISESMGAEVYNVDEHSDLRRDQVHEVNARLEDVQNVLRNTQQTLEAELAQISQSLSAWMITISK... | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartmen... |
O13742 | MSPSLFRSEEVSLVQLYLPTESARPIMSALGELSTIHFKDLNPDVVAFQRSFVREIRRLTDTERLLRYLHSEIDLNGIHVPDHNLPPSYESVLESSTIEDIIERITRLEARVRQLVESSQLLEARYLQQLEFANVLTKADAFFSKSGNTVDPLRNNYETSSIFSGEDDTTAPLIENALELGTTGTFDSEETSPQMNTTLDFVSGIIPTVKFQFLERILWRTLRGNLFIHQVRADDSLIHGAEKNEEKTIFLVIAHGTQILLRIRKISESLGATLFPVEEDAPGRTSQIQQANVSISDLNAVLENTRSALYTELTFIAEHI... | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartmen... |
A1A5G6 | MGELFRSEEMTLAQLFLQSEAAYCCVSELGELGKVQFRDLNPDVNVFQRKFVNEVRRCEEMDRKLRFVEKEVKKANISILDTGENPEVPFPRDMIDLEANFEKIEIELKEINTNQEALKRNFLELTELKFILRKTQQFFDEMADPDLLEESSSLLEPSEMGRGAPLRLGFVAGVINRERIPTFERMLWRVCRGNVFLRQAEIENPLEDPVTGDSVHKSVFIIFFQGDQLKNRVKKICEGFRASLYPCPETPQERKEMATGVNTRIEDLQMVLNQTEDHRQRVLQAAAKSLRVWFIKVRKMKAIYHTLNLCNIDVTQKCLI... | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartmen... |
P32563 | MAEKEEAIFRSAEMALVQFYIPQEISRDSAYTLGQLGLVQFRDLNSKVRAFQRTFVNEIRRLDNVERQYRYFYSLLKKHDIKLYEGDTDKYLDGSGELYVPPSGSVIDDYVRNASYLEERLIQMEDATDQIEVQKNDLEQYRFILQSGDEFFLKGDNTDSTSYMDEDMIDANGENIAAAIGASVNYVTGVIARDKVATLEQILWRVLRGNLFFKTVEIEQPVYDVKTREYKHKNAFIVFSHGDLIIKRIRKIAESLDANLYDVDSSNEGRSQQLAKVNKNLSDLYTVLKTTSTTLESELYAIAKELDSWFQDVTREKAIF... | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons . V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments . Is present... |
G5EEK9 | MGSLSRSEEMRFCQLIVEKDAAFNIVAEIGKQPYVQFKDLNPNVNSFQRTFVKDIRRYDEMERKLRFLESQIVKDEIVIPGRVDTGDYTILPTSELNTLEGTLTELEKDVKSMNDSDSQLKANFMDLKEWDAVLDKTDEFFQGGVDDQAQEELENLDEEGAVPRVEKGPVNYLVGIIRRERLNGFERVLWRACHHTAYIRSSDIEEELEDPGTGEKVHKSVFIIFLKGDRMRSIVEKVCDGFKAKLFKNCPKTFKERQSARNDVRARIQDLQTVLGQTREHRFRVLQAAANNHHQWLKQVRMIKTVFHMLNLFTFDGIGR... | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartmen... |
Q9Y487 | MGSLFRSETMCLAQLFLQSGTAYECLSALGEKGLVQFRDLNQNVSSFQRKFVGEVKRCEELERILVYLVQEINRADIPLPEGEASPPAPPLKQVLEMQEQLQKLEVELREVTKNKEKLRKNLLELIEYTHMLRVTKTFVKRNVEFEPTYEEFPSLESDSLLDYSCMQRLGAKLGFVSGLINQGKVEAFEKMLWRVCKGYTIVSYAELDESLEDPETGEVIKWYVFLISFWGEQIGHKVKKICDCYHCHVYPYPNTAEERREIQEGLNTRIQDLYTVLHKTEDYLRQVLCKAAESVYSRVIQVKKMKAIYHMLNMCSFDVT... | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartmen... |
P37296 | MNQEEAIFRSADMTYVQLYIPLEVIREVTFLLGKMSVFMVMDLNKDLTAFQRGYVNQLRRFDEVERMVGFLNEVVEKHAAETWKYILHIDDEGNDIAQPDMADLINTMEPLSLENVNDMVKEITDCESRARQLDESLDSLRSKLNDLLEQRQVIFECSKFIEVNPGIAGRATNPEIEQEERDVDEFRMTPDDISETLSDAFSFDDETPQDRGALGNDLTRNQSVEDLSFLEQGYQHRYMITGSIRRTKVDILNRILWRLLRGNLIFQNFPIEEPLLEGKEKVEKDCFIIFTHGETLLKKVKRVIDSLNGKIVSLNTRSSE... | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons . V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments . Is present... |
G5EGP4 | MGSIYRSEHMKLCQIFFQSESAYQCVAELGELGMAQFIDLNEEQNAYTRKFVNEVRRCDEMERKINFVEDEITKDLVPIPDYDEHIPAPQPKHMGEMEANLEKLEEELVQINKNCKVLKNNHVQLLEMKAVLEHVTSLLDPHSKREAAMSISEAARGEAGPISFGMKDEFDKPVKDEKELKFVTGVVKRSKAIAFERFLWRLSRAKVFAKFIQIQEQTELFSNEFEDKCVFILFFSGEQLRAKVKKICDGFQAKCYTVPENPAERTKLLLNIKVQTTDMKAVIEKTLDYRSKCIHAAATNLRKWGIMLLKLKSIFHTLNM... | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartmen... |
Q13488 | MGSMFRSEEVALVQLFLPTAAAYTCVSRLGELGLVEFRDLNASVSAFQRRFVVDVRRCEELEKTFTFLQEEVRRAGLVLPPPKGRLPAPPPRDLLRIQEETERLAQELRDVRGNQQALRAQLHQLQLHAAVLRQGHEPQLAAAHTDGASERTPLLQAPGGPHQDLRVNFVAGAVEPHKAPALERLLWRACRGFLIASFRELEQPLEHPVTGEPATWMTFLISYWGEQIGQKIRKITDCFHCHVFPFLQQEEARLGALQQLQQQSQELQEVLGETERFLSQVLGRVLQLLPPGQVQVHKMKAVYLALNQCSVSTTHKCLIA... | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartmen... |
Q9HBG4 | MVSVFRSEEMCLSQLFLQVEAAYCCVAELGELGLVQFKDLNMNVNSFQRKFVNEVRRCESLERILRFLEDEMQNEIVVQLLEKSPLTPLPREMITLETVLEKLEGELQEANQNQQALKQSFLELTELKYLLKKTQDFFETETNLADDFFTEDTSGLLELKAVPAYMTGKLGFIAGVINRERMASFERLLWRICRGNVYLKFSEMDAPLEDPVTKEEIQKNIFIIFYQGEQLRQKIKKICDGFRATVYPCPEPAVERREMLESVNVRLEDLITVITQTESHRQRLLQEAAANWHSWLIKVQKMKAVYHILNMCNIDVTQQC... | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartmen... |
O49048 | MVLVTSVRDYINRMLQDISGMKVLILDSETVSNVSIVYSQSELLQKEVFLVEMIDSISVSKESMSHLKAVYFIRPTSDNIQKLRYQLANPRFGEYHLFFSNLLKDTQIHILADSDEQEVVQQVQEYYADFVSGDPYHFTLNMASNHLYMIPAVVDPSGLQRFSDRVVDGIAAVFLALKRRPVIRYQRTSDTAKRIAHETAKLMYQHESALFDFRRTESSPLLLVIDRRDDPVTPLLNQWTYQAMVHELIGLQDNKVDLKSIGSLPKDQQVEVVLSSEQDAFFKSNMYENFGDIGMNIKRMVDDFQQVAKSNQNIQTVEDM... | Function: Involved in the protein transport to the vacuole, probably at the level of vesicle fusion at the trans-Golgi network (TGN) and not in transport from the TGN to the prevacuolar compartment, by promoting the recycling of vacuolar sorting receptors back to the TGN . Involved in early endosomal vesicle traffickin... |
Q54GE3 | MSGKQMDVIASIQEYINKILTNIQGMKVLVLDKETAGIVSMVYTQSEILQKEVFLFEKIENTKEKMLHMKGVYFIRPTQENIQSICDELKDPKFNKYHLFFTNTISKVSLDEIAKADEQDVVSEIQEYFGDFFAVNPDTFTLNLPGMLTKKSPRWQGDVGRVVDGLFSSLLALKKKPVIRYSSNSDTTRYLAEKITERMNRDRDLFDFRRQGEPLLLILDRKDDPITPLLHQWTYQAMIHELLTINNNRVSLAKAPGIKDELKEVVLSLDHDIFYKENLYKNFGDLGASIKDLVDQFQDKMNTNQNIQTIDDMKKFIENY... | Function: May play a role in vesicle-mediated protein trafficking from the Golgi stack through the trans-Golgi network.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 64570
Sequence Length: 563
Subcellular Location: Golgi apparatus membrane
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Q9NRW7 | MNVVFAVKQYISKMIEDSGPGMKVLLMDKETTGIVSMVYTQSEILQKEVYLFERIDSQNREIMKHLKAICFLRPTKENVDYIIQELRRPKYTIYFIYFSNVISKSDVKSLAEADEQEVVAEVQEFYGDYIAVNPHLFSLNILGCCQGRNWDPAQLSRTTQGLTALLLSLKKCPMIRYQLSSEAAKRLAECVKQVITKEYELFEFRRTEVPPLLLILDRCDDAITPLLNQWTYQAMVHELLGINNNRIDLSRVPGISKDLREVVLSAENDEFYANNMYLNFAEIGSNIKNLMEDFQKKKPKEQQKLESIADMKAFVENYPQ... | Function: May play a role in vesicle-mediated protein trafficking from the Golgi stack through the trans-Golgi network.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65077
Sequence Length: 570
Subcellular Location: Golgi apparatus membrane
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Q09805 | MDLVSASQSYFKRIFQEVSDLKILLLEEDTTKIVSSCITQSNLLEQQIYLTVLLGNKREKLRHLKCVAFLRPTPTTLRLLCEELRDPKYAEYHLYFTNVIPKSFLERLAESDDFEAVKSIQEFFLDYLVVNNDLASFNIPHIIEDSPDNWQDGAFHRTHQGIISLLLSLKKKPVIRYDNNSLLCLKLAEEVSYTIQHESQLFNFRKPDTAPILLLLDRKNDPITPLLTQWTYQAMVHELFGIDNGRVSFSNSTSDNEKSTEIVLNPTLDPFYKETRFDNFGDLGVKIKDYVSHLQTKSTKKASEIESIADMKQFLEAYPE... | Function: Vacuolar protein sorting-associated protein involved in Golgi-to-vacuole protein transport.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63552
Sequence Length: 558
Subcellular Location: Cytoplasm
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P38932 | MNLFDVADFYINKIVTSQSKLSVANVNEHQRIKVLLLDKNTTPTISLCATQSELLKHEIYLVERIENEQREVSRHLRCLVYVKPTEETLQHLLRELRNPRYGEYQIFFSNIVSKSQLERLAESDDLEAVTKVEEIFQDFFILNQDLFSFDLQPREFLSNKLVWSEGGLTKCTNSLVSVLLSLKIKPDIRYEGASKICERLAKEVSYEIGKNERTFFDFPVMDSTPVLLILDRNTDPITPLLQPWTYQSMINEYIGIKRNIVDLSKVPRIDKDLEKVTLSSKQDAFFRDTMYLNFGELGDKVKQYVTTYKDKTQTNSQINS... | Function: Essential for vacuolar protein sorting. Function in membrane traffic between the Golgi and the vacuole.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67017
Sequence Length: 577
Subcellular Location: Cytoplasm
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Q9UN37 | MTTSTLQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSDKAKESIRAKCVQYLDRAEKLKDYLRSKEKHGKKPVKENQSEGKGSDSDSEGDNPEKKKLQEQLMGAVVMEKPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDGTLVLGATNIPWVLDSAIRRRFEKRIYIPLPEEAARAQMFRLHLGSTPHNLTDANIH... | Function: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs conta... |
Q8VEJ9 | MTTSTLQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSDKAKESIRAKCMQYLDRAEKLKDYLRNKEKHGKKPVKENQSEGKGSDSDSEGDNPEKKKLQEQLMGAVVMEKPNIRWNDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLMSKWLGESEKLVKNLFELARQHKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGVGNNNDGTLVLGATNIPWVLDSAIRRRFEKRIYIPLPEEAARAQMFRLHLGSTPHNLTDANIH... | Function: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs conta... |
O75351 | MSSTSPNLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQGDKAKQSIRAKCTEYLDRAEKLKEYLKNKEKKAQKPVKEGQPSPADEKGNDSDGEGESDDPEKKKLQNQLQGAIVIERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDNDGILVLGATNIPWVLDSAIRRRFEKRIYIPLPEPHARAAMFKLHLGTTQNS... | Function: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their ATP-dependent disassembly, possibly in combination with membrane fission . Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sort... |
P46467 | MASTNTNLQKAIDLASKAAQEDKAGNYEEALQLYQHAVQYFLHVVKYEAQGDKAKQSIRAKCTEYLDRAEKLKEYLKKKEKKPQKPVKEEQSGPVDEKGNDSDGEAESDDPEKKKLQNQLQGAIVIERPNVKWSDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWRGILLFGPPGTGKSYLAKAVATEANNSTFFSISSSDLVSKWLGESEKLVKNLFQLARENKPSIIFIDEIDSLCGSRSENESEAARRIKTEFLVQMQGVGVDNDGILVLGATNIPWVLDSAIRRRFEKRIYIPLPEAHARAAMFRLHLGSTQNS... | Function: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs conta... |
Q9ZNT0 | MYSNFKEQAIEYVKQAVHEDNAGNYNKAFPLYMNALEYFKTHLKYEKNPKIREAITQKFTEYLRRAEEIRAVLDEGGSGPGSNGDAAVATRPKTKPKDGEGGGKDGEDPEQSKLRAGLNSAIVREKPNIKWSDVAGLESAKQALQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFEMARESAPSIIFVDEIDSLCGTRGEGNESEASRRIKTELLVQMQGVGHNDEKVLVLAATNTPYALDQAIRRRFDKRIYIPLPEAKARQHMFKVHLGDTPHNLT... | Function: Involved in the transport of biosynthetic membrane proteins from the prevacuolar/endosomal compartment to the vacuole. Required for multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent dissociation of class E VPS proteins from endosomal membranes, such as the disassembly of the ESCRT-III com... |
D0FH76 | MTSSNTLQKAIDLVTKATEEDKNKNYEEALRLYEHGVEYFLHAVKYEAQGERAKESIRAKCLQYLDRAEKLKEYLKKDQKKKPVKDGESKSDDKKSDSDSDSDDPEKKKLQGKLEGAIVVEKPHVKWSDVAGLEAAKEALKEAVILPIKFPHLFTGKRIPWKGILLFGPPGTGKSYLAKAVATEANNSTFFSVSSSDLVSKWLGESEKLVKNLFDLARQHKPSIIFIDEIDSLCSSRSDNESESARRIKTEFLVQMQGVGNDMDGILVLGATNIPWVLDSAIRRRFEKRIYIALPEEHARLDMFKLHLGNTRHQLSEQDM... | Function: Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequenc... |
P37370 | MAGAPAPPPPPPPPALGGSAPKPAKSVMQGRDALLGDIRKGMKLKKAETNDRSAPIVGGGVVSSASGSSGTVSSKGPSMSAPPIPGMGAPQLGDILAGGIPKLKHINNNASTKPSPSASAPPIPGAVPSVAAPPIPNAPLSPAPAVPSIPSSSAPPIPDIPSSAAPPIPIVPSSPAPPLPLSGASAPKVPQNRPHMPSVRPAHRSHQRKSSNISLPSVSAPPLPSASLPTHVSNPPQAPPPPPTPTIGLDSKNIKPTDNAVSPPSSEVPAGGLPFLAEINARRSERGAVEGVSSTKIQTENHKSPSQPPLPSSAPPIPTS... | Function: Involved in cytoskeletal organization and cellular growth. May exert its effects on the cytoskeleton directly, or indirectly via proline-binding proteins (e.g. profilin) or proteins possessing SH3 domains.
PTM: N-glycosylated.
Sequence Mass (Da): 82594
Sequence Length: 817
Subcellular Location: Cytoplasm
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D7PHZ3 | MAPYLQHFIAWFGKDSILSKLIQIFNPPSHSDSAKIIISDDDGRSPEPPGGEEILWRHSAPKSTQMWAFLQKVNKKYGYSLRTYQDLHHWSITHRGQFWGEAWDYCGIRHSRQYDEVVDEAAAMWPRPAWFRGARLNFAENLLFPKVPQAVSDEAIAVISVDEGGKRDFITWQDLRERVRRCQSGMRALKIQPSDRVAGYVANHSNALVAMLATASLGAIWTAVSPDTGVIGAVDRLVQIEPRLLFTDNAVIYNGRIHPVLTKTQEIITALPSLEAVVVMRTVAGVQEDLPSSPRSPAKRLTYNSFLAQGPETQKLEFVH... | Function: Malonamoyl-CoA synthetase; part of the gene cluster that mediates the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid with a unique, fused spirobicyclic ring system . The first step of the pathway is the production of the malonamoyl-CoA starter unit for the polyketide synthase vrtA ... |
Q9PRW4 | VIGGDECNINEHRSLVAIFDS | Function: Snake venom serine protease that completely cleaves fibrinogen Aalpha chain (FGA), partially cleaves Bbeta chain (FGB) and has no activity on gamma chain. Is more potent that A2 and A3 alpha-fibrinogenases. Very active within 5 minutes.
Sequence Mass (Da): 2289
Sequence Length: 21
Subcellular Location: Secret... |
Q9PRW3 | VPGGDECNINEHRSL | Function: Snake venom serine protease that cleaves fibrinogen Aalpha chain (FGA), partially cleaves Bbeta chain (FGB) and has no activity on gamma chain. Is more potent than A3 alpha-fibrinogenases and less potent than A1.
Sequence Mass (Da): 1640
Sequence Length: 15
Subcellular Location: Secreted
EC: 3.4.21.-
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Q9PRM8 | VIGGAECNINEHRSLVLLYXSSSXFGE | Function: Snake venom serine protease that exhibits alpha-fibrinase and beta-fibrinogenase activities. It replaces missing factors VIII (F8) and IX (F9) in deficient plasmas by activating purified human factor X (F10) into factor Xa. It releases serotonin from platelets and induces platelet aggregation in human (but no... |
P81038 | VIGGAECNINEHRSLVLLYYSSRLFGGGTLINKEWVLSAAHCDGENMKIIYXXXXXXXXXXKDRQIRVAKKYFCRDRKKSVIDKDIMLIKKPVNGSTH | Function: Thrombin-like snake venom serine protease that preferentially cleaves the alpha-chain of fibrinogen (FGA). Induce platelet aggregation in the presence of exogenous fibrinogen. Possesses esterase and amidolytic activities.
Sequence Mass (Da): 11168
Sequence Length: 98
Subcellular Location: Secreted
EC: 3.4.21.... |
Q32L63 | MAALATLPPLPPQFKSIQHHLRTAQEHDKRDPVVAYYCRLYAMQTGMKIDSKTPECRKFLSRLMDQLEALKKQLGDNEAITQEIVGSAHLENYALKMFLYADNEDRAGRFHKNMIKSFYTASLLIDVITVFGELTDENVKHRKYARWKATYIHNCLKNGETPQAGPVGIEEDNVDVEEYEDAGATSLPTQPLQPSSSTYDPSNMPSSSYTGIQIPPGAHAPANTPAEVPHSTGVTSNTIQPTPQTIPAIDPALFSTVSQGDIRLTPEDFARAQKYCKYAGSALQYEDVSTAVQNLQKALKLLTTGRE | Function: Involved in the endosomal multivesicular bodies (MVB) pathway. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor ... |
Q55B11 | MDLASLPPALKPIIPYLKQSQQLEKHDLLMAYYCRVHAIQMAMDIKQKMGASGSFLSIPIVKILDQGDADKAKLGSRLDEEDEAKYVEAFAMKAFSFADTQDRAGKANKATSTTFYSAFLFFNVLEHMGEVSEEVKLKKKYASWRSVDINTAIKNGVAPSPPPSIDQNEEGGASGETEEDAQLKQLEMELNLAKATLQQDNNNNNNMSSSTIITTNSVSEGMSSSLSFPSFPSIPNNNNNNNNTTPSFPSFPSFPSPTNSDNNSNNNKPAFPSFPSFPSPPTTTNSDSAPSFPKFPSTPSPTNSSSNNSQQPSFPSFPSF... | Function: Involved in the endosomal multivesicular bodies (MVB) pathway. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and are delivered to lysosomes enabling degradation of membrane proteins. Thought to be a cofactor of VPS4, which ... |
Q9NP79 | MAALAPLPPLPAQFKSIQHHLRTAQEHDKRDPVVAYYCRLYAMQTGMKIDSKTPECRKFLSKLMDQLEALKKQLGDNEAITQEIVGCAHLENYALKMFLYADNEDRAGRFHKNMIKSFYTASLLIDVITVFGELTDENVKHRKYARWKATYIHNCLKNGETPQAGPVGIEEDNDIEENEDAGAASLPTQPTQPSSSSTYDPSNMPSGNYTGIQIPPGAHAPANTPAEVPHSTGVASNTIQPTPQTIPAIDPALFNTISQGDVRLTPEDFARAQKYCKYAGSALQYEDVSTAVQNLQKALKLLTTGRE | Function: Involved in the endosomal multivesicular bodies (MVB) pathway. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor ... |
O13703 | MIQIDTIPKELQSIQPFVRRFNELEAHNPVIAYWSLYWAAQMALSSSHGVSNECKDFLLSLIEHLEDLRKNLGENENVSDETSAKAYVESFSLEVLVQAERNSKNGKPDVQAYLAARDFLELSRIWGPPTEQITKSIKFCKLRALQVANPQRKAKTPSNHATEELQQSSTNSTTLPTQEAAVETNASASHETSFALPTTSPAASLSISPTKSAAVSSEPNVEADVKSLSSTPAAPQLNSPSHSYEPTTFPSTTSITENLPTIDPTRSTRSSSHIQSLSPESKQTSDGHRPPSPTSITTTSTSIDPSVAFSSKSTLATTRT... | Function: Has a role in the formation of the multivesicular body (MVB). Required for the sorting of lipids to form intralumenal vesicles and for fluid-phase transport to the vacuole. Required for sorting several plasma membrane proteins into the MVB (By similarity).
Location Topology: Peripheral membrane protein
Sequen... |
Q06263 | MASNAARVVATAKDFDKVGLGIIGYYLQLYAVELILSEEDRSQEMTALATELLDTIEAFKKEIGGESEAEDSDKSLHVMNTLIHDQEKAKIYMLNFTMSLYNEKLKQLKDGPWDVMLKRSLWCCIDLFSCILHLWKENISETSTNSLQKRIKYCKIYLSKLAKGEIGSSDEKTLDYADFADDSEEIKDEDVDHQTSDLENNNNDKVEGLAPKDQTTSYEPVDEVPEFIDDADSVNEEEQTVDKNEDAITKDEQQVVKKEVDLTRPSAPSEPAAAEHKSYTKDELTKIMDRASKIEQIQKLAKYAISALNYEDLPTAKDEL... | Function: Has a role in the formation of the multivesicular body (MVB). Required for the sorting of lipids to form intralumenal vesicles and for fluid-phase transport to the vacuole. Required for sorting the plasma membrane proteins STE2 and STE3 into the MVB. Acts a cofactor of VSP4, promotes the oligomerization of VP... |
Q9UR17 | MSTQPLLQTTPGKRIALPVRVEPKVFFANERTFLSWLSFAVVLGGLSVGLLNFGDRIGKISAGLFTIVAIGTMGYALGIYHWRASAIRRRGSGPYDDRLGPTILCFVLLAAIITNFVLRMLF | Function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to ... |
Q57UM0 | MASVIEKGLASICCVTTSSKPWAEGEADGDVKYEDLRGPGGRNTSGSVSDKRICVPQKIDPKTFFANERTFLKWMSISVMIGMMSLTLLNFGDTSSNASELAGLVLLPVSILFMIHSLFVFKDRANKIYMREPMRYDDTKGPTILVLVLGVSLGIAAIFSVQKQYYRTASSSFNDGPRFS | Function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to ... |
P40046 | MSSAPLLQRTPGKKIALPTRVEPKVFFANERTFLSWLNFTVMLGGLGVGLLNFGDKIGRVSAGLFTFVAMGTMIYALVTYHWRAAAIRRRGSGPYDDRLGPTLLCFFLLVAVIINFILRLKYNDANTKL | Function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to ... |
O13718 | MRFSDSIEAGIYEPWRDKYMNYPELKHLLKTEEEAPSWGENDESKFVSVMDAQLEKVYAFHLEILKELNESVDWVKSKVSASQEPDGPPISKEEAIKLLERLDSCTETVKKLEKYTRLNLTGFFKIVKKHDKLYPGYSLRPVFQVRLRACPLGSVQFNPLLAEIFSLYNTLRDGLSAPSNSVQVKPKHEHNVDYNSSMYRRRTFRFWVHPDNVMEVKTYIMRHLPVLYYSGKQGFDKDQNGVSGILDPISTCLYLDNSNFDLYSQNLERSEQAYSLRLHWYGKLTPKTDIIVERMVRQGSTLSHSEDRFTIREKKVRELL... | Function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to ... |
P43585 | MLFGVKLANEVYPPWKGSYINYEGLKKFLKEDSVKDGSNDKKARWDDSDESKFVEELDKELEKVYGFQLKKYNNLMERLSHLEKQTDTEAAIKALDADAFQRVLEELLSESTELDNFKRLNFTGFAKIVKKHDKLYPKYPSVKSLLEVRLKELPSHSEEYSPLLYRISFLYNILRSNFNTASEPLASASKFSSIVSNDIDMNFRSFKFWVHNDNLMEVKTRILRHLPVLVYANVPSENDDLVNRFESDISNNDEIVGSSSSTSSVEHGLGARSFDPLINTLYFDNEHFELYNDKLLKLNSAPTLRLRWTGQLSDKPDIFL... | Function: Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to ... |
Q9M8S8 | MADNDSLDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKATLDDTTNRINSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASNASLKELFAEALRLTGA | Function: Phosphatase acting on L-galactose 1-phosphate (L-Gal 1-P), D-myoinositol 3-phosphate (D-Ins 3-P) and D-myoinositol 1-phosphate (D-Ins 1-P). Can also use beta-glycerophosphate (glycerol 2-P) and, to a lesser extent, D-galactose 1-phosphate (D-Gal 1-P), alpha-D-glucose 1-phosphate (a-D-Glc 1-P), D-mannitol 1-ph... |
P78810 | MKFGQLLKETLMYEYKYSYVNYDKLKKEIKRRNDQGGWSEEDESDFVELLEKELDKVYSFQKNKSAEVMERIRFCEEQTDEVVRRLDSDNPPNENDFAILETELTDIMATVHDLAKFSELNYTAFYKIIKKHDKHTGWILKPVFAARLNAKPFFKEQYDLLVVKLSKLYDFVRTRGSPIKGDSAAGGTQQNFVRQTTKYWVHPNNVTELKIYILKHLPVLVFNPNKEFAREDAAITSIYYDNDDLDFYLGRLEKREGAEAIRLRWYGNMDNNNIFVERKTHREDWTGEKSVKARFPLKEKYVNAFLRGDYTVEEAFAKMR... | Function: Catalytic subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain vtc4 to ... |
Q382V9 | MPFSKAWRSAVYPDFREQGAYINYKATKDTLHRMKEDIANPATPDELYNSLLMQKATVYKWCENKVKELQMMAEALMKASDYLSEEETPTNMSMVFSMVGSSEAKYLPPSDARRVADAITYELLRFVECRNLNTDTIEHIIARMYRYAVLGPTGDRWKNINKEYDYHALSIDEIFFMLSKVYEHVNEVESMRRDGRSSIPCGTVGSQVFDRRSVKYWVHMQDLPFVIARIIPHLPLSTFQDTYAMSKERGVPFTLGSPISSVYYDNDKFLLYHRRLERLDGATLIRMRWYGRPLDSDWNKLESKDSVFMEIKVHHEAWSG... | Function: Component of a polyphosphate synthase complex that utilizes ATP to synthesize and translocate polyphosphate to acidocalcisomes in epimastigotes, insect-stages of Trypanosoma brucei . Catalytic subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as vacuolar polyphosphate polymeras... |
O45797 | MRPAAPGTTPNGASSDIRHQRGVAPIPFGSTNSAIDAHHNSEIRVGRHRAKLDEIRESLKAYEHEAGLLSSHVALGSLATPSSSSVSHSDITNDNAEVMNFSSSSSNAAATTTTVSSAAVSNSNSFRTEGGGHKMRITPMPQRHLMMDTGANETVFRSGKEMIRNGNPSTTISSTPSTTTEESIRIHPAGYRYDMPTPAYHMNNNAPQYSPGYSRPPPPAYDSSPVNTRMTPVATDNYRTHLHMKVHPVVKAPPPNPTMLNHNKNMAPPPPPPAKSTISIETMSEERKADNIQRLYHTSMDKKTASSVVSINVASPHTTK... | Function: Phosphorylates yap-1 which may negatively regulate yap-1 nuclear localization . Plays an essential role in larval development . Regulates growth, the formation of gut granules, lifespan and cell and body sizes probably in synergy with the TGF-beta sma/mab pathway . Does not appear to regulate apoptosis and pr... |
Q55FJ2 | MNSSNLNYLDELVKEYLIFRGFTQTNHYFSLEKKGDKLKGFQVDRILEQINIYISSYDINHLVELWNFLDITFFSKIDYNKSNAYNNNNNNNNNYNSNHNSNGSYTSYRNNNNDLQSTIKKLSSSLRKYYVIYAINNNKIDKVKEFFDQYSLELLKDPDWQSWFALPYIRNPQSDPLFEIYFSKTWSEAFSLSLRNFLSTIFKNIPLPKILQFNLERQNRKRLETQVENLLSINEELRSQVDKLEYQNKRDQNNSGSNNNSNNNSNSGFTIGNVSQRKESNVNNFNSGNDLNSSNEREVNSFSRVSKRFEPRSTSSTNIA... | Function: Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endosome transport.
Location Topology: Peripheral ... |
A4D1P6 | MAEAVERTDELVREYLLFRGFTHTLRQLDAEIKADKEKGFRVDKIVDQLQQLMQVYDLAALRDYWSYLERRLFSRLEDIYRPTIHKLKTSLFRFYLVYTIQTNRNDKAQEFFAKQATELQNQAEWKDWFVLPFLPSPDTNPTFATYFSRQWADTFIVSLHNFLSVLFQCMPVPVILNFDAECQRTNQVQEENEVLRQKLFALQAEIHRLKKEEQQPEEEEALVQHKLPPYVSNMDRLGDSELAMVCSQRNASLSQSPRVGFLSSLLPQSKKSPSRLSPAQGPPQPQSSAKKESFGGQGTKGKDPTSGAKDGKSLLSGLAT... | Function: Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes via BECN1, a core subunit of the PI3K complex. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endo... |
Q7TMQ7 | MAEAVERTDELVREYLLFRGFTHTLRQLDAEIKADKEKGFRVDKIVDQLQQLMQVYDLAALRDYWSYLERRLFSRLEDIYRPTINKLKTSLFRFYLVYTIQTNRNDKAQEFFAKQATELQNQAEWKDWFVLPFLPSPDTNPTFATYFSRQWADTFIISLHNFLSVLFQCMPVPVILNFDAECQRTNQVQEENEVLRQKLFALQAEIHRLKKEEQQQEEEAAALVQHKLPPYVSSMDRLGDSELALVCSQRPASLSQSPRVGFLSSLLPQSKKSPSRLSPAQGPPQAQSSAKKDSFSSQATKGKDSVPGAKDGKSLLSGPV... | Function: Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes via BECN1, a core subunit of the PI3K complex. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endo... |
A0QTT1 | MSIAMTAPTTGVAPMTCETRLPAVPCHVGDPDLWFAENPGDLERAKALCAGCPIRVQCLTAALERQEPWGVWGGEILDRGSIVARKRPRGRPRKDSGGNPAAA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA (By similarity). Participates in maintaining a reduced cytoplas... |
Q9ZX29 | MHMHMGGDPSAICAQTDPELWFPDKGQSTRDAKRMCMRCPLLDECRALALRDPHLVGVWGGLSAQERRRIRKGASA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Contains 1 [2Fe-2S] cluster after reconstitution of overexpressed protein from E.coli. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: A dominant-negative regulator of endogenous whiB2 expression. Low level expression in ... |
Q7AKN0 | MTELVQQLLVDDADEELGWQERALCAQTDPESFFPEKGGSTREAKKVCLACEVRSECLEYALANDERFGIWGGLSERERRRLKKAAV | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA (By similarity). Complements a whiB2 disruption mutant in M.sme... |
Q7AKI9 | MADFSRLPGPNADLWDWQLLAACRGVDSSLFFHPEGERGAARSARENSAKEVCMRCPVRAECAAHALAVREPYGVWGGLTEDEREELMGRARNRLVAATASASAGGEAAGPH | Cofactor: Anaerobically binds 1 [4Fe-4S] cluster per subunit; cluster is lost on exposure to O(2). Cluster is stabilized in the presence of mycothiol. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: Acts as a transcriptional regulator. Probably redox-responsive. The ap... |
Q27256 | MTINTDDQYGDAESKTTISSSRRYSSSSYQDQSMDDALNTTLTNDKATLIQVWKPKSYGSVKGQIPQCERLTYTWKEIDVFGEAPTDGKPREPLCTRLRNCCTRQRKDFNPRKHLLKNVTGVAKSGELLAVMGSSGAGKTTLLNALAFRSPPGVKISPNAVRALNGVPVNAEQLRARCAYVQQDDLFIPSLTTREHLLFQAMLRMGRDVPASVKQHRVQEVLQELSLVKCADTIIGAPGRIKGLSGGERKRLAFASETLTDPHLLLCDEPTSGLDSFMAHSVLQVLKGMAMKGKTIILTIHQPSSELYCLFDKILLVAEG... | Function: May be part of a membrane-spanning permease system necessary for the transport of pigment precursors into pigment cells responsible for eye color.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77219
Sequence Length: 695
Subcellular Location: Membrane
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P10090 | MGQEDQELLIRGGSKHPSAEHLNNGDSGAASQSCINQGFGQAKNYGTLLPPSPPEDSGSGSGQLAENLTYAWHNMDIFGAVNQPGSGWRQLVNRTRGLFCNERHIPAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGIQVSPSGMRLLNGQPVDAKEMQARCAYVQQDDLFIGSLTAREHLIFQAMVRMPRHLTYRQRVARVDQVIQELSLSKCQHTIIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVA... | Function: ATP-dependent transporter of the ATP-binding cassette (ABC) family which transports various molecules including bioamines, neurotransmitters, metabolic intermediates and second messengers . In the eye, required for the transport of the eye red and brown pigment precursors, guanine and tryptophan, into pigment... |
Q11180 | MHKAPISTLILDSLFSNMMLAEMMNDDQLELLKHQQTGIQPVVPEGCNLYWSSLNVTGPETKPTNFVDRFRNNMPKRRVKEILHNVSGMAESGKLLAILGSSGAGKTTLMNVLTSRNLTNLDVQGSILIDGRRANKWKIREMSAFVQQHDMFVGTMTAREHLQFMARLRMGDQYYSDHERQLRVEQVLTQMGLKKCADTVIGIPNQLKGLSCGEKKRLSFASEILTCPKILFCDEPTSGLDAFMAGHVVQALRSLADNGMTVIITIHQPSSHVYSLFNNVCLMACGRVIYLGPGDQAVPLFEKCGYPCPAYYNPADHLIR... | Function: Required for efficient RNA interference (RNAi) . Plays a role in germline development .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75210
Sequence Length: 671
Subcellular Location: Membrane
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Q09466 | MPFDLLAERKRWNAGYESIDTSSQKLTEVVTPITVTWENIEVKTRKKLFSKKQKQLLNRVSGIAKPGEMVALMGASGAGKTTLMNVLMCRNMKGLEKNGTVKVNGTKIGKEISLISGFAQQQEIFIPTLTVDEYLMIQARLRMKANKHTRRERVDEIIEMLRLQNCRDLKIGTPGLVKGISGGEARRLTFACELLSNPSLLFADEPTSGLDSFMAASVVQILKNLANSGRTLIHQPTAELFFQFDKIIFLSMGKTAFMGTPHESVKFFADCGHPIPKLFNPPEWIQSKLSVIPNNETKSRETIGKIIEFYEKSIIHQKSI... | Function: Required for efficient RNA interference (RNAi) of pop-1 indicating a role in the germline development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69175
Sequence Length: 610
Subcellular Location: Membrane
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P22724 | MSPRSCLRSLRLLVFAVFSAAASNWLYLAKLSSVGSISEEETCEKLKGLIQRQVQMCKRNLEVMDSVRRGAQLAIEECQYQFRNRRWNCSTLDSLPVFGKVVTQGTREAAFVYAISSAGVAFAVTRACSSGELEKCGCDRTVHGVSPQGFQWSGCSDNIAYGVAFSQSFVDVRERSKGASSSRALMNLHNNEAGRKAILTHMRVECKCHGVSGSCEVKTCWRAVPPFRQVGHALKEKFDGATEVEPRRVGSSRALVPRNAQFKPHTDEDLVYLEPSPDFCEQDIRSGVLGTRGRTCNKTSKAIDGCELLCCGRGFHTAQV... | Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Plays an important role in the embryonic development of the urogenital tract and the lung . Required for normal mesenchyme to epithelium transition during embryonic kidney development . Required for the formation of early e... |
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