ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A0A3B1EFP9 | MGASHSTVSDPHRFAVAITGSDDDVRSLQAHPTKSYDYIVVGGGTAGCVLASRLSEDSRVNVLLVEAGYSNHGVTNSIIPLAFPMLMKSKYDWNYETVGMAGINGRTSYWPRGRLLGGTSSINGSMYHRCAPEDFSAWVEEGAKGWEYENMKPYFRKAEGYNPHPDHPNIDPALHGTVGPAKVTHGPIAFLSQPITKDILQSSINVGIRQVHDFNTDVGPTGVGLFARNVFPNGTRVSAATGYLTPSVLARPNLTVAVECMAEKIVLSSDEKVPRAKGLIFSTSRDGQRFYVPASKELILSSGVIGTPQVLMLSGIGPAA... | Function: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis begins with construction of benzoyl CoA by ... |
A0A3B1EFQ0 | MGSDLTHLEGRPPQRWQWRVFVLAALLSATFAFFTHTCSSPLPQRCRPYLPNVFNKHSLQHNEPEVRDALLAVDSFVRQSFHENPEIDGLVAAVVTANGAIYETALGPLKANETRPEDRGAVDRYSIFRLASGSKLFAMLEILILRERGALQLDDPIAKYLPQFAHKHGGWANEDDIDEGPITIRHLASHMSGMTREYPRGNMDHWPHSLEGIGPPPMNGAPFPDTLEETVLGISHYPLNLPTSTYPVYSNAGMALLGQIAVVANAAAERSQGVDVAR | Function: Beta-lactamase-like protein; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis begins with construction of b... |
Q9DBN1 | MLAASTRTRQINITCDNPVDREVFLHYSLIPSLCIILVLSFLQRREHRRQRDDTSYLLGNHFGIIVPLDFVGTFSNRWSYGAAFGATANKVMFLFSEGYQPLTVPQWAQAFVLFIGGMEVGLSYFPFFACLSSEFQLVSSILGFSYSLTWFVVTVLQISQCPHGQFLGRFETLVFYWPSLLCLGFLLGRFLHMFLKALPVHLGLEPQTEEKSMLEAHQAKHVKQLLSKPRPQEGEKSWFQTRVYEWDPCFQFPSRMVGTLLLAFICLYLFIVIEFCVFLHVRDKLDMFEDKLESYLTHMNETGTLTPIILQVKELISVTK... | Function: Acts as a high-affinity cell-surface receptor for retinol-binding protein RBP4 and mediates RBP4-dependent retinol uptake in the liver.
PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71003
Sequence Length: 621
Subcellular Location: Cell membrane
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Q3T075 | MAPDPWFSTYDSTCQIAQEIAEKIQQRNQYERNGENTTKLTVTIRALLQKLKEKIALLKDLLLRAVATHQITQLEGDRRQNLLDDLVTRERLLLASFKNEGAEPDLIRSSLMTGGAKRGAPNPWLLEEPEETRGLGFDEIRQQQQKIIQEQDAGLDALSSIISRQKQMGQEIGNELDEQNEIIDDLANLVENTDEKLRTETRRVNLVDRKSTSCGMIMVILLLLVAIVVVAVWPTK | Function: Vesicle trafficking protein that functions in the early secretory pathway, possibly by mediating retrograde transport from cis-Golgi membranes to the ER.
PTM: Ubiquitinated by HECTD3.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 26760
Sequence Length: 236
Subcellular Location: M... |
Q9UNK0 | MAPDPWFSTYDSTCQIAQEIAEKIQQRNQYERKGEKAPKLTVTIRALLQNLKEKIALLKDLLLRAVSTHQITQLEGDRRQNLLDDLVTRERLLLASFKNEGAEPDLIRSSLMSEEAKRGAPNPWLFEEPEETRGLGFDEIRQQQQKIIQEQDAGLDALSSIISRQKQMGQEIGNELDEQNEIIDDLANLVENTDEKLRNETRRVNMVDRKSASCGMIMVILLLLVAIVVVAVWPTN | Function: Vesicle trafficking protein that functions in the early secretory pathway, possibly by mediating retrograde transport from cis-Golgi membranes to the ER.
PTM: Ubiquitinated by HECTD3.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 26907
Sequence Length: 236
Subcellular Location: M... |
P31377 | MDVLKLGYELDQLSDLVEERTRLVSVLKLAPTSNDNVTLKRQLGSILELLQKCAPNDELISRYNTILDKIPDTAVDKELYRFQQQVARNTDEVSKESLKKVRFKNDDELTVMYKDDDEQDEESPLPSTHTPYKDEPLQSQLQSQSQPQPPQPMVSNQELFINQQQQLLEQDSHLGALSQSIGRTHDISLDLNNEIVSQNDSLLVDLENLIDNNGRNLNRASRSMHGFNNSRFKDNGNCVIILVLIVVLLLLLLVL | Function: t-SNARE which may play a role in determining the specificity of membrane fusion, protein transport and vesicle trafficking within the Golgi/endosomal and plasma membrane/endosomal systems.
PTM: Palmitoylated by SWF1.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 29049
Sequence Le... |
P09385 | MKCILFKWVLCLLLGFSSVSYSREFTIDFSTQQSYVSSLNSIRTEISTPLEHISQGTTSVSVINHTPPGSYFAVDIRGLDVYQARFDHLRLIIEQNNLYVAGFVNTATNTFYRFSDFTHISVPGVTTVSMTTDSSYTTLQRVAALERSGMQISRHSLVSSYLALMEFSGNTMTRDASRAVLRFVTVTAEALRFRQIQREFRQALSETAPVYTMTPGDVDLTLNWGRISNVLPEYRGEDGVRVGRISFNNISAILGTVAVILNCHHQGARSVRAVNEESQPECQITGDRPVIKINNTLWESNTAAAFLNRKSQFLYTTGK | Function: The A subunit is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits. After endocytosis, the A subunit is cleaved by furin in two fragments, A1 and A2: A1 is the catalytically active fragment, and A2 is essential for holotoxin assembly with the B subunits.... |
A0ZSK3 | MSSDLVMPALGRPFTLGMLYDTRREKLIPGFSLFGDETLQQYQSSNTQRSSEFKIVASDSTESKSSAMDIEASLGVSFLGGLVEVGGSAKYLNNTKKYQNQSRVTLKYKATTIYKQFTAPPGTVKVQETVITQRGLATHVVTGILYGANAFFVFDSDKVEDTNLQDIQGKMEAVIKKIPTISIEGSASVQLTDEEKSLASNLSCKFHGDFLLESLPTTFEDAVTTYQTLPTLLGEDGASAVPMKVWLVPLKKFFSKAKLLTQEITVSKVRRIHTTLEELYKLKRRANEAMDDKLVQQIPLIHDKISNFHQIFQDYMLTVQ... | Function: Has hemolytic and lethal activities. Its hemolytic activity is inhibited by anionic lipids, especially potently by cardiolipin.
PTM: Not glycosylated.
Sequence Mass (Da): 79670
Sequence Length: 703
Subcellular Location: Secreted
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P03083 | MDKVLNREESMELMDLLGLDRSAWGNIPVMRKAYLKKCKELHPDKGGDEDKMKRMNFLYKKMEQGVKVAHQPDFGTWNSSEVGCDFPPNSDTLYCKEWPNCATNPSVHCPCLMCMLKLRHRNRKFLRSSPLVWIDCYCFDCFRQWFGCDLTQEALHCWEKVLGDTPYRDLKL | Function: Promotes efficient viral genome replication by modulating several host signaling pathways including transport network, interferon production or cell cycle progression . Inhibits host PP2A phosphatase activity and thereby prevents agnoprotein dephosphorylation . Inactivation of PP2A also results in the transac... |
P04009 | MDQTLSKEERNELMDLLQITRAAWGNLSMMKKAYKNVSKLYHPDKGGDSAKMQRLNELFQRVQVTLMEIRSQCGSSSSQVAWFFWDENFRTLGAFLGEKFNEKIIGLYPTCTKFVRANCNCIVCLLKKQHAGTKKNLKKPCLVWGECWCYKCYLVWFGFPEDFTSFRYWTLLMANMDLSMLKLWTELGF | Function: Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle. Inhibits host PP2A by binding to the A subunit, thereby displacing lower affinity regulatory B subunit. Inactivation of PP2A in turn results in the transactivation of cyclin A and cyclin D1 promoters... |
P68835 | MDRVLSRADKERLLELLKLPRQLWGDFGRMQQAYKQQSLLLHPDKGGSHALMQELNSLWGTFKTEVYNLRMNLGGTGFQVRRLHADGWNLSTKDTFGDRYYQRFCRMPLTCLVNVKYSSCSCILCLLRKQHRELKDKCDARCLVLGECFCLECYMQWFGTPTRDVLNLYADFIASMPIDWLDLDVHSVYNPRLSP | Function: Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle. Inhibits host PP2A by binding to the A subunit, thereby displacing lower affinity regulatory B subunit. Inactivation of PP2A in turn results in the transactivation of cyclin A and cyclin D1 promoters... |
Q3L6L4 | MDKVLNREESMELMDLLGLERAAWGNLPLMRKAYLRKCKEFHPDKGGDEDKMKRMNTLYKKMEQDVKVAHQPDFGAWHSSEVGSDFPPCPDTLYCKDWPLCATKPSAHCPCMLCQLRNKHVYRKFLRRDPLVWIDCYCFDCFRQWFGLDLNEEALLWWSHIIGETPFRDLKL | Function: Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle. Inhibits host PP2A by binding to the A subunit, thereby displacing lower affinity regulatory B subunit. Inactivation of PP2A in turn results in the transactivation of cyclin A and cyclin D1 promoters... |
A8Y985 | MDYTLTREESKLLMELLGLPMEQYGNFPLMRKAFLQKCKIMHPDKGGDEQTAKMLISLYKKLESEVKSLNTDDGFSTEEVCKISKLTYIKDWLTCSFGSFSCKCLFCLLLKSHKQELTKKPKVWGDCLCFKCYTLWFGLQYTVDIYQSWQALIGVTLFKNLNI | Function: Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle. Inhibits host PP2A by binding to the A subunit, thereby displacing lower affinity regulatory B subunit. Inactivation of PP2A in turn results in the transactivation of cyclin A and cyclin D1 promoters... |
A5HBD7 | MDKTLSRNEAKELMQLLGLDMTCWGNLPLMRTKYLSKCKEFHPDKGGNEEKMKKLNSLYLKLQECVSTVHQLNEEEDEVWSSSQVECTELCCNFPPRKYRLVGEVYGDVFEEYILKDWDICLKGFYYLCNCFYCFLDKRHKQKYKIFRKPPMWIECYCYRCYREWFGFEISAETFFYWKKIIFLTTMQGVGLTR | Function: Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle. Inhibits host PP2A by binding to the A subunit, thereby displacing lower affinity regulatory B subunit. Inactivation of PP2A in turn results in the transactivation of cyclin A and cyclin D1 promoters... |
P03081 | MDKVLNREESLQLMDLLGLERSAWGNIPLMRKAYLKKCKEFHPDKGGDEEKMKKMNTLYKKMEDGVKYAHQPDFGGFWDATEVFASSLNPGVDAMYCKQWPECAKKMSANCICLLCLLRMKHENRKLYRKDPLVWVDCYCFDCFRMWFGLDLCEGTLLLWCDIIGQTTYRDLKL | Function: Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle. Inhibits host PP2A by binding to the A subunit, thereby displacing lower affinity regulatory B subunit. Inactivation of PP2A in turn results in the transactivation of cyclin A and cyclin D1 promoters... |
O22637 | MAQQLPCVSSPRPLLAVPAGRWRAGVRGRPNVAGLGRGRLSLHAAAARPVAEAVQAEEDDDDDDEEVAEERFALGGACRVLAGMPAPLGATALRGGVNFAVYSSGASAASLCLFAPGDLKADRVTEEVPLDPLLNRTGNVWHVFIHGDQLHGMLYGYRFDGVFAPERGQYYDVSNVVVDPYAKAVVSRGEYGVPAPGGSCWPQMAGMIPLPYNKFDWQGDLPLGYHQKDLVIYEMHLRGFTKHNSSKTKHPGTYIGAVSKLDHLKELGVNCIELMPCHEFNELEYFSSSSKMNFWGYSTINFFSPMARYSSSGIRDSGCG... | Function: Isoamylase starch-debranching enzyme involved in amylopectin biosynthesis in endosperm . Functions by removing excess branches or improper branches that interfere with the formation of double helices of the cluster chains of amylopectin and crystallization of starch .
Catalytic Activity: Hydrolysis of (1->6)-... |
P39153 | MKTKRWFVDVTDELSTNDPQIAQAAALLRENEVVAFPTETVYGLGANAKNTDAVKKIYEAKGRPSDNPLIVHIADISQLEDLTGPAPEKAKTLMKRFWPGALTLILPCKPDALSPRVTAGLETVAIRMPDHPLALALIRESGLPIAAPSANLSGKPSPTKAEHVAHDLDGRIAGIVDGGPTGIGVESTVLSCADDIPVLLRPGGITKEQIEAVIGPIHVDKGLSDQNEKPISPGMKYTHYAPTAPLAICEGSPERIQHLIQEYQQGGRRVGVLTTEEKAGVYSADYVKSCGRRAQLETVAAGLYDALRSFDENKVDFIIA... | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosp... |
Q9UYB2 | MTIIINVRERIEEWKIRIAAGFIREGKLVAFPTETVYGLGANALDENAVKRIFEAKGRPADNPLIIHIASFEQLEVLAKEIPEEAEMLAKRFWPGPLTLVLPKSEVVPRVITGGLDTVAVRMPAHEIALKLIELSERPIAAPSANISGKPSPTSAHHVAEDFYGKIECIIDGGETRIGVESTVIDLTEWPPVLLRPGGLPLEEIEKVIGEIRIHPAVYGKSVDTAKAPGMKYRHYAPSAEVIVVEGPRDKVRRKIEELIAKFKEEGKKVGVIGSGSYDADEVFYLGDTVEEIARNLFKALRHMDRTGVDVILAEGVEEKG... | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Likely catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of ... |
O94530 | METKIQTVDTRLISFEKPSNDSEHPFEHTRVSIPPSETRSALENAANILRNTDYPVAFPTETVYGLGADARRTEAVLSIYKAKNRPADNPLIVHVASLDQLRRLLLSAYPKAKSEVKNQAHDSEEIIPKVYLPLIKKFWPGPLSILLPVVDEANPPVSPIVTAGQKTFAVRMPQHPVALALISISDSPLAAPSANASTRPSPTLAKHVYNDLQGKIPLILDGGACGVGVESTVVNGLCDPPVILRPGGISLEEIQSSGGAWERTKVFVAKKSDMETDFIPQTPGMKYRHYSPTAKVLLFVNYTESDAYGVFEKYLSEQGI... | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Likely catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of ... |
Q970S6 | MTQIIKIDPLNPEIDKIKIAADVIRNGGTVAFPTETVYGLGANAFDGNACLKIFQAKNRPVDNPLIVHIADFNQLFEVAKDIPDKVLEIAQIVWPGPLTFVLKKTERVPKEVTAGLDTVAVRMPAHPIALQLIRESGVPIAAPSANLATRPSPTKAEDVIVDLNGRVDVIIDGGHTFFGVESTIINVTVEPPVLLRPGPFTIEELKKLFGEIVIPEFAQGKKEAEIALAPGMKYKHYAPNTRLLLVENRNIFKDVVSLLSKKYKVALLIPKELSKEFEGLQQIILGSDENLYEVARNLFDSFRELDKLNVDLGIMIGFPE... | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine (By similarity). Probably catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, wi... |
C0H4D0 | MKFLFAFNFFSLYIYLYEFLCIHLCGSQVTPAGTVLNSNSALISRRINRRKMKNCNNNDLLKVLKMETTYNELPAHNLLMSSKNDINKLFDYINKNEELSKLMNSCGTYVYLKYLGVVIFSIKENVQISHLSEFIQYLLNKNVCIEFNQNVML | Function: Acts as a specific inhibitor of subtilisin-like protease SUB1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17892
Sequence Length: 153
Subcellular Location: Secreted
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P00782 | MRGKKVWISLLFALALIFTMAFGSTSSAQAAGKSNGEKKYIVGFKQTMSTMSAAKKKDVISEKGGKVQKQFKYVDAASATLNEKAVKELKKDPSVAYVEEDHVAHAYAQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQDNNSHGTHVAGTVAALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSIQSTLPGNK... | Cofactor: Binds 2 calcium ions per subunit.
Function: Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.
Catalytic Activity: Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for... |
P07518 | AQSVPYGISQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLNVRGGASFVPSETNPYQDGSSHGTHVAGTIAALNNSIGVLGVAPSSALYAVKVLDSTGSGQYSWIINGIEWAISNNMDVINMSLGGPTGSTALKTVVDKAVSSGIVVAAAAGNEGSSGSTSTVGYPAKYPSTIAVGAVNSANQRASFSSAGSELDVMAPGVSIQSTLPGGTYGAYNGTSMATPHVAGAAALILSKHPTWTNAQVRDRLESTATYLGSSFYYGKGLINVQAAAQ | Cofactor: Binds 2 calcium ions per subunit.
Function: Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
Catalytic Activity: Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes... |
P28842 | MKRSGKIFTTAMLAVTLMMPAMGVSANEGNAAAEGNEKFRVLVDSVDQKNLKNAKQQYGVHWDFAGEGFTTDMNEKQFNALKKNKNLTVEKVPELEIATATDKPEALYNAMAASQSTPWGIKAIYNNSSITQTSGGGGINIAVLDTGVNTNHPDLRNNVEQCKDFTVGTTYTNNSCTDRQGHGTHVAGSALADGGTGNGVYGVAPDADLWAYKVLGDDGSGYADDIAAAIRHAGDQATALNTKVVINMSLGSSGESSLITNAVNYSYNKGVLIIAAAGNSGPYQGSIGYPGALVNAVAVAALENKVENGTYRVADFSSRG... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
Catalytic Activity: Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes p... |
P29141 | MKKGIIRFLLVSFVLFFALSTGITGVQAAPASSKTSADLEKAEVFGDIDMTTSKKTTVIVELKEKSLAEAKEAGESQSKSKLKTARTKAKNKAIKAVKNGKVNREYEQVFSGFSMKLPANEIPKLLAVKDVKAVYPNVTYKTDNMKDKDVTISEDAVSPQMDDSAPYIGANDAWDLGYTGKGIKVAIIDTGVEYNHPDLKKNFGQYKGYDFVDNDYDPKETPTGDPRGEATDHGTHVAGTVAANGTIKGVAPDATLLAYRVLGPGGSGTTENVIAGVERAVQDGADVMNLSLGNSLNNPDWATSTALDWAMSEGVVAVTS... | Function: Serine protease . Involved in the production of the competence and sporulation stimulating factor CSF . Is directly involved in the processing of pro-CSF to CSF . Can also cleave pro-PhrA to PhrA, but cannot cleave pro-PhrE . Shows fibrinolytic activity in vitro . Not essential for growth or sporulation .
PTM... |
Q8RWZ1 | MSFTRWEVFFGLSVLALTMPFSAGVTNLRDVSAINNLYITLGAPSLHHWLAFGGDPCGEKWQGVVCDSSNITEIRIPGMKVGGGLSDTLADFSSIQVMDFSSNHISGTIPQALPSSIRNLSLSSNRFTGNIPFTLSFLSDLSELSLGSNLLSGEIPDYFQQLSKLTKLDLSSNILEGHLPSSMGDLASLKILYLQDNKLTGTLDVIEDLFLTDLNVENNLFSGPIPPNLLKIPNFKKDGTPFNTSIITPPPPPVVDPPPATHRAPPVPRIPPVSGVPPAPFAPFAPLQPQQHPPPSPPLVWSPPSSDNGGGDPWNSVSGQ... | Function: Regulates the expression of transcription factors that define the cell fates. Acts in a non-cell-autonomous fashion, functions in a radial inside-out signaling process, and mediates cell morphogenesis and cell fate across clonally distinct cell layers in floral primordia, developing ovules, and root meristems... |
Q39232 | MGAYETEKPTKDAAALETQSPEDFDQPSPLRKIISVASIAAGVQFGWALQLSLLTPYVQLLGIPHKWSSLIWLCGPVSGMIVQPIVGFHSDRCRSKFGRRRPFIATGAALVAVAVFLIGYAADFGYKMGDKLEEKVKVRAIGIFALGFWILDVANNTLQGPCRAFLADLAAGDAKRTRVANAFFSFFMAVGNVLGYAAGSYTNLHKMFPFTMTKACDIYCANLKTCFFLSITLLLIVTVTSLWYVNDKQWSPPPRNADDDEKTSSVPLFGEIFGAFKVMKRPMWMLLIVTALNWIAWFPFLLFDTDWMGREVFGGDSDGN... | Function: Responsible for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). This transport is both voltage- and energy-dependent. Can also transport other glucosides such as maltose, alpha-phenylglucoside and beta-phenylglucoside. May also transport biotin. Required for no... |
Q39231 | MVSHPMEKAANGASALETQTGELDQPERLRKIISVSSIAAGVQFGWALQLSLLTPYVQLLGIPHKWASLIWLCGPISGMLVQPIVGYHSDRCTSRFGRRRPFIVAGAGLVTVAVFLIGYAADIGHSMGDQLDKPPKTRAIAIFALGFWILDVANNTLQGPCRAFLADLSAGNAKKTRTANAFFSFFMAVGNVLGYAAGSYRNLYKVVPFTMTESCDLYCANLKTCFFLSITLLLIVTFVSLCYVKEKPWTPEPTADGKASNVPFFGEIFGAFKELKRPMWMLLIVTALNWIAWFPFLLFDTDWMGREVYGGNSDATATAA... | Function: Responsible for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). Can also transport other glucosides such as maltose, arbutin (hydroquinone-beta-D-glucoside), salicin (2-(hydroxymethyl)phenyl-beta-D-glucoside), alpha-phenylglucoside, beta-phenylglucoside, alpha-... |
O80605 | MSDSVSISVPYRNLRKEIELETVTKHRQNESGSSSFSESASPSNHSDSADGESVSKNCSLVTLVLSCTVAAGVQFGWALQLSLLTPYIQTLGISHAFSSFIWLCGPITGLVVQPFVGIWSDKCTSKYGRRRPFILVGSFMISIAVIIIGFSADIGYLLGDSKEHCSTFKGTRTRAAVVFIIGFWLLDLANNTVQGPARALLADLSGPDQRNTANAVFCLWMAIGNILGFSAGASGKWQEWFPFLTSRACCAACGNLKAAFLLAVVFLTICTLVTIYFAKEIPFTSNKPTRIQDSAPLLDDLQSKGLEHSKLNNGTANGIK... | Function: Responsible for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). Can also transport maltose at a lesser rate. May also transport biotin. Probably involved in carpel maturation that leads to pod shatter and seed dispersal.
Catalytic Activity: H(+)(out) + sucrose(... |
Q9FE59 | MATSDQDRRHRVTRNRPPIARPSTSSSRPVVSPPRSKVSKRVLLRVASVACGIQFGWALQLSLLTPYVQELGIPHAWASVIWLCGPLSGLFVQPLVGHSSDRCTSKYGRRRPFIVAGAVAISISVMVIGHAADIGWAFGDREGKIKPRAIVAFVLGFWILDVANNMTQGPCRALLADLTENDNRRTRVANGYFSLFMAVGNVLGYATGSYNGWYKIFTFTKTVACNVECANLKSAFYIDVVFIAITTILSVSAAHEVPLASLASEAHGQTSGTDEAFLSEIFGTFRYFPGNVWIILLVTALTWIGWFPFILFDTDWMGRE... | Function: Responsible for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system) . Can also transport maltose at a lesser rate. May also transport biotin .
Catalytic Activity: H(+)(out) + sucrose(out) = H(+)(in) + sucrose(in)
Location Topology: Multi-pass membrane protein
Sequen... |
Q9C8X2 | MGALEAERAANNATALETQSSPEDLGQPSPLRKIISVASIAAGVQFGWALQLSLLTPYIQLLGIPHKWSSYMWLCGPISGMIVQPIVGYHSDRCESRFGRRRPFIAAGVALVAVSVFLIGFAADMGHSFGDKLENKVRTRAIIIFLTGFWFLDVANNTLQGPCRAFLADLAAGDAKKTRVANACFSFFMAVGNVLGYAAGSYTNLHKMFPFTMTKACDIYCANLKTCFFLSITLLLIVTFSSLWYVKDKQWSPPQGDKEEKTSSLFFFGEIFGAVRHMKRPMVMLLIVTVINWIAWFPFILYDTDWMGREVYGGNSDGDE... | Function: Responsible in a heterologous system for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). Can also transport biotin, and probably maltose at a lesser rate. In planta, the role of SUC5 for the transport of sucrose seems to be negligible. Plays a role in the nutri... |
Q9ZVK6 | MSDLQAKNDVVAVDRQSSSSLADLDGPSPLRKMISVASIAAGIQFGWALQLSLLTPYVQLLGVPHKWSSFIWLCGPVSGLLVQPSVGYFSDRCTSRFGRRRPFIATGALLVAVAVVLIGYAADFGHSMGDKIDKPVKMRAVVIFALGFWILDVANNTLQGPCRAFLGDLAAGDAKKTRTANAFFSFFMAVGNVLGYAAGSYTNLYKIFPFTMTKACDIYCANLKSCFFLSITLLLVVTIIALWYVEDKQWSPKADSDNEKTPFFGEIFGAFKVMKRPMWMLLIVTALNWIAWFPFLLYDTDWMGREVYGGDSKGDDKMKK... | Function: Responsible for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). Can also transport maltose at a lesser rate. May also transport biotin.
Catalytic Activity: H(+)(out) + sucrose(out) = H(+)(in) + sucrose(in)
Location Topology: Multi-pass membrane protein
Sequence... |
A7GYI5 | MNIHEFQAKEILKRYGVNVAKGAVAENLEQASEILNDLEGEIFALKAQIHAGGRGLAGGVKIASSREQAIQFASKLLGMTLITPQTPKNGILVRKIYIEEGLNFKQEIYLSLAFDRNSEKISLIVSKDGGVSIEETAKQNPHLIKTISIDPQIGLCGFHTKELINFLQIDKILWSKLDTLLQNLYKIYIFKDANLIEINPLVLTQDDEFYALDAKMSFDDSALFRHEDIRALNDETQTDTSENEAKAQRLNYIKLEGSVGCVVNGAGLAMATMDIIKELGGEAANFLDVGGAATGEGVAKAFRLILNDRRVKVIFVNIFG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specif... |
A9WJ74 | MKLHEYQARDLLARFGIPVTGGGVAVTPVEARTIAAEIGGPVVVKAQVHVGGRGKAGGVKLAQTPTEAEQVARQILGMNIKGLTVEKVLVAEAVSYKRELYLSAILDRGSKRVMMIASAEGGVEIEEVAKTNPDAIIKIPAHPTMGLLDFQARELAFRIGLNDGKQARQFAQIASALYRAFVECDASLVEINPLVVKADGSLLALDSKILLDESALFRHPDLAALHDPSAEPEAERRAREAGITYIKLDGNIGCMVNGAGLAMATMDVIKLSGGEPANFLDIGGGAGKEKVKAALQIILSDPNVKAVLFNIFGGITRVDE... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specif... |
Q9CNZ0 | MNLHEYQAKQIFAEYQLPVGKGYACKSADEAADAIKKLNGDVWVAKCQVHAGGRGKAGGVKLVRNEAEVRAFADQWLGQRLVTFQTDVNGQPVNTLYVEEGSSIARELYLGAVLDRASQRVVFMVSTEGGVNIEEVAEKTPHLLHKMAIDPLTGGMPYQGRELAFKLGLKGDQIKQFAHIFVQMAKMFVEKDLALLEVNPLVVTKEGNLLCLDAKIVVDSNALYRQPALKAMQDPSQEDPREALAESHQLNYVALEGNIGCMVNGAGLAMGTMDIIKLHGGQPANFLDVGGGATKERVAEAFKIILSDSAVKAVLVNIFG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specif... |
Q51567 | MSVLINKDTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGLPVFNTVKEAVEATGAEASVIYVPAPFCKDSILEAAFGGIKLIVCITEGIPTLDMLDAKVKCDELGVRLIGPNCPGVITPGECKIGIMPGHIHLPGKVGIVSRSGTLTYEAVKQTTDAGFGQSTCVGIGGDPIPGSNFIDILKLFQEDPQTEAIVMIGEIGGSAEEEAAAFIKANVTKPVVSYIAGVTAPPGKRMGHAGAIISGGKGTADEKFAALQDAGVKTVRSLADIGKALAELTGWEVKKA | Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while ... |
O08371 | MAILINKKTKVICQGFTGSQGTFHSEQAIAYGTNMVGGVTPGKGGHTHLNLPVYNTVHEAKAKTGANASVIYVPPGFAADSILEAIDAKIEVVVCITEGIPVLDMIKVKRALIGSKTRLIGPNCPGVITPGECKIGIMPGHIHKIGDIGIVSRSGTLTYEAVAQTTAAGLGQSTCVGIGGDPVNGTSFVDCIEMFLQDDETKAIIMIGEIGGSAEEDAADFIKQSKIKKPIVSFIAGITAPADKRMGHAGAIISGGKGSAEDKVEVLQSAGVIITRSPADIGKTMLDLLNKI | Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while ... |
P09143 | MILVNRETRVLVQGITGREGQFHTKQMLDYGTKIVAGVTPGKGGTEVLGVPVYDTVKEAVAHHEVDASIIFVPAPAAADAALEAAHAGIPLIVLITEGIPTLDMVRAVEEIKALGSRLIGGNCPGIISAEETKIGIMPGHVFKRGRVGIISRSGTLTYEAAAALSQAGLGTTTTVGIGGDPVIGTTFKDLLPLFNEDPETEAVVLIGEIGGSDEEEAAAWVKDHMKKPVVGFIGGRSAPKGKRMGHAGAIIMGNVGTPESKLRAFAEAGIPVADTIDEIVELVKKALG | Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while ... |
Q9HAC7 | MPSETHAMLATLARVAALRRTCLFSGRGGGRGLWTGRPQSDMNNIKPLEGVKILDLTRVLAGPFATMNLGDLGAEVIKVERPGAGDDTRTWGPPFVGTESTYYLSVNRNKKSIAVNIKDPKGVKIIKELAAVCDVFVENYVPGKLSAMGLGYEDIDEIAPHIIYCSITGYGQTGPISQRAGYDAVASAVSGLMHITGPENGDPVRPGVAMTDLATGLYAYGAIMAGLIQKYKTGKGLFIDCNLLSSQVACLSHIAANYLIGQKEAKRWGTAHGSIVPYQAFKTKDGYIVVGAGNNQQFATVCKILDLPELIDNSKYKTNH... | Function: Catalyzes the succinyl-CoA-dependent conversion of glutarate to glutaryl-CoA. Can use different dicarboxylic acids as CoA acceptors, the preferred ones are glutarate, succinate, adipate, and 3-hydroxymethylglutarate.
Catalytic Activity: 3-hydroxy-3-methylglutarate + succinyl-CoA = (3S)-hydroxy-3-methylglutary... |
Q0TUK6 | MKPNIVLIMVDQMRGDCLGVNGNEFIETPNLDMMATEGYNFENAYTAVPSCIASRASILTGMSQKSHGRVGYEDGVSWNYENTIASEFSKAGYHTQCIGKMHVYPERNLCGFHNIMLHDGYLHFARNKEGKASTQIEQCDDYLKWFREKKGHNVDLIDIGLDCNSWVSRPWGYEENLHPTNWVVNESIDFLRRKDPSKPFFLKMSFVRPHSPLDPPKFYFDMYKDEDLPEPLMGDWANKEDEENRGKDINCVKGIINKKALKRAKAAYYGSITHIDHQIGRFLIALSEYGELNNTIFLFVSDHGDMMGDHNWFRKGIPYE... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Has sulfatase activity toward para-nitrophenyl sulfate, which is increased in presence of calcium ion.
PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is... |
Q9URY8 | MRAWGWVRNKFSSEDDYNDGASNKDYPDRFNEFDNSQNDHNDYTQNNAQFQNAQTTTFGRTISRVKAYYEIPEDDELDELASIPQWFKKNVTSNIFKNFLHYLKSLFPIIEWLPNYNPYWLINDLIAGITVGCVVVPQGMSYAKVATLPSEYGLYSSFVGVAIYCFFATSKDVSIGPVAVMSLITAKVIANVMAKDETYTAPQIATCLALLAGAITCGIGLLRLGFIIEFIPVPAVAGFTTGSALNILSGQVPALMGYKNKVTAKATYMVIIQSLKHLPDTTVDAAFGLVSLFILFFTKYMCQYLGKRYPRWQQAFFLTN... | Function: High affinity uptake of sulfate into the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 93518
Sequence Length: 840
Subcellular Location: Membrane
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O59782 | MSSPSENHLLGPKTSFIDNRTSTSRPLHEIPSYQSLARRSSTWKRANIPQQKPSLVRRINYYIPVLHWLPNYSLRNIIWDVLAGCSTACLSVPIALSFAQTFLGVPPIYILTGTAIGPILYCLFTACPLISIGPEAGMCLLIAENIHQRVLSKADVPQETAILVTGLIAFIAGIINLAAGLFRLGFLDALVSPVLLRGCILSISMIIMINQGSVFFGFSGVKYKGSDFPIDKLMFLIRNMSKANIYTTILSCITISLLIGCRNLKSKLSAKYPRIVSIPDAVIILLLGSFLSKKFDWHSNYGIAILGEIKTTILLPKLPL... | Function: Possible sulfate transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73468
Sequence Length: 667
Subcellular Location: Endoplasmic reticulum membrane
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Q8RVC7 | MERVCSHQLASSRGRPCIAGVQRSPIRLGTSSVAHVQVSPAGLGRYQRQRLQVVASAAAAAAFDPPGGVSAGFSQPQQQLPQQHPRQPQAVAEVAVAESVSAPASAAPSNDGSPTASMDGGPSSGLSAVPAAATATDLFSAAARLRLPNLSPIITWTFMLSYMAFMLIMPITALLQKASLVPLNVFIARATEPVAMHAYYVTFSCSLIAAAINCVFGFVLAWVLVRYNFAGKKILDAAVDLPFALPTSVAGLTLATVYGDEFFIGQFLQAQGVQVVFTRLGVVIAMIFVSFPFVVRTMQPVMQEIQKEMEEAAWSLGASQ... | Function: Part of the ABC-type chloroplast envelope-localized sulfate transporter. Required for primary uptake and assimilation of sulfate and chloroplast protein biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43709
Sequence Length: 411
Subcellular Location: Plastid
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Q6QJE2 | MASTTLLQPALGLPSRVGPRSPLSLPKIPRVCTHTSAPSTSKYCDSSSVIESTLGRQTSVAGRPWLAPRPAPQQSRGDLLVSKSGAAGGMGAHGGGLGEPVDNWIKKLLVGVAAAYIGLVVLVPFLNVFVQAFAKGIIPFLEHCADPDFLHALKMTLMLAFVTVPLNTVFGTVAAINLTRNEFPGKVFLMSLLDLPFSISPVVTGLMLTLLYGRTGWFAALLRETGINVVFAFTGMALATMFVTLPFVVRELIPILENMDLSQEEAARTLGANDWQVFWNVTLPNIRWGLLYGVILCNARAMGEFGAVSVISGNIIGRTQ... | Function: Part of the ABC-type chloroplast envelope-localized sulfate transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39479
Sequence Length: 369
Subcellular Location: Plastid
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Q94225 | MYKKMSLRQLFSDRPPLNAVLQEKAQKLRYACSPSKCIHSLLSFLPIITWLPKYDWSHSFFGDLSGGLTMAVFSVPQGIALASITGVPPVYGLYTAIFPSFLYIFFGTSKHNALGGFAVLSLMTHGAIEKVMLRTATSYNATAYVNHTLDELLDKENETALISNTTLMQILGNETSFVEEVTMEMWTEGVTPVKQIHVATTIIFLAGVIQVFMGVFRLQYLTSLFSEQVMSGFVVGGGIHVFFAQIGNMLGIELPRRSGPGYLYYRIWDLVENLDNVHIPTVCISLSSFLFLVFGKEYLAPWLNSAFNYPVPFELVLVVV... | Function: Possible sulfate transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87475
Sequence Length: 782
Subcellular Location: Membrane
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O34734 | MELAAILFSLFFAMNIGASGAAASMGVAYGSGAIKKKTYALILCAVGVFAGAVIGGGEVVKTISSGIIPEQTITLTIVCIIIGAAALSLFTANLLGIPLSTSEVTVGAVVGVGVAYKVLFVNNLLIIVSFWVFVPLFAFGFTYFVSKLFRYFKIEVKSSKKQKILGIVLLVAGFFEAFSAGMNNVANAVGPLVAAGVLDVGKGTLYGGAFVALGALLLGRRVLETNGKKITRFSKGEGILLSGTGAGLVIISSVFGMPVPLAQVTSSSIIGIGMAKNGPNVFHKQVVQTMLKVWIVSPFLSLSISYLLVSLFLKADYYSI... | Function: Involved in the import of sulfate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36836
Sequence Length: 354
Subcellular Location: Cell membrane
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A8J6J0 | MKRNTSNVDTGGVPAPLNSTPSTRLIQNGYGDSKYETERMEFPFPEDPRYHPRDSVKGAWEKVKEDHHHRVATYNWVDWLAFFIPCVRWLRTYRRSYLLNDIVAGISVGFMVVPQGLSYANLAGLPSVYGLYGAFLPCIVYSLVGSSRQLAVGPVAVTSLLLGTKLKDILPEAAGISNPNIPGSPELDAVQEKYNRLAIQLAFLVACLYTGVGIFRLGFVTNFLSHAVIGGFTSGAAITIGLSQVKYILGISIPRQDRLQDQAKTYVDNMHNMKWQEFIMGTTFLFLLVLFKEVGKRSKRFKWLRPIGPLTVCIIGLCAV... | Function: H(+)/sulfate cotransporter with a probable high-affinity for sulfate and a proteasome independent turnover.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83230
Sequence Length: 764
Subcellular Location: Cell membrane
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P82609 | SFFEQNXKIVYVARNAKD | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic compounds.
Catalytic Activity: 3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate + H(+)
Sequence Mass (Da): 2141
Sequence Length: 18
Subc... |
P46549 | MAPAVLQKPGVIKDPSIAALFSNKDPEQRYQDLREIGHGSFGAVYFAYDKKNEQTVAIKKMNFSGKQAVEKWNDILKEVSFLNTVVHPHIVDYKACFLKDTTCWLVMEYCIGSAADIVDVLRKGMREVEIAAICSQTLDALRYLHSLKRIHRDIKAGNILLSDHAIVKLADFGSASLVDPAQTFIGTPFFMAPEVILAMDEGHYTDRADIWSLGITCIELAERRPPLFSMNAMSALYHIAQNDPPTLSPIDTSEQPEWSLEFVQFIDKCLRKPAEERMSAEECFRHPFIQRSRPSDTIQELIQRTKNMVLELDNFQYKKM... | Function: Acts as a negative regulator of cortical contractions during early embryonic cell division, possibly by regulating rho-1-dependent actomyosin contractility . Plays a role in polarity establishment in early embryos by regulating the size of the anterior and posterior cortex in the first asymmetric cell divisio... |
P53394 | MTSNNSLLGRGRMSYSSTAPPRFKRSVDQRDTFSDNFDYDKDSSNRGRTYIAASNSTTGVPPPNNSRSGCTNNTNNTNNTSNTSNTNNNDSVDENTVFETLPYYLPCFSWLPEYTFNKLWGDVIAGISVASFQIPLALSYTTSIAHVPPLCGLYSLAISPFVYGILGSVPQMIVGPESAISLVVGQAVESITLHKENVSLIDISTVITFVSGTILLFSGISRFGFLGNVLSKALLRGFISSVGLVMIINSLISELKLDKFLVSLPQHYHTPFEKILFLIDYAPAQYHIPTAIFSGCCLIVLFLTRLLKRKLMKYHKSAIF... | Function: Possible sulfate transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83384
Sequence Length: 754
Subcellular Location: Endoplasmic reticulum membrane
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Q8NBK3 | MAAPALGLVCGRCPELGLVLLLLLLSLLCGAAGSQEAGTGAGAGSLAGSCGCGTPQRPGAHGSSAAAHRYSREANAPGPVPGERQLAHSKMVPIPAGVFTMGTDDPQIKQDGEAPARRVTIDAFYMDAYEVSNTEFEKFVNSTGYLTEAEKFGDSFVFEGMLSEQVKTNIQQAVAAAPWWLPVKGANWRHPEGPDSTILHRPDHPVLHVSWNDAVAYCTWAGKRLPTEAEWEYSCRGGLHNRLFPWGNKLQPKGQHYANIWQGEFPVTNTGEDGFQGTAPVDAFPPNGYGLYNIVGNAWEWTSDWWTVHHSVEETLNPKG... | Cofactor: The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation.
Function: Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins, using molecular oxygen and an unidentified reducing agent . 3-oxoalanine modification, which is also named formylglycine (f... |
Q3IFD3 | MNLKKLLTSAVLSISLCQSAFAAPVEIDKVIGIVNQGVILKSEVDTIVNRVKKQAEEQSQELPKDETLRVQAVERLVNQTLMMQMAERMGLEISDSQLDQTLASMAKEQGGSIADLRRTIEGSGESFQAYREEIRKEITTQQVMRANVDRRVYVSEQEVDNLLKIMESQGQNAEEYDIGHILIDIPSDASADEIASAKTRADKVIELLNDEQEFKRIAISSSSGSQALEGGQLGWMGINEMPSLFAEAVKGKKQGAIIGPLRSGAGFHIIKVQDVRGRQVVETTETRSRHILIKPSIILSEEKARSMLAGFVKDLRADKA... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q4ZMG7 | MLGALLLSGAVHAAVQPLDSVVAIVDNDVIMKSQMDQRVREVQQTIAKRGSGVPPAEALQPQVLDRLILENLQLQMGERSGIRVSDEELNQAIGTIAQRNNMSVEQFRAALAHDGLSYNDAREQVRREMIISRVRQRRVAERIQVSQQEVKNFLASDMGKAQLSEEFHLANILIATPDSASSDAIQAAAVKAKGIYDQLKKGADFTRLAATSSSSENALEGGDMGWRKAAQLPPPFGDMLSSMPVGDVTPPARTPGGFIILKLLEKRGGQGQAQMRDEVHVRHILIKPSEIRNEEETKRLAQKIYDRIENGEDFAELAKS... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q8Y220 | MACKSTAVRSATRVAPTRRLGMVTGALVALMAGAALLPAAHAQQTQKKSAPLRGIFTTPDASPSQPLLRGTLPGPSTASGAARSQLVDEVVAVVNTDIITRRELLDRADLVERTLQSQNRQVPVRADLLGEVLEQLILERVQAQTAKESGIRVSDADVDRAVESVAQRNNLSVSQLKSKLAQSGLAYDKYREDLRQEILLARLRDREVDSKVQVFDGEIDNFLAQQGGSAASSGVQEYNVAQILVPVAEDASAEQKAAARGKAESLLKQVQGGADFAKLARDSSGAPEAAQGGELGLRPIGRLPAQFANAVVDLKPGQVV... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q21MS8 | MQIIKTTIATFTAIAFTGAASFTSAEVVPLDRVVAVVDNRAITQTELDSRVQDVQVRSQAAGMRLPEADILNKQIIDQLISETLQLEMADRYGVQVSDQEVNASIGNIIQNAQMTEQQFVQQLASEGVSINEFRASIRRQLTMRSITEGLVSRRIRISEQEVDNFLKSADAQFWVSPDYHLGHILVALPSSPSSEAIVEAEEKANALYEKLKAGANFAEVAIAESNGPSALQGGDLGWRKSAELPTLFAELLPSLNNGDVTKPTRSQAGFHIIKLYESRGGQKQIVNQTRARHILVKTSEILNDAKAEAKLKDIRQQILD... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q8EB95 | MKPSKHLIFALFALAISQPTMAAPQPLDRVAVQINDGIVLESEITNMIDTVKANAKAANQSLPSDSALRTQVIERLILTRLQLQMADRIGLHIGDLQLDQAIENIAREQKMTVAQMQQKIASEGISFSQYREQLREEITLGEIQRIQVQRRIQVSPQEITGLVKLIQEQGMKDVEYQIGHILIDVPNNPTSEQLEASSKRANAVLERLKSGEDFRRTAIASSSGPKALEGGIWDYMNINEMPTLFAEVINGAKKGDIIGPIKTGAGFHIIKIMDARGLQTKEIEEVRARHILLKPSPILSEDRAKAMLEQFLKQIRSGEA... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q2NVX4 | MKNWRTFILGLALCANGALAAPQVVDKVAAVVDNGIVLESEVDNMLSTVKHGAQEANQQLPDDTTLRRQILDRLIMDNIILQLAQRTNITISDEQLDQAIGNIAAQNHMSLDQLRSRLPYDGIDYNTYRTQIRKEMLIAEVRNGEVRRRVTILPQEVESLAQQIAAQTGNGAEFNLSHILIPLPENPTQDQLDKAEELATSIVEQSKSGADFGKLAITYSADAQALKGGQMGWGKLEELPSLFAARLQGAQKGSIVGPIRSGVGFHILKVNDIRGGDQKVAVTEVHARHIMLRTSVVMTDQQARAKLEDIAAQIKSGRIS... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
Q3SGF9 | MKFFQRPERRLKQWGLALLLAASALLPARADVVPLNHIVAVVNDEVITRQELAKRYDEVVRNLSRQNTPLPPRNVLEKQLLERMVTELALQQHARNTGVRADPTLVERALQRIAAQNKLDMAGLQAALEKEGQTLDGMRNTIRNELLIARARERDVDNRISVSDAEIDGYLQTQAQQGAETEYNFSHILVSVPENASPEQIRERRARAEDILAQLAAGADFAQLSASHSDAPDALKGGNFGWRASGKLPALFVEALKPMQPGEISPLLRSGNGFHILKLVDKRGLDATLSVTQTHARHILIKTNEITSEADARNRLLQLK... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
B9E0C7 | MRLLLTNDDGIMAEGIQVLAKHFEKDNEVIIAAPDVQRSGSGHCITTVPGELIIQEVKLEGINSKAYSITGTPADCARLGVRKLGNNQIDMVISGINNGFNLGIDSLYSGTVSAAIEAAICETPSIAVSLDTKGGNYDYNIAAEYALEVFSIYKDKYKNKDENVVLSLNVPCLPREKIKGLKVCRVGFKYHLQEIYDKGEKTEELSYNYTDIYYVKRGYAALSPLHYDLTNYKILGDINNLFTEK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 27106
Sequence Length: 245
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q899M5 | MRLLLTNDDGVNSKGIYTLAKELQKEHEIIIAAPSIEMSAKSHSITIAKPLFIKEVELDDINATTYSISGTPADCVKVAMDKILDKPVDMVISGINYGTNLGIDILYSGTVSAAIEAAIHNIPSIAMSAEVKNGDINFDTAASIARELVKISQENSMKGNLVLNVNVPCLDKDSLKGLKVCQMGGRTFTSYFEKIEKNKEVSYMLKGELTNNHKPTTDIHFLRKGYTTITPLHYDLTNFKIMNDVSNWF | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 27449
Sequence Length: 249
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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A9KDH9 | MKKTATPKLRLLLSNDDGVYAKGLAILAKTLADLGEVDVVAPDRNRSGASNSLTLNAPLHIKNLENGMISVEGTPTDCVHLAITGVLPEMPDMVVAGINAGPNLGDDVWYSGTVAAAMEGRFLGLPALAVSLGGELFRYYETAAKVVYQLIQRIEKDSLPPSTILNINVPDLPYEELKGFEVTRLGTRHRAEPTIRQIDPRGHPIYWVGAAGPEQDSGPGTDFFAMNHHCVSITPLRVDLTHYEAFDQLASWVKRLEM | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 28056
Sequence Length: 258
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q0K950 | MHILLANDDGYLAPGLAVLHAALAPLGRITVIAPEQNHSGASNSLTLQRPLSIYEAREGVQKGFRFVNGTPTDCVHIALTGLLEEKPDLVVSGINQGQNMGEDVLYSGTVAAAIEGYLLGIPSVAFSQVDKGWEHLDAAARVARTVVERIIGTPPAEPFLLNVNIPNLPFEHIKGYRATRLGKRHPSQPVITQVNPRGDTNYWIGPAGDARDASEGTDFHAAAAGYVSLTPLQLDLTHRGQLDALDQWLK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 26860
Sequence Length: 250
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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A6LF90 | MTNERPLILITNDDGVWAKGINELIECLKDLGDLVVFAPDGPRSGMGSAITSLVPIKYTLLKKEEGLTIYSCTGTPVDCVKLAINEVLERKPDLLVSGINHGGNMAICVNYSGTMGAAAEGCIFNVPSMGVSLLDHAADADFSECCRLGRMLARRVLKEGLPHGTYLNLNVPKLPQVKGLKVCRQADGRWVREFKRSENASGEPVFWLTGAFESAKPIHPDNDMLALDSGYASLVPCKIDVTDYDFMATLNNWIL | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 27746
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q6MCW1 | MSSKPLILVTNDDGVHAKGIRHLWQSIQDLADLIIVAPQQEQSAVSLSITVRRPLHIEKVDWLNAQADVWSVNGTPADCVKLALNVVLPKRPQLIVSGINRGTNAGRNIFYSGTVAAIMEGVMQGIPGIAFSYGDYFNPSYHLIESFIPGIVNYALQNAMQEGTFLNVNFPKTEHGPIKGIRLTTQGKEYWAENPEKRQHPAEQNSYYWLGSKLAEYDEREDSDIFLLRKGFATVVPLHIGDLTNHSHLLKEKLAFETFVN | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 29165
Sequence Length: 261
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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A5D2G6 | MRILISNDDGIQAEGINALRACLQEQNEIYIVAPDRERSATGHKITMHRPLRVKEWHYPEAKTVGWAVDGTPADCVKLGLEALLPAPPDLVISGINLGPNLGTDVLYSGTVSAAIEGIINGIPAIAVSLASYDYRDFSFSGKLIKELVSAFGNRLPDKTLLNINVPPGKPCGIKVTRLGNRRYINIFDKRTDPRGRVYYWMAGEPFDLDEDDPDTDVWAVKEGYVSITPVHFDLTDYKIMERLKKLLKTAKILNRELKD | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 28848
Sequence Length: 259
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q6LMT6 | MRILISNDDGIFAEGINTLATVLSELGEVTIVAPDRNRSGASNSLTLDYPLRIREEGDRRISVDGTPTDCVHFALNEWLDYRPDIVVAGINHGANLGDDVLYSGTVAAATEGHFLGVPAIAISLVGSTHFDTAAQVVKSIVVNLLEKPLPKNKILNINVPDIPFAELKGWKVTRLGARHRAEQMVKDVDPRGKVLYWLGPPGACQDAGPGTDFHAVEQNLVSITPLQVDLTAHDALESVELWMNEVGKK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 26946
Sequence Length: 249
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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Q6KZ11 | MILVTNDDGYNSYGIRVLYRAAASIAESYIVAPDHGRSATGMSTTYNVPLRAFKFDYGYAISGFPADSVYMARYALYNDKKIDLIVSGINHGDNISLRSLYSSGTIGATMAGALIGIKGIAFSMSYNGISNEKIDLAEPYIKAIIENAMERFPDDVDILNVNFPGNLNRNTRILPARMSYNIFDDNIIKRLDPNGHEYYWFGNKRHERCPENCDYDVVYRKNSISITPITVKGYLDDLRSTEEFISFINVKELLG | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 28645
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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A4SYE9 | MSKQPHILVSNDDGYLAPGLLALVNAVRPLGRITVIAPEQNHSGASNSLTLSRPLSIHRVAGGERDGFFFVNGTPTDCVHVAMTGFLDEKPDLVISGINQGENMGEDTLYSGTVAAAVEGVMFGVPGIAFSQIDRGWNRIEDAAKAAHDVVAQMLVSALARTEGTATLLNVNIPNRPYADLYRWRVTRLGNRHHSQPVVVQDSPRGEKIYWIGAAGEVKEGSEGTDFHAIAEGCISITPMQLDLTHHARLAAMRANGWDRG | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Sequence Mass (Da): 28084
Sequence Length: 261
Subcellular Location: Cytoplasm
EC: 3.1.3.5
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A7YY49 | MGQNDLMGTAEDFADQFLRVTKQYLPHVARLCLISTFLEDGIRMWFQWSEQRDYIDTTWNCGYLLASSFVFLNLLGQLTGCILVLSRNFVQYACFGLFGIIALQTIAYSILWDLKFLMRNLALGGGLLLLLAESRSEGKSMFAGVPTMRESSPKQYMQLGGRVLLVLMFMTLLHFDASFFSILQNIVGTALMILVAIGFKTKLAALTLVVWLFAINVYFNAFWTIPVYKPMHDFLKYDFFQTMSVIGGLLLVVALGPGGVSMDEKKKEW | Function: Endoplasmic reticulum cargo receptor that mediates the export of lipoproteins by recruiting cargos into COPII vesicles to facilitate their secretion. Acts as a cargo receptor for lipoproteins bearing both APOB and APOA1, thereby regulating lipoprotein delivery and the maintenance of lipid homeostasis. Synergi... |
Q18864 | MNQFRAPGGQNEMLAKAEDAAEDFFRKTRTYLPHIARLCLVSTFLEDGIRMYFQWDDQKQFMQESWSCGWFIATLFVIYNFFGQFIPVLMIMLRKKVLVACGILASIVILQTIAYHILWDLKFLARNIAVGGGLLLLLAETQEEKASLFAGVPTMGDSNKPKSYMLLAGRVLLIFMFMSLMHFEMSFMQVLEIVVGFALITLVSIGYKTKLSAIVLVIWLFGLNLWLNAWWTIPSDRFYRDFMKYDFFQTMSVIGGLLLVIAYGPGGVSVDDYKKRW | Function: Endoplasmic reticulum cargo receptor that mediates the export of the yolk proteins from intestinal cells by recruiting cargos into COPII vesicles to facilitate their secretion . Required for the endoplasmic reticulum export of the yolk protein vit-2, which is synthesized as a lipoprotein complex, from intesti... |
O18405 | MSIPNEYIAKTEDVAEQVIKRGKNVLPTVARLCLIATFFEDGLRMYIQWNEQREYMDMSWGCGKFLATVFVLVNLLGQLGGCGMVMARFKVDIAVGLLFFIVVLQTVAYSILWDFQFLLRNFALIGALLLVLAEARIEGRSLFAGVPSMGENKPKNFMQLAGRILLAFMFITLIRFELSVWQVIQDIIGSILMVLVVLGYKTKLSALILVALLTILNLYHNAWWTIPSYKPLRDFLKYDFFQTLSVIGGLLMIVSLGPGGVSMDEHKKKW | Function: Endoplasmic reticulum cargo receptor that mediates the export of lipoproteins by recruiting cargos into COPII vesicles to facilitate their secretion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30546
Sequence Length: 270
Domain: The di-lysine motif confers endoplasmic reticulum localiza... |
O15260 | MGQNDLMGTAEDFADQFLRVTKQYLPHVARLCLISTFLEDGIRMWFQWSEQRDYIDTTWNCGYLLASSFVFLNLLGQLTGCVLVLSRNFVQYACFGLFGIIALQTIAYSILWDLKFLMRNLALGGGLLLLLAESRSEGKSMFAGVPTMRESSPKQYMQLGGRVLLVLMFMTLLHFDASFFSIVQNIVGTALMILVAIGFKTKLAALTLVVWLFAINVYFNAFWTIPVYKPMHDFLKYDFFQTMSVIGGLLLVVALGPGGVSMDEKKKEW | Function: Endoplasmic reticulum cargo receptor that mediates the export of lipoproteins by recruiting cargos into COPII vesicles to facilitate their secretion . Acts as a cargo receptor for lipoproteins bearing both APOB and APOA1, thereby regulating lipoprotein delivery and the maintenance of lipid homeostasis . Syner... |
Q64310 | MGQNDLMGTAEDFADQFLRVTKQYLPHVARLCLISTFLEDGIRMWFQWSEQRDYIDTTWSCGYLLASSFVFLNLLGQLTGCVLVLSRNFVQYACFGLFGIIALQTIAYSILWDLKFLMRNLALGGGLLLLLAESRSEGKSMFAGVPTMRESSPKQYMQLGGRVLLVLMFMTLLHFDASFFSIIQNIVGTALMILVAIGFKTKLAALTLVVWLFAINVYFNAFWTIPVYKPMHDFLKYDFFQTMSVIGGLLLVVALGPGGVSMDEKKKEW | Function: Endoplasmic reticulum cargo receptor that mediates the export of lipoproteins by recruiting cargos into COPII vesicles to facilitate their secretion. Acts as a cargo receptor for lipoproteins bearing both APOB and APOA1, thereby regulating lipoprotein delivery and the maintenance of lipid homeostasis. Synergi... |
O74559 | MTSRSPFSTIPLSMNQDSYQTRTTVGIRKKTFSERACQFMEQAETFMAPFTPYMPLLGRFLIVATYFEDAIRIVTQWPEQVSYMRDYRRFRFGTAPLLLFVCVVLMLVGSTLVVFKKRQAYAIGSLLFVTLLQAFAYGLITSGEMFFRNMSVIGGLCLVASDTFIHRRINRFAGLPAVSEHNKRTYFQLAGRVLLIFMFLGLLAKEGSGISWTRILVHILSVTACAMVVIGFKAKFFAAVLVLILSVANFIINSFWSVPRESPYRDFYRYDFFQTLSIVGGLLYLVNTGPGKFSVDEKKKIY | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34386
Sequence Length: 302
Domain: The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins.
Subcellular Location: Endoplasmic reticulum membrane
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O57590 | MGQEDLMNRAEDVADQFLRVTKQYLPHLARLCLISTFLEDGIRMWFQWNEQRDYIEATWSCGYFLATCFVLLNLIGQLGGCVLILSRNFVQYACFGLFGIIALQTVAYSILWDLKFLMRNLALGGGLLLLLAESRSEGKSMFAGVPSMGESSPKQYMQLGGRVLLVLMFMTLLHFDFNFFSILQNLVGTALIILVAIGFKTKLAALTLVLWLLVINVYFNAFWTIPAYKPMHDFLKYDFFQTTSVIGGLLLVVALGPGGVSMDEKKKEW | Function: Endoplasmic reticulum cargo receptor that mediates the export of lipoproteins by recruiting cargos into COPII vesicles to facilitate their secretion. Acts as a cargo receptor for lipoproteins bearing both APOB and APOA1, thereby regulating lipoprotein delivery and the maintenance of lipid homeostasis.
Locatio... |
P70279 | MASLLAKDTYLQDLAKKICAQPGPERQRSTWGVRTKGSEAAGAPKKKRKKTQKKSPEQEQKAMDHKTKALGKKPPTSSRPKNPMVSKQEKGLSSLGSPKDSQGTARESVFALDFLRQRLHEKIQLARGQGSTKELSAATLEKRQRRKQERERKKRKRKERQAKQQVAEAEKKEEPVEVTPKMACKELQESGLIFNKVEVTEEEPASKAQRKKEKRQKVKGNLTPLTGRNYRQLLDRLQARQGRLDELRDQDAAKAQELEAKMKWTNLLYKAEGVKIRDDERLLQEALKRKEKRRAQRQRKWEKRSEHVVEKMQQRQDKRR... | Function: Binds to both DNA and RNA in vitro, with a stronger binding capacity for RNA. May represent a nucleolar constitutive protein involved in ribosomal biosynthesis or assembly.
PTM: Citrullinated by PADI4.
Sequence Mass (Da): 41235
Sequence Length: 355
Subcellular Location: Nucleus
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Q9LP74 | MTKLVSKIFKRLISQSQYMSSSTTSNLPAASQTSNLESQLLSSAPPPAKKKRGSALLWYLVGFTTYGLGETYKFLQTQVEHLDSRKQCLEMKPMKLNTTKDLDGLGFRRVVCKGIFDEQRSIYVGPKPRSMSKSSEIGFYVITPLLPIPNEPNSMKSPILVNRGWVPSDWKENSLESLGTGGLVAAAKESRKANKLLSSQQSLLSKFWYKLNNPMIVEDQVSRAMHVEVVGVVRKSETPGIYTLVNYPSSLAWFYLDVPKLALAMGFGEDTMYIESTYTDMDESRTYPVPRDVENLTRSKDIPLDYHLYTVLWHWSSLTC... | Function: May be involved in the biogenesis of the COX complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43185
Sequence Length: 384
Subcellular Location: Mitochondrion inner membrane
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Q9XU75 | MRYLCKSILLAVHTILLVGSVCCSTDVHNTDDKYALIHVSAHDEQSLHLIKQLQLNDFKYDLDFWKSPSSISDKADIMVKRGKSERMLRQILSFANVTVSMSVPDVEKLIMRNEGTTSKSHLGFGSLSKWLHDDPILDSEPDLDLTKVGALKKAKYPFGDYASYADMVKYMRTIEFYYPRIAKIVRIGATHEGKPIEGLKIGARSSHKKRAVWVDGNIHAREWASSHTALYFINQLVSEYGKDAQITNYVDTLDFYIVPCLNPDGYEYTRTSPIPTVRLWRKNRSPELCRPSLWGGEKCCRGVDLNRNFRFHWAERGSSY... | Function: May play a role in processing or organization of cuticle collagen proteins, including rol-6 and col-19.
Sequence Mass (Da): 75153
Sequence Length: 664
Domain: The ShKT and Thr-rich domains are required for body morphogenesis.
Subcellular Location: Cytoplasmic vesicle
EC: 3.4.17.-
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Q09885 | MKAWLQSSISYYTGTAEPVYGPEAIQPVTASVQGINPFHRLEADDFKWSTPSSSHVETQVFYIKPNEGDYMCFVQLIHSNLGSWTTTAQSTCRIFDLKHPENDLWTSTNMDQFSFENDKTSFVAKNCSVVLEDQKRYRIRASINMDSIIDITVHQDAPPFKIGEDGNSTYGTDPSKPWASMKHTFWPRTRVEGSIVARGRVVDVTGPGMFVHALQNGKPHHLASSWEFALLQHKKFTAIMMQFKTPPSYGSTIVNIGGIAMKDKIISATVDNTIEHVETTLDPDTEWHEPTRISYEWDGKDAETYTEDIHLSVDAPLGRR... | Function: Ceramide-binding protein that may transfer ceramides from the endoplasmic reticulum membrane to the cis-Golgi network membrane, and is thereby required for the biosynthesis of complex sphingolipids.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42961
Sequence Length: 380
Subcellular Locat... |
Q6CBN5 | MLKWVQGGVSALTGSAEPEYGAEAFESVSKSVDGKNPYGSLTLPELNWLKPAGSNVETQTFYFFSKDGKQFGHVQIIHSNPLGIQNTAQFTFRLSNADKPEENVWSSTNVEEFEPVGPNFTAKGPMDGVNIKLVPSVDDDGKTTEAFHVKIHVSDEVKLDLTFTRSVEGFKIGPTGQSKYGEDLNNPWGAMRHSFWPRASVSGTIEVANKDKMELDNDFGFFVHATQGMKPHHAASKWNFITYQSPKYSAVVMDYTTPPSYGSSRVTIGGVASAEKLLFTSANATVEHVETKEDEEVGWQVPTLIKFECEGPKVDVADED... | Function: Ceramide-binding protein that may transfer ceramides from the endoplasmic reticulum membrane to the cis-Golgi network membrane, and is thereby required for the biosynthesis of complex sphingolipids.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 44000
Sequence Length: 398
Subcellular Locat... |
Q05515 | MLKWIKGGISAVTGMAEPEYGKDYIHSVADRVKNKQPYRETSREDFFWQAPDHTNVESVIFYFSDLKTGIFGFAQVIHSNIIGLHTASQFTFRIFDSKNPEDLNIWTSTKLENFYIEGPNFYADNLSVELSEDGESYHIQSSVCDLSVVDLHIRRLTPGAKIGDDPATYYGNNINEPWGSMRHVFWPRNACHGTIKVKKEVIPESDEEESSADEDDNEDEDEESGDSEEESGSEEESDSEEVEITYEDRTITFKEEDPAISTFIMAFQGMKPHHAAKAWNFMFFHSEKYSAVLMEFTTPKSYANTKISAGIITDDKEVLA... | Function: Ceramide-binding protein that may transfer ceramides from the endoplasmic reticulum membrane to the cis-Golgi network membrane, and is thereby required for the biosynthesis of complex sphingolipids . Required for survival in response to oxidative stress . Involved in the diauxic shift .
PTM: Acetylated at the... |
Q966A0 | MRLFHFLKFLTINNFSRYCLKIVKVHIIWITIICIIYFNWRFKKLDFMAIPYPPAVIKFNTSAKYLSSNLASSSQLGNNIFEIASLYGLSKHLNRTPLFFIENGYHKKMLDNLRKTMPRLMEKFRILNGSVPRSISETKFQRACCLHKSPWSLEKNRDEYLHLSGKYYQSWKYFPNMRNELIEFLNPTSIQIFGNLPISDDQNHVTCVHSRRGDFVEYLFYASDPKFMKNAVTFLNENEKVGSRNRKIVLFGDDLNFLETYFSDAVLSTDVGKNAEYYISQNPPIDDFLYSKNNCDVVLITAPRSTFGWWIGYFSKGNKV... | Function: Mediates the transfer of fucose to the terminal galactose on glycan chains of cell surface glycoproteins and glycolipids (By similarity). Required for axon regeneration after injury .
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 42570
Sequence Length: 364
Subcellular Location: G... |
Q17800 | MYIVIVTMRTILFFGIFFIFIFQCAKCIELKIFEDLLEVRSQSGLFFPLCSKSFHQKYGEQACASISSTFLSYSTVSLQQYTYSVGCTTSVCFTFLSSFCKTGVKVFCSPSLCASGTLQIGSKCLSISTVPVQGYSEANYYCNPATLISSLKPTEIESIRDTILPTFADTRLFLTSGLRQGATWKWGNGDTVEQEVTGTGRCLALQAGNLVAIDCDSEAYVFCESGRECIARDKEYSGTANRTSDGKMCLMWNDPTVLFRRERDLEILNHNFCRFVNDADGKKSATPVCYTKPNELSQCYIPPCPESFNDVVPIESGDSC... | Function: Serine protease which ensures proper pharyngeal pumping during larval growth by regulating the levels of extracellular matrix component fbl-1 . Independently of its enzymatic activity and probably by acting as a ligand for tyrosine-protein kinase receptor svh-2, involved in axon regeneration after injury by p... |
P0C0A9 | MGLCFPCPAESAPPSPSPEEKRAKLAEAAERRQKEAASRGILDIQSVEAKKKKKEQLEKQMETSGPPAGGLRWTVS | Function: Overexpression causes the formation of large vacuoles that seemed to be derived from the endoplasmic reticulum.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 8248
Sequence Length: 76
Subcellular Location: Smooth endoplasmic reticulum membrane
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O61122 | MASKKGDPEELYVRQEKIGKGSFGEVFKGINKKTNETIAIKTIDLEDAEDEIEDIQQEINVLSQCESPFVTKYFGSFLKGSKLWIIMEYLAGGSVLDLMKPGPFDEGYIAIILRELLKGLEYLHSEGKIHRDIKAANVLLSASGDVKLADFGVSGQLTDQMTKRNTFVGTPFWMAPEVIKQTGYDSKADIWSMGITALEMAKGEPPRADLHPMRALFLIPKDPPPTLEGNFSKGFKEFCALCLNKDPNQRPTAKDLLKHKFIKAAKKTSSLTDLIERRQKWLQLNGNNADDENDDLDRDAKSNEEDFGWEFPTIKQKSPV... | Function: Involved in regulation of actin cytoskeleton organization during cell motility; F-actin fragmenting and capping protein allowing dynamic rearrangements of the actin cytoskeleton. Also part of a regulatory pathway from the centrosome to the midzone, thus regulating the completion of cell division.
PTM: Autopho... |
P09959 | MALEEVVRYLGPHNEIPLTLTRDSETGHFLLKHFLPILQQYHDTGNINETNPDSFPTDEERNKLLAHYGIAVNTDDRGELWIELEKCLQLLNMLNLFGLFQDAFEFEEPETDQDEEDPSHSKLPENKTKSENSKDNISSKRINNLQDMSLDSDAHRELGSPLKKLKIDTSVIDAESDSTPNTARGKPNDDINKGPSGDNENNGTDDNDRTAGPIITFTHDLTSDFLSSPLKIMKALPSPVVNDNEQKMKLEAFLQRLLFPEIQEMPTSLNNDSSNRNSEGGSSNQQQQHVSFDSLLQEVNDAFPNTQLNLNIPVDEHGNT... | Function: Part of a complex involved in cell-cycle-dependent transcription. SWI4 and SWI6 are required for formation of the cell-cycle box factor-DNA complex. The repeated element in the upstream region of HO (5'-CACGAAAA-3') is called the cell cycle box (CCB).
PTM: Phosphorylated by CDC28 and dephosphorylated by CDC14... |
Q9ZSD4 | MNDLFSSSFSRFRSGEPSPRRDVAGGGDGVQMANPAGSTGGVNLDKFFEDVESVKEELKELDRLNETLSSCHEQSKTLHNAKAVKDLRSKMDGDVGVALKKAKMIKVKLEALDRANAANRSLPGCGPGSSSDRTRTSVLNGLRKKLMDSMDSFNRLRELISSEYRETVQRRYFTVTGENPDERTLDRLISTGESERFLQKAIQEQGRGRVLDTINEIQERHDAVKDIEKNLRELHQVFLDMAVLVEHQGAQLDDIESHVGRASSFIRGGTDQLQTARVYQKNTRKWTCIAIIILIIIITVVVLAVLKPWNNSSGGGGGGG... | Function: Vesicle trafficking protein that functions in the secretory pathway (By similarity). Together with SYP61, regulates the post-Golgi trafficking of the aquaporin PIP2-7 to the plasma membrane, thus modulating cell membrane water permeability .
Location Topology: Single-pass type IV membrane protein
Sequence Mas... |
Q6F3B4 | MNNLFSSSWKRTGGGGGGDGDIESGGGVEMAPPPGAAAGASLDRFFEDVESIKDELRDLERIQRSLHDANEGGKSLHDAAAVRALRARMDADVAAAIKKAKVVKLRLESLDRANAANRSVPGCGPGSSTDRTRTSVVAGLRKKLRDSMESFSSLRARISSEYRETVARRYYTVTGEQPDEATLDNLAETGEGERFLQRAIAEQGRGEVLGVVAEIQERHGAVAELERSLLELHQVFNDMAVLVAAQGEQLDDIETHVGRARSFVDRGREQLVVARKHQKSTRKWTCIAIIILLVLILVVVLPIVLKFVNNNKSSSSSPAP... | Function: Vesicle trafficking protein that functions in the secretory pathway . Involved in plant defense by mediating host resistance to the rice blast fungus Magnaporthe oryzae . The interaction with SNAP32 may contribute to host resistance to the rice blast fungus .
Location Topology: Single-pass type IV membrane pr... |
Q9SVC2 | MNDLLSGSFKTSVADGSSPPHSHNIEMSKAKVSGGSCHGGNNLDTFFLDVEVVNEDLKELDRLCHNLRSSNEQSKTLHNANAVKELKKKMDADVTAALKTARRLKGNLEALDRANEVNRSLPESGPGSSSDRQRTSVVNGLRKKLKDEMEKFSRVRETITNEYKETVGRMCFTVTGEYPDEATLERLISTGESETFLQKAIQEQGRGRILDTINEIQERHDAVKDIEKSLNELHQVFLDMAVLVEHQGAQLDDIEGNVKRANSLVRSGADRLVKARFYQKNTRKWTCFAILLLLIIVVLIVVFTVKPWESNGGGGGGAPR... | Function: Vesicle trafficking protein that functions in the secretory pathway.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 37837
Sequence Length: 341
Subcellular Location: Membrane
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Q9ZQZ8 | MNDLISSSFKRYTDLNHQVQLDDIESQNVSLDSGNLDEFFGYVESVKEDMKAVDEIHKRLQDANEESKTVHDSKAVKKLRARMDSSVTEVLKRVKMIKTKLVALEKSNAAQRKVAGCGPGSSADRTRTSVVSGLGKKLKDMMDDFQRLRTKMATEYKETVERRYFTVTGQKADEETVEKLISSGESERFLQKAIQEQGRGQVMDTLSEIQERHDTVKEIERSLLELHQVFLDMAALVEAQGNMLNDIESNVSKASSFVMRGTDQLHGAKVLQRNNRKWACIATILAIVVVIVILFPILFNTLLRP | Function: Vesicle trafficking protein that functions in the secretory pathway (Probable). Acts in coordination with SYP132 to mediate tip-focused membrane trafficking for root hair tip growth . Functions in root hair elongation by forming SNARE complexes with VAMP721,VAMP722 or VAMP724 .
Location Topology: Single-pass ... |
Q8VZU2 | MNDLLKGSFELPRGQSSREGDVELGEQQGGDQGLEDFFKKVQVIDKQYDKLDKLLKKLQASHEESKSVTKAPAMKAIKKTMEKDVDEVGSIARFIKGKLEELDRENLANRQKPGCAKGSGVDRSRTATTLSLKKKLKDKMAEFQVLRENIQQEYRDVVDRRVYTVTGERADEDTIDELIETGNSEQIFQKAIQEQGRGQVMDTLAEIQERHDAVRDLEKKLLDLQQIFLDMAVLVDAQGEMLDNIESQVSSAVDHVQSGNTALQRAKSLQKNSRKWMCIAIIILLIVVAVIVVGVLKPWKNKSA | Function: Vesicle trafficking protein that functions in the secretory pathway (Probable). Acts in coordination with SYP123 to mediate tip-focused membrane trafficking for root hair tip growth . Functions in root hair elongation by forming SNARE complexes with VAMP721,VAMP722 or VAMP724 . Involved in cytokinesis . Acts ... |
Q7XIE2 | MNNLLTDSFELPRGGSSRDGDIEMGMQADPSDNLKGFLKKVDAIESLIAKLTNLLHKLQTANEESKAVTKARDMKAIKQRMEKDIDEVGKIARMAKTKVDELEKDNLSNRQKPGCGKGSAVDRSREQTTGAVKKKLKERMDDFQVLREAIRQEYRDVVERRVFTVTGSRPDEETVDNLIETGRSEQIFQEAIQQQGRGQILDTVAEIQERHDAVRDLERKLLELQQIFMDMAVLVDAQGDMINNIETHVSNATNHIQQGVSALQNAKKLQKNSRKWMCYAIILLLIIVVIIVVAVIQPWKKGA | Function: Vesicle trafficking protein that functions in the secretory pathway (By similarity). Required for plant growth and seed development .
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 34250
Sequence Length: 303
Subcellular Location: Cell membrane
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P24505 | MKLTEAYHDALAALPATPPLPTAVANATEAAAGSEEGKQDGFSKVKVKEKFMNELNKIPLPPWALVAIAIVAIILGLTCCFCICKKCLLKKKNKKKGKEKGGKNAMTMKDVKEMGKSGKEQALKDEDEDAETGLTTDGKEEEKEDEKLGKLQFSLDYDFQNNQLIVGIIQAAELPALDVGGTSDPYVKVFVLPDKKKKYETKVHRKTLNPVFNESFIFKIPYSELGGKTLVMAVYDFDRFSKHDVIGEAKVPMNTVDFGHVTEEWRDLQGAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKI... | Cofactor: Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains.
Function: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head... |
P24507 | MSGDGEDELCRNALALVNELCFSVRGNHNNEKCIEFSYLLRDRDRTRHIETDISVSLLSVIVTFCGIVLLGVSLFVSWKLCWIPWRDKGLNPQRRDSQHHPHQHLHHHHSHFTDLTVERVDCGPEMPERSYLDLESYPESGIKLSQTSPDIPVDTSSGSKENNIPNAHSQQQVSAPPPATRFNSLPRPIPQQLSSPEFGTQADEKVEQVTSIGQIKPELYKQRSIDTEAKKHQKVNCGRINFMLRYTYTTEQLVVKILKALDLPAKDANGFSDPYVKIYLLPDRKKKFQTKVHRKTLNPIFNETFQFNVPFNELQNRKLH... | Cofactor: Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains.
Function: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head... |
P21521 | MPPNAKSETDAKPEAEPAPASEPAADLESVDQKLEETHHSKFREVDRQEQEVLAEKAAEAASQRIAQVESTTRSATTEAQESTTTAVPVIKKIEHVGEVVTEVIAERTGLPTWGVVAIIILVFLVVFGIIFFCVRRFLKKRRTKDGKGKKGVDMKSVQLLGSAYKEKVQPDMEELTENAEEGDEEDKQSEQKLGRLNFKLEYDFNSNSLAVTVIQAEELPALDMGGTSDPYVKVYLLPDKKKKFETKVHRKTLSPVFNETFTFKSLPYADAMNKTLVFAIFDFDRFSKHDQIGEVKVPLCTIDLAQTIEEWRDLVSVEGE... | Cofactor: Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains.
Function: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head... |
A9KMW7 | MKVYGVNELRKMYLDFFESKGHLKLNSFSLVPQNDKSLLLINSGMAPLKPYFTGQEIPPKKRVTTCQKCIRTGDIENIGKTARHGTFFEMLGNFSFGDYFKHEAIAWSWEFLTEVVGLSGDRLYPSIYLEDDEAFDIWNKEVGIAPERIFRMGKADNFWEHGAGPCGPCSEIYYDRGEKYGCGDPNCTVGCECDRFIEVWNNVFTQFNSDGNGNYEELENKNIDTGMGLERLAVVVQDVDTLFDIDTMKAIRDHVCKMANAEYKVDPKKDMSIRLITDHIRSVTFMTSDGIIPSNEGRGYVLRRLLRRAARHGRLLGIQG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
A9KLZ5 | MTANELRKMYVDYFKERGHQEIASASLLPENDPTVLFTTAGMHPLVPYLLGENHPKGTRLVSVQKCVRTGDIDEVGDDTHLTFFEMLGNWSLGEYFKEESISISYDFLTTCLNIPKEKLAVTVFEGDELVPRDEEVSQTWKSKGLQDNQIFYYGREENWWGPAGQTGPCGTDTEIFYDMGKPSCGVNCGPACDCGKYVEIWNNVFMQYHKKPDGSYEEMKQKNVDTGMGFERVLTILNGYTNVYETELFLPVKNRLDEIIEANEAKLSEKSKRIICEHIRAVTFLLGDPKMIVPSNSEQGYILRRLIRRMIRHLKQVSIE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (By si... |
O01541 | MKHLTASEVRSTFINFFREKKEHTYVHSSSVIPHDDPTLLFANAGMNQFKPLFLGIADPNSDLAKLKRAVNTQKCIRAGGKHNDLDDVGKDVYHHTYFEMLGNWSFGDYFKKEIITWAWELLTTVYGIPAERLYVSVFGGDEANGVPADSEARDIWRSVGVPDERILNFGMKDNFWEMGDVGPCGPCSEIHYDRIGNRDASHLVNADDPMVVEIWNLVFIQFNREEGGVLKPLPAKHIDCGLGLERLIAVMQDKTSNYDTDIFQPIFEAIHKGSGVRAYTGFIGDEDKDGVDMAYRVVADHVRTLTIALSDGGRPDNSGR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Catalytic Activity: ATP + L... |
A7ZQC5 | MSKSTAEIRQAFLDFFHSKGHQVVASSSLVPHNDPTLLFTNAGMNQFKDVFLGLDKRNYSRATTSQRCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKHDAIQFAWELLTSEKWFALPKERLWVTVYESDDEAYEIWEKEVGIPRERIIRIGDNKGAPYASDNFWQMGDTGPCGPCTEIFYDHGDHIWGGPPGSPEEDGDRYIEIWNIVFMQFNRQADGTMEPLPKPSVDTGMGLERIAAVLQHVNSNYDIDLFRTLIQAVAKVTGATDLSNKSLRVIADHIRSCAFLIADGVMPSNENRGYVLRRIIRRAVRH... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
Q3YSV8 | MKESNLVGDIRKLFVDFFIKNGHQLFPSSPLIVKDDPSLLFTNAGMVQFKHVFTDASNANVGTAVSSQKCLRVGGKHNDLENVGYTNRHHTFFEMLGNFSFGDYFKEFAVELAWSFVTKELALNKDKLYFTVYHEDQETFDLWKKISGFSENRIIKIKTNDNFWSMGSTGPCGPCSEIFYDYGEDIEGGLPGTPEEDGARFTEIWNLVFMQYNRKSDGELCALPKKCIDTGMGLERISAVMQGVHDNYDINLFKDLIKVSKKQSGNTNNELAHRVIADHVRSAAFLIAEGLTPGNEGRDYILRRIIRRAARYVYMLKYDG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Catal... |
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