ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P81103 | MAYTGLTVPLIVMSVFWGIVGFLVPWFIPKGPNRGVIITMLVTCSVCCYLFWLIAILAQLNPLFGPQLKNETIWYLKYHWP | 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... |
Q9BDP4 | MAYHGLTVPLIVMSVFWGFVGFCVPWFIPKGPNRGVIITMLVTCSVCCYLFWLIAILAQLNPLFGPQLKNETIWYLKYHWP | 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... |
O15342 | MAYHGLTVPLIVMSVFWGFVGFLVPWFIPKGPNRGVIITMLVTCSVCCYLFWLIAILAQLNPLFGPQLKNETIWYLKYHWP | 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 and in some ... |
Q84WW5 | MTTGDLVNIHPTELKFPFELKKQSSCSMQLTNKTTTQCVAFKVKTTNPRKYCVRPNTGVVLPGDSCNVTVTMQAQKEAPLDMQCKDKFLVQTVVVSDGTTSKEVLAEMFNKEAGRVIEDFKLRVVYIPANPPSPVPEGSEEGNSPMASLNDIASQSASLFDDVSRTFEETSEKSSEAWSMISKLTEEKTSATQQSQKLRLELEMLRKETSKKQSGGHSLLLMLLVGLLGCVIGYLLNRI | Function: May play a role in vesicle trafficking.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 26374
Sequence Length: 239
Subcellular Location: Endoplasmic reticulum membrane
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Q9SYC9 | MSTDELLTFDHVDIRFPIELNKQGSCSLNLTNKTDNYVAFKAQTTKPKMYCVKPSVGVVLPRSSCEVLVVMQALKEAPADRQCKDKLLFQCKVVEPGTMDKEVTSEMFSKEAGHRVEETIFKIIYVAPPQPQSPVQEGLEDGSSPSASVSDKGNASEVFVGPSVGIVDLIRMSDELLIIDPVDVQFPIELNKKVSCSLNLTNKTENYVAFKAKTTNAKKYYVRPNVGVVLPRSSCEVLVIMQALKEAPADMQCRDKLLFQCKVVEPETTAKDVTSEMFSKEAGHPAEETRLKVMYVTPPQPPSPVQEGTEEGSSPRASVS... | Function: May play a role in vesicle trafficking.
Catalytic Activity: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide
Sequence Mass (Da): 64407
Sequence Length: 571
Domain: The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
EC: 3.2.2.6
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Q06155 | TDIGGGLDVGGGLRGGLDIDAKGPDVDIKGPKVGGDISGPDLDVSGPDLDIDGGGKKGKGGFGFGLKMPKFGFGGHGKGDIDVDADVDIERPDLDVSGDADLPSGGVGLDVGGGIGGGLGGGLDIDANGPDVDIKGPKVGGDISGPDLDVSGPDLDIDVDGKKKGKGGFGFGMKMPKFGFGGHGKGDIDVDADVDIERPDLDVSGDADLPSGGVGLDVGGGIGGGLGGGLDIDANGPDVDIKGPKVGGDISGPDLDVSGPDLDIDVDGKKKGKGGFGFGLKIPKFMDPTFGFGGHGKGDIDVDADGGVVIPEGDIKVKTG... | Function: May function as a multidomain RNA-binding protein. May play a role in nuclear RNA processing and in early development.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42126
Sequence Length: 433
Subcellular Location: Microsome membrane
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Q9LVU1 | MTGVGENQLISIQPDELKFLFELEKQSYCDLKVANKTENYVAFKVKTTSPKKYFVRPNTGVIQPWDSCIIRVTLQAQREYPPDMQCKDKFLLQSTIVPPHTDVDELPQDTFTKDSGKTLTECKLKVSYITPSTTQRSSESGATNGDGQSSETISTIQRLKEERDAAVKQTQQLQHELETVRRRRNQRNSGNGLSLKLAAMVGLIGLIIGFILKLTLASPT | Function: May play a role in vesicle trafficking.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 24667
Sequence Length: 220
Subcellular Location: Endoplasmic reticulum membrane
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B9DHD7 | MNMPLLDIQPRTLQFAVDLKKQTSCVVQLTNTTHHYVAFKVKTTSPKKYCVRPNVGVVAPKSTCEFTVIMQAFKEPPPDMVCKDKFLIQSTAVSAETTDEDITASMFSKAEGKHIEENKLRVTLVPPSDSPELSPINTPKQGAVFEDSILKDRLYSQSETLAPPQYEGEIVKEPRMVGHDELKAADNAKELKTPKMATVDFVEDRYTANDLKATKDSYDSSRMAKETGFDPIRSHKDADDGRAIKATTNLDAPMKKAMDLPRDQGFTNGIAVDSEPKISKERDVVQLQKTDGQNVRGLDELKLVKDIEEMKLKVDALESK... | Function: May play a role in vesicle trafficking.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 43270
Sequence Length: 386
Subcellular Location: Endoplasmic reticulum membrane
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Q9P0L0 | MASASGAMAKHEQILVLDPPTDLKFKGPFTDVVTTNLKLRNPSDRKVCFKVKTTAPRRYCVRPNSGIIDPGSTVTVSVMLQPFDYDPNEKSKHKFMVQTIFAPPNTSDMEAVWKEAKPDELMDSKLRCVFEMPNENDKLNDMEPSKAVPLNASKQDGPMPKPHSVSLNDTETRKLMEECKRLQGEMMKLSEENRHLRDEGLRLRKVAHSDKPGSTSTASFRDNVTSPLPSLLVVIAAIFIGFFLGKFIL | Function: Endoplasmic reticulum-anchored protein that mediates the formation of contact sites between the endoplasmic (ER) and late endosomes via interaction with STARD3 . In addition, mediates recruitment of VAPA to plasma membrane sites through OSBPL3 binding . The OSBPL3-VAPA complex stimulates RRAS signaling which ... |
Q9Z270 | MASASGAMAKHEQILVLDPPSDLKFKGPFTDVVTTNLKLQNPSDRKVCFKVKTTAPRRYCVRPNSGVIDPGSIVTVSVMLQPFDYDPNEKSKHKFMVQTIFAPPNISDMEAVWKEAKPDELMDSKLRCVFEMPNENDKLNDMEPSKAVPLNASKQDGPLPKPHSVSLNDTETRKLMEECKRLQGEMMKLSEENRHLRDEGLRLRKVAHSDKPGSTSAVSFRDNVTSPLPSLLVVIAAIFIGFFLGKFIL | Function: Endoplasmic reticulum-anchored protein that mediates the formation of contact sites between the endoplasmic (ER) and late endosomes via interaction with STARD3. In addition, mediates recruitment of VAPA to plasma membrane sites through OSBPL3 binding. The OSBPL3-VAPA complex stimulates RRAS signaling which in... |
O23654 | MPAFYGGKLTTFEDDEKESEYGYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKTIARISGDVYIPRGVSVPALDKDCLWEFQPNKFVEGDTITGGDLYATVFENTLMNHLVALPPDAMGKITYIAPAGQYSLKDTVIELEFQGIKKSYTMLQSWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTMTLPDGREESVMKRTTLVANTSN... | Function: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Location Topology: Peripheral membrane protein
Seque... |
Q39442 | MPAVYGDRMTTFEDSEKESEYGYIRKVSGPVVVADGMNGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETGGLTVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKTIAKRSGDVYIPRGVSVPPLDKDTQWDFQPKKLGVGDLLTGGDLYAIVDENSLMQHHVVLPPDAMGKITYIAPAGNYTIQDTVLELEFQGVVKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAILGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTMTLPDGREESVMKRTTLVANTSN... | Function: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Sequence Mass (Da): 68548
Sequence Length: 623
EC: 7... |
Q0SP70 | MNTKGKVVGVNGNLVTIEVEGSVSMNEVLFVKTGGRNLKAEVIRVRGNEVDAQVFELTKGISVGDLVEFTDKLLTVELGPGLLTQVYDGLQNPLPELAIKCGFFLERGVYLRPLNKDKKWNFKKTSKVGDSVIAGDFLGFVIEGTVHHQIMIPFYKRDSYKIVEIVNDGDYSIDEQIAVIEDDSGMRHSITMSFHWPVKIPITNYKQRLIPSEPMLTQTRIIDTFFPVAKGGTFCIPGPFGAGKTVLQQVTSRNADVDIVIIAACGERAGEVVETLKEFPELIDPKTGKSLMDRTCIICNTSSMPVAAREASVYTAITIG... | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Sequence Mass (Da): 64012
Sequence Length: 575
EC: 7.1.2.2
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Q9XW92 | MAAESSYGFVYGVSGPVVTAEKMAGSAMYELVRVGHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIMGSIFDGIQRPLKDIADITQSIYIPKGVSTNALSREARWDFVVSKDLRVGGHVTGGDIIGTVDENLLIKHKILLPPSACGTITFVAPSGQYTVEDTLLELEFAGRKQKFSMLQIWPVRSPRPVTEKLAANNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEMSEVLRDFPELTMEVEGVTTSIMKRTALVANTSNMPVAAREASIYTGI... | Function: Catalytic subunit of the V1 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 ... |
Q9SDS7 | MTSRYWVVSLPVKDSASSLWNRLQEQISKHSFDTPVYRFNIPNLRVGTLDSLLALGDDLLKSNSFVEGVSQKIRRQIEELERISGVESNALTVDGVPVDSYLTRFVWDEAKYPTMSPLKEVVDNIQSQVAKIEDDLKVRVAEYNNIRGQLNAINRKQSGSLAVRDLSNLVKPEDIVESEHLVTLLAVVPKYSQKDWLACYETLTDYVVPRSSKKLFEDNEYALYTVTLFTRVADNFRIAAREKGFQVRDFEQSVEAQETRKQELAKLVQDQESLRSSLLQWCYTSYGEVFSSWMHFCAVRTFAESIMRYGLPPAFLACVL... | Function: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
PTM: P... |
Q9XXU9 | MSSATSGEYWLISVPGEKGANDAWDKLNRSTGNTSTNSKYLIPDLKVGTLDQLVGLSDDLSKLDTSAEAVIRKLVQYFTEVLEEDKSKIAENLVIGNKDMKTYVTKFQWEGAKYPLKQSLKVLSEIIGKQISQIDNDLKVKSLTYNNLKNALASMDRKTVGSLLTKDLADLVKADDFVLNSEYLQTVIVVVPKISVKEWEQKYATLSSMVVPGSSKLLTEEGEHALYTVTLFKKVIDEFKNTARENKFIVRDFVYDEETLKAGRTERDKLMAEKQRQYAPLIRWLKINFGEIFAAYIHIKALRVFVESVLRYGLPVNFQA... | Function: Subunit of the V1 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 (Probable). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments an... |
P50515 | MSTDLCPVYAPFFGVMGCTAAIVFASFGAAYGTAKAGVGISAMGVLRPDLIVKNTIPVVMAGIIAIYGLVVSVLISGNLKQILSLYSGFIQLGAGLSVGLAGLAAGFAIGIVGDAGVRGTAQQPRLFVAMILILIFAEVLGLYGLIVALLLNTRATDNVTC | Function: Proton-conducting pore forming 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... |
P25515 | MTELCPVYAPFFGAIGCASAIIFTSLGAAYGTAKSGVGICATCVLRPDLLFKNIVPVIMAGIIAIYGLVVSVLVCYSLGQKQALYTGFIQLGAGLSVGLSGLAAGFAIGIVGDAGVRGSSQQPRLFVGMILILIFAEVLGLYGLIVALLLNSRATQDVVC | Function: Proton-conducting pore forming 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 intracel... |
P59228 | MASTFSGDETAPFFGFLGAAAALVFSCMGAAYGTAKSGVGVASMGVMRPELVMKSIVPVVMAGVLGIYGLIIAVIISTGINPKAKSYYLFDGYAHLSSGLACGLAGLSAGMAIGIVGDAGVRANAQQPKLFVGMILILIFAEALALYGLIVGIILSSRAGQSRAE | Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16643
Sequence Length: 165
Subcellular Location:... |
C0HLB3 | MSYDLETAERAAYAPFFGYMGAASAQIFTVLGAAYGTAKSAVGICSMGVMRPELIMKSVIPVIMAGIIGIYGLVVAMVLKGKVTSASAGYDLNKGFAHLAAGLTCGLCGLGAGYAIGIVGDAGVRGTAQQPRLFVGMILILIFSEVLGLYGMIVALILGTS | Function: Proton-conducting pore forming 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... |
Q9Y874 | MAEIMADSELAPKFAPFIGMAGIAAAMIFGSAGAAYGTAKSGIGIAGVGTFRPDLIMKCLIPVVMSGIIAVYALVVAVLIAQDLGPPGSGQHYSLFNGFMHLACGLSVGLTGLAAGYCIGIVGDKGVRSFMLQSRIFVGMVLILIFGEVLGLYGLIVALILNTKSKG | Function: Proton-conducting pore forming 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... |
Q9URZ8 | MSSNLCPIYSSFFGFAGVCASMVFSCLGAGYGTALAGRGIAAVGAFRPEIVMKSLIPVVMSGIIGVYGLVMSVLIAGDMSPDNDYSLFSGFIHLSAGLAVGLTGVAAGYAIGVVGDRGVQSFMRQDRIFVSMVLILIFAEVLGLYGLIVGLILQTKTSNVCY | Function: Proton-conducting pore forming 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... |
P32842 | MSTQLASNIYAPLYAPFFGFAGCAAAMVLSCLGAAIGTAKSGIGIAGIGTFKPELIMKSLIPVVMSGILAIYGLVVAVLIAGNLSPTEDYTLFNGFMHLSCGLCVGFACLSSGYAIGMVGDVGVRKYMHQPRLFVGIVLILIFSEVLGLYGMIVALILNTRGSE | Function: Proton-conducting pore forming 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 intracel... |
P59229 | MASSGFSGDETAPFFGFLGAAAALVFSCMGAAYGTAKSGVGVASMGVMRPELVMKSIVPVVMAGVLGIYGLIIAVIISTGINPKAKSYYLFDGYAHLSSGLACGLAGLSAGMAIGIVGDAGVRANAQQPKLFVGMILILIFAEALALYGLIVGIILSSRAGQSRAE | Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16686
Sequence Length: 166
Subcellular Location:... |
P23957 | MSSVFSGDETAPFFGFLGAAAALVFSCMGAAYGTAKSGVGVASMGVMRPELVMKSIVPVVMAGVLGIYGLIIAVIISTGINPKAKPYFLFDGYAHLSSGLACGLAGLAAGMAIGIVGDAGVRANAQQPKLFVGMILILIFAEALALYGLIVGIILSSRAGQSRAD | Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16621
Sequence Length: 165
Subcellular Location:... |
Q9TT13 | MCNTPTYCDLGKAAKDVFNKGYGFGMVKIDLRTKSCSGVEFSTSGHAYTDTGKASGNLETKYKVCNYGLTFTQKWNTDNTLGTEISLENKLAEGLKLTLDTIFVPNTGKKSGKLKASYKRDCFSLGSNVDIDFSGPTIYGWAVLAFEGWLAGYQMSFDTAKSKLSQNNFALGYKAADFQLHTHVNDGTEFGGSIYQKVNEKIETSINLAWTAGSNNTRFGIAAKYKLDCRTSLSAKVNNASLIGLGYTQTLRPGVKLTLSALIDGKNFNAGGHKVGLGFELEA | Function: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules (By similarity). Involved in male fertility and sperm mitochondrial sheath formation (By similarity).
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitopha... |
Q9R1Z0 | MCSTPTYCDLGKAAKDVFNKGYGFGMVKIDLKTKSCSGVEFSTSGHAYTDTGKASGNLETKYKVCNYGLIFTQKWNTDNTLGTEISWENKLAEGLKLTVDTIFVPNTGKKSGKLKASYRRDCFSVGSKVDIDFSGPTIYGWAVLAFEGWLAGYQMSFDTAKSKLCQNNFALGYKAEDFQLHTHVNDGTEFGGSIYQRVNEKIETSINLAWTAGSNNTRFGIAAKYRLDCRTSLSAKVNNASLIGLGYTQSLRPGVKLTLSALVDGKNFNAGGHKVGLGFELEA | Function: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules (By similarity). Involved in male fertility and sperm mitochondrial sheath formation (By similarity).
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitopha... |
Q9FKM2 | MGSSPAPFADIGKKAKDLLNKDYIFDHKFTLTMLSATGTEFVATGLKKDDFFFGDISTLYKGQNTIVDLKIDSHSSVSTKVTLKNLLPSAKAVISFKIPDHKSGKLDVQYVHPHATLNSSIGLNPTPLLDLSATIGSQNVCLGGEVSFDTASSSLTKYNAGIGFNNQGVSAALILEDKGESLRATYVHTVNPTTSFGAELIRRFSNYNNSFTVGSSHSVDQFTVVKTRFSNSGKAGMVVQREWRPKSHITFSAEYDSKAVTSSPKLGLALALKP | Function: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state ... |
Q9M2W6 | MSKGPGLFADIGKYAKDLLTRDYSTDQKFSISTNSVSGVALTSTALKNGVLHAANVATQYKYRNTFFDVKIDTDFNVKSLVYPMNKFVSIDHNTLTGYDTTSRTFTKYNVGVSVTKPDQCVSIILGDKGDSIKASYVYYLDESTRSATVGEVIRKISTNETTVTVGGLYAVDHLTNVKAKLNSNGKFGALLQHEGLPKSIVTISGEIDTKTLDKYPRLGLSLSLKP | Function: Putative channel that allows diffusion of small hydrophilic molecules through membranes.
Sequence Mass (Da): 24631
Sequence Length: 226
Domain: Consists mainly of membrane-spanning sided beta-sheets.
Subcellular Location: Mitochondrion outer membrane
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Q84P97 | MAMKGPGLFSDIGKRAKDLLTKDYTYDQKLTVSTVSSSGVGLTSTAVKKGGLYTLDVSSVYKYKSTLVDVKVDTESNISTTLTVFDVLPSTKLVTSVKLPDYNSGKVEMQYFHENASFATAVGMKPSPVVEFSGTAGAQGLAFGAEAGFDTATGKFTKYSAAIGVTKPDYHAAIVLADKGDTVKVSGVYHLDDKQKSSVVAELTRRLSTNENTLTVGGLYKVDPETAVKARLNNTGKLAALLQHEVKPKSVLTISGEFDTKALDRPPKFGLALALRP | Function: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state ... |
Q10S27 | MSKGPAPFLNIGKRAKDLLYKDYNFDQKFSLTTTSNSGLGLTATGVKIDELFIGDIQTQHKSGKTTVDVKIDSESRVSTTVTVDEALTGLKTSFSFRVPDQKSGKLDLQYLHDHFALNSTIGLTSTPLIELAATIGTNELSAGAEVGFDSTSASVTKYNSGICYNKHDFSAAVLLADKGETLKASYIHTFNETNGATVAAEVTHKLKTKENYFTIGSSHAIDSSTLLKTRFSNGGKVGVLCQHEWRPKSTVSISAEYDPKVVSSPSRFGVAIALKP | Function: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state ... |
Q21752 | MAPPTFADLGKSAKDLFNKGYNFGFLKIDSTTRAGDNKEVEFKSAASHNIGSGKLGGNLDVKYKIPQYGITLTEKWNTENQLGTVIEVNEQFGRGLKVTLDSLYAPHAGKRSGKVKLDWALPTARVTADVGVTSAPVINAAGVFSRDGWLIGAAATFDSSSNKLAATSLAFGHSTPQYTLHSFVINSTDFGASLYHKVASNVEVGTQLGWKVGGNGADYALATKYAPSRDLTVRAKVNSSSQVAVAATHSLSPALKLTLSTQFNLAANDAHKFGLGLEFDPSN | Function: Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules (By similarity). Plays a role in maintaining mitochondrial morphology .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29961
Sequence Length: 283
Domain: Consists mainly of membrane-spanning side... |
Q01501 | MNPGLYADLTKPTADFIKKDFAETFKLDTTFKGKYGSIVAVTDIKDSGVVASIQPKADFTKYLGKVSNGNFTVDTNGVKKGEFTIENIIPGLKAVANGDSKQNFSTEFQYKKDKIAFTLFGHNNKSFNTSLAFLINPTFSVGVQAEGNAKNTLKNVNATITIRPRPDVFVSIVDRFMDKQILLSTLYTATSKLSFAGDVTVDLKASEKAPSFNVGTQYKIDSASLLKAKVNNNRKVNISYIYNTSNNTKFVLGWNVNTKNFKQGNTFGATVNLTL | Function: Forms a channel of about 1,7 nM through the cell membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 20 mv. The open state has a weak anion selectivity whereas the closed state is... |
P82945 | VPPVYADLGKGARDLFSKGYNYGFSKL | Function: Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules.
Sequence Mass (Da): 2963
Sequence Length: 27
Domain: Consists mainly of membrane-spanning sided beta-sheets.
Subcellular Location: Mitochondrion outer membrane
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Q94920 | MAPPSYSDLGKQARDIFSKGYNFGLWKLDLKTKTSSGIEFNTAGHSNQESGKVFGSLETKYKVKDYGLTLTEKWNTDNTLFTEVAVQDQLLEGLKLSLEGNFAPQSGNKNGKFKVAYGHENVKADSDVNIDLKGPLINASAVLGYQGWLAGYQTAFDTQQSKLTTNNFALGYTTKDFVLHTAVNDGQEFSGSIFQRTSDKLDVGVQLSWASGTSNTKFAIGAKYQLDDDASVRAKVNNASQVGLGYQQKLRDGVTLTLSTLVDGKNFNAGGHKIGVGLELEA | Function: Forms a channel through the mitochondrial outer membrane and also the plasma membrane (By similarity). The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis (By similarity). It adopts an op... |
P42057 | MVVAVGLYTDIGKKTRDLLYKDYNTHQKFCLTTSSPNGVAITAAGTRKNESIFGELHTQIKNKKLTVDVKANSESDLLTTITVDEFGTPGLKSIINLVVPDQRSGKLEFQYLHEYAGVNASVGLNSNPMVNLSGAFGSKALSVGVDVSFDTATSDFTKYNAALSLTSPDLIASLHLNNHGDTLVASYYHLVKNHSGTAVGAELSHSMSRNESTLIFGSQHSLDPHTTIKTRFNNYGMASALVQHEWRPKSFVTISGDVDTKAIEKSTKVGLSLVLKH | Function: Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selec... |
P07144 | MAVPAFSDIAKSANDLLNKDFYHLAAGTIEVKSNTPNNVAFKVTGKSTHDKVTSGALEGKFTDKPNGLTVTQTWNTANALETKVEMADNLAKGLKAEGIFSFLPATNARGAKFNLHFKQSNFHGRAFFDLLKGPTANIDAIVGHEGFLAGASAGYDVQKAAITGYSAAVGYHAPTYSAAITATDNLSVFSASYYHKVNSQVEAGSKATWNSKTGNTVGLEVATKYRIDPVSFVKGKINDRGVAAIAYNVLLREGVTLGVGASFDTQKLDQATHKVGTSFTFES | Function: Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selec... |
Q9P544 | MAPPAYAAINKLCNDLLQRDFPVGATLLSVRTTAPNGVVFNVSGNQDAKGVISGKLETSFNDKANGLTISQGWTTANVLESKVGLSEQFAPGLHLNVNTTFSPATAAKTAILNLEHQHPLIHTHASVNALERKFLGDFTVGHEGFLAGAEFGYDVQKGNVSNYAATIGYLASPLSVALQASNNLSVFRASYYHRVSSDVEAGGNVTWDAASTANAITLELASKYALDKDTFVKGKINSAGVATLSYFQTVRPGVTVGLGLQLDTQRLGQPAHKAGLSLAFSA | Function: Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules.
Sequence Mass (Da): 29653
Sequence Length: 282
Domain: Consists mainly of membrane-spanning sided beta-sheets.
Subcellular Location: Mitochondrion outer membrane
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Q80930 | MTQMETQETLSARFLAQQDIQLNLIEKDSKNLKDHIDYWESMRKEQVLAFYAKKENMSRLGLQPLPPAKVSEQKAKDAIRIQLLLQSLYKSDFGSEPWTLSECSLEMLNAPPRNCFKKQPFTVTVQFDNDPKNVYPYICYEYIYYQDDRDKWHKVKGLVDHNGLYFKEVTGDSVYFKLFQPDATVYGKSGQWTVIFKNKTIHSSVTSSSRSAFGPADEQPGPSTSYDKSQQERSGSGQPKALQDTEPPTSTSTVRLRRGRREREHHSYRHRKSQSELGADSAPTPEEVGRRSHTVAAHGLSRLRRLQEEARDPPVLIITG... | Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding t... |
P36796 | MESIPARLNAVQEKILDLYEADSNDLNAQIEHWKLTRMECVLFYKAKELGITHIGHQVVPPMAVSKAKACQAIELQLALEALNKTQYSTDGWTLQQTSLEMWRAEPQKYFKKHGYTITVQYDNDKNNTMDYTNWKEIYLLGECECTIVEGQVDYYGLYYWCDGEKIYFVKFSNDAKQYCVTGVWEVHVGGQVIVCPASVSSNEVSTTETAVHLCTETSKTSAVSVGAKDTHLQPPQKRRRPDVTDSRNTKYPNNLLRGQQSVDSTTRGLVTATECTNKGRVAHTTCTAPIIHLKGDPNSLKCLRYRVKTHKSLYVQISST... | Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding t... |
P36797 | METLCQRLDACQEKILDCFERDSKNITDHIDYWKAVRQENVIYYKARENNMTKLGHQVVPCLQVCKAKACVAIELQIALESLCKTEYNMEEWTLRDVCESMWYTEPKQCFKKQGQHIEVWFDGSKDNRAEYVVWKWVYYCGEDGWCKVSSAVSYEGIYYIHDGHKTYYTNFKDEATKYGCKGTWEVHMGKQSIYCPDSVSSTFRSNVSSVETVNEYYSHKTPTTSTPVGTYEASSSLRPGKRPRTTEPDSTDSTTQSTTTARESYAECVARNTDNTNNNTRKHLPGGASCNNTEIDSGYKTAPVVHIKGEANRLKCLRYR... | Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding t... |
Q81021 | METLATRLDVCQERLLDLYEKDSNKLEDQIEHWKCIRLECALQYKAREMGYKVLQHQALPALAVSKGKGHKAIELQLALETLQKTVYSTEPWTLQDTCLERWNAPPTGCLKRRGQTVDVIFDGHQDNTMQYVMWGDIYYQNCDGEGWTKVCSNIDAMGIYYMDAEHKVYYVDFKKEASKYGEYGQWEVRMGSSIIFSPASVSSTEEALSISSTGTAEHTRPANSTPRTDNSTKAIPCTPPPRKRARVYSTDQQPHSTSDPVGCDNDRHISDDNNKNQGRHTSSGDTTPIVHFKGEPNTLKCFRQRIQKYKHLFEQASSTW... | Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding t... |
Q80937 | METIAKHLDVCQEQLLELYEENSNNLTKHIQHWKCIRYECVLLHKAKQMGLNHIGMQVVPALTVSQTKGHQAIEMQMTLETLLNSDYGMEPWTLQDTSREMWLTAPKYCFKKQGQTVEVKYDCNADNIMEYVSWKYIYVHDTDKWVKVTGHIDYKGLYYVHGGHKTYYTNFEKEAKKYGNSLQWEVCIGSSVICSPASISSTVQDVSIAGPASHTSSSTTTTLAQASPALPTCTSEERVDPPPCKRPRGPTTNTNNARDTVSVRHSDSVDSTNNNIYPNSYNSNKGRDNNFCTATPVVQLQGDPNCLKCLRYRLHAKHKT... | Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding t... |
Q80944 | MNQADLTERSDALQEQILNLYEQDSKDIQAQIQYWDLNRKLYVTYYYARKEGYSHLGLQPLPALQVSEYKAKQAIEMGLLLTSLSKSQYASELWGLTDTSAELLLTPPRNTFKKKGYTVNVWFDNNENNTFPYTNWEYIYYQDDIEQWHRTRGEVDYNGLYFTENNGNRAYFLLFDSDAQTYSQTGTWTVHYKNQIISAPVTSSSKQSSDDYTSKAGQQPHFFASSSSPTTTDGGQTSQEGVSSSTTSPSAVRLRRRRSNEQQRELSSRESPRTKRRRVPDEVDRQSAVGSAPTAEEVGSRHRSLPRSGISRLARLQGEA... | Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding t... |
Q80951 | MRMESLADRLDACQEKLLDLYEKDSNKLEDQILHWHYVRLENAMLFKARQAGLTRVGHQMVPTLSVTKGKAHKAIEVHLSLQGLQTSAYAHEPWTLQTTSLEMWNTQPQRCWKKKGRRLTVKFDGEDHKAVEYVSWGYIYVQSTETDLWYKVPGKVSYKGLYYEMEGQEHYYVTFAQEAQKYGETGKWEVHMGNTVIYEPCASVSSTQDAVREVSTAETAGHLRDNTTQTTTTPTCVGPTQTSTSVQTPPHKRQRLHRDREQQPDTTQKDNHKRVDSTDQWINGHRNSTETGDNCDSYSSPVIHLKGDPNKLKCFRYRLQ... | Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding t... |
Q89759 | MIGQCATLLDIVLTEQPEPIDLQCYEQLPSSDEEEEEEEPTEKNVYRIEAACGFCGKGVRFFCLSQKEDLRVLQVTLLSLSLVCTTCVQTAKLDHGG | Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating ... |
P03130 | MIGRTPKLSELVLGETAEALSLHCDEALENLSDDDEEDHQDRQVFIERPYAVSVPCKRCRQTISFVCVCAPEAIRTLNRLLSASLSLVCPECCN | Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating ... |
Q07857 | MRGAAPTVADLNLELNDLVLPANLLSEEVLQSSDDEYEITEEESVVPFRIDTCCYRCEVAVRITLYAAELGLRTLEQLLVEGKLTFCCTACARSLNRNGR | Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating ... |
P06932 | MIGKEVTVQDIILELSEVQPEVLPVDLFCEEELPNEQETEEEPDNERISYKVIAPCGCRNCEVKLRIFVHATEFGIRAFQQLLTGDLQLLCPDCRGNCKHDGS | Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating ... |
P06465 | MVGEMPALKDLVLQLEPSVLDLDLYCYEEVPPDDIEEELVSPQQPYAVVASCAYCEKLVRLTVLADHSAIRQLEELLLRSLNIVCPLCTLQRQ | Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating ... |
P04020 | MHGRLVTLKDIVLDLQPPDPVGLHCYEQLEDSSEDEVDKVDKQDAQPLTQHYQILTCCCGCDSNVRLVVECTDGDIRQLQDLLLGTLNIVCPICAPKP | Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating ... |
P03129 | MHGDTPTLHEYMLDLQPETTDLYCYEQLNDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPICSQKP | Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating ... |
P06788 | MHGPKATLQDIVLHLEPQNEIPVDLLCHEQLSDSEEENDEIDGVNHQHLPARRAEPQRHTMLCMCCKCEARIKLVVESSADDLRAFQQLFLNTLSFVCPWCASQQ | Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating ... |
A0A1V6NYL5 | MSTAVNTIRCSLLLLGLVGIYTVWISSFRNGLFLRNEEFAGKGQLPGTPNATLRTHFTGIDTLDKALGIFVVFYWPVCQGNLRSLSLIAFPAAVGVGEMWILFALQFSQSNSPTRAMGKMAMFGMGLMLVGPGIFLPIYCSLDLSSTHRLDDSPSSAAEGHLCRNLRSCLLGGYYILVILLALPSPAVVSYGSKQGIIALLQGWPLLVSAMLWLTHLCGKDRTADFQATLSTARTSIYISAMACATISHLVPLLISLLADSSDICPGKVFVPHLAWPSRRVTSVEEGLLRFFQWDYGLGSLALLLWAVGLHIQRRQQISQ... | Function: Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the neurotoxin verrucosidin, a methylated alpha-pyrone polyketide that inhibits oxidative phosphorylation in mitochondria and thereby causes neurological diseases . The carbon backbone of verrucosidin is synthesized by the HR-PKS verA... |
Q40316 | MAEGKGRVCVTGGTGFLGSWIIKSLLENGYSVNTTIRADPERKRDVSFLTNLPGASEKLHFFNADLSNPDSFAAAIEGCVGIFHTASPIDFAVSEPEEIVTKRTVDGALGILKACVNSKTVKRFIYTSSGSAVSFNGKDKDVLDESDWSDVDLLRSVKPFGWNYAVSKTLAEKAVLEFGEQNGIDVVTLILPFIVGRFVCPKLPDSIEKALVLVLGKKEQIGVTRFHMVHVDDVARAHIYLLENSVPGGRYNCSPFIVPIEEMSQLLSAKYPEYQILTVDELKEIKGARLPDLNTKKLVDAGFDFKYTIEDMFDDAIQCC... | Function: Stereospecific enzyme that catalyzes the NADPH-dependent reduction of (3R)-vestitone to (3R,4R)-4'-methoxyisoflavan-2',4,7-triol (DMI). Has no activity with (3S)-vestitone. Catalyzes the penultimate step in the biosynthesis of the phytoalexin medicarpin, and thereby contributes to plant defense reactions.
Cat... |
Q38065 | MSGVVAVQVCTAWTSTPEGFMACRELAWQQAYLIPPEAAGYVDILVNGGFSPEAFGIGAAGVLGSFVTGLLIGWVASLLRKAK | Function: May play a role in phage assembly.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8618
Sequence Length: 83
Subcellular Location: Host membrane
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O15240 | MKALRLSASALFCLLLINGLGAAPPGRPEAQPPPLSSEHKEPVAGDAVPGPKDGSAPEVRGARNSEPQDEGELFQGVDPRALAAVLLQALDRPASPPAPSGSQQGPEEEAAEALLTETVRSQTHSLPAPESPEPAAPPRPQTPENGPEASDPSEELEALASLLQELRDFSPSSAKRQQETAAAETETRTHTLTRVNLESPGPERVWRASWGEFQARVPERAPLPPPAPSQFQARMPDSGPLPETHKFGEGVSSPKTHLGEALAPLSKAYQGVAAPFPKARRPESALLGGSEAGERLLQQGLAQVEAGRRQAEATRQAAAQ... | Function: Secreted polyprotein that is packaged and proteolytically processed by prohormone convertases PCSK1 and PCSK2 in a cell-type-specific manner (By similarity). VGF and peptides derived from its processing play many roles in neurogenesis and neuroplasticity associated with learning, memory, depression and chroni... |
P20156 | MKTFTLPASVLFCFLLLIRGLGAAPPGRSDVYPPPLGSEHNGQVAEDAVSRPKDDSVPEVRAARNSEPQDQGELFQGVDPRALAAVLLQALDRPASPPAVPAGSQQGTPEEAAEALLTESVRSQTHSLPASEIQASAVAPPRPQTQDNDPEADDRSEELEALASLLQELRDFSPSNAKRQQETAAAETETRTHTLTRVNLESPGPERVWRASWGEFQARVPERAPLPPSVPSQFQARMSENVPLPETHQFGEGVSSPKTHLGETLTPLSKAYQSLSAPFPKVRRLEGSFLGGSEAGERLLQQGLAQVEAGRRQAEATRQA... | Function: Secreted polyprotein that is packaged and proteolytically processed by prohormone convertases PCSK1 and PCSK2 in a cell-type-specific manner . VGF and peptides derived from its processing play many roles in neurogenesis and neuroplasticity associated with learning, memory, depression and chronic pain (By simi... |
P01136 | MSMKYLMLLFAAMIIRSFADSGNAIETTSPEITNATTDIPAIRLCGPEGDGYCLHGDCIHARDIDGMYCRCSHGYTGIRCQHVVLVDYQRSENPNTTTSYIPSPGIMLVLVGIIIITCCLLSVYRFTRRTKLPIQDMVVP | Function: Stimulates cellular proliferation (hyperplasia)and mobility around infected cells to promote rapid and efficient spread of infection. This effect is beneficial for virus replication in vivo, because poxviruses replicate possibly better in proliferating cells than in quiescent cells. Acts by binding host EGFR,... |
P12504 | MENRWQVMIVWQVDRMRINTWKRLVKHHMYISRKAKDWFYRHHYESTNPKISSEVHIPLGDAKLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPDLADQLIHLHYFDCFSESAIRNTILGRIVSPRCEYQAGHNKVGSLQYLALAALIKPKQIKPPLPSVRKLTEDRWNKPQKTKGHRGSHTMNGH | Function: Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyu... |
Q2YJ78 | MFGRKQSPQKSVKNGQGNAPSVYDEALNWEAAHVRLVEKSERRAWKIAGAFGTITVLLGIGIAGMLPLKQHVPYLVRVNAQTGAPDILTSLDEKSVSYDTVMDKYWLSQYVIARETYDWYTLQKDYETVGMLSSPSEGQSYASQFQGDKALDKQYGSNVRTSVTIVSIVPNGKGIGTVRFAKTTKRTNETGDGETTHWIATIGYQYVNPSLMSESARLTNPLGFNVTSYRVDPEMGVVQ | Function: The virB operon is essential for intracellular survival and is not involved in the invasion process. Constitutes a major determinant of virulence in mice.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26446
Sequence Length: 239
Subcellular Location: Cell inner membrane
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P0A3W6 | MTRKALFILACLFAAATGAEAEDTPMAGKLDPRMRYLAYNPDQVVRLSTAVGATLVVTFATNETVTSVAVSNSKDLAALPRGNYLFFKASQVLTPQPVIVLTASDSGMRRYVFSISSKTLSHLDKEQPDLYYSVQFAYPADDAAARRREAQQRAVVDRLHAEAQYQRKAEDLLDQPVTALGATDSNWHYVAQGDRSLLPLEVFDNGFTTVFHFPGNVRIPSIYTINPDGKEAVANYSVKGSDVEISSVSRGWRLRDGHTVLCIWNAAYDPVGQRPQTGTVRPDVKRVLKGAKG | Function: Is essential for the biogenesis of the T-pilus, which is required for virulence and T-DNA transfer to plant cells. When is associated with virB7, might function as a nucleation center for recruitment of VirB proteins during assembly of the T-DNA transfer machine.
Location Topology: Peripheral membrane protein... |
P17800 | MNDDNQQSAHDVDASGSLVSDTHHRRLSGAQKLIVGGVVLALSLSLIWLGGREKKENGDAPPSTMIATNTKPFHPAPIDVTLDPPAAQEAVQPTAPPPARSEPERHEPRPEETPIFAYTSGDQGTSKRVQQGETDRRREGNGEDSPLPKVEVSAENDLSIRMKPTELQPTRATLLPHPDFMVTEGTIIPCILQTAIDTSLAGYVKCVLPWDVRGTTNNVVLLDRGTTVVGEIQRGLQQGDARVFVLWDRAETPDHAMISLASPSADELGRSGLPGTVDNHFWQRFSGAMLLSVVQGAFQAASTYAGSSGGGTSFNSVQNN... | Function: VirB proteins are suggested to act at the bacterial surface and there play an important role in directing T-DNA transfer to plant cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 40555
Sequence Length: 377
Subcellular Location: Cell inner membrane
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Q6G2B2 | MNDPMDENNLLNDRDMIKDGHGKKQRPNTSKAAALVILFGVCLYLAYSTLFTEKQQPVEVQKEGIIKQTELFRPAPPKPVSLEPTIEKNNVLLPKVELPTPPKKTTNSDDSLLEAAQRAPVLAYANTQKGQGSTEKNKDISANQPEAKPDETAQRFNHLLKPTTLEGIRAAKLGNRNYIIAMGASIPCILETAISSDQQGFASCIVSRDILSDNGRVVLLDKGTQIVGEYRAGLKKGQKRLFVLWNRAKTPNGIIITLASPATDALGRSGMDGDIDNHWLERIGSALLVSIVKDATNYVKGRLPKDQDKNNSETISSGQN... | Function: The type IV secretion system VirB/VirD4 is a major virulence determinant for subversion of human endothelial cell (HEC) function. VirB-dependent changes of HEC include massive cytoskeletal rearrangements, a pro-inflammatory activation by nuclear factor NF-kappa-B, inhibition of early and late events of apopto... |
Q80925 | MSLRRRKRASPTDLYKTCLQGGDCIPDVKNKFENSTIADWLLKIFGSLVYFGNLGIGSGKGSGGSFGYRPLGSAGSGRPATDLPVTRPNVVIEPIGPQSIVPIDPGASSIVPLVEGGPDISFIAPDAGPGIGGEDIELFTFRDPATDVGGVSGGPTTISTEESETAIIDALPSATTPKQLFYDSYTQTILQTQVNPFLNNAISDTNVFVDPLFAGETIGDNIFEEIPLQNLNFSFPRESTPVKPGRGLRTPAQRSYSRFMEQYPIQAPEFLSQPSRLVQFEFENPAFDPDISIQFQRDVNSLEAAPNPAFADIAYLSRPH... | Function: Minor protein of the capsid that localizes along the inner surface of the virion, within the central cavities beneath the L1 pentamers. Plays a role in capsid stabilization through interaction with the major capsid protein L1. Once the virion enters the host cell, L2 escorts the genomic DNA into the nucleus b... |
Q80932 | MLRRRKRASPTDLYRSCLQGGDCIPDVQNKFEGNTIADWLLKIFGGLVYFGNLGIGTGRGTGGTFGYRPFGAPGSGRPTQELPIARPNVVIDPLGPAPIVPVDPSAASIVPLVEGAPDVGFAAPDAGPAAGGTDIELYTITNSTTDVGAVGGGPTVTSNEEFEVAVIDAQPIAPYPKQLLYDSTIAATFETQINPFINPDINNVNVLVDPSFAGDTVGDYFYEEIPLERLDIQTFDILEPPTESTPTQLGNRFVSRARDLYSRFVAQQPISEPDFLSQPSRLVQFEYRNPAFDPDVSLYFERDLEGLRAAPLQEFADVVY... | Function: Minor protein of the capsid that localizes along the inner surface of the virion, within the central cavities beneath the L1 pentamers. Plays a role in capsid stabilization through interaction with the major capsid protein L1. Once the virion enters the host cell, L2 escorts the genomic DNA into the nucleus b... |
Q80946 | MYARVKRVKRDSVENLYKQCQLGADCPPDVRNKVEGTTLADRLLQIFGSILYLGNLGIGTGKGSGGATGYTPLGTARVPASTPGTVIKPTRPFSVPLDPIGSGIPSQPVGGRLPVDIIDASASSIIPLQEVLPETTIIVGGDSGPGLGASEIDIVSEPRPDVVGVDTQPTVYTSIDNTVATLDITPATPPVKKIILDPISSGSEGAAAITFSDISAADLNVFVDPQGAGDRISFGEEIELGPINQPAQFEIEEPPRTSTPGEGFQRVTTRARELYNRFVQQQPTQNIDFLGRPSRAVQFEFENPAFFNDEVTMQFEQDLQ... | Function: Minor protein of the capsid that localizes along the inner surface of the virion, within the central cavities beneath the L1 pentamers. Plays a role in capsid stabilization through interaction with the major capsid protein L1. Once the virion enters the host cell, L2 escorts the genomic DNA into the nucleus b... |
O93516 | NEYQTYLTDRNPQCILNEPLRTDTVSTPVSGNELLEAGKECDCGAPANPCCDAATCKLRPGEQCAEGLCCDQCRFMKEGTICQEAKGDWNDDTCTGQSADCPRNGFYG | Cofactor: Binds 1 zinc ion per subunit.
Function: Impairs hemostasis in the envenomed animal.
Sequence Mass (Da): 11726
Sequence Length: 108
Subcellular Location: Secreted
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P54219 | MLRTILDAPQRLLKEGRASRQLVLVVVFVALLLDNMLFTVVVPIVPTFLYDMEFKEVNSSLHLGHAGSSPHALASPAFSTIFSFFNNNTVAVEESVPSGIAWMNDTASTIPPPATEAISAHKNNCLQGTGFLEEEITRVGVLFASKAVMQLLVNPFVGPLTNRIGYHIPMFAGFVIMFLSTVMFAFSGTYTLLFVARTLQGIGSSFSSVAGLGMLASVYTDDHERGRAMGTALGGLALGLLVGAPFGSVMYEFVGKSAPFLILAFLALLDGALQLCILQPSKVSPESAKGTPLFMLLKDPYILVAAGSICFANMGVAILE... | Function: Electrogenic antiporter that exchanges one cationic monoamine with two intravesicular protons across the membrane of secretory and synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to accumulate high concentrations of monoamines inside the vesicles prior ... |
Q8R090 | MFQVVLGAPQRLLKEGRQSRKLVLVVVFVALLLDNMLLTVVVPIVPTFLYATEFKDINSSLLRGPSVSSQQALTSPAFSTTFSFFDNTTMTVEEHVPFRVAWINGTIPPPVTEAGSVPKNNCLQGIEFLEEENVRIGILFASKALMQLLVNPFVGPLTNRIGYHIPMFVGFMIMFLSTLMFAFSGTYALLFVARTLQGIGSSFSSVAGLGMLASVYTDNYERGRAMGIALGGLALGLLVGAPFGSVMYEFVGKSSPFLILAFLALLDGALQFCILWPSKVSPESAMGTPLLTLLKDPYILVAAGSICLANMGVAILEPTL... | Function: Electrogenic antiporter that exchanges one cationic monoamine with two intravesicular protons across the membrane of secretory and synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to accumulate high concentrations of monoamines inside the vesicles prior ... |
Q05940 | MALSELALVRWLQESRRSRKLILFIVFLALLLDNMLLTVVVPIIPSYLYSIKHEKNATEIQTARPVHTASISDSFQSIFSYYDNSTMVTGNATRDLTLHQTATQHMVTNASAVPSDCPSEDKDLLNENVQVGLLFASKATVQLITNPFIGLLTNRIGYPIPIFAGFCIMFVSTIMFAFSSSYAFLLIARSLQGIGSSCSSVAGMGMLASVYTDDEERGNVMGIALGGLAMGVLVGPPFGSVLYEFVGKTAPFLVLAALVLLDGAIQLFVLQPSRVQPESQKGTPLTTLLKDPYILIAAGSICFANMGIAMLEPALPIWMM... | Function: Electrogenic antiporter that exchanges one cationic monoamine with two intravesicular protons across the membrane of secretory and synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to accumulate high concentrations of monoamines inside the vesicles prior ... |
Q8BRU6 | MALSDLVLLRWLRDSRHSRKLILFIVFLALLLDNMLLTVVVPIIPSYLYSIKHEKNTTEIQTARPALTASTSESFHSIFSYYNNSTVFTGNATGGLPGGESPKATTTQHTVTNTTVPPDCPSEDKDLLNENVQVGLLFASKATVQLLTNPFIGLLTNRIGYPIPMFAGFCIMFISTVMFAFSSSYAFLLIARSLQGIGSSCSSVAGMGMLASVYTDDEERGNAMGIALGGLAMGVLVGPPFGSVLYEFVGKTAPFLVLAALVLLDGAIQLFVLQPSRVQPESQKGTPLTTLLKDPYILIAAGSICFANMGIAMLEPALPI... | Function: Electrogenic antiporter that exchanges one cationic monoamine with two intravesicular protons across the membrane of secretory and synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to accumulate high concentrations of monoamines inside the vesicles prior ... |
Q01827 | MALSDLVLLRWLRDSRHSRKLILFIVFLALLLDNMLLTVVVPIIPSYLYSIKHEKNSTEIQTTRPELVVSTSESIFSYYNNSTVLITGNATGTLPGGQSHKATSTQHTVANTTVPSDCPSEDRDLLNENVQVGLLFASKATVQLLTNPFIGLLTNRIGYPIPMFAGFCIMFISTVMFAFSSSYAFLLIARSLQGIGSSCSSVAGMGMLASVYTDDEERGKPMGIALGGLAMGVLVGPPFGSVLYEFVGKTAPFLVLAALVLLDGAIQLFVLQPSRVQPESQKGTPLTTLLKDPYILIAAGSICFANMGIAMLEPALPIWM... | Function: Electrogenic antiporter that exchanges one cationic monoamine with two intravesicular protons across the membrane of secretory and synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to accumulate high concentrations of monoamines inside the vesicles prior ... |
A3EXG9 | MSNNCTNTVPRPEVIAALKDWNFAVSVILLFITVLLQWGYPSRCKPIWVIKMFILWLLWPLSIAAAVFAAIHPINSVAFGFAIAFACISGIMWLSYFISSFRLLCRTGSAWSFMPETDMLINIPLLGRTVTRPIISDSPAVQFLIIRGELRFDGFTLGRCDPGDMPDIVTIARPNALHWYKRALTRNMYTRSAILVYIKYKVGNHRVQNTTEDGDRLAMFVA | Function: Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25138
Sequence Length: 222
Subcellular Location: Virion membrane
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P06492 | MDLLVDELFADMNADGASPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSALPTNADLYRECKFLSTLPSDVVEWGDAYVPERTQIDIRAHGDVAFPTLPATRDGLGLYYEALSRFFHAELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRDRDLGEMLRATIADRYYRETARLARVLFLHLYLFLTREILWAAYAEQMMRPDLFDCLCCDLESWRQLAGLFQPFMFVNGALTVRGVPIEARRLRELNHIREHLNLPLVRSAATEEPGAPLT... | Function: In the early stage of viral replication, acts as a transcriptional activator of immediate-early (IE) gene products (alpha-genes), which is released by invading virions . Recruits P-TEFb to the viral alpha-gene promoters and overcomes transcriptional inhibition by ICP22 to promote transcription of IE genes . V... |
P27389 | MPFGLIVIGIILAIAAYRDTLGELFSIIKDVSKDAKGFGYWVLAAVILGFAASIKPIKEPVNAFMILLMIVLLIRKRGAIDQISNQLRGS | 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: Multi-pass membrane protein
Sequence Mass (D... |
P17462 | MAYRKRGATVEADINNNDRMQEKDDEKQDQNNRMQLSDKVLSKKEEVVTDSQEEIKIRDEVKKSTKEESKQLLEVLKTKEEHQKEIQYEILQKTIPTFEPKESILKKLEDIKPEQAKKQTKLFRIFEPRQLPIYRANGEKELRNRWYWKLKKDTLPDGDYDVREYFLNLYDQVLTEMPDYLLLKDMAVENKNSRDAGKVVDSETASICDAIFQDEETEGAVRRFIAEMRQRVQADRNVVNYPSILHPIDYAFNEYFLQHQLVEPLNNDIIFNYIPERIRNDVNYILNMDRNLPSTARYIRPNLLQDRLNLHDNFESLWDT... | Function: Inner capsid protein that self-assembles to form an icosahedral capsid with a T=2 symmetry, which consists of 120 copies of VP2, with channels at each of its five-fold vertices. This capsid constitutes the innermost concentric layer of the viral mature particle . It encapsidates the polymerase VP1, the cappin... |
Q9E7N7 | MDSESLDFSSADTVILRSPNAGTNPDGHPDTVECPDFDTDIPKTSDDSSKMDNKGSSSSSKAVKDLLELAAKSQGIVVTDVMQNTAIALHHNLGLDASSLDWFVAGITFANNSMIMEKMVSAIKELQIEVRNIQVASSGIKGTSEELVSKMKANKNDIVKELVKTRDSVLSAMGGILSAPEIEQQPVKTVTIGASQGRRKSTVVPPIEINPELESPVLSKTVSTATPEERIRHEKEKLLADLDWEIGEIAQYTPLIVDFLVPDDILAMAADGLTPELKEKIQNEIIENHIALMALEEYSS | Function: Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA (By similarity).
PTM: Phosphorylated by host kinases.
Seque... |
B2BNE4 | MGNVQTSTNVYNIDGNGNTFAPSSQMASTASPAIDLKPGVLNPTGKLWQTMGTGAPSADSLVLVVDNKGEYTYLSENMRETLNKAVTDVNMWQPLFQATKSGCGPVVLANFTTISTGYVGATADDAFSNGLVSNGPFLATMHIMELQKTIAARMRDVAIWQKHLDTAMTLMTPDVSAGDVTCKWRSLLEFAQDILPLDNLCRSYPNEFYTVAAQRYPAIRPGQPDTQVALPQPHPLGEVAGSFNAPTSEVGSLVGAGAALSDAISTLASKDLDLVEADTPLPVSVFTPSLAPRTYRPAFIDPQDAAWIAQWNGDANIRII... | Function: Interacts with VP7 to form the outer icosahedral capsid with an incomplete T=13 symmetry, about 80 nm in diameter, and consisting of 200 VP4-VP7 trimers. Myristoylated N-terminal peptide may be released in the endosome and involved in permeabilization and delivery of transcriptionally active viral particles i... |
Q45UF2 | MLLFIILSVGVDAISYIQNDRSNDLCIVYEMTSFGTSFNNANDSLVKLHKHMGLKYEVCKIESNANALTQMQKCNCIYDDTPQIVVFTNFKKSSLKTLIGTENKCELLPQTTIYTPTVDIESEYFIYGNDVKICYLDKNLLGIGCDATDTTSWLDLDAGLPTNHALDIPEITSDGFKLFAKYSDSFLCQRLMDEPKKQIQFYAEVDNVPSNDVIESSRSWASVWKVVKTVLHFTYHILDLFYGNRRATARMIEHSPLG | Function: Outer capsid protein involved in attachment and possibly entry into the host epithelial cell. It is subsequently lost, together with VP4, following virus entry into the host cell. The outer layer contains 780 copies of VP7, grouped as 260 trimers. Rotavirus attachment and entry into the host cell probably inv... |
O94753 | MSFKTLSALALALGAAVQFASAAVPLVQKRATCDDGRTTANAACCILFPILDDIQENLFDGAQCGEEVHESLRLTFHDAIGFSPTLGGGGADGSIIAFDTIETNFPANAGIDEIVSAQKPFVAKHNISAGDFIQFAGAVGVSNCPGGVRIPFFLGRPDAVAASPDHLVPEPFDSVDSILARMGDAGFSPVEVVWLLASHSIAAADKVDPSIPGTPFDSTPGVFDSQFFIETQLKGRLFPGTADNKGEAQSPLQGEIRLQSDHLLARDPQTACEWQSMVNNQPKIQNRFAATMSKMALLGQDKTKLIDCSDVIPTPPALVG... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase.
Catalytic Activity: 1-(4-hydroxy-3-methoxyphenyl)-2-(2-met... |
P30628 | MGDYVTPGEEPPQPGIYRSEQMCLAQLYLQSDASYQCVAELGELGLVQFRDLNPDVSSFQRKYVNEVRRCDEMERKLRYLEREIKKDQIPMLDTGENPDAPLPREMIDLEATFEKLENELREVNKNEETLKKNFSELTELKHILRKTQTFFEEVDHDRWRILEGGSGRRGRSTEREETRPLIDIGDMDDDSAARMSAQAAMLRLGFVAGVIQRERLPAFERLLWRACRGNVFLRTSEIDDVLNDTVTGDPVNKCVFIIFFQGDHLKTKVKKICEGFRATLYPCPDTPQERREMSIGVMTRIEDLKTVLGQTQDHRHRVLV... | 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... |
Q93050 | MGELFRSEEMTLAQLFLQSEAAYCCVSELGELGKVQFRDLNPDVNVFQRKFVNEVRRCEEMDRKLRFVEKEIRKANIPIMDTGENPEVPFPRDMIDLEANFEKIENELKEINTNQEALKRNFLELTELKFILRKTQQFFDEMADPDLLEESSSLLEPSEMGRGTPLRLGFVAGVINRERIPTFERMLWRVCRGNVFLRQAEIENPLEDPVTGDYVHKSVFIIFFQGDQLKNRVKKICEGFRASLYPCPETPQERKEMASGVNTRIDDLQMVLNQTEDHRQRVLQAAAKNIRVWFIKVRKMKAIYHTLNLCNIDVTQKCLI... | 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 transports protons across cellular membranes. V-ATPase is responsible for the acidification of various organelles, such as lyso... |
Q9Z1G4 | MGELFRSEEMTLAQLFLQSEAAYCCVSELGELGKVQFRDLNPDVNVFQRKFVNEVRRCEEMDRKLRFVEKEIRKANIPIMDTGENPEVPFPRDMIDLEANFEKIENELKEINTNQEALKRNFLELTELKFILRKTQQFFDEAELHHQQMADPDLLEESSSLLEPNEMGRGAPLRLGFVAGVINRERIPTFERMLWRVCRGNVFLRQAEIENPLEDPVTGDYVHKSVFIIFFQGDQLKNRVKKICEGFRASLYPCPETPQERKEMASGVNTRIDDLQMVLNQTEDHRQRVLQAAAKNIRVWFIKVRKMKAIYHTLNLCNID... | 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 the acidification of various organelles, such as lysosomes, e... |
Q9SJ40 | MYQLRKFDFFEEKYGGKIPEDVTGDIQCCSSGRGKVVIGSNDGSVSFLDRGVKFDSGFQAHSSSVLFLQHLKQRNFLVTVGEDEQISPQQSGMCLKVFDLDKVQEEGTSSSAPECIGILRIFTNQFPEAKITSFLVLEEVPPILLIAIGLDNGCIYCVKGDIARERITRFKLQVDGRSAITGLGFRMDGQALLLFAVTPESVNLFSMQAQPPKLQTLDHIGGSVNTVTMSDRSELIVGRPEAVYFYEVDGRGPCWAFEGEKKFMGWFRGYLLCVIDDSKTGNTVFNVYDLRNRLIAYSIVVDKVSNMLCEWGNIILIKAD... | Function: Involved in regulating membrane fusion at the tonoplast and the prevacuolar compartment.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 105713
Sequence Length: 932
Subcellular Location: Vacuole membrane
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Q09600 | MTEFGWRRFNFFDRSVVFDKDDPKQKFMGLKDVAVDCWCSSGGSVYLGEAKGGVFQLTNQFSEYYWKAYQKSLASLHSADKYLFSIGEDDETVNTLLKIWDPERVEKNTPHVMRTIRMSPLNPTSSSPACSIAVHSSLQSVVVGYTDGTVLFYQGDVLHDKSLNSRWIKVRDSSVGEGSVTGLAIAVLPASKTVVFVITQKHVHSYVLENGRTVIAHKKHDANGATADCWTFDESTGQLIVASREMLFFYDADQCIDMDGGEVGRCLQLGRGHEKLQLVASGQYLALLTKHHSLIQKERDSEFMTMLSVYDIKGQYVGFS... | Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport pathways . Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the rab-5-to-rab-7 endosome conversion pro... |
Q54YP4 | MNNWKRFTFFDIETVKQVEKEDGSSLQKLSITCTTSGRGSLIIGDAEGFINFVDREFGISSFQAYQQSVSLIYQLKERNFLSSVGHDDIGGAAILKIWNLDKTDKNEQPICVRSIKLEKSVTVTCFTLLEDLSQIIVGLANGEIIIIRADIFRDKVIKQKIIKVPNDSPITGLGFFPTKSQQSASAGAVLFVVTTTHVITYHTAHKDQETIIDDEGGDIGSFLMSDDGSPIIARSDAIYFYNVDGRGPCFGFTGVKTKVLWFRSYLVVIGYDTNNTNALFPGAVVGGQNSIGGLGSQTGSIGSPSVMVQNTKNNVLNIYD... | Function: May play a role in vesicle-mediated protein trafficking.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 108280
Sequence Length: 952
Subcellular Location: Vacuole membrane
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Q9H270 | MAAYLQWRRFVFFDKELVKEPLSNDGAAPGATPASGSAASKFLCLPPGITVCDSGRGSLVFGDMEGQIWFLPRSLQLTGFQAYKLRVTHLYQLKQHNILASVGEDEEGINPLVKIWNLEKRDGGNPLCTRIFPAIPGTEPTVVSCLTVHENLNFMAIGFTDGSVTLNKGDITRDRHSKTQILHKGNYPVTGLAFRQAGKTTHLFVVTTENVQSYIVSGKDYPRVELDTHGCGLRCSALSDPSQDLQFIVAGDECVYLYQPDERGPCFAFEGHKLIAHWFRGYLIIVSRDRKVSPKSEFTSRDSQSSDKQILNIYDLCNKF... | Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome co... |
Q60V75 | MKESTRTSTPSSGAKPKGDREICLRPSSSVFLGDQQLYFTQEYLATNSLNMKYVVYFAACQFSGPIAVIYAAPKSWFIWIRTISGRILKRDLPCTDPVFIDWTRAHCLLVLSKNGRAQVLSSIGEKVSEVFFDNQVSDVHECRTFATSRGDSGIAVMDVDGQVAVVNSVSEPVIWSMRPPYSELPTAWTAFQPHSQLTHILLIFEAVFLMGCQGESLQVQNHASVWVDSSTKYVKCVVDDARSRIAMMTENGKIQIVSIDLSTCFCTVEVTEHEIGKCINFGWVGNSVVFVQMSSSLTVFVNVSARRKPGDEVRFMSIKM... | Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the rab-5-to-rab-7 endosome conversion prob... |
Q11182 | MGESHAPSKPKLDGELCLRPSSSVFLGDQQLYFTQEYLRTNSLNLKYVVYFTACQFSGPIAVAYSPRPASWYIWIRTISGRILKRDMAFNEPVFMEWTRAHCLLVLNKAGRAHIFSSLGEKISEVIFDSQMSDVHECRTFATSRGDSGIAVMDVDGQVSVVNSVSEPVIWSMKPPYSEMPTAWTAFQPHSQLTHILLIFEAVFLMGCQGESLREQSHAASWVDSNTKYVKCVVDDARSRIAMMTESGKIQIVSIDLSTCFCTVEITDHDIAKCINFGWVGNSAVFVQMSPSLIVFVNVSARRKPGDEVQIYEKMTANAKI... | Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport pathways . Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the rab-5-to-rab-7 endosome conversion pro... |
Q55C58 | MIAAQWKIIGNSTYIKKEIYSMSWDVDLKQQVSVGSPFAGPIAVMRDSSKFVEMNSQNMKPYLKIFTASGDLISQMIWDSSKNIVAMDWIEKERLVIVLQNATVLIFNVFCEQMTQFSLGDIVREEEILECKIWSDGIVVLTSASQLYSVPSINDFFVESGRVIRLPPLPEEPKARPEWAILEPQFSLSQSIEIFMSINGTLYLIDEDKVESQLEATEPIQKMVVSPCGKKLACFDTKGTLLILKTDGSTTNPDRMDTKATKSPVLKWCGSDGVMMYWDSIKDPILFYFSKGDSWAKFTLDQPVSLVTEIDGLRIISDTT... | Function: May play a role in vesicle-mediated protein trafficking to endosomal/lysosomal compartments and in membrane docking/fusion reactions.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 94870
Sequence Length: 832
Subcellular Location: Endosome membrane
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Q9H269 | MDCYTANWNPLGDSAFYRKYELYSMDWDLKEELRDCLVAAAPYGGPIALLRNPWRKEKAASVRPVLDIYSASGMPLASLLWKSGPVVSLGWSAEEELLCVQEDGAVLVYGLHGDFRRHFSMGNEVLQNRVLDARIFHTEFGSGVAILTGAHRFTLSANVGDLKLRRMPEVPGLQSAPSCWTVLCQDRVAHILLAVGPDLYLLDHAACSAVTPPGLAPGVSSFLQMAVSFTYRHLALFTDTGYIWMGTASLKEKLCEFNCNIRAPPKQMVWCSRPRSKERAVVVAWERRLMVVGDAPESIQFVLDEDSYLVPELDGVRIFS... | Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome co... |
P08805 | MSILQIVAIVAIIVALILAIVVWTIVYIEYKRLLRQRKIDWLIDRIRERAEDSGNESEGDTEELSTLVEMEPDNFRNDNDM | Function: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion buddi... |
P08807 | NQSERAEDSGNESDGDKDELSTLVEMGHHAPWDIDDM | Function: Enhances virion budding, by targeting human CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its receptor human CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion bu... |
P08806 | TIVFIEYRKIRKEKKIEYLIDRIRERAEDSGNESEGDTGELAKLVEMGDFDPWVGDNL | Function: Enhances virion budding, by targeting human CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its receptor human CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion bu... |
P17286 | MTLLVGLVLILVGLIAWNICIWGYIIKWGYRRYKRHRLETEIERLNLILRERAEDSGNESNGEEEERLEQLIHNYNHNNHFANPMFDL | Function: Enhances virion budding, by targeting human CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its receptor human CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion bu... |
Q1A244 | MLLLIKLGFIGLAIETLIVIVVWAIVYRIYREVKVEEKISQLRQRIRDRAEDSGNESDGDAEELANLLPPDRIDQDNWV | Function: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion buddi... |
Q1A262 | MDIVQQVGLLVVLIIELVIVIVIWVKVYKLCKEDRRQKKIDRLIARIRERAEDSGNESDGDTEELQDLITEGDNLMHIGIRDNRNN | Function: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion buddi... |
Q8AIH6 | MIKIVVGSVSTNVIGILCILLILIGGGLLIGIGIRRELERERQHQRVLERLARRLSIDSGVEEDEEFNWNNFDPHNYNPRDWI | Function: Enhances virion budding, by targeting human CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its receptor human CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion bu... |
P92127 | MLLTAFYVVLGSFAAPCQQDGDHIVTCQVNKCETVGLFEICTECKTGGVPVDGFCRPFGSIQAAAAGCTKADGTALDKTATTCGKCGDGYFLFMGGCYKTESQPGSEICTTASNGLCTACKVDSQYIFQNKATPSEKGSECILCWDTTDRNGVMGVANCATCTAPASSTGPATCTECMAGTYKKSDTECAACHSDCATCSGEANNQCTSCETGKYLKSNQCVEKNTCNTNHYPDDTSMTCVACTVLDANCATCSFDSATAKGKCLTCNSNKIPRTTLDGTSTCVENSYAGCQGADNELFMKEDQSACLLCGDTKEASNDK... | PTM: O-glycosylated. The major glycan is a trisaccharide with Glc at the reducing terminus.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 70857
Sequence Length: 687
Subcellular Location: Cell membrane
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