ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
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 compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 9304
Sequence Length: 81
Subcellular Location: Membrane
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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 compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 9364
Sequence Length: 81
Subcellular Location: Membrane
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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 cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 9374
Sequence Length: 81
Subcellular Location: Membrane
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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 | MSTDELLTFDHVDIRFPIELNKQGSCSLNLTNKTDNYVAFKAQTTKPKMYCVKPSVGVVLPRSSCEVLVVMQALKEAPADRQCKDKLLFQCKVVEPGTMDKEVTSEMFSKEAGHRVEETIFKIIYVAPPQPQSPVQEGLEDGSSPSASVSDKGNASEVFVGPSVGIVDLIRMSDELLIIDPVDVQFPIELNKKVSCSLNLTNKTENYVAFKAKTTNAKKYYVRPNVGVVLPRSSCEVLVIMQALKEAPADMQCRDKLLFQCKVVEPETTAKDVTSEMFSKEAGHPAEETRLKVMYVTPPQPPSPVQEGTEEGSSPRASVSDNGNASEAFVDMLRSLLVPLFSNAASSTDDHGITLPQYQVFINFRGDELRNSFVGFLVKAMRLEKINVFTDEVELRGTNLNYLFRRIEESRVAVAIFSERYTESCWCLDELVKMKEQMEQGKLVVVPVFYRLNATACKRFMGAFGDNLRNLEWEYRSEPERIQKWKEALSSVFSNIGLTSDIRRYNLINKNMDHTSEFLYIVLILNFFSEISDMTGLTTSYQFLLMMKSNLISYDIYIYPTKFCVNVFIGV | 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 | TDIGGGLDVGGGLRGGLDIDAKGPDVDIKGPKVGGDISGPDLDVSGPDLDIDGGGKKGKGGFGFGLKMPKFGFGGHGKGDIDVDADVDIERPDLDVSGDADLPSGGVGLDVGGGIGGGLGGGLDIDANGPDVDIKGPKVGGDISGPDLDVSGPDLDIDVDGKKKGKGGFGFGMKMPKFGFGGHGKGDIDVDADVDIERPDLDVSGDADLPSGGVGLDVGGGIGGGLGGGLDIDANGPDVDIKGPKVGGDISGPDLDVSGPDLDIDVDGKKKGKGGFGFGLKIPKFMDPTFGFGGHGKGDIDVDADGGVVIPEGDIKVKTGKPDIGGDVDLPSGGVDLDVGGGIGGGLGGGLDIDAKGPDVDIKGPRVGGDISGPDLDVSGPDLDIDGDGKKKGKGGFGFGLKMPKFGFGGHGKGDIDVDADVDIERPDLNVSG | 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 | MNMPLLDIQPRTLQFAVDLKKQTSCVVQLTNTTHHYVAFKVKTTSPKKYCVRPNVGVVAPKSTCEFTVIMQAFKEPPPDMVCKDKFLIQSTAVSAETTDEDITASMFSKAEGKHIEENKLRVTLVPPSDSPELSPINTPKQGAVFEDSILKDRLYSQSETLAPPQYEGEIVKEPRMVGHDELKAADNAKELKTPKMATVDFVEDRYTANDLKATKDSYDSSRMAKETGFDPIRSHKDADDGRAIKATTNLDAPMKKAMDLPRDQGFTNGIAVDSEPKISKERDVVQLQKTDGQNVRGLDELKLVKDIEEMKLKVDALESKLKQADSTISKLMEERSISSQHRQSLQHELAELRTKKIVKEVHNGFPLLYVCVVAFIAYVIGHFLRT | 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 in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface . With OSBPL3, may regulate ER morphology . May play a role in vesicle trafficking .
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 27893
Sequence Length: 249
Subcellular Location: Endoplasmic reticulum membrane
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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 turn attenuates integrin beta-1 (ITGB1) activation at the cell surface. With OSBPL3, may regulate ER morphology (By similarity). May play a role in vesicle trafficking .
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 27841
Sequence Length: 249
Subcellular Location: Endoplasmic reticulum membrane
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O23654 | MPAFYGGKLTTFEDDEKESEYGYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKTIARISGDVYIPRGVSVPALDKDCLWEFQPNKFVEGDTITGGDLYATVFENTLMNHLVALPPDAMGKITYIAPAGQYSLKDTVIELEFQGIKKSYTMLQSWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTMTLPDGREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEKFDPDFINIRTKAREVLQREDDLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERAAGMDGQKITYTLIKHRLGDLFYRLVSQKFEDPAEGEDTLVEKFKKLYDDLNAGFRALEDETR | 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
Sequence Mass (Da): 68812
Sequence Length: 623
Subcellular Location: Vacuole membrane
EC: 7.1.2.2
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Q39442 | MPAVYGDRMTTFEDSEKESEYGYIRKVSGPVVVADGMNGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETGGLTVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKTIAKRSGDVYIPRGVSVPPLDKDTQWDFQPKKLGVGDLLTGGDLYAIVDENSLMQHHVVLPPDAMGKITYIAPAGNYTIQDTVLELEFQGVVKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAILGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTMTLPDGREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSGSRWAEALREISGRLAEMPADSGYPAYLAARLASFYEAAGKVKCLGGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSGALESFYEKFDSEFIDIRTKAREVLQREDDLNEIVQLVGKDALAETDKITLDTAKLLREDYLAQNAFTAYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGSDGQKITYSLIKLRLGDLFYRLVSQKFEDPAEGEDALVAKFKKLNEDLTAAFRNLEDETR | 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: 7.1.2.2
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Q0SP70 | MNTKGKVVGVNGNLVTIEVEGSVSMNEVLFVKTGGRNLKAEVIRVRGNEVDAQVFELTKGISVGDLVEFTDKLLTVELGPGLLTQVYDGLQNPLPELAIKCGFFLERGVYLRPLNKDKKWNFKKTSKVGDSVIAGDFLGFVIEGTVHHQIMIPFYKRDSYKIVEIVNDGDYSIDEQIAVIEDDSGMRHSITMSFHWPVKIPITNYKQRLIPSEPMLTQTRIIDTFFPVAKGGTFCIPGPFGAGKTVLQQVTSRNADVDIVIIAACGERAGEVVETLKEFPELIDPKTGKSLMDRTCIICNTSSMPVAAREASVYTAITIGEYYRQMGLDILLLADSTSRWAQAMREMSGRLEEIPGEEAFPAYLESVIASFYERAGIVVLNNGDIGSVTVGGSVSPAGGNFEEPVTQATLKVVGAFHGLTRERSDARKFPAISPLESWSKYKGVIDSKKTEYVRSFLVKGNEINQMMKVVGEEGISNEDFLIYLKSELLDSCYLQQNSFDSIDAAVNSERQNYMFDIVYNILKTNFEFSDKLQARDFINELRQNLLDMNLSSFKDSKFNKLEHTLSELVNFKKVI | 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 | MAAESSYGFVYGVSGPVVTAEKMAGSAMYELVRVGHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIMGSIFDGIQRPLKDIADITQSIYIPKGVSTNALSREARWDFVVSKDLRVGGHVTGGDIIGTVDENLLIKHKILLPPSACGTITFVAPSGQYTVEDTLLELEFAGRKQKFSMLQIWPVRSPRPVTEKLAANNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEMSEVLRDFPELTMEVEGVTTSIMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGRVKCLGSPEREGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSEYMRALEEFYEKNYPEFVSLRTKCKEILQEEEDLSEIVQLVGKASLAESDKVTLEVAKIIKDDFLQQNGYTKYDRFCPFYKTVGMLKNMIGFYDLARHAVEATAQSDNKITWNVIKDSMGDLIYQLSAMKFKDPVADGEAKIRKDYEDLAEAMANAFRNLED | 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 compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Required along with other vacuolar ATPase components for the removal of protein aggregates which form in immature oocytes in the distal gonad . This removal occurs as the oocytes mature and move to the proximal gonad, is triggered by the introduction of sperm through mating and occurs before fertilization . The introduction of sperm triggers V-ATPase accumulation in proximal oocytes and induces lysosomal acidification which leads to engulfing of protein aggregates by lysosomes and subsequent clearance of the aggregates . Lysosomal acidification also leads to changes in mitochondrial morphology and function . Mitochondria in distal immature oocytes are fragmented, produce high levels of reactive oxygen species (ROS) and have high membrane potential, indicative of metabolic inactivity . In contrast, mitochondria in proximal mature oocytes are tubular with lower ROS levels and membrane potential, indicative of an active metabolic state required for aggregate mobilization before clearance . Involved in receptor-mediated endocytosis .
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Sequence Mass (Da): 66460
Sequence Length: 606
EC: 7.1.2.2
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Q9SDS7 | MTSRYWVVSLPVKDSASSLWNRLQEQISKHSFDTPVYRFNIPNLRVGTLDSLLALGDDLLKSNSFVEGVSQKIRRQIEELERISGVESNALTVDGVPVDSYLTRFVWDEAKYPTMSPLKEVVDNIQSQVAKIEDDLKVRVAEYNNIRGQLNAINRKQSGSLAVRDLSNLVKPEDIVESEHLVTLLAVVPKYSQKDWLACYETLTDYVVPRSSKKLFEDNEYALYTVTLFTRVADNFRIAAREKGFQVRDFEQSVEAQETRKQELAKLVQDQESLRSSLLQWCYTSYGEVFSSWMHFCAVRTFAESIMRYGLPPAFLACVLSPAVKSEKKVRSILERLCDSTNSLYWKSEEDAGAMAGLAGDSETHPYVSFTINLA | 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: Phosphorylated on Ser/Thr residues by WNK8.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42619
Sequence Length: 375
Subcellular Location: Vacuole membrane
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Q9XXU9 | MSSATSGEYWLISVPGEKGANDAWDKLNRSTGNTSTNSKYLIPDLKVGTLDQLVGLSDDLSKLDTSAEAVIRKLVQYFTEVLEEDKSKIAENLVIGNKDMKTYVTKFQWEGAKYPLKQSLKVLSEIIGKQISQIDNDLKVKSLTYNNLKNALASMDRKTVGSLLTKDLADLVKADDFVLNSEYLQTVIVVVPKISVKEWEQKYATLSSMVVPGSSKLLTEEGEHALYTVTLFKKVIDEFKNTARENKFIVRDFVYDEETLKAGRTERDKLMAEKQRQYAPLIRWLKINFGEIFAAYIHIKALRVFVESVLRYGLPVNFQAAVIEPAKGQQKKLRQELHKLYIHLDGSAAGPIDTLEDSPALMSLGVNEYYPYVFFKLNIDFLNK | 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 and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). 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 (By similarity). Has roles in embryogenesis and ovulation .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 43459
Sequence Length: 384
Subcellular Location: Cytoplasm
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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 pH of intracellular compartments (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16326
Sequence Length: 161
Subcellular Location: Vacuole membrane
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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 intracellular compartments .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16351
Sequence Length: 160
Subcellular Location: Vacuole membrane
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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: Vacuole membrane
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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 pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Involved in necrotic cell death . Required along with other vacuolar ATPase components for the removal of protein aggregates which form in immature oocytes in the distal gonad . This removal occurs as the oocytes mature and move to the proximal gonad, is triggered by the introduction of sperm through mating and occurs before fertilization . The introduction of sperm triggers V-ATPase accumulation in proximal oocytes and induces lysosomal acidification which leads to engulfing of protein aggregates by lysosomes and subsequent clearance of the aggregates . Lysosomal acidification also leads to changes in mitochondrial morphology and function . Mitochondria in distal immature oocytes are fragmented, produce high levels of reactive oxygen species (ROS) and have high membrane potential, indicative of metabolic inactivity . In contrast, mitochondria in proximal mature oocytes are tubular with lower ROS levels and membrane potential, indicative of an active metabolic state required for aggregate mobilization before clearance .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16410
Sequence Length: 161
Subcellular Location: Membrane
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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 pH of intracellular compartments (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17029
Sequence Length: 167
Subcellular Location: Vacuole membrane
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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 pH of intracellular compartments (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16785
Sequence Length: 162
Subcellular Location: Vacuole membrane
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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 intracellular compartments .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17037
Sequence Length: 164
Subcellular Location: Vacuole membrane
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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: Vacuole membrane
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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: Vacuole membrane
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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 mitophagy. Deubiquitinated by USP30.
Sequence Mass (Da): 30652
Sequence Length: 283
Domain: Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands.
Subcellular Location: Mitochondrion outer membrane
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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 mitophagy. Deubiquitinated by USP30.
Sequence Mass (Da): 30798
Sequence Length: 283
Domain: Consists mainly of a membrane-spanning beta-barrel formed by 19 beta-strands.
Subcellular Location: Mitochondrion outer membrane
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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 is cation-selective (By similarity). Involved in plant growth and development at the vegetative and reproductive stages. Is important for leaf and pollen development and mitochondrial membrane potential steady state. May be involved in disease resistance.
Sequence Mass (Da): 29505
Sequence Length: 274
Domain: Consists mainly of membrane-spanning sided beta-sheets.
Subcellular Location: Cell membrane
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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 is cation-selective (By similarity).
Sequence Mass (Da): 29475
Sequence Length: 277
Domain: Consists mainly of membrane-spanning sided beta-sheets.
Subcellular Location: Mitochondrion outer membrane
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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 is cation-selective (By similarity).
Sequence Mass (Da): 29683
Sequence Length: 276
Domain: Consists mainly of membrane-spanning sided beta-sheets.
Subcellular Location: Mitochondrion outer membrane
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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 sided beta-sheets.
Subcellular Location: Mitochondrion outer membrane
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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 cation-selective.
Sequence Mass (Da): 30158
Sequence Length: 275
Domain: Consists mainly of membrane-spanning sided beta-sheets.
Subcellular Location: Mitochondrion outer membrane
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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 open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (By similarity). The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity). In depolarized mitochondria, acts downstream of park to promote mitophagy or prevent apoptosis; polyubiquitination by park promotes mitophagy, while monoubiquitination by park decreases mitochondrial calcium influx which ultimately inhibits apoptosis .
PTM: Ubiquitinated . Undergoes monoubiquitination and polyubiquitination by park; monoubiquitination at Lys-273 inhibits apoptosis, whereas polyubiquitination at Lys-11, Lys-19, Lys-52 and Lys-109 may promote mitophagy .
Sequence Mass (Da): 30550
Sequence Length: 282
Domain: Consists mainly of membrane-spanning sided beta-sheets.
Subcellular Location: Mitochondrion outer membrane
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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-selective (By similarity).
Sequence Mass (Da): 29977
Sequence Length: 277
Domain: Consists mainly of membrane-spanning sided beta-sheets.
Subcellular Location: Plastid outer membrane
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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-selective.
Sequence Mass (Da): 30000
Sequence Length: 283
Domain: Consists mainly of membrane-spanning sided beta-sheets.
Subcellular Location: Mitochondrion outer membrane
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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 | MTQMETQETLSARFLAQQDIQLNLIEKDSKNLKDHIDYWESMRKEQVLAFYAKKENMSRLGLQPLPPAKVSEQKAKDAIRIQLLLQSLYKSDFGSEPWTLSECSLEMLNAPPRNCFKKQPFTVTVQFDNDPKNVYPYICYEYIYYQDDRDKWHKVKGLVDHNGLYFKEVTGDSVYFKLFQPDATVYGKSGQWTVIFKNKTIHSSVTSSSRSAFGPADEQPGPSTSYDKSQQERSGSGQPKALQDTEPPTSTSTVRLRRGRREREHHSYRHRKSQSELGADSAPTPEEVGRRSHTVAAHGLSRLRRLQEEARDPPVLIITGQQNNLKCWRYRFSQKYADLYECCSSAWKWLGPKSEGYRGDAKLLIAFKNPEQRLSFLNTVGLPKNTTYSMGHLDSL | 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 to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
PTM: Phosphorylated.
Sequence Mass (Da): 45557
Sequence Length: 396
Subcellular Location: Host nucleus
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P36796 | MESIPARLNAVQEKILDLYEADSNDLNAQIEHWKLTRMECVLFYKAKELGITHIGHQVVPPMAVSKAKACQAIELQLALEALNKTQYSTDGWTLQQTSLEMWRAEPQKYFKKHGYTITVQYDNDKNNTMDYTNWKEIYLLGECECTIVEGQVDYYGLYYWCDGEKIYFVKFSNDAKQYCVTGVWEVHVGGQVIVCPASVSSNEVSTTETAVHLCTETSKTSAVSVGAKDTHLQPPQKRRRPDVTDSRNTKYPNNLLRGQQSVDSTTRGLVTATECTNKGRVAHTTCTAPIIHLKGDPNSLKCLRYRVKTHKSLYVQISSTWHWTSNECTNNKLGIVTITYSDETQRQQFLKTVKIPNTVQVIQGVMSL | 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 to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
PTM: Phosphorylated.
Sequence Mass (Da): 41739
Sequence Length: 368
Subcellular Location: Host nucleus
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P36797 | METLCQRLDACQEKILDCFERDSKNITDHIDYWKAVRQENVIYYKARENNMTKLGHQVVPCLQVCKAKACVAIELQIALESLCKTEYNMEEWTLRDVCESMWYTEPKQCFKKQGQHIEVWFDGSKDNRAEYVVWKWVYYCGEDGWCKVSSAVSYEGIYYIHDGHKTYYTNFKDEATKYGCKGTWEVHMGKQSIYCPDSVSSTFRSNVSSVETVNEYYSHKTPTTSTPVGTYEASSSLRPGKRPRTTEPDSTDSTTQSTTTARESYAECVARNTDNTNNNTRKHLPGGASCNNTEIDSGYKTAPVVHIKGEANRLKCLRYRFQKHKQLFVTVSSTYHWTNVNCAVNNSYITVVYKDETQRQKFLDIVKIPPSVSLVLGHMTCVDM | 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 to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
PTM: Phosphorylated.
Sequence Mass (Da): 44160
Sequence Length: 384
Subcellular Location: Host nucleus
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Q81021 | METLATRLDVCQERLLDLYEKDSNKLEDQIEHWKCIRLECALQYKAREMGYKVLQHQALPALAVSKGKGHKAIELQLALETLQKTVYSTEPWTLQDTCLERWNAPPTGCLKRRGQTVDVIFDGHQDNTMQYVMWGDIYYQNCDGEGWTKVCSNIDAMGIYYMDAEHKVYYVDFKKEASKYGEYGQWEVRMGSSIIFSPASVSSTEEALSISSTGTAEHTRPANSTPRTDNSTKAIPCTPPPRKRARVYSTDQQPHSTSDPVGCDNDRHISDDNNKNQGRHTSSGDTTPIVHFKGEPNTLKCFRQRIQKYKHLFEQASSTWHWACVPGTTKNRGIVTLTYSSVEQRQQFLVTVRIPPSISMSLGVMSL | 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 to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
PTM: Phosphorylated.
Sequence Mass (Da): 41690
Sequence Length: 367
Subcellular Location: Host nucleus
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Q80937 | METIAKHLDVCQEQLLELYEENSNNLTKHIQHWKCIRYECVLLHKAKQMGLNHIGMQVVPALTVSQTKGHQAIEMQMTLETLLNSDYGMEPWTLQDTSREMWLTAPKYCFKKQGQTVEVKYDCNADNIMEYVSWKYIYVHDTDKWVKVTGHIDYKGLYYVHGGHKTYYTNFEKEAKKYGNSLQWEVCIGSSVICSPASISSTVQDVSIAGPASHTSSSTTTTLAQASPALPTCTSEERVDPPPCKRPRGPTTNTNNARDTVSVRHSDSVDSTNNNIYPNSYNSNKGRDNNFCTATPVVQLQGDPNCLKCLRYRLHAKHKTLFVAASSTWRWTCSDTSSKHALVTLTYVNEEQREQFLNTVRLPPTVTYKVGYMSLQLL | 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 to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
PTM: Phosphorylated.
Sequence Mass (Da): 42900
Sequence Length: 378
Subcellular Location: Host nucleus
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Q80944 | MNQADLTERSDALQEQILNLYEQDSKDIQAQIQYWDLNRKLYVTYYYARKEGYSHLGLQPLPALQVSEYKAKQAIEMGLLLTSLSKSQYASELWGLTDTSAELLLTPPRNTFKKKGYTVNVWFDNNENNTFPYTNWEYIYYQDDIEQWHRTRGEVDYNGLYFTENNGNRAYFLLFDSDAQTYSQTGTWTVHYKNQIISAPVTSSSKQSSDDYTSKAGQQPHFFASSSSPTTTDGGQTSQEGVSSSTTSPSAVRLRRRRSNEQQRELSSRESPRTKRRRVPDEVDRQSAVGSAPTAEEVGSRHRSLPRSGISRLARLQGEARDPPILLIKGLANSLKCWRYRLKKYTRYFKCMSTVFRWVDIDVPESSRHKLLVVFNDTTQRDVFMKLVTLPRGCTYTFGTLNSL | 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 to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
PTM: Phosphorylated.
Sequence Mass (Da): 46535
Sequence Length: 404
Subcellular Location: Host nucleus
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Q80951 | MRMESLADRLDACQEKLLDLYEKDSNKLEDQILHWHYVRLENAMLFKARQAGLTRVGHQMVPTLSVTKGKAHKAIEVHLSLQGLQTSAYAHEPWTLQTTSLEMWNTQPQRCWKKKGRRLTVKFDGEDHKAVEYVSWGYIYVQSTETDLWYKVPGKVSYKGLYYEMEGQEHYYVTFAQEAQKYGETGKWEVHMGNTVIYEPCASVSSTQDAVREVSTAETAGHLRDNTTQTTTTPTCVGPTQTSTSVQTPPHKRQRLHRDREQQPDTTQKDNHKRVDSTDQWINGHRNSTETGDNCDSYSSPVIHLKGDPNKLKCFRYRLQHSVPELFDKASSTWHWAGGQSTTRAAFVTLWYVNVEQRKQFLNRVTIPKGIQATAGYMSMCI | 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 to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
PTM: Phosphorylated.
Sequence Mass (Da): 43944
Sequence Length: 382
Subcellular Location: Host nucleus
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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 activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
PTM: Highly phosphorylated.
Sequence Mass (Da): 10798
Sequence Length: 97
Domain: The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell.
Subcellular Location: Host cytoplasm
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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 activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
PTM: Highly phosphorylated.
Sequence Mass (Da): 10467
Sequence Length: 94
Domain: The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell.
Subcellular Location: Host cytoplasm
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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 activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
PTM: Highly phosphorylated.
Sequence Mass (Da): 11127
Sequence Length: 100
Domain: The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell.
Subcellular Location: Host cytoplasm
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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 activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
PTM: Highly phosphorylated.
Sequence Mass (Da): 11677
Sequence Length: 103
Domain: The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell.
Subcellular Location: Host cytoplasm
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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 activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
PTM: Highly phosphorylated.
Sequence Mass (Da): 10500
Sequence Length: 93
Domain: The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell.
Subcellular Location: Host cytoplasm
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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 activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
PTM: Highly phosphorylated.
Sequence Mass (Da): 10889
Sequence Length: 98
Domain: The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell.
Subcellular Location: Host cytoplasm
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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 activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
PTM: Highly phosphorylated.
Sequence Mass (Da): 11022
Sequence Length: 98
Domain: The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell.
Subcellular Location: Host cytoplasm
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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 activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta) .
PTM: Highly phosphorylated.
Sequence Mass (Da): 11995
Sequence Length: 105
Domain: The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell.
Subcellular Location: Host cytoplasm
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A0A1V6NYL5 | MSTAVNTIRCSLLLLGLVGIYTVWISSFRNGLFLRNEEFAGKGQLPGTPNATLRTHFTGIDTLDKALGIFVVFYWPVCQGNLRSLSLIAFPAAVGVGEMWILFALQFSQSNSPTRAMGKMAMFGMGLMLVGPGIFLPIYCSLDLSSTHRLDDSPSSAAEGHLCRNLRSCLLGGYYILVILLALPSPAVVSYGSKQGIIALLQGWPLLVSAMLWLTHLCGKDRTADFQATLSTARTSIYISAMACATISHLVPLLISLLADSSDICPGKVFVPHLAWPSRRVTSVEEGLLRFFQWDYGLGSLALLLWAVGLHIQRRQQISQGINYLRLIPEALFLSVMMSPCGAAALYLYRHNSTNCASKTGDKSGSG | 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, and further modified by the other verrucodidin cluster enzymes (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39830
Sequence Length: 367
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 5.4.99.-
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Q40316 | MAEGKGRVCVTGGTGFLGSWIIKSLLENGYSVNTTIRADPERKRDVSFLTNLPGASEKLHFFNADLSNPDSFAAAIEGCVGIFHTASPIDFAVSEPEEIVTKRTVDGALGILKACVNSKTVKRFIYTSSGSAVSFNGKDKDVLDESDWSDVDLLRSVKPFGWNYAVSKTLAEKAVLEFGEQNGIDVVTLILPFIVGRFVCPKLPDSIEKALVLVLGKKEQIGVTRFHMVHVDDVARAHIYLLENSVPGGRYNCSPFIVPIEEMSQLLSAKYPEYQILTVDELKEIKGARLPDLNTKKLVDAGFDFKYTIEDMFDDAIQCCKEKGYL | 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.
Catalytic Activity: a (3R,4R)-4,2'-dihydroxyisoflavan + NADP(+) = a (3R)-2'-hydroxyisoflavanone + H(+) + NADPH
Sequence Mass (Da): 35918
Sequence Length: 326
EC: 1.1.1.348
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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 | MKALRLSASALFCLLLINGLGAAPPGRPEAQPPPLSSEHKEPVAGDAVPGPKDGSAPEVRGARNSEPQDEGELFQGVDPRALAAVLLQALDRPASPPAPSGSQQGPEEEAAEALLTETVRSQTHSLPAPESPEPAAPPRPQTPENGPEASDPSEELEALASLLQELRDFSPSSAKRQQETAAAETETRTHTLTRVNLESPGPERVWRASWGEFQARVPERAPLPPPAPSQFQARMPDSGPLPETHKFGEGVSSPKTHLGEALAPLSKAYQGVAAPFPKARRPESALLGGSEAGERLLQQGLAQVEAGRRQAEATRQAAAQEERLADLASDLLLQYLLQGGARQRGLGGRGLQEAAEERESAREEEEAEQERRGGEERVGEEDEEAAEAEAEAEEAERARQNALLFAEEEDGEAGAEDKRSQEETPGHRRKEAEGTEEGGEEEDDEEMDPQTIDSLIELSTKLHLPADDVVSIIEEVEEKRKRKKNAPPEPVPPPRAAPAPTHVRSPQPPPPAPAPARDELPDWNEVLPPWDREEDEVYPPGPYHPFPNYIRPRTLQPPSALRRRHYHHALPPSRHYPGREAQARRAQEEAEAEERRLQEQEELENYIEHVLLRRP | 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 chronic pain (By similarity).
PTM: Multiple peptides are derived from VGF, with activities in synaptic plasticity, antidepression, penile erection, autonomic activation, and increases in energy expenditure.
Sequence Mass (Da): 67258
Sequence Length: 615
Subcellular Location: Secreted
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P20156 | MKTFTLPASVLFCFLLLIRGLGAAPPGRSDVYPPPLGSEHNGQVAEDAVSRPKDDSVPEVRAARNSEPQDQGELFQGVDPRALAAVLLQALDRPASPPAVPAGSQQGTPEEAAEALLTESVRSQTHSLPASEIQASAVAPPRPQTQDNDPEADDRSEELEALASLLQELRDFSPSNAKRQQETAAAETETRTHTLTRVNLESPGPERVWRASWGEFQARVPERAPLPPSVPSQFQARMSENVPLPETHQFGEGVSSPKTHLGETLTPLSKAYQSLSAPFPKVRRLEGSFLGGSEAGERLLQQGLAQVEAGRRQAEATRQAAAQEERLADLASDLLLQYLLQGGARQRDLGGRGLQETQQERENEREEEAEQERRGGGEDEVGEEDEEAAEAEAEAEEAERARQNALLFAEEEDGEAGAEDKRSQEEAPGHRRKDAEGTEEGGEEDDDDEEMDPQTIDSLIELSTKLHLPADDVVSIIEEVEEKRKRKKNAPPEPVPPPRAAPAPTHVRSPQPPPPAPARDELPDWNEVLPPWDREEDEVFPPGPYHPFPNYIRPRTLQPPASSRRRHFHHALPPARHHPDLEAQARRAQEEADAEERRLQEQEELENYIEHVLLHRP | 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 similarity).
PTM: Multiple peptides are derived from VGF, with activities in synaptic plasticity, antidepression, penile erection, autonomic activation, and increases in energy expenditure.
Sequence Mass (Da): 68179
Sequence Length: 617
Subcellular Location: Secreted
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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, inducing its dimerization, autophosphorylation and leading to activation of several cellular pathways regulating cell proliferation or cell survival. The activation by host EGFR of mitogen activated protein kinases (MAPK) and extracellular-signal regulated kinases (ERK) are essential for the positive effect of vaccinia growth factor on poxvirus virulence in vivo.
PTM: Cleaved at the cell surface by host ADAM10, thereby releasing the secreted form of VGF.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 15524
Sequence Length: 140
Subcellular Location: Host membrane
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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 polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.
PTM: Highly phosphorylated on serine and threonine residues. Thr-96 and Ser-165 are phosphorylated by the mitogen activated kinase MAP4K1. As the HIV-1 replication can be activated by stress and mitogens, these phosphorylations could be involved in this process. Ser-144 phosphorylation may inhibit elongin BC complex binding.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22699
Sequence Length: 192
Domain: The BC-like-box motif mediates the interaction with elongin BC complex.
Subcellular Location: Host cytoplasm
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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
Sequence Mass (Da): 32172
Sequence Length: 293
Subcellular Location: Cell membrane
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P17800 | MNDDNQQSAHDVDASGSLVSDTHHRRLSGAQKLIVGGVVLALSLSLIWLGGREKKENGDAPPSTMIATNTKPFHPAPIDVTLDPPAAQEAVQPTAPPPARSEPERHEPRPEETPIFAYTSGDQGTSKRVQQGETDRRREGNGEDSPLPKVEVSAENDLSIRMKPTELQPTRATLLPHPDFMVTEGTIIPCILQTAIDTSLAGYVKCVLPWDVRGTTNNVVLLDRGTTVVGEIQRGLQQGDARVFVLWDRAETPDHAMISLASPSADELGRSGLPGTVDNHFWQRFSGAMLLSVVQGAFQAASTYAGSSGGGTSFNSVQNNGEQTADTALKATINIPPTLKKNQGDTVSIFVARDLDFSGIYQLRMAGRAARGRDRRP | 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 | MNDPMDENNLLNDRDMIKDGHGKKQRPNTSKAAALVILFGVCLYLAYSTLFTEKQQPVEVQKEGIIKQTELFRPAPPKPVSLEPTIEKNNVLLPKVELPTPPKKTTNSDDSLLEAAQRAPVLAYANTQKGQGSTEKNKDISANQPEAKPDETAQRFNHLLKPTTLEGIRAAKLGNRNYIIAMGASIPCILETAISSDQQGFASCIVSRDILSDNGRVVLLDKGTQIVGEYRAGLKKGQKRLFVLWNRAKTPNGIIITLASPATDALGRSGMDGDIDNHWLERIGSALLVSIVKDATNYVKGRLPKDQDKNNSETISSGQNIANIAVENYANIPPTLSKNQGEMVNVFVARDLDFSNVYKLKVIENKKQIVNRALSRNFYKNSAVICNEPKLAHIER | 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 apoptosis, leading to an increased cell survival, and, at high infection doses, a cytostatic or cytotoxic effect, which interfers with a potent VirB-independent mitogenic activity. These changes of HEC require the T4S coupling protein VirD4 and at least one of the effector proteins BepA-G.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 43654
Sequence Length: 396
Subcellular Location: Cell inner membrane
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Q80925 | MSLRRRKRASPTDLYKTCLQGGDCIPDVKNKFENSTIADWLLKIFGSLVYFGNLGIGSGKGSGGSFGYRPLGSAGSGRPATDLPVTRPNVVIEPIGPQSIVPIDPGASSIVPLVEGGPDISFIAPDAGPGIGGEDIELFTFRDPATDVGGVSGGPTTISTEESETAIIDALPSATTPKQLFYDSYTQTILQTQVNPFLNNAISDTNVFVDPLFAGETIGDNIFEEIPLQNLNFSFPRESTPVKPGRGLRTPAQRSYSRFMEQYPIQAPEFLSQPSRLVQFEFENPAFDPDISIQFQRDVNSLEAAPNPAFADIAYLSRPHMSATSEGLVRVSRIGSRAVLQTRSGLTIGPKVHYYMDLSAISTEAIELQTFADSGHVHTIVDDFLSVTALDDPANIADINYTEDDLLDPLLENFNNSHITVQGVDEEGETVALPIPSITNSSKTFVTDIAENGLFANDTDSLLTPASTIVPAINWFPLFDSYSDFALDPFFIPRKKRRLDIL | 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 by promoting escape from the endosomal compartments and traffic through the host Golgi network. Mechanistically, the C-terminus of L2 possesses a cell-penetrating peptide that protudes from the host endosome, interacts with host cytoplasmic retromer cargo and thereby mediates the capsid delivery to the host trans-Golgi network. Plays a role through its interaction with host dynein in the intracellular microtubule-dependent transport of viral capsid toward the nucleus. Mediates the viral genome import into the nucleus through binding to host importins. Once within the nucleus, L2 localizes viral genomes to host PML bodies in order to activate early gene expression for establishment of infection. Later on, promotes late gene expression by interacting with the viral E2 protein and by inhibiting its transcriptional activation functions. During virion assembly, encapsidates the genome by direct interaction with the viral DNA.
PTM: Highly phosphorylated.
Sequence Mass (Da): 54436
Sequence Length: 502
Subcellular Location: Virion
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Q80932 | MLRRRKRASPTDLYRSCLQGGDCIPDVQNKFEGNTIADWLLKIFGGLVYFGNLGIGTGRGTGGTFGYRPFGAPGSGRPTQELPIARPNVVIDPLGPAPIVPVDPSAASIVPLVEGAPDVGFAAPDAGPAAGGTDIELYTITNSTTDVGAVGGGPTVTSNEEFEVAVIDAQPIAPYPKQLLYDSTIAATFETQINPFINPDINNVNVLVDPSFAGDTVGDYFYEEIPLERLDIQTFDILEPPTESTPTQLGNRFVSRARDLYSRFVAQQPISEPDFLSQPSRLVQFEYRNPAFDPDVSLYFERDLEGLRAAPLQEFADVVYLGRPRVSSTSEGTIRVSRLGTRAALTTRSGLSVGPQVHFYMDLSDIPPEDSIELHTLNVTPQTSTIVDDILATTTFDDPANSLFTQFNEDVLTDDVEHNFTESHLVIPATDEENDTAINIINLRNIPLTVGMNSGDISTTLSDYNILDASLIVKSNVSEQPLFVLDYSDYDLHPGLLPKRRRIDYF | 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 by promoting escape from the endosomal compartments and traffic through the host Golgi network. Mechanistically, the C-terminus of L2 possesses a cell-penetrating peptide that protudes from the host endosome, interacts with host cytoplasmic retromer cargo and thereby mediates the capsid delivery to the host trans-Golgi network. Plays a role through its interaction with host dynein in the intracellular microtubule-dependent transport of viral capsid toward the nucleus. Mediates the viral genome import into the nucleus through binding to host importins. Once within the nucleus, L2 localizes viral genomes to host PML bodies in order to activate early gene expression for establishment of infection. Later on, promotes late gene expression by interacting with the viral E2 protein and by inhibiting its transcriptional activation functions. During virion assembly, encapsidates the genome by direct interaction with the viral DNA.
PTM: Highly phosphorylated.
Sequence Mass (Da): 55198
Sequence Length: 506
Subcellular Location: Virion
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Q80946 | MYARVKRVKRDSVENLYKQCQLGADCPPDVRNKVEGTTLADRLLQIFGSILYLGNLGIGTGKGSGGATGYTPLGTARVPASTPGTVIKPTRPFSVPLDPIGSGIPSQPVGGRLPVDIIDASASSIIPLQEVLPETTIIVGGDSGPGLGASEIDIVSEPRPDVVGVDTQPTVYTSIDNTVATLDITPATPPVKKIILDPISSGSEGAAAITFSDISAADLNVFVDPQGAGDRISFGEEIELGPINQPAQFEIEEPPRTSTPGEGFQRVTTRARELYNRFVQQQPTQNIDFLGRPSRAVQFEFENPAFFNDEVTMQFEQDLQEVAAAPDQDFADVRELGRARFSETSAGTIRVSRLGTKGTMKTRSGLTIGQKVHFYFDISDIPAAETIQLRTLGESSHDFSAVDNITESTYINLTETTNEGLIPDNILEDEFTENFNNAQLIFATIDEGESMIMPTIPPGVALKLFIPEIAASVLNVVHPSSEWTILIPNVPDEIIQPAMAVDVYDDFYLHPHLLRRRKRKRLDFF | 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 by promoting escape from the endosomal compartments and traffic through the host Golgi network. Mechanistically, the C-terminus of L2 possesses a cell-penetrating peptide that protudes from the host endosome, interacts with host cytoplasmic retromer cargo and thereby mediates the capsid delivery to the host trans-Golgi network. Plays a role through its interaction with host dynein in the intracellular microtubule-dependent transport of viral capsid toward the nucleus. Mediates the viral genome import into the nucleus through binding to host importins. Once within the nucleus, L2 localizes viral genomes to host PML bodies in order to activate early gene expression for establishment of infection. Later on, promotes late gene expression by interacting with the viral E2 protein and by inhibiting its transcriptional activation functions. During virion assembly, encapsidates the genome by direct interaction with the viral DNA.
PTM: Highly phosphorylated.
Sequence Mass (Da): 56999
Sequence Length: 525
Subcellular Location: Virion
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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 | MLRTILDAPQRLLKEGRASRQLVLVVVFVALLLDNMLFTVVVPIVPTFLYDMEFKEVNSSLHLGHAGSSPHALASPAFSTIFSFFNNNTVAVEESVPSGIAWMNDTASTIPPPATEAISAHKNNCLQGTGFLEEEITRVGVLFASKAVMQLLVNPFVGPLTNRIGYHIPMFAGFVIMFLSTVMFAFSGTYTLLFVARTLQGIGSSFSSVAGLGMLASVYTDDHERGRAMGTALGGLALGLLVGAPFGSVMYEFVGKSAPFLILAFLALLDGALQLCILQPSKVSPESAKGTPLFMLLKDPYILVAAGSICFANMGVAILEPTLPIWMMQTMCSPKWQLGLAFLPASVSYLIGTNLFGVLANKMGRWLCSLIGMLVVGTSLLCVPLAHNIFGLIGPNAGLGLAIGMVDSSMMPIMGHLVDLRHTSVYGSVYAIADVAFCMGFAIGPSTGGAIVKAIGFPWLMVITGVINIVYAPLCYYLRSPPAKEEKLAILSQDCPMETRMYATQKPTKEFPLGEDSDEEPDHEE | 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 to their release via exocytosis. Transports catecholamines and indolamines with higher affinity for serotonin . Regulates the transvesicular monoaminergic gradient that determines the quantal size. Mediates presynaptic monoaminergic vesicle transport in the amygdala and prefrontal brain regions related with emotion processing in response to environmental stimuli .
Catalytic Activity: 2 H(+)(out) + serotonin(in) = 2 H(+)(in) + serotonin(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56257
Sequence Length: 525
Subcellular Location: Cytoplasmic vesicle
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Q8R090 | MFQVVLGAPQRLLKEGRQSRKLVLVVVFVALLLDNMLLTVVVPIVPTFLYATEFKDINSSLLRGPSVSSQQALTSPAFSTTFSFFDNTTMTVEEHVPFRVAWINGTIPPPVTEAGSVPKNNCLQGIEFLEEENVRIGILFASKALMQLLVNPFVGPLTNRIGYHIPMFVGFMIMFLSTLMFAFSGTYALLFVARTLQGIGSSFSSVAGLGMLASVYTDNYERGRAMGIALGGLALGLLVGAPFGSVMYEFVGKSSPFLILAFLALLDGALQFCILWPSKVSPESAMGTPLLTLLKDPYILVAAGSICLANMGVAILEPTLPIWMMQTMCSPEWQLGLAFLPASVAYLIGTNLFGVLANKMGRWLCSLVGMVAVGISLLCVPLAHNIFGLIGPNAGLGFAIGMVDSSLMPIMGYLVDLRHTSVYGSVYAIADVAFCVGFAIGPSTGGVIVPVIGFPWLMVIIGTINIIYAPLCCFLQNPPAKEEELAILNQECPTETQMYTIQRPTKEFPLGENSDDPGSEE | 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 to their release via exocytosis. Transports catecholamines and indolamines with higher affinity for serotonin . Regulates the transvesicular monoaminergic gradient that determines the quantal size. Mediates presynaptic monoaminergic vesicle transport in the amygdala and prefrontal brain regions related with emotion processing in response to environmental stimuli (By similarity).
Catalytic Activity: 2 H(+)(out) + serotonin(in) = 2 H(+)(in) + serotonin(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56033
Sequence Length: 521
Subcellular Location: Cytoplasmic vesicle
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Q05940 | MALSELALVRWLQESRRSRKLILFIVFLALLLDNMLLTVVVPIIPSYLYSIKHEKNATEIQTARPVHTASISDSFQSIFSYYDNSTMVTGNATRDLTLHQTATQHMVTNASAVPSDCPSEDKDLLNENVQVGLLFASKATVQLITNPFIGLLTNRIGYPIPIFAGFCIMFVSTIMFAFSSSYAFLLIARSLQGIGSSCSSVAGMGMLASVYTDDEERGNVMGIALGGLAMGVLVGPPFGSVLYEFVGKTAPFLVLAALVLLDGAIQLFVLQPSRVQPESQKGTPLTTLLKDPYILIAAGSICFANMGIAMLEPALPIWMMETMCSRKWQLGVAFLPASISYLIGTNIFGILAHKMGRWLCALLGMIIVGVSILCIPFAKNIYGLIAPNFGVGFAIGMVDSSMMPIMGYLVDLRHVSVYGSVYAIADVAFCMGYAIGPSAGGAIAKAIGFPWLMTIIGIIDILFAPLCFFLRSPPAKEEKMAILMDHNCPIKTKMYTQNNIQSYPIGEDEESESD | 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 to their release via exocytosis. Transports a variety of catecholamines such as dopamine, adrenaline and noradrenaline, histamine, and indolamines such as serotonin . Regulates the transvesicular monoaminergic gradient that determines the quantal size. Mediates somatodendritic dopamine release in hippocampal neurons, likely as part of a regulated secretory pathway that integrates retrograde synaptic signals (By similarity). Acts as a primary transporter for striatal dopamine loading ensuring impulse-dependent release of dopamine at the synaptic cleft (By similarity). Responsible for histamine and serotonin storage and subsequent corelease from mast cell granules (By similarity).
Catalytic Activity: 2 H(+)(out) + serotonin(in) = 2 H(+)(in) + serotonin(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55713
Sequence Length: 514
Subcellular Location: Cytoplasmic vesicle
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Q8BRU6 | MALSDLVLLRWLRDSRHSRKLILFIVFLALLLDNMLLTVVVPIIPSYLYSIKHEKNTTEIQTARPALTASTSESFHSIFSYYNNSTVFTGNATGGLPGGESPKATTTQHTVTNTTVPPDCPSEDKDLLNENVQVGLLFASKATVQLLTNPFIGLLTNRIGYPIPMFAGFCIMFISTVMFAFSSSYAFLLIARSLQGIGSSCSSVAGMGMLASVYTDDEERGNAMGIALGGLAMGVLVGPPFGSVLYEFVGKTAPFLVLAALVLLDGAIQLFVLQPSRVQPESQKGTPLTTLLKDPYILIAAGSICFANMGIAMLEPALPIWMMETMCSRKWQLGVAFLPASISYLIGTNIFGILAHKMGRWLCALLGMIVVGISILCIPFAKNIYGLIAPNFGVGFAIGMVDSSMMPIMGYLVDLRHVSVYGSVYAIADVAFCMGYAIGPSAGGAIAKAIGFPWLMTIIGIIDIVFAPLCFFLRSPPAKEEKMAILMDHNCPIKTKMYTQNNVQPYPVGDDEESESD | 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 to their release via exocytosis. Transports a variety of catecholamines such as dopamine, adrenaline and noradrenaline, histamine, and indolamines such as serotonin (By similarity). Regulates the transvesicular monoaminergic gradient that determines the quantal size. Mediates somatodendritic dopamine release in hippocampal neurons, likely as part of a regulated secretory pathway that integrates retrograde synaptic signals (By similarity). Acts as a primary transporter for striatal dopamine loading ensuring impulse-dependent release of dopamine at the synaptic cleft . Responsible for histamine and serotonin storage and subsequent corelease from mast cell granules (By similarity).
Catalytic Activity: 2 H(+)(out) + serotonin(in) = 2 H(+)(in) + serotonin(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55754
Sequence Length: 517
Subcellular Location: Cytoplasmic vesicle
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Q01827 | MALSDLVLLRWLRDSRHSRKLILFIVFLALLLDNMLLTVVVPIIPSYLYSIKHEKNSTEIQTTRPELVVSTSESIFSYYNNSTVLITGNATGTLPGGQSHKATSTQHTVANTTVPSDCPSEDRDLLNENVQVGLLFASKATVQLLTNPFIGLLTNRIGYPIPMFAGFCIMFISTVMFAFSSSYAFLLIARSLQGIGSSCSSVAGMGMLASVYTDDEERGKPMGIALGGLAMGVLVGPPFGSVLYEFVGKTAPFLVLAALVLLDGAIQLFVLQPSRVQPESQKGTPLTTLLKDPYILIAAGSICFANMGIAMLEPALPIWMMETMCSRKWQLGVAFLPASISYLIGTNIFGILAHKMGRWLCALLGMVIVGISILCIPFAKNIYGLIAPNFGVGFAIGMVDSSMMPIMGYLVDLRHVSVYGSVYAIADVAFCMGYAIGPSAGGAIAKAIGFPWLMTIIGIIDIAFAPLCFFLRSPPAKEEKMAILMDHNCPIKRKMYTQNNVQSYPIGDDEESESD | 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 to their release via exocytosis. Transports a variety of catecholamines such as dopamine, adrenaline and noradrenaline, histamine, and indolamines such as serotonin . Regulates the transvesicular monoaminergic gradient that determines the quantal size. Mediates somatodendritic dopamine release in hippocampal neurons, likely as part of a regulated secretory pathway that integrates retrograde synaptic signals . Acts as a primary transporter for striatal dopamine loading ensuring impulse-dependent release of dopamine at the synaptic cleft (By similarity). Responsible for histamine and serotonin storage and subsequent corelease from mast cell granules (By similarity).
Catalytic Activity: 2 H(+)(out) + serotonin(in) = 2 H(+)(in) + serotonin(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55690
Sequence Length: 515
Subcellular Location: Cytoplasmic vesicle
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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 | MDLLVDELFADMNADGASPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSALPTNADLYRECKFLSTLPSDVVEWGDAYVPERTQIDIRAHGDVAFPTLPATRDGLGLYYEALSRFFHAELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRDRDLGEMLRATIADRYYRETARLARVLFLHLYLFLTREILWAAYAEQMMRPDLFDCLCCDLESWRQLAGLFQPFMFVNGALTVRGVPIEARRLRELNHIREHLNLPLVRSAATEEPGAPLTTPPTLHGNQARASGYFMVLIRAKLDSYSSFTTSPSEAVMREHAYSRARTKNNYGSTIEGLLDLPDDDAPEEAGLAAPRLSFLPAGHTRRLSTAPPTDVSLGDELHLDGEDVAMAHADALDDFDLDMLGDGDSPGPGFTPHDSAPYGALDMADFEFEQMFTDALGIDEYGG | 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 . VP16-induced complex represents a regulatory switch: when it is on, it promotes IE-gene expression and thus lytic infection, and when it is off, it limits IE-gene transcription favoring latent infection . Acts as a key activator of lytic infection by initiating the lytic program through the assembly of the transcriptional regulatory VP16-induced complex composed of VP16 and two cellular factors, HCFC1 and POU2F1 . This complex recognizes the core motif 'TAATGARAT' in alpha-gene promoters . In the late stage of viral replication, VP16, as a tegument, is involved in viral assembly .
Sequence Mass (Da): 54345
Sequence Length: 490
Domain: The transcriptional activation region seems to target many proteins of the RNA polymerase II transcription machinery.
Subcellular Location: Virion tegument
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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 (Da): 9789
Sequence Length: 90
Subcellular Location: Virion membrane
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P17462 | MAYRKRGATVEADINNNDRMQEKDDEKQDQNNRMQLSDKVLSKKEEVVTDSQEEIKIRDEVKKSTKEESKQLLEVLKTKEEHQKEIQYEILQKTIPTFEPKESILKKLEDIKPEQAKKQTKLFRIFEPRQLPIYRANGEKELRNRWYWKLKKDTLPDGDYDVREYFLNLYDQVLTEMPDYLLLKDMAVENKNSRDAGKVVDSETASICDAIFQDEETEGAVRRFIAEMRQRVQADRNVVNYPSILHPIDYAFNEYFLQHQLVEPLNNDIIFNYIPERIRNDVNYILNMDRNLPSTARYIRPNLLQDRLNLHDNFESLWDTITTSNYILARSVVPDLKELVSTEAQIQKMSQDLQLEALTIQSETQFLTGINSQAANDCFKTLIAAMLSQRTMSLDFVTTNYMSLISGMWLLTVVPNDMFIRESLVACQLAIVNTIIYPAFGMQRMHYRNGDPQTPFQIAEQQIRKFSGSGIGWHFVNNNQFRQVVIDGVLNQVLNDNIRNVHVIKQLMQALMQLSRQQFPTMPVDYKRSIQRGILLLSNRLGQLVDLTRLLAYNYETLMACVTMNMQHVQTLTTEKLQLTSVTSLCMLIGNATVIPSPQTLFHYYNVNVNFHSNYNERINDAVAIITAANRLNLYQKKMKAIVEDFLKRLHIFDVARVPDDQMYRLRDRLRLLPVEVRRLDIFNLILMNMDQIERASDKIAQGVIIAYRDMQLERDEMYGYVNIARNLDGFQQINLEELMRTGDYAQITNMLLNNQPVALVGALPFVTDSSVISLIAKLDATVFAQIVKLRKVDTLKPILYKINSDSNDFYLVANYDWVPTSTTKVYKQVPQQFDFRNSMHMLTSNLTFTVYSDLLAFVSADTVEPINAVAFDNMRIMNEL | 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 capping enzyme VP3 and the genomic dsRNA, thereby defining the core . The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus . Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels formed by VP2 N-termini . VP2 is required for the replicase activity of VP1 polymerase (By similarity). Probably recruits a copy of a VP1-VP3 complex, potentially along with a segment of plus-strand RNA, as a decamer of VP2 assembles . May activate the autoinhibited VP1/RNA complex to coordinate packaging and genome replication (By similarity).
PTM: Sumoylated with SUMO1 and SUMO2. Sumoylation of viral proteins seems to have a positive role on viral replication.
Sequence Mass (Da): 102488
Sequence Length: 881
Domain: The N-terminus binds RNA (By similarity). It is necessary for encapsidation of VP1 and VP3 (By similarity). The N-termini of 10 VP2 molecules form a cylindrical hub underneath each 5-fold axis of the inner capsid .
Subcellular Location: Virion
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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.
Sequence Mass (Da): 32499
Sequence Length: 300
Subcellular Location: Virion
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B2BNE4 | MGNVQTSTNVYNIDGNGNTFAPSSQMASTASPAIDLKPGVLNPTGKLWQTMGTGAPSADSLVLVVDNKGEYTYLSENMRETLNKAVTDVNMWQPLFQATKSGCGPVVLANFTTISTGYVGATADDAFSNGLVSNGPFLATMHIMELQKTIAARMRDVAIWQKHLDTAMTLMTPDVSAGDVTCKWRSLLEFAQDILPLDNLCRSYPNEFYTVAAQRYPAIRPGQPDTQVALPQPHPLGEVAGSFNAPTSEVGSLVGAGAALSDAISTLASKDLDLVEADTPLPVSVFTPSLAPRTYRPAFIDPQDAAWIAQWNGDANIRIITTYQSTDYTVQLGPGPTRVIDMNAMIDAKLTLDVSGTILPFQENNDLSSAIPAFVLIQTKVPLHSVTQASDVEGITVVSAAESSAINLSVNVRGDPRFDMLHLHAMFERETIAGIPYIYGIGTFLIPSITSSSSFCNPTLMDGELTVTPLLLRETTYKGAVVDTVTPSEVMANQTSEEVASALANDAVLLVSGQLERLATVVGDVIPIASGEDDAATSAIVGRLAIEATMRARHGGDTRALPNFGQLWKRAKRAASMFASNPALALQVGVPVLADSGILSALTSGVSTAIRTGSLGKGVSDASSKLNARQSLTLARKTFFKKVEELWPSQ | 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 into the host cell cytoplasm (Potential).
PTM: Cleaved during the endosomal proteolytic disassembly of the outer capsid.
Sequence Mass (Da): 68988
Sequence Length: 650
Subcellular Location: Virion
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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 involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 29265
Sequence Length: 258
Subcellular Location: Virion
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O94753 | MSFKTLSALALALGAAVQFASAAVPLVQKRATCDDGRTTANAACCILFPILDDIQENLFDGAQCGEEVHESLRLTFHDAIGFSPTLGGGGADGSIIAFDTIETNFPANAGIDEIVSAQKPFVAKHNISAGDFIQFAGAVGVSNCPGGVRIPFFLGRPDAVAASPDHLVPEPFDSVDSILARMGDAGFSPVEVVWLLASHSIAAADKVDPSIPGTPFDSTPGVFDSQFFIETQLKGRLFPGTADNKGEAQSPLQGEIRLQSDHLLARDPQTACEWQSMVNNQPKIQNRFAATMSKMALLGQDKTKLIDCSDVIPTPPALVGAAHLPAGFSLSDVEQACAATPFPALTADPGPVTSVPPVPGS | 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-methoxyphenoxy)propane-1,3-diol + H2O2 = glycolaldehyde + guaiacol + H2O + vanillin
Sequence Mass (Da): 37624
Sequence Length: 361
Subcellular Location: Secreted
EC: 1.11.1.16
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P30628 | MGDYVTPGEEPPQPGIYRSEQMCLAQLYLQSDASYQCVAELGELGLVQFRDLNPDVSSFQRKYVNEVRRCDEMERKLRYLEREIKKDQIPMLDTGENPDAPLPREMIDLEATFEKLENELREVNKNEETLKKNFSELTELKHILRKTQTFFEEVDHDRWRILEGGSGRRGRSTEREETRPLIDIGDMDDDSAARMSAQAAMLRLGFVAGVIQRERLPAFERLLWRACRGNVFLRTSEIDDVLNDTVTGDPVNKCVFIIFFQGDHLKTKVKKICEGFRATLYPCPDTPQERREMSIGVMTRIEDLKTVLGQTQDHRHRVLVAASKNVRMWLTKVRKIKSIYHTLNLFNIDVTQKCLIAEVWCPIAELDRIKMALKRGTDESGSQVPSILNRMETNEAPPTYNKTNKFTKGFQNIVDAYGIATYREINPAPYTMISFPFLFAVMFGDMGHGAIMLLAALFFILKEKQLEAARIKDEIFQTFFGGRYVIFLMGAFSIYTGFMYNDVFSKSINTFGSSWQNTIPESVIDYYLDDEKRSESQLILPPETAFDGNPYPIGVDPVWNLAEGNKLSFLNSMKMKMSVLFGIAQMTFGVLLSYQNFIYFKSDLDIKYMFIPQMIFLSSIFIYLCIQILSKWLFFGAVGGTVLGYKYPGSNCAPSLLIGLINMFMMKSRNAGFVDDSGETYPQCYLSTWYPGQATIEIILVVLALVQVPIMLFAKPYFLYRRDKQQSRYSTLTAESNQHQSVRADINQDDAEVVHAPEQTPKPSGHGHGHGDGPLEMGDVMVYQAIHTIEFVLGCVSHTASYLRLWALSLAHAQLSDVLWTMVFRNAFVLDGYTGAIATYILFFIFGSLSVFILVLMEGLSAFLHALRLHWVEFQSKFYGGLGYEFAPFSFEKILAEEREAEENL | 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 compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Required for assembly and activity of the vacuolar ATPase (By similarity). Regulates the size of gut granules during embryonic development . In neurons, required for necrotic cell death by promoting intracellular acidification . Required for cell death induced by hypoxia . Required for acidification of synaptic vesicles and the release of neurotransmitters from adult neurons .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 103401
Sequence Length: 905
Subcellular Location: Membrane
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Q93050 | MGELFRSEEMTLAQLFLQSEAAYCCVSELGELGKVQFRDLNPDVNVFQRKFVNEVRRCEEMDRKLRFVEKEIRKANIPIMDTGENPEVPFPRDMIDLEANFEKIENELKEINTNQEALKRNFLELTELKFILRKTQQFFDEMADPDLLEESSSLLEPSEMGRGTPLRLGFVAGVINRERIPTFERMLWRVCRGNVFLRQAEIENPLEDPVTGDYVHKSVFIIFFQGDQLKNRVKKICEGFRASLYPCPETPQERKEMASGVNTRIDDLQMVLNQTEDHRQRVLQAAAKNIRVWFIKVRKMKAIYHTLNLCNIDVTQKCLIAEVWCPVTDLDSIQFALRRGTEHSGSTVPSILNRMQTNQTPPTYNKTNKFTYGFQNIVDAYGIGTYREINPAPYTIITFPFLFAVMFGDFGHGILMTLFAVWMVLRESRILSQKNENEMFSTVFSGRYIILLMGVFSMYTGLIYNDCFSKSLNIFGSSWSVRPMFTYNWTEETLRGNPVLQLNPALPGVFGGPYPFGIDPIWNIATNKLTFLNSFKMKMSVILGIIHMLFGVSLSLFNHIYFKKPLNIYFGFIPEIIFMTSLFGYLVILIFYKWTAYDAHTSENAPSLLIHFINMFLFSYPESGYSMLYSGQKGIQCFLVVVALLCVPWMLLFKPLVLRRQYLRRKHLGTLNFGGIRVGNGPTEEDAEIIQHDQLSTHSEDADEPSEDEVFDFGDTMVHQAIHTIEYCLGCISNTASYLRLWALSLAHAQLSEVLWTMVIHIGLSVKSLAGGLVLFFFFTAFATLTVAILLIMEGLSAFLHALRLHWVEFQNKFYSGTGFKFLPFSFEHIREGKFEE | 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 lysosomes, endosomes, the trans-Golgi network, and secretory granules, including synaptic vesicles . In certain cell types, can be exported to the plasma membrane, where it is involved in the acidification of the extracellular environment (By similarity). Required for assembly and activity of the vacuolar ATPase (By similarity). Through its action on compartment acidification, plays an essential role in neuronal development in terms of integrity and connectivity of neurons .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96413
Sequence Length: 837
Subcellular Location: Cytoplasmic vesicle
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Q9Z1G4 | MGELFRSEEMTLAQLFLQSEAAYCCVSELGELGKVQFRDLNPDVNVFQRKFVNEVRRCEEMDRKLRFVEKEIRKANIPIMDTGENPEVPFPRDMIDLEANFEKIENELKEINTNQEALKRNFLELTELKFILRKTQQFFDEAELHHQQMADPDLLEESSSLLEPNEMGRGAPLRLGFVAGVINRERIPTFERMLWRVCRGNVFLRQAEIENPLEDPVTGDYVHKSVFIIFFQGDQLKNRVKKICEGFRASLYPCPETPQERKEMASGVNTRIDDLQMVLNQTEDHRQRVLQAAAKNIRVWFIKVRKMKAIYHTLNLCNIDVTQKCLIAEVWCPVTDLDSIQFALRRGTEHSGSTVPSILNRMQTNQTPPTYNKTNKFTHGFQNIVDAYGIGTYREINPAPYTVITFPFLFAVMFGDFGHGILMTLFAVWMVLRESRILSQKHENEMFSMVFSGRYIILLMGLFSIYTGLIYNDCFSKSLNIFGSSWSVRPMFTQGNWTEETLLGSSVLQLNPAIPGVFGGPYPFGIDPIWNIATNKLTFLNSFKMKMSVILGIIHMLFGVSLSLFNHIYFKKPLNIYFGFIPEIIFMSSLFGYLVILIFYKWTAYDAHSSRNAPSLLIHFINMFLFSYPESGNAMLYSGQKGIQCFLIVVAMLCVPWMLLFKPLILRHQYLRKKHLGTLNFGGIRVGNGPTEEDAEIIQHDQLSTHSEDAEEFDFGDTMVHQAIHTIEYCLGCISNTASYLRLWALSLAHAQLSEVLWTMVIHIGLHVRSLAGGLGLFFIFAAFATLTVAILLIMEGLSAFLHALRLHWVEFQNKFYTGTGFKFLPFSFEHIREGKFDE | 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, endosomes, the trans-Golgi network, and secretory granules, including synaptic vesicles. In certain cell types, can be exported to the plasma membrane, where it is involved in the acidification of the extracellular environment (By similarity). Required for assembly and activity of the vacuolar ATPase (By similarity). Through its action on compartment acidification, plays an essential role in neuronal development in terms of integrity and connectivity of neurons .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96467
Sequence Length: 839
Subcellular Location: Cytoplasmic vesicle
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Q9SJ40 | MYQLRKFDFFEEKYGGKIPEDVTGDIQCCSSGRGKVVIGSNDGSVSFLDRGVKFDSGFQAHSSSVLFLQHLKQRNFLVTVGEDEQISPQQSGMCLKVFDLDKVQEEGTSSSAPECIGILRIFTNQFPEAKITSFLVLEEVPPILLIAIGLDNGCIYCVKGDIARERITRFKLQVDGRSAITGLGFRMDGQALLLFAVTPESVNLFSMQAQPPKLQTLDHIGGSVNTVTMSDRSELIVGRPEAVYFYEVDGRGPCWAFEGEKKFMGWFRGYLLCVIDDSKTGNTVFNVYDLRNRLIAYSIVVDKVSNMLCEWGNIILIKADKSLLCITEKDMESKLDMLFKKNLYTVAINLVQSQHADAAATANVMRKYGDHLYGKQDFDEAMLQYINTIGYLEPSFVIQKFLDAQRIYNLTNYLEKLHEKGLASKDHTTLLLNCYTKLKDVEKLNTFIRKEDGIGELKFDVETAIRVCRAANYHEHAMYVAKKAGKHEWYLKILLEDLGNYDEALQYVSSLEPSQAGVTIEQYGKILIEHKPKETIDILMRLCTEQGIPNGVFLSMLPSPVDFITVFVQHPHSLMHFLERYAEIVQDSPAQAEINNTLLELYLSRDLNFPSISLSENGLDKDLIDHSVAAAVSKADPEKKTNADSKDAMEKDCTERQQKGLELLKMAWPSDLEQPLYDVDLAVILCEMNSFKDGLLYLYEKMKFYKEVIACYMQNHDHEGLIACCKRLGDSSKGGDPSLWADLLKYFGEIGEDCTKEVKEVLTYIERDDILPPIIVLQTLAKNPCLTLSVIKDYIARKLEQESKIIEEDRRAVEKYQETTKNMRKEIEDLRTNARIFQLSKCTACTFTLDIPAVHFMCMHSFHQRCLGDNEKECPECAPEYRSVMEMKRSLEQNSKDQDLFFQQVKGSKDGFSVIAEYFGKGIISKTRDATS | 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 | MTEFGWRRFNFFDRSVVFDKDDPKQKFMGLKDVAVDCWCSSGGSVYLGEAKGGVFQLTNQFSEYYWKAYQKSLASLHSADKYLFSIGEDDETVNTLLKIWDPERVEKNTPHVMRTIRMSPLNPTSSSPACSIAVHSSLQSVVVGYTDGTVLFYQGDVLHDKSLNSRWIKVRDSSVGEGSVTGLAIAVLPASKTVVFVITQKHVHSYVLENGRTVIAHKKHDANGATADCWTFDESTGQLIVASREMLFFYDADQCIDMDGGEVGRCLQLGRGHEKLQLVASGQYLALLTKHHSLIQKERDSEFMTMLSVYDIKGQYVGFSCSLPNLCRLFIAGSTMLVLSHDGLLSELIEKNLATKLDILVKKSMFDVAVLIAKNSRDGGDYLKGIHAKYGNYLYGKGDYENAIQQYKETIGMLEPSYVMKRYLDSSKIKELCIYLECLHDAKRDNEHQTKILMNAYAKQGEKKKLMEFVNKITDGTRVSRMRDVFEILLKWNYLAEASLLATKFQMHEDALNVIIHHMHKYTMGVTYISKMPIESVIEMTGKFGRDLLIHARDDLMHMLWEKIQENTDAKKNNFMRIFDIFMGDMDASRVFLSYIENQTNEHDEFIIPILECQMRLFKVNSDWSQERLEEDIYRFINKKNEDAALQMAQLFDCTPVIEHILMRCHKSKELMMYHQKKRDLEAIIRLCQSCSKEEKRRLWLDALSFIGKHATARDELIIIDLLKEIEASEQIHPLVVLELLAKNEHLTISSVRDYIIAWLRKQQIIIEEDRNTIKENNKAMGELDGTVESLKFNAQIMQVTKCSACDTPLQLPTVHFLCKHAYHVHCFESYNMDGSDKCPACQTTRDTTRDEEISYHKFQKELAEASNGMELIAMYLQRGLFDEKTKKTKKSEAKKDPFSTGRASTTTNPFDDDEVTTISRTMSTVSSNMATPSRQRSITRKDDDSTNPFFNSDSGTRLSTYDESKNPFGAPAPSTNPFD | 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 probably implicating sand-1, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion (By similarity). The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes (By similarity). Within the HOPS complex, contributes to the normal development of gut granules in embryonic and adult intestinal cells . The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations (By similarity). Required for fusion of endosomes and autophagosomes with lysosomes . Involved in cargo transport from early to late endosomes and required for the transition from early to late endosomes (By similarity). Possibly has a role in clearance of apoptotic cells during programmed cell death .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 112009
Sequence Length: 980
Subcellular Location: Late endosome membrane
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Q54YP4 | MNNWKRFTFFDIETVKQVEKEDGSSLQKLSITCTTSGRGSLIIGDAEGFINFVDREFGISSFQAYQQSVSLIYQLKERNFLSSVGHDDIGGAAILKIWNLDKTDKNEQPICVRSIKLEKSVTVTCFTLLEDLSQIIVGLANGEIIIIRADIFRDKVIKQKIIKVPNDSPITGLGFFPTKSQQSASAGAVLFVVTTTHVITYHTAHKDQETIIDDEGGDIGSFLMSDDGSPIIARSDAIYFYNVDGRGPCFGFTGVKTKVLWFRSYLVVIGYDTNNTNALFPGAVVGGQNSIGGLGSQTGSIGSPSVMVQNTKNNVLNIYDLKNKYIGFTEKFDTVSHICSEWGSIFIFGADGKVFQLEEKDTQTKLETLFKKHSYQVAIDLAKSQHYDNSAIADVYREYGDRLYAKGDYDGAITQYLCTIGQLEPSYVIRKFLDAQRIHNLTSYIQALHEKNLATANHTTLLLNCYTKLKDVKKLDHFIMTDNGTFDVETAIKVCRQGGYFDRALFLASKHSRHDWYLKILLEDLNEYRKALDYIQTLDWEEADKNLKKYGKQLVSEIPEETTGVLMKLCTNYQPVQAFDSLTALNLNGLTISNQTTTTTTVTNVTNNNNQNNNSNNNNQNNNNNNNNNIGFKQKSAPEEFIHIFVSQADWLVKFLEYMVQQGNNESSLIYNTLLELYLRDDVNQTDDERIKRKAKAYEFLTNPKSKFDQDHALILVQVHNWKEGVLYLYEKLELFNEIIEYHMENNDYDGLIKACKRYGVKDPNLWVRALSFFSTNKQDCQDEIIEVLTNIDKENLIPPLLVIQILSQNKNTTLAVIKDYISRRLSQETQQIDKDYTQIRQYADETEKMRHEINELRTNSKIFQQTKCIACLLALDLPSVHFLCQHSFHQRCLGENERECPSCAGANKRIQEIKRSQADSANQHDQFFKLLRSSPDGFTTVSEYFGRGILN | 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 | MAAYLQWRRFVFFDKELVKEPLSNDGAAPGATPASGSAASKFLCLPPGITVCDSGRGSLVFGDMEGQIWFLPRSLQLTGFQAYKLRVTHLYQLKQHNILASVGEDEEGINPLVKIWNLEKRDGGNPLCTRIFPAIPGTEPTVVSCLTVHENLNFMAIGFTDGSVTLNKGDITRDRHSKTQILHKGNYPVTGLAFRQAGKTTHLFVVTTENVQSYIVSGKDYPRVELDTHGCGLRCSALSDPSQDLQFIVAGDECVYLYQPDERGPCFAFEGHKLIAHWFRGYLIIVSRDRKVSPKSEFTSRDSQSSDKQILNIYDLCNKFIAYSTVFEDVVDVLAEWGSLYVLTRDGRVHALQEKDTQTKLEMLFKKNLFEMAINLAKSQHLDSDGLAQIFMQYGDHLYSKGNHDGAVQQYIRTIGKLEPSYVIRKFLDAQRIHNLTAYLQTLHRQSLANADHTTLLLNCYTKLKDSSKLEEFIKKKSESEVHFDVETAIKVLRQAGYYSHALYLAENHAHHEWYLKIQLEDIKNYQEALRYIGKLPFEQAESNMKRYGKILMHHIPEQTTQLLKGLCTDYRPSLEGRSDREAPGCRANSEEFIPIFANNPRELKAFLEHMSEVQPDSPQGIYDTLLELRLQNWAHEKDPQVKEKLHAEAISLLKSGRFCDVFDKALVLCQMHDFQDGVLYLYEQGKLFQQIMHYHMQHEQYRQVISVCERHGEQDPSLWEQALSYFARKEEDCKEYVAAVLKHIENKNLMPPLLVVQTLAHNSTATLSVIRDYLVQKLQKQSQQIAQDELRVRRYREETTRIRQEIQELKASPKIFQKTKCSICNSALELPSVHFLCGHSFHQHCFESYSESDADCPTCLPENRKVMDMIRAQEQKRDLHDQFQHQLRCSNDSFSVIADYFGRGVFNKLTLLTDPPTARLTSSLEAGLQRDLLMHSRRGT | 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 conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations . Required for fusion of endosomes and autophagosomes with lysosomes . Involved in cargo transport from early to late endosomes and required for the transition from early to late endosomes . Involved in the retrograde Shiga toxin transport .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 107837
Sequence Length: 941
Subcellular Location: Endosome
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Q60V75 | MKESTRTSTPSSGAKPKGDREICLRPSSSVFLGDQQLYFTQEYLATNSLNMKYVVYFAACQFSGPIAVIYAAPKSWFIWIRTISGRILKRDLPCTDPVFIDWTRAHCLLVLSKNGRAQVLSSIGEKVSEVFFDNQVSDVHECRTFATSRGDSGIAVMDVDGQVAVVNSVSEPVIWSMRPPYSELPTAWTAFQPHSQLTHILLIFEAVFLMGCQGESLQVQNHASVWVDSSTKYVKCVVDDARSRIAMMTENGKIQIVSIDLSTCFCTVEVTEHEIGKCINFGWVGNSVVFVQMSSSLTVFVNVSARRKPGDEVRFMSIKMTANARISVEPDGIRLFESTRVEFVEAASREKIAVLNRSLNEDGAYLYKAAQEMEQGTGHNSFAASTVIQDMYKAIDDCISTACDTWQPEEQKLLLKAARFGMAYTNTTPDTTKLMRAIKEIRVLNELRMVRTGIPLTHRQYRIIGDTCIINRLIDMGSYSVAIKVAQWLGGENCESVDRVLLEWVRRSISKVSRSNMKMDQPALEALDEKISAKLLQFPHVSMADAARRAIEAKLPELARLFIRRETDDESHVAVLLQLNDVSAALTKAAASQRPQLIHQVVRHLMTSESRSSYELAISRIPLAQCLYQDLVRQEGETRGISSRQMLALLEQASDFERQTLFHFDVAEIERNPSERLNALRRAKDAAKSMGDKAIEEILNDVSAFAPLQIQRGQADMSVRDTIIEIADDTAKVAQLKQQARLNDKQVLLWTIEGLAKKGKMEQLFDLAQKRSPIGYAPFVKACVRYKRNEEVNKYFAKANGYSDLVAANLAKKNYVDAAKLAYDRRDREVLHAIHMKSHDDPVQCPRVKQLLNSMDQA | 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 probably implicating sand-1, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to rab-7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. Within the HOPS complex, contributes to the normal development of gut granules in the adult intestine. The CORVET complex is proposed to function as a rab-5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for recruitment of vps-33.1 to the HOPS complex. Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with vps-33.1 but not vps-33.2.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 96378
Sequence Length: 858
Subcellular Location: Late endosome membrane
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Q11182 | MGESHAPSKPKLDGELCLRPSSSVFLGDQQLYFTQEYLRTNSLNLKYVVYFTACQFSGPIAVAYSPRPASWYIWIRTISGRILKRDMAFNEPVFMEWTRAHCLLVLNKAGRAHIFSSLGEKISEVIFDSQMSDVHECRTFATSRGDSGIAVMDVDGQVSVVNSVSEPVIWSMKPPYSEMPTAWTAFQPHSQLTHILLIFEAVFLMGCQGESLREQSHAASWVDSNTKYVKCVVDDARSRIAMMTESGKIQIVSIDLSTCFCTVEITDHDIAKCINFGWVGNSAVFVQMSPSLIVFVNVSARRKPGDEVQIYEKMTANAKISIEPDGIRLFESTQVEFVEAASREKIAVLNRNPNEDGAHLYKAAQEMSQGTGHNSFAASTVIQDLYKAIDDCISTACDTWQPEEQKLLLKAARFGMAYTNTTPDTTKLMRAIKEIRVLNELRMVRTGIPLTHRQFRAIGETCVINRLIDMGSYSVAIKVAQWLGGETSENVDRVLLEWVRRSISKVSKSNMKMDQPALEALDEKISAKLLQFPHVSIADAARRAIEAKLPELARLFIRRETDDANHVAVLLQLNDVSAALQKASASQRPQLIHQVVRHLMNSESRSSYELAISRIPLAQCLYQDLVRQEGETRGASSRQMLALLEQASDFERQTLFHFDVAETERNPDERLNALRRAKDAAKSMGDKAIEEILNDVSAFAPLQIQRGQADMSVRDTVIEMAHDTAKVAQLKQQARLTDKQVLLWTIEGLAKKGKMEQLFDLAQKRSPIGYAPFVKACVRYKRLDEIKKYFAKVNGYPDLVAAHLAMKNYVEAAKLAYDRRDRDVLHAVHMKSHEDPTQCPRVGQFLRSLDQN | 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 probably implicating sand-1, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion (By similarity). The HOPS complex is proposed to be recruited to rab-7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes (By similarity). Within the HOPS complex, contributes to the normal development of gut granules in the adult intestine . The CORVET complex is proposed to function as a rab-5 effector to mediate early endosome fusion probably in specific endosome subpopulations (By similarity). Required for recruitment of vps-33.1 to the HOPS complex (By similarity). Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with vps-33.1 but not vps-33.2 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 95843
Sequence Length: 852
Subcellular Location: Late endosome membrane
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Q55C58 | MIAAQWKIIGNSTYIKKEIYSMSWDVDLKQQVSVGSPFAGPIAVMRDSSKFVEMNSQNMKPYLKIFTASGDLISQMIWDSSKNIVAMDWIEKERLVIVLQNATVLIFNVFCEQMTQFSLGDIVREEEILECKIWSDGIVVLTSASQLYSVPSINDFFVESGRVIRLPPLPEEPKARPEWAILEPQFSLSQSIEIFMSINGTLYLIDEDKVESQLEATEPIQKMVVSPCGKKLACFDTKGTLLILKTDGSTTNPDRMDTKATKSPVLKWCGSDGVMMYWDSIKDPILFYFSKGDSWAKFTLDQPVSLVTEIDGLRIISDTTSEFFHKVSDVTIDIFKIGTTSPASILYDATDHFISKSPQADESIRSINDQLEDAVNDCILAAGFEFNGGEQSKLLKAASFGKCFLENYNPSQFVTMCRSLRVLNAVRHHEIGIPLSIKQYYHIGIEELIDRLISRRKHLLAWRICDYLKIKSDVVLNHWACTKVRTDIPDQELGKIIIKKLESVPGISFANIASAAYLAGRSKLATKLLEYEPKAAEQVPPLIKMGESGLALNKAIESGDTDLVYLVLLAMQRSLPLADFLELTFSKVVALDLLISMCKQKNDFPLLREIYHIKDQSKEMGNIYLQEALSSHPSQLDQRIKAYNKSIEHYHHSKDKDDQATSKFIDDQIKLEMLQKELETNLQDESFVGISINDTIYKLITMNQPKKAQSIRSEFKVPDKRFWWIKIKALSIMNDWEELMKFSKEKKSPIGYEPFVEVCLDQKNQIEALKYIPKITDILPKIQFYIQIGYFREAADIAFKEKNFDLLNLISRKCTNNEILNIIEQMKSQIRR | 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 | MDCYTANWNPLGDSAFYRKYELYSMDWDLKEELRDCLVAAAPYGGPIALLRNPWRKEKAASVRPVLDIYSASGMPLASLLWKSGPVVSLGWSAEEELLCVQEDGAVLVYGLHGDFRRHFSMGNEVLQNRVLDARIFHTEFGSGVAILTGAHRFTLSANVGDLKLRRMPEVPGLQSAPSCWTVLCQDRVAHILLAVGPDLYLLDHAACSAVTPPGLAPGVSSFLQMAVSFTYRHLALFTDTGYIWMGTASLKEKLCEFNCNIRAPPKQMVWCSRPRSKERAVVVAWERRLMVVGDAPESIQFVLDEDSYLVPELDGVRIFSRSTHEFLHEVPAASEEIFKIASMAPGALLLEAQKEYEKESQKADEYLREIQELGQLTQAVQQCIEAAGHEHQPDMQKSLLRAASFGKCFLDRFPPDSFVHMCQDLRVLNAVRDYHIGIPLTYSQYKQLTIQVLLDRLVLRRLYPLAIQICEYLRLPEVQGVSRILAHWACYKVQQKDVSDEDVARAINQKLGDTPGVSYSDIAARAYGCGRTELAIKLLEYEPRSGEQVPLLLKMKRSKLALSKAIESGDTDLVFTVLLHLKNELNRGDFFMTLRNQPMALSLYRQFCKHQELETLKDLYNQDDNHQELGSFHIRASYAAEERIEGRVAALQTAADAFYKAKNEFAAKATEDQMRLLRLQRRLEDELGGQFLDLSLHDTVTTLILGGHNKRAEQLARDFRIPDKRLWWLKLTALADLEDWEELEKFSKSKKSPIGYLPFVEICMKQHNKYEAKKYASRVGPEQKVKALLLVGDVAQAADVAIEHRNEAELSLVLSHCTGATDGATADKIQRARAQAQKK | 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 conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations . Required for recruitment of VPS33A to the HOPS complex . Required for fusion of endosomes and autophagosomes with lysosomes; the function is dependent on its association with VPS33A but not VPS33B . The function in autophagosome-lysosome fusion implicates STX17 but not UVRAG .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 94694
Sequence Length: 839
Subcellular Location: Late endosome membrane
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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 budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Acts as a viroporin that forms an oligomeric ion channel in membranes. Modulates the host DNA repair mechanisms to promote degradation of nuclear viral cDNA in cells that are already productively infected in order to suppress immune sensing and proviral hyper-integration (superinfection). Manipulates PML-NBs and modulates SUMOylation of host BLM protein thereby enhancing its DNA-end processing activity toward viral unintegrated linear DNA. Also inhibits RAD52-mediated homologous repair of viral cDNA, preventing the generation of dead-end circular forms of single copies of the long terminal repeat and permitting sustained nucleolytic attack.
PTM: Phosphorylated by host CK2. This phosphorylation is necessary for interaction with human BTRC and degradation of CD4.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 9463
Sequence Length: 81
Domain: The N-terminus and transmembrane domains are required for self-oligomerization and proper virion budding, whereas the cytoplasmic domain is required for CD4 degradation. The cytoplasmic domain is composed of 2 amphipathic alpha helix that form a U-shape.
Subcellular Location: Host membrane
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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 budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to interfere with the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Acts as a viroporin that forms an oligomeric ion channel in membranes. Modulates the host DNA repair mechanisms to promote degradation of nuclear viral cDNA in cells that are already productively infected in order to suppress immune sensing and proviral hyper-integration (superinfection). Manipulates PML-NBs and modulates SUMOylation of host BLM protein thereby enhancing its DNA-end processing activity toward viral unintegrated linear DNA. Also inhibits RAD52-mediated homologous repair of viral cDNA, preventing the generation of dead-end circular forms of single copies of the long terminal repeat and permitting sustained nucleolytic attack.
PTM: Phosphorylated by host CK2. This phosphorylation is necessary for interaction with human BRCP and degradation of CD4 (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 4131
Sequence Length: 37
Domain: The N-terminus and transmembrane domains are required for self-oligomerization and proper virion budding, whereas the cytoplasmic domain is required for CD4 degradation. The cytoplasmic domain is composed of 2 amphipathic alpha helix that form a U-shape.
Subcellular Location: Host membrane
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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 budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to interfere with the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Acts as a viroporin that forms an oligomeric ion channel in membranes. Modulates the host DNA repair mechanisms to promote degradation of nuclear viral cDNA in cells that are already productively infected in order to suppress immune sensing and proviral hyper-integration (superinfection). Manipulates PML-NBs and modulates SUMOylation of host BLM protein thereby enhancing its DNA-end processing activity toward viral unintegrated linear DNA. Also inhibits RAD52-mediated homologous repair of viral cDNA, preventing the generation of dead-end circular forms of single copies of the long terminal repeat and permitting sustained nucleolytic attack.
PTM: Phosphorylated by host CK2. This phosphorylation is necessary for interaction with human BRCP and degradation of CD4 (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 6789
Sequence Length: 58
Domain: The N-terminus and transmembrane domains are required for self-oligomerization and proper virion budding, whereas the cytoplasmic domain is required for CD4 degradation. The cytoplasmic domain is composed of 2 amphipathic alpha helix that form a U-shape.
Subcellular Location: Host membrane
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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 budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to interfere with the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Acts as a viroporin that forms an oligomeric ion channel in membranes. Modulates the host DNA repair mechanisms to promote degradation of nuclear viral cDNA in cells that are already productively infected in order to suppress immune sensing and proviral hyper-integration (superinfection). Manipulates PML-NBs and modulates SUMOylation of host BLM protein thereby enhancing its DNA-end processing activity toward viral unintegrated linear DNA. Also inhibits RAD52-mediated homologous repair of viral cDNA, preventing the generation of dead-end circular forms of single copies of the long terminal repeat and permitting sustained nucleolytic attack.
PTM: Phosphorylated by host CK2. This phosphorylation is necessary for interaction with host BRCP and degradation of CD4, but not for enhancement of virion budding (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 10565
Sequence Length: 88
Domain: The N-terminus and transmembrane domains are required for self-oligomerization and proper virion budding, whereas the cytoplasmic domain is required for CD4 degradation. The cytoplasmic domain is composed of 2 amphipathic alpha helix that form a U-shape.
Subcellular Location: Host membrane
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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 budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Acts as a viroporin that forms an oligomeric ion channel in membranes. Modulates the host DNA repair mechanisms to promote degradation of nuclear viral cDNA in cells that are already productively infected in order to suppress immune sensing and proviral hyper-integration (superinfection). Manipulates PML-NBs and modulates SUMOylation of host BLM protein thereby enhancing its DNA-end processing activity toward viral unintegrated linear DNA. Also inhibits RAD52-mediated homologous repair of viral cDNA, preventing the generation of dead-end circular forms of single copies of the long terminal repeat and permitting sustained nucleolytic attack.
PTM: Phosphorylated by host CK2. This phosphorylation is necessary for interaction with human BTRC and degradation of CD4.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 9136
Sequence Length: 79
Domain: The N-terminus and transmembrane domains are required for self-oligomerization and proper virion budding, whereas the cytoplasmic domain is required for CD4 degradation. The cytoplasmic domain is composed of 2 amphipathic alpha helix that form a U-shape.
Subcellular Location: Host membrane
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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 budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Acts as a viroporin that forms an oligomeric ion channel in membranes. Modulates the host DNA repair mechanisms to promote degradation of nuclear viral cDNA in cells that are already productively infected in order to suppress immune sensing and proviral hyper-integration (superinfection). Manipulates PML-NBs and modulates SUMOylation of host BLM protein thereby enhancing its DNA-end processing activity toward viral unintegrated linear DNA. Also inhibits RAD52-mediated homologous repair of viral cDNA, preventing the generation of dead-end circular forms of single copies of the long terminal repeat and permitting sustained nucleolytic attack.
PTM: Phosphorylated by host CK2. This phosphorylation is necessary for interaction with human BTRC and degradation of CD4.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 9985
Sequence Length: 86
Domain: The N-terminus and transmembrane domains are required for self-oligomerization and proper virion budding, whereas the cytoplasmic domain is required for CD4 degradation. The cytoplasmic domain is composed of 2 amphipathic alpha helix that form a U-shape.
Subcellular Location: Host membrane
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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 budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to interfere with the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Acts as a viroporin that forms an oligomeric ion channel in membranes. Modulates the host DNA repair mechanisms to promote degradation of nuclear viral cDNA in cells that are already productively infected in order to suppress immune sensing and proviral hyper-integration (superinfection). Manipulates PML-NBs and modulates SUMOylation of host BLM protein thereby enhancing its DNA-end processing activity toward viral unintegrated linear DNA. Also inhibits RAD52-mediated homologous repair of viral cDNA, preventing the generation of dead-end circular forms of single copies of the long terminal repeat and permitting sustained nucleolytic attack.
PTM: Phosphorylated by host CK2. This phosphorylation is necessary for interaction with host BRCP and degradation of CD4, but not for enhancement of virion budding (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 9580
Sequence Length: 83
Domain: The N-terminus and transmembrane domains are required for self-oligomerization and proper virion budding, whereas the cytoplasmic domain is required for CD4 degradation. The cytoplasmic domain is composed of 2 amphipathic alpha helix that form a U-shape.
Subcellular Location: Host membrane
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P92127 | MLLTAFYVVLGSFAAPCQQDGDHIVTCQVNKCETVGLFEICTECKTGGVPVDGFCRPFGSIQAAAAGCTKADGTALDKTATTCGKCGDGYFLFMGGCYKTESQPGSEICTTASNGLCTACKVDSQYIFQNKATPSEKGSECILCWDTTDRNGVMGVANCATCTAPASSTGPATCTECMAGTYKKSDTECAACHSDCATCSGEANNQCTSCETGKYLKSNQCVEKNTCNTNHYPDDTSMTCVACTVLDANCATCSFDSATAKGKCLTCNSNKIPRTTLDGTSTCVENSYAGCQGADNELFMKEDQSACLLCGDTKEASNDKGVANCRTCTKNANDSPPTCTACLDGYFLERGSCTTTCADNCATCSEATTEDKCKICKAGFFLASPGEGKCISCSDTNNGGIDGCAECTKEPAGPLKCTKCKPNRKPAGTSDNYTCTEKTCEDPTVCGGTSGACDAIVIDANGKEHYYCSYCGETNKFPIDGLCTDNKGTNAGCTDHTCSYCAAGFFLYMGGCYKIDTVPGSYMCSKSTTAGVCDTPNANNRFFVVPKAISAEQSVLACGNPLGTIAGGNAYVGVEGCSQCTAPDARADGGMAVATCTACEDGKKPGKSGTGCVACPDANCKSCTMDDVCEECADGFSLDNGKCVSSGTNKSGLSTGAIAGISVAAIVVVGGLVGFLCWWFICRGKAQ | 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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