ID  P29165;
PN  Non-structural protein 2A;
GN  POLG;
OS  31641;
SL  Nucleus Position: SL-0382;
SL  Comments: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Envelope protein E]: Virion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P03314}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P03314}; Multi-pass membrane protein {ECO:0000255}. Note=ER membrane retention is mediated by the transmembrane domains. {ECO:0000250|UniProtKB:P03314}. [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.
DR  UNIPROT: P29165;
DR  Pfam: PF01003;
DR  Pfam: PF02832;
DR  Pfam: PF00869;
DR  Pfam: PF01004;
DR  Pfam: PF00948;
DR  Pfam: PF01570;
DE  Function: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. {ECO:0000250|UniProtKB:P17763}. [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}. [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}. [Protein prM]: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}. [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. {ECO:0000250|UniProtKB:P17763}. [Non-structural protein 1]: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3). {ECO:0000250|UniProtKB:Q9Q6P4}. [Non-structural protein 2A]: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response. {ECO:0000250|UniProtKB:P17763}.
DE  Reference Proteome: No;
GO  GO:0005576;
GO  GO:0044167;
GO  GO:0042025;
GO  GO:0044220;
GO  GO:0016021;
GO  GO:0019028;
GO  GO:0019031;
GO  GO:0055036;
GO  GO:0005524;
GO  GO:0004386;
GO  GO:0016787;
GO  GO:0046983;
GO  GO:0005198;
GO  GO:0075512;
GO  GO:0039654;
GO  GO:0019062;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MSGRKAQGKTLGVNMVRQGVRSLSNKIKQKTKQIGNRPGPSRGVQGFIFFFLFNVLTGRKITAHLKKLWRMLDPRQGLAV
SQ  LKKVKRVVASLMRGLSSRKRRSYEVLTVQFLILGMLLMTGGVTLVRKSRWLLLNVTSEDLGKTFSVGTGNCTTNILEAKN
SQ  WCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGKCDSAGRSRRSRRAIDLPTHENHGLKTRQEKWMTGRMGERQLQ
SQ  KIERWLVRNPFFAVTALAIAYLVGSNMTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSATLEQDKCVTVMA
SQ  PDKPSLDISLETVAIDGPAEARKVCYSAVLTHVKINDKCPSTGEAHLAEENEGDHACKRTYSDRGWGNGCGLFGKGSIVA
SQ  CAKFTCAKSMSLFEVDQTKIQYVIRAQLHVGAKQENWNADIKTLKFDALSGSQEAEFTGYGKATLECQVQTAVDFSNSYI
SQ  AEMEKESWIVDRQWAQDLTLPWQSGSGGVWREMHHLVEFEPPHAATIKVLALGNQEGSLKTALTGAMRVTKDTNGSNLYK
SQ  LHGGHVSCRVKLSALTLKGTSYKMCTDKMSFVKNPTDTGHGTAVMQVKVPKGAPCRIPVMVADDLTASVNKGILVTVNPI
SQ  ASTNEDEVLIEVNPPFGDSYIIVGTGDSRLTYQWHKEGSSIGKLFTQTMKGAERLAVMGDAAWDFSSAGGFFTSVGKGIH
SQ  MVFGSAFQGLFGGLSWITKVIMGAVLIWVGINMRNMTMSMSMILVGVIMMFLSLGVGADQGCAINFGKRELKCGDGVFIF
SQ  RDSDDWLNKYSYYPEDPVKLASIVKASFEEGKCGLNSVDSLEHEMWRSRADEINAILEENEVDISVVVQDPKNIYQRGTH
SQ  PFSRIRDGLQYGWKTWGKNLVFSPGRKNGSFIIDGKSRKECPFSNRVWNSLQIEEFGTGVFTTRVYMDAVFEYTMDCDGS
SQ  ILGAAVNGKKSAHGSPTFWMGSHEVNGTWMIHTLETLDYKECEWPLTHTIGTSVEESDMFMPRSIGGPVSSHNHIPGYKV
SQ  QTNGPWMQVPLEVKREACPGTSVVVDGGCDGRGKSTRSTTDSGKIIPEWCCRSCTMPPVSFHGSDGCWYPMEIRPRKTHD
SQ  NHLVRSWVTAGEVHAVPFGLVSMMIAMEVFLKKRQGPKQILVG
//