VP1_POVS1
ID VP1_POVS1 Reviewed; 362 AA.
AC Q1W5X1; Q3L6L6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 02-JUN-2021, entry version 57.
DE RecName: Full=Major capsid protein VP1;
DE AltName: Full=Major structural protein VP1;
OS Simian virus 12 (strain wt100) (SV-12) (Baboon polyomavirus 1).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; unclassified Polyomaviridae.
OX NCBI_TaxID=557605;
OH NCBI_TaxID=36229; Papio hamadryas ursinus (Chacma baboon).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SA12;
RX PubMed=16189011; DOI=10.1128/jvi.79.20.13094-13104.2005;
RA Cantalupo P., Doering A., Sullivan C.S., Pal A., Peden K.W., Lewis A.M.,
RA Pipas J.M.;
RT "Complete nucleotide sequence of polyomavirus SA12.";
RL J. Virol. 79:13094-13104(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SA12;
RX PubMed=16731904; DOI=10.1128/jvi.00056-06;
RA Perez-Losada M., Christensen R.G., McClellan D.A., Adams B.J.,
RA Viscidi R.P., Demma J.C., Crandall K.A.;
RT "Comparing phylogenetic codivergence between polyomaviruses and their
RT hosts.";
RL J. Virol. 80:5663-5669(2006).
RN [3]
RP REVIEW.
RX PubMed=19157478; DOI=10.1016/j.virol.2008.12.021;
RA Neu U., Stehle T., Atwood W.J.;
RT "The Polyomaviridae: Contributions of virus structure to our understanding
RT of virus receptors and infectious entry.";
RL Virology 384:389-399(2009).
CC -!- FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and a 40 nm
CC diameter. The capsid is composed of 72 pentamers linked to each other
CC by disulfide bonds and associated with VP2 or VP3 proteins. Interacts
CC with sialic acids on the cell surface to provide virion attachment to
CC target cell. Once attached, the virion is internalized by endocytosis
CC and traffics to the endoplasmic reticulum. Inside the endoplasmic
CC reticulum, the protein folding machinery isomerizes VP1 interpentamer
CC disulfide bonds, thereby triggering initial uncoating. Next, the virion
CC uses the endoplasmic reticulum-associated degradation machinery to
CC probably translocate in the cytosol before reaching the nucleus.
CC Nuclear entry of the viral DNA involves the selective exposure and
CC importin recognition of VP2/Vp3 nuclear localization signal. In late
CC phase of infection, neo-synthesized VP1 encapsulates replicated genomic
CC DNA in the nucleus, and participates in rearranging nucleosomes around
CC the viral DNA. {ECO:0000250|UniProtKB:P03087,
CC ECO:0000305|PubMed:19157478}.
CC -!- SUBUNIT: Homomultimer; disulfide-linked. The virus capsid is composed
CC of 72 icosahedral units, each one composed of five disulfide-linked
CC copies of VP1. Interacts with minor capsid proteins VP2 and VP3.
CC {ECO:0000250|UniProtKB:P03087}.
CC -!- SUBCELLULAR LOCATION: Virion. Host nucleus
CC {ECO:0000250|UniProtKB:P03087}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=5;
CC Name=VP1; Synonyms=Major capsid protein VP1;
CC IsoId=Q1W5X1-1; Sequence=Displayed;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=Q3L6L8-1; Sequence=External;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=Q3L6L8-2; Sequence=External;
CC Name=VP4; Synonyms=Viroporin VP4;
CC IsoId=Q3L6L8-3; Sequence=External;
CC Name=Agno;
CC IsoId=Q3L6L9-1; Sequence=External;
CC -!- DOMAIN: A DNA-binding domain overlapping a bipartite nuclear
CC localization signal is present in the N-terminal region of the protein
CC and is required for efficient virus formation.
CC {ECO:0000250|UniProtKB:P03087}.
CC -!- MISCELLANEOUS: [Isoform VP1]: Produced by alternative splicing of the
CC late mRNA.
CC -!- SIMILARITY: Belongs to the polyomaviruses coat protein VP1 family.
CC {ECO:0000305}.
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DR EMBL; DQ435829; ABD92876.1; -; Genomic_DNA.
DR EMBL; AY614708; AAV75982.1; -; Genomic_DNA.
DR SMR; Q1W5X1; -.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039620; C:T=7 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.60.175.10; -; 1.
DR InterPro; IPR000662; Capsid_VP1_Polyomavir.
DR InterPro; IPR011222; dsDNA_vir_gr_I_capsid.
DR InterPro; IPR036931; Polyomavir_VP1_sf.
DR Pfam; PF00718; Polyoma_coat; 1.
DR PIRSF; PIRSF003376; Capsid_VP1_Polyomavir; 1.
DR SUPFAM; SSF88648; SSF88648; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Alternative initiation; Alternative splicing; Capsid protein;
KW Disulfide bond; Host nucleus; Host-virus interaction; Late protein;
KW Phosphoprotein; T=7 icosahedral capsid protein;
KW Viral attachment to host cell; Viral penetration into host cytoplasm;
KW Virion; Virus endocytosis by host; Virus entry into host cell.
FT CHAIN 1..362
FT /note="Major capsid protein VP1"
FT /id="PRO_0000356258"
FT MOTIF 5..19
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P03087"
FT MOD_RES 338
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000250"
FT DISULFID 10
FT /note="Interchain (with C-10)"
FT /evidence="ECO:0000250"
FT DISULFID 105
FT /note="Interchain (with C-105)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 362 AA; 40183 MW; 4BCB6D289801811D CRC64;
MPPAKRKGEC PGAAPKKPKD PVRVPKLLIR GGVEVLEVKT GVDSITEVEC FLTPEMGDAN
EHLRGYSQRV TCDVTFENDA PQKKTLPCYS TARIPLPNLN EDLTCGNILM WEAVTVKTEV
LGVTSMLNLH AEAQKVHDNG AGRPVQGSNF HFFSVGGEPL ELQGVLHNYR TTYPEGTIAP
KNPTAESQVM NTEHKAYLDK TGAYPVECWV PDPSRNENTR YFGTYTGGEN VPPVLHVTNT
ATTVLLDEQG VGPLCKADSL YVSAVDICGL FTNSSGTQQW RGLSRYFKIS LRKRSVKNPY
PISFLLSDLI NRRTTRVQGQ PMYGMNAQVE EVRVYDGTEE LPGDPDMMRY IDKYGQHQTK
ML
