VP1_POVSM
ID VP1_POVSM Reviewed; 357 AA.
AC A8Y983;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 23-FEB-2022, entry version 56.
DE RecName: Full=Major capsid protein VP1;
DE AltName: Full=Major structural protein VP1;
GN Name=VP1;
OS Squirrel monkey polyomavirus.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX NCBI_TaxID=452475;
OH NCBI_TaxID=39432; Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Squi0106;
RX PubMed=18089736; DOI=10.1099/vir.0.83287-0;
RA Verschoor E.J., Groenewoud M.J., Fagrouch Z., Kewalapat A., van Gessel S.,
RA Kik M.J., Heeney J.L.;
RT "Molecular characterization of the first polyomavirus from a New World
RT primate: squirrel monkey polyomavirus.";
RL J. Gen. Virol. 89:130-137(2008).
RN [2]
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=A8Y983-1; Sequence=Displayed;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=A8Y987-1; Sequence=External;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=A8Y987-2; Sequence=External;
CC Name=VP4;
CC IsoId=A8Y987-3; Sequence=External;
CC Name=Agno;
CC IsoId=A8Y986-1; 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 -!- DOMAIN: The intrinsically disordered C-terminal arm interacts with
CC neighboring pentamers. The unstructured nature of this region allows to
CC make different interactions depending on the structural context:
CC pentamers present at the 12 icosahedral fivefold axes bind five
CC pentamers, whereas pentamers present at the 60 icosahedral six-fold
CC axes interact with six pentamers. {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; AM748741; CAO03082.1; -; Genomic_DNA.
DR RefSeq; YP_001531348.1; NC_009951.1. [A8Y983-1]
DR SMR; A8Y983; -.
DR GeneID; 5714858; -.
DR KEGG; vg:5714858; -.
DR Proteomes; UP000135044; Genome.
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.
PE 3: Inferred from homology;
KW Alternative initiation; Alternative splicing; Capsid protein;
KW Disulfide bond; Host nucleus; Host-virus interaction; Late protein;
KW Phosphoprotein; Reference proteome; 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..357
FT /note="Major capsid protein VP1"
FT /id="PRO_0000356257"
FT REGION 296..357
FT /note="C-terminal arm"
FT /evidence="ECO:0000250|UniProtKB:P03087"
FT MOTIF 4..13
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P03087"
FT MOD_RES 329
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 357 AA; 39811 MW; DEC16F9FE3B16F25 CRC64;
MPLKKRSASA PRKTPQEVPR LLISGGVEVL GLKTGPDSIT EVEAFLNPRM GLENTDNHYG
YSENVTVAKK KDDDKPLKNQ LPCYSVAKIE LPMLNEDLTN DTILMWECIS VKTEVVGINT
LVNTHSYGKR DGESPSMPIV GLNYHFFAVG GEPIEMQYIV QNFQCDYPVG VVAMKPSPLS
TQVLDPKQKS KLTGDGIFPI ECWAPDPSKN ENARYFATYT GGLNTPPVLN ITNTVTTILL
NENGVGPLCK GDQLHIAAAD ICGFHIEEDN KYKYRGLPRY FKLVLRKRVV KNPYPVSTLL
NTLFTQMSPN VQGQDMTKQV EEVKIYEGTE KLPGDPDMIR FRNQFGQEET VIPVITN
