VP1_POVBA
ID VP1_POVBA Reviewed; 362 AA.
AC P14996;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 02-JUN-2021, entry version 93.
DE RecName: Full=Major capsid protein VP1;
DE AltName: Full=Major structural protein VP1;
OS BK polyomavirus (strain AS) (BKPyV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX NCBI_TaxID=10631;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2536111; DOI=10.1128/jvi.63.2.901-911.1989;
RA Tavis J.E., Walker D.L., Gardner S.D., Frisque R.J.;
RT "Nucleotide sequence of the human polyomavirus AS virus, an antigenic
RT variant of BK virus.";
RL J. Virol. 63:901-911(1989).
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 50 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 gangliosides GT1b and GD1b containing terminal alpha(2-8)-linked
CC sialic acids on the cell surface to provide virion attachment to target
CC cell. This attachment induces virion internalization predominantly
CC through caveolin-mediated endocytosis and traffics to the endoplasmic
CC reticulum. Inside the endoplasmic reticulum, the protein folding
CC machinery isomerizes VP1 interpentamer disulfide bonds, thereby
CC triggering initial uncoating. Next, the virion uses the endoplasmic
CC reticulum-associated degradation machinery to probably translocate in
CC the cytosol before reaching the nucleus. Nuclear entry of the viral DNA
CC involves the selective exposure and importin recognition of VP2/Vp3
CC nuclear localization signal. In late phase of infection, neo-
CC synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and
CC participates in rearranging nucleosomes around the viral DNA.
CC {ECO:0000250|UniProtKB:P03087, 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;
CC IsoId=P14996-1; Sequence=Displayed;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P14997-1; Sequence=External;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P14997-2; Sequence=External;
CC Name=VP4; Synonyms=Viroporin VP4;
CC IsoId=P14997-3; Sequence=External;
CC Name=Agno;
CC IsoId=P14998-1; 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; M23122; AAA46882.1; -; Genomic_DNA.
DR PIR; D33278; VVVP1S.
DR SMR; P14996; -.
DR Proteomes; UP000008166; 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:0075513; P:caveolin-mediated endocytosis of virus by 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 Caveolin-mediated endocytosis of virus by host; Disulfide bond;
KW Host nucleus; Host-virus interaction; Late protein; Phosphoprotein;
KW T=7 icosahedral capsid protein; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT CHAIN 1..362
FT /note="Major capsid protein VP1"
FT /id="PRO_0000115017"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 40113 MW; 5BDCEC52F247F238 CRC64;
MAPTKRKGEC PGAAPKKPKE PVQVPKLLIK GGVEVLEVKT GVDAITEVEC FLNPEMGDPD
DNLRGYSQHL SAENAFESDS PDRKMLPCYS TARIPLPNLN EDLTCGNLLM WEAVTVKTEV
IGITSMLNLH AGSQKVHENG GGKPVQGSNF HFFAVGGDPL EMQGVLMNYR TKYPQGTITP
KNPTAQSQVM NTDHKAYLDK NNAYPVECWI PDPSRNENTR YFGTYTGGEN VPPVLHVTNT
ATTVLLDEQG VGPLCKADSL YVSAADICGL FTNSSGTQQW RGLARYFKIR LRKRSVKNPY
PISFLLSDLI NRRTQKVDGQ PMYGMESQVE EVRVFDGTEQ LPGDPDMIRY IDRQGQLQTK
MV
