VP1_POVBK
ID VP1_POVBK Reviewed; 362 AA.
AC P03088; Q84322;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 29-SEP-2021, entry version 118.
DE RecName: Full=Major capsid protein VP1;
DE AltName: Full=Major structural protein VP1;
OS BK polyomavirus (BKPyV) (Human polyomavirus 1).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX NCBI_TaxID=1891762;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Dunlop;
RX PubMed=229976; DOI=10.1016/0092-8674(79)90209-5;
RA Seif I., Khoury G., Dhar R.;
RT "The genome of human papovavirus BKV.";
RL Cell 18:963-977(1979).
RN [2]
RP ERRATUM OF PUBMED:229976, AND SEQUENCE REVISION TO 158 AND 171.
RA Seif I., Khoury G., Dhar R.;
RL Cell 19:567-567(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MM;
RX PubMed=228391; DOI=10.1126/science.228391;
RA Yang R.C.A., Wu R.;
RT "BK virus DNA: complete nucleotide sequence of a human tumor virus.";
RL Science 206:456-462(1979).
RN [4]
RP FUNCTION.
RX PubMed=16415013; DOI=10.1128/jvi.80.3.1361-1366.2006;
RA Low J.A., Magnuson B., Tsai B., Imperiale M.J.;
RT "Identification of gangliosides GD1b and GT1b as receptors for BK virus.";
RL J. Virol. 80:1361-1366(2006).
RN [5]
RP FUNCTION.
RX PubMed=15479799; DOI=10.1128/jvi.78.21.11583-11590.2004;
RA Eash S., Querbes W., Atwood W.J.;
RT "Infection of vero cells by BK virus is dependent on caveolae.";
RL J. Virol. 78:11583-11590(2004).
RN [6]
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:0000269|PubMed:15479799,
CC ECO:0000269|PubMed:16415013, 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=P03088-1; Sequence=Displayed;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P03094-1; Sequence=External;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P03094-2; Sequence=External;
CC Name=VP4; Synonyms=Viroporin VP4;
CC IsoId=P03094-3; Sequence=External;
CC Name=Agno;
CC IsoId=P03085-1; 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; V01108; CAA24299.1; -; Genomic_DNA.
DR EMBL; V01109; CAA24307.1; -; Genomic_DNA.
DR PIR; E03632; VVVP1B.
DR RefSeq; YP_717939.1; NC_001538.1. [P03088-1]
DR PDB; 4MJ0; X-ray; 1.70 A; A/B/C/D/E=31-301.
DR PDB; 4MJ1; X-ray; 2.00 A; A/B/C/D/E=31-301.
DR PDB; 5FUA; EM; 7.60 A; 1/2/3/4/5/6=1-362.
DR PDB; 6ESB; EM; 3.40 A; 1/2/3/4/5/6=2-362.
DR PDB; 6GG0; EM; 4.24 A; 1/2/3/4/5/6=1-362.
DR PDBsum; 4MJ0; -.
DR PDBsum; 4MJ1; -.
DR PDBsum; 5FUA; -.
DR PDBsum; 6ESB; -.
DR PDBsum; 6GG0; -.
DR SMR; P03088; -.
DR UniLectin; P03088; -.
DR ABCD; P03088; 1 sequenced antibody.
DR DNASU; 29031008; -.
DR GeneID; 29031008; -.
DR KEGG; vg:29031008; -.
DR Proteomes; UP000008475; Genome.
DR Proteomes; UP000008990; 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 1: Evidence at protein level;
KW 3D-structure; 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_0000115018"
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"
FT VARIANT 158
FT /note="E -> D (in strain: MM)"
FT VARIANT 171
FT /note="S -> T (in strain: MM)"
FT VARIANT 219
FT /note="A -> T (in strain: MM)"
FT VARIANT 301
FT /note="P -> L (in strain: MM)"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:4MJ0"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4MJ1"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 109..121
FT /evidence="ECO:0007829|PDB:4MJ0"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6ESB"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:4MJ0"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:4MJ1"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:4MJ0"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:6ESB"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:4MJ0"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 259..273
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 284..297
FT /evidence="ECO:0007829|PDB:4MJ0"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:6ESB"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:6ESB"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:6ESB"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:6ESB"
SQ SEQUENCE 362 AA; 40109 MW; DB2C67C22B174698 CRC64;
MAPTKRKGEC PGAAPKKPKE PVQVPKLLIK GGVEVLEVKT GVDAITEVEC FLNPEMGDPD
ENLRGFSLKL SAENDFSSDS PERKMLPCYS TARIPLPNLN EDLTCGNLLM WEAVTVQTEV
IGITSMLNLH AGSQKVHEHG GGKPIQGSNF HFFAVGGEPL EMQGVLMNYR SKYPDGTITP
KNPTAQSQVM NTDHKAYLDK NNAYPVECWV PDPSRNENAR YFGTFTGGEN VPPVLHVTNT
ATTVLLDEQG VGPLCKADSL YVSAADICGL FTNSSGTQQW RGLARYFKIR LRKRSVKNPY
PISFLLSDLI NRRTQRVDGQ PMYGMESQVE EVRVFDGTER LPGDPDMIRY IDKQGQLQTK
ML
