ID   VP1_POVK3               Reviewed;         378 AA.
AC   P0DOI4; A3R4M8; A3R4N3; A3R4N8;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2017, sequence version 1.
DT   02-JUN-2021, entry version 11.
DE   RecName: Full=Major capsid protein VP1;
DE   AltName: Full=Major structural protein VP1;
OS   KI polyomavirus (isolate Stockholm 380) (KIPyV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX   NCBI_TaxID=423448;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17287263; DOI=10.1128/jvi.00028-07;
RA   Allander T., Andreasson K., Gupta S., Bjerkner A., Bogdanovic G.,
RA   Persson M.A., Dalianis T., Ramqvist T., Andersson B.;
RT   "Identification of a third human polyomavirus.";
RL   J. Virol. 81:4130-4136(2007).
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. The virus capsid is composed of 72 icosahedral
CC       units, each one composed of five disulfide-linked copies of VP1.
CC       Interacts with minor capsid proteins VP2 and VP3.
CC       {ECO:0000250|UniProtKB:P03087}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03087}. Host
CC       nucleus {ECO:0000250|UniProtKB:P03087}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC       Name=VP1;
CC         IsoId=P0DOI4-1, A3R4N3-1;
CC         Sequence=Displayed;
CC       Name=VP2; Synonyms=Minor capsid protein VP2;
CC         IsoId=P0DOJ3-1, A3R4N1-1;
CC         Sequence=External;
CC       Name=VP3; Synonyms=Minor capsid protein VP3;
CC         IsoId=P0DOJ3-2, A3R4N1-2;
CC         Sequence=External;
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; EF127908; ABN09927.1; -; Genomic_DNA.
DR   SMR; P0DOI4; -.
DR   Proteomes; UP000166765; 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   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   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..378
FT                   /note="Major capsid protein VP1"
FT                   /id="PRO_0000442711"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   378 AA;  41578 MW;  34B60D4A14583C31 CRC64;
     MSCTPCRPQK RLTRPRSQVP RVQTLATEVK KGGVEVLAAV PLSEETEFKV ELFVKPVIGN
     TTAAQDGREP TPHYWSISSA IHDKESGSSI KVEETPDADT TVCYSLAEIA PPDIPNQVSE
     CDMKVWELYR METELLVVPL VNALGNTNGV VHGLAGTQLY FWAVGGQPLD VVGVTPTDKY
     KGPTTYTINP PGDPRTLHVY NSNTPKAKVT SERYSVESWA PDPSRNDNCR YFGRVVGGAA
     TPPVVSYGNN STIPLLDENG IGILCLQGRL YITCADMLGT ANSRIHTPMA RFFRLHFRQR
     RVKNPFTMNV LYKQVFNRPT ETVDAQVGVT EVTMVEEIGP LPPSIQTTLP TSVNLTQLPR
     TVTLQSQAPL LNTQQNSK