VP1_POVK6
ID VP1_POVK6 Reviewed; 378 AA.
AC P0DOI3; A3R4M8; A3R4N3; A3R4N8;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Major capsid protein VP1;
DE AltName: Full=Major structural protein VP1;
OS KI polyomavirus (isolate Stockholm 60) (KIPyV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX NCBI_TaxID=423446;
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).
RN [3] {ECO:0007744|PDB:3S7V}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 32-304.
RX PubMed=21543504; DOI=10.1128/jvi.00382-11;
RA Neu U., Wang J., Macejak D., Garcea R.L., Stehle T.;
RT "Structures of the major capsid proteins of the human Karolinska Institutet
RT and Washington University polyomaviruses.";
RL J. Virol. 85:7384-7392(2011).
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=P0DOI3-1, A3R4N3-1;
CC Sequence=Displayed;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P0DOJ2-1, A3R4N1-1;
CC Sequence=External;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P0DOJ2-2, 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF127906; ABN09917.1; -; Genomic_DNA.
DR PDB; 3S7V; X-ray; 2.55 A; A/B/C/D/E/F/G/H/I/J=32-304.
DR PDBsum; 3S7V; -.
DR SMR; P0DOI3; -.
DR UniLectin; P0DOI3; -.
DR Proteomes; UP000107189; 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 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing; Capsid protein;
KW Disulfide bond; Host nucleus; Host-virus interaction; Late protein;
KW 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..378
FT /note="Major capsid protein VP1"
FT /id="PRO_0000442710"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:3S7V"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:3S7V"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 124..136
FT /evidence="ECO:0007829|PDB:3S7V"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:3S7V"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:3S7V"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:3S7V"
FT STRAND 289..302
FT /evidence="ECO:0007829|PDB:3S7V"
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
