VP1_POVWU
ID VP1_POVWU Reviewed; 369 AA.
AC A5HBD5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 02-JUN-2021, entry version 67.
DE RecName: Full=Major capsid protein VP1;
DE AltName: Full=Major structural protein VP1;
OS WU polyomavirus (WUPyV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX NCBI_TaxID=440266;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate B0, Isolate S1, Isolate S2, Isolate S3, Isolate S4, and
RC Isolate S5;
RX PubMed=17480120; DOI=10.1371/journal.ppat.0030064;
RA Gaynor A.M., Nissen M.D., Whiley D.M., Mackay I.M., Lambert S.B., Wu G.,
RA Brennan D.C., Storch G.A., Sloots T.P., Wang D.;
RT "Identification of a novel polyomavirus from patients with acute
RT respiratory tract infections.";
RL PLoS Pathog. 3:595-604(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. Host nucleus
CC {ECO:0000250|UniProtKB:P03087}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=VP1;
CC IsoId=A5HBD5-1; Sequence=Displayed;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=A5HBE1-1; Sequence=External;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=A5HBE1-2; 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; EF444549; ABQ09289.1; -; Genomic_DNA.
DR EMBL; EF444550; ABQ09296.1; -; Genomic_DNA.
DR EMBL; EF444551; ABQ09301.1; -; Genomic_DNA.
DR EMBL; EF444552; ABQ09306.1; -; Genomic_DNA.
DR EMBL; EF444553; ABQ09311.1; -; Genomic_DNA.
DR EMBL; EF444554; ABQ09316.1; -; Genomic_DNA.
DR RefSeq; YP_001285487.1; NC_009539.1. [A5HBD5-1]
DR PDB; 3S7X; X-ray; 2.90 A; A/B/C/D/E=34-296.
DR PDBsum; 3S7X; -.
DR SMR; A5HBD5; -.
DR UniLectin; A5HBD5; -.
DR GeneID; 5309723; -.
DR KEGG; vg:5309723; -.
DR Proteomes; UP000096057; Genome.
DR Proteomes; UP000114161; Genome.
DR Proteomes; UP000118542; Genome.
DR Proteomes; UP000119623; Genome.
DR Proteomes; UP000148617; Genome.
DR Proteomes; UP000153939; 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..369
FT /note="Major capsid protein VP1"
FT /id="PRO_0000295816"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:3S7X"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3S7X"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:3S7X"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 113..127
FT /evidence="ECO:0007829|PDB:3S7X"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3S7X"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3S7X"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3S7X"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 262..275
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:3S7X"
FT STRAND 281..295
FT /evidence="ECO:0007829|PDB:3S7X"
SQ SEQUENCE 369 AA; 39875 MW; E0641F7A7829A189 CRC64;
MACTAKPACT AKPGRSPRSQ PTRVQSLPKQ VRKGGVDVLA AVPLSEETEF KVELFVKPVI
GNAEGTTPHY WSISSPLKTA EAANVTPDAD TTVCYSLSQV APPDIPNQVS ECDMLIWELY
RMETEVLVLP VLNAGILTTG GVGGIAGPQL YFWAVGGQPL DVLGLAPTEK YKGPAQYTVN
PKTNGTVPHV YSSSETPRAR VTNEKYSIES WVADPSRNDN CRYFGRMVGG AATPPVVSFS
NNSTIPLLDE NGIGILCLQG RLYITCADLL GVNKNRVHTG LSRFFRLHFR QRRVRNPYTI
NLLYKQVFNK PADDISGQLQ VTEVTMTEET GPLPPTVEGN VGVPTTSNLS HLPATVTLQA
TGPILNTQG
