VP1_POVMA
ID VP1_POVMA Reviewed; 383 AA.
AC P03090;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 104.
DE RecName: Full=Major capsid protein VP1;
DE AltName: Full=Major structural protein VP1;
OS Murine polyomavirus (strain A2) (MPyV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Alphapolyomavirus.
OX NCBI_TaxID=10636;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6243401; DOI=10.1038/283445a0;
RA Soeda E., Arrand J.R., Smolar N., Walsh J.E., Griffin B.E.;
RT "Coding potential and regulatory signals of the polyoma virus genome.";
RL Nature 283:445-453(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6251237; DOI=10.1128/jvi.33.2.619-630.1980;
RA Soeda E., Arrand J.R., Griffin B.E.;
RT "Polyoma virus DNA: complete nucleotide sequence of the gene which codes
RT for polyoma virus capsid protein VP1 and overlaps the VP2/VP3 genes.";
RL J. Virol. 33:619-630(1980).
RN [3]
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 terminal alpha(2,3)-linked sialic acids on the cell surface to
CC provide virion attachment to target cell. Once attached, the virion is
CC internalized by caveolin-mediated endocytosis and traffics to the
CC endoplasmic reticulum. Inside the endoplasmic reticulum, the protein
CC folding 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=3;
CC Name=VP1;
CC IsoId=P03090-1; Sequence=Displayed;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P03096-1; Sequence=External;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P03096-2; 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 -!- DOMAIN: The intrinsically disordered C-terminal arm interacts with
CC neighboring pentamers. The unstructured nature of this region allows to
CC make different interactions depending on the structural context:
CC pentamers present at the 12 icosahedral fivefold axes bind five
CC pentamers, whereas pentamers present at the 60 icosahedral six-fold
CC axes interact with six pentamers. {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; J02288; AAB59902.1; -; Genomic_DNA.
DR PIR; A03628; VVVP1.
DR SMR; P03090; -.
DR DIP; DIP-1088N; -.
DR ELM; P03090; -.
DR Proteomes; UP000008479; 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 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 INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..383
FT /note="Major capsid protein VP1"
FT /id="PRO_0000115024"
FT REGION 321..383
FT /note="C-terminal arm"
FT /evidence="ECO:0000250|UniProtKB:P03087"
FT MOTIF 4..18
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P03087"
FT MOD_RES 357
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000250"
FT DISULFID 12
FT /note="Interchain (with C-12)"
FT /evidence="ECO:0000250"
FT DISULFID 114
FT /note="Interchain (with C-114)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 383 AA; 42452 MW; 4339D86A900DBCBD CRC64;
MAPKRKSGVS KCETKCTKAC PRPAPVPKLL IKGGMEVLDL VTGPDSVTEI EAFLNPRMGQ
PPTPESLTEG GQYYGWSRGI NLATSDTWIP RNNTLPTWSM AKSSFPCLNE DLTCDTLQMW
EAVSVKTEVV GSGSLLDVHG FNKTHRFSKH KGNSTPVEGS QYHVFAGGGE PLDLQGLVTD
ARTKYKEEGV VTIKTITKKD MVNKDQVLNP ISKAKLDKDG MYPVEIWHPD PAKNENTRYF
GNYTGGTTAP PVLQFTNTLT TVLLDENGVG PLCKGEGLYL SCVDIMGWRV TRNYVSSLEK
GFPRYFKITL RKRWVKNPYP MASLISSLFN NMLPQVQGQP MEGENTQVEE VRVYDGTEPV
PGDPDMTRYV DRFGKTKTVF PGN
