VP1_POVMP
ID VP1_POVMP Reviewed; 384 AA.
AC P49302;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Capsid protein VP1;
OS Murine polyomavirus (strain P16 small-plaque) (MPyV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Alphapolyomavirus.
OX NCBI_TaxID=47935;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1845896; DOI=10.1128/jvi.65.1.350-355.1991;
RA Freund R., Garcea R.L., Sahli R., Benjamin T.L.;
RT "A single-amino-acid substitution in polyomavirus VP1 correlates with
RT plaque size and hemagglutination behavior.";
RL J. Virol. 65:350-355(1991).
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]
RP X-RAY CRYSTALLOGRAPHY (3.65 ANGSTROMS).
RX PubMed=8177322; DOI=10.1038/369160a0;
RA Stehle T., Yan Y., Benjamin T.L., Harrison S.C.;
RT "Structure of murine polyomavirus complexed with an oligosaccharide
RT receptor fragment.";
RL Nature 369:160-163(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.65 ANGSTROMS).
RX PubMed=8805524; DOI=10.1016/s0969-2126(96)00021-4;
RA Stehle T., Harrison S.C.;
RT "Crystal structures of murine polyomavirus in complex with straight-chain
RT and branched-chain sialyloligosaccharide receptor fragments.";
RL Structure 4:183-194(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=9305654; DOI=10.1093/emboj/16.16.5139;
RA Stehle T., Harrison S.C.;
RT "High-resolution structure of a polyomavirus VP1-oligosaccharide complex:
RT implications for assembly and receptor binding.";
RL EMBO J. 16:5139-5148(1997).
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. This attachment induces
CC virion internalization predominantly through caveolin-mediated
CC endocytosis. Once attached, the virion is internalized by caveolin-
CC mediated endocytosis and traffics to the endoplasmic reticulum. Inside
CC the endoplasmic reticulum, the protein folding machinery isomerizes VP1
CC interpentamer disulfide bonds, thereby triggering initial uncoating.
CC Next, the virion uses the endoplasmic reticulum-associated degradation
CC machinery to probably translocate in the cytosol before reaching the
CC nucleus. Nuclear entry of the viral DNA involves the selective exposure
CC and importin recognition of VP2/Vp3 nuclear localization signal. In
CC late phase of infection, neo-synthesized VP1 encapsulates replicated
CC genomic DNA in the nucleus, and participates in rearranging nucleosomes
CC around the viral DNA. {ECO:0000250|UniProtKB:P03087,
CC 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 -!- 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 -!- SIMILARITY: Belongs to the polyomaviruses coat protein VP1 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure in complex with 3'sialyl lactose;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1sid";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure in complex with a disialylated oligosaccharide;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1sie";
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DR EMBL; M34958; AAA46561.1; -; Genomic_DNA.
DR PDB; 1CN3; X-ray; 2.20 A; A/B/C/D/E=35-317.
DR PDB; 1SID; X-ray; 3.65 A; A/B/C/D/E/F=2-384.
DR PDB; 1SIE; X-ray; 3.65 A; A/B/C/D/E/F=2-384.
DR PDB; 1VPN; X-ray; 2.00 A; A/B/C/D/E=33-321.
DR PDB; 1VPS; X-ray; 1.90 A; A/B/C/D/E=33-321.
DR PDB; 5CPU; X-ray; 1.64 A; A/B/C/D/E=34-317.
DR PDB; 5CPW; X-ray; 1.75 A; A/B/C/D/E=34-317.
DR PDB; 5CPX; X-ray; 1.87 A; A/B/C/D/E=34-317.
DR PDB; 5CPY; X-ray; 1.93 A; A/B/C/D/E=34-317.
DR PDB; 5CPZ; X-ray; 1.71 A; A/B/C/D/E=34-317.
DR PDB; 5CQ0; X-ray; 1.90 A; A/B/C/D/E=34-317.
DR PDB; 7K25; EM; 2.90 A; A/B/C/D/E=2-384.
DR PDBsum; 1CN3; -.
DR PDBsum; 1SID; -.
DR PDBsum; 1SIE; -.
DR PDBsum; 1VPN; -.
DR PDBsum; 1VPS; -.
DR PDBsum; 5CPU; -.
DR PDBsum; 5CPW; -.
DR PDBsum; 5CPX; -.
DR PDBsum; 5CPY; -.
DR PDBsum; 5CPZ; -.
DR PDBsum; 5CQ0; -.
DR PDBsum; 7K25; -.
DR SMR; P49302; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR TCDB; 1.A.83.1.5; the sv40 virus viroporin vp2 (sv40 vp2) family.
DR UniLectin; P49302; -.
DR EvolutionaryTrace; P49302; -.
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; 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 INIT_MET 1
FT /note="Removed; by host"
FT CHAIN 2..384
FT /note="Capsid protein VP1"
FT /id="PRO_0000115025"
FT REGION 322..384
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 358
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000250"
FT DISULFID 12
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 115
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5CPU"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:5CPU"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:7K25"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 118..130
FT /evidence="ECO:0007829|PDB:5CPU"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:5CPU"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:7K25"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:5CPU"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:5CPU"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:7K25"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:5CPU"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 278..291
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:5CPU"
FT STRAND 305..317
FT /evidence="ECO:0007829|PDB:5CPU"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:7K25"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:7K25"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:7K25"
SQ SEQUENCE 384 AA; 42505 MW; 324AACBB94BAA63B CRC64;
MAPKRKSGVS KCETKCTKAC PRPAPVPKLL IKGGMEVLDL VTGPDSVTEI EAFLNPRMGQ
PPTPESLTEG GQYYGWSRGI NLATSDTEDS PGNNTLPTWS MAKLQLPMLN EDLTCDTLQM
WEAVSVKTEV VGSGSLLDVH GFNKPTDTVN TKGISTPVEG SQYHVFAVGG EPLDLQGLVT
DARTKYKEEG VVTIKTITKK DMVNKDQVLN PISKAKLDKD GMYPVEIWHP DPAKNENTRY
FGNYTGGTTT PPVLQFTNTL TTVLLDENGV GPLCKGEGLY LSCVDIMGWR VTRNYDVHHW
RGLPRYFKIT LRKRWVKNPY PMASLISSLF NNMLPQVQGQ PMEGENTQVE EVRVYDGTEP
VPGDPDMTRY VDRFGKTKTV FPGN
