VP1_POVLY
ID VP1_POVLY Reviewed; 368 AA.
AC P04010;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 3.
DT 02-JUN-2021, entry version 95.
DE RecName: Full=Major capsid protein VP1;
DE AltName: Full=Major structural protein VP1;
OS B-lymphotropic polyomavirus (LPV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; unclassified Polyomaviridae.
OX NCBI_TaxID=332091;
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2998001; DOI=10.1016/0042-6822(85)90108-4;
RA Pawlita M., Clad A., zur Hausen H.;
RT "Complete DNA sequence of lymphotropic papovavirus: prototype of a new
RT species of the polyomavirus genus.";
RL Virology 143:196-211(1985).
RN [2]
RP SEQUENCE REVISION.
RA Pawlita M., Clad A., zur Hausen H.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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 a N-linked glycoprotein containing sialic acids on the cell
CC surface to provide virion attachment to target cell. Once attached, the
CC virion is internalized by endocytosis and traffics to the endoplasmic
CC reticulum. Inside the endoplasmic reticulum, the protein folding
CC 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}.
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=P04010-1; Sequence=Displayed;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P04011-1; Sequence=External;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P04011-2; 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; K02562; AAA47062.2; -; Genomic_DNA.
DR PIR; A03627; VVVP1L.
DR RefSeq; NP_848007.2; NC_004763.2.
DR PDB; 4MBX; X-ray; 1.92 A; A/B/C/D/E/F/G/H/I/J=29-302.
DR PDB; 4MBY; X-ray; 1.48 A; A/B/C/D/E/F/G/H/I/J=29-302.
DR PDB; 4MBZ; X-ray; 1.75 A; A/B/C/D/E/F/G/H/I/J=29-302.
DR PDBsum; 4MBX; -.
DR PDBsum; 4MBY; -.
DR PDBsum; 4MBZ; -.
DR SMR; P04010; -.
DR UniLectin; P04010; -.
DR PRIDE; P04010; -.
DR GeneID; 1494437; -.
DR KEGG; vg:1494437; -.
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 PIRSF; PIRSF003376; Capsid_VP1_Polyomavir; 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 Phosphoprotein; 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..368
FT /note="Major capsid protein VP1"
FT /id="PRO_0000115022"
FT REGION 303..368
FT /note="C-terminal arm"
FT /evidence="ECO:0000250|UniProtKB:P03087"
FT MOTIF 5..14
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P03087"
FT MOD_RES 339
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000250"
FT DISULFID 105
FT /note="Interchain (with C-105)"
FT /evidence="ECO:0000250"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4MBY"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 105..120
FT /evidence="ECO:0007829|PDB:4MBY"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:4MBY"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:4MBY"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:4MBY"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 260..273
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:4MBY"
FT STRAND 286..298
FT /evidence="ECO:0007829|PDB:4MBY"
SQ SEQUENCE 368 AA; 40023 MW; BB14F280D634C74E CRC64;
MAPQRKRQDG ACKKTCPIPA PVPRLLVKGG VEVLEVRTGP DAITQIEAYL NPRMGNNIPS
EDLYGYSNSI NTAFSKASDT PNKDTLPCYS VAVIKLPLLN EDMTCDTILM WEAVSVKTEV
VGISSLVNLH QGGKYIYGSS SGCVPVQGTT YHMFAVGGEP LELQGLVASS TATYPDDVVA
IKNMKPGNQG LDPKAKALLD KDGKYPVEVW CPDPSKNENT RYYGSFTGGA TTPPVMQFTN
SVTTVLLDEN GVGPLCKGDK LFLSCADIAG VHTNYSETQV WRGLPRYFNV TLRKRIVKNP
YPVSSLLNSF FSGLMPQIQG QPMEGVSGQV EEVRIFEGTE GLPGDPDLNR YVDKFCQHQT
VLPVSNDM
