VP2_POVBO
ID VP2_POVBO Reviewed; 353 AA.
AC P24849;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 91.
DE RecName: Full=Minor capsid protein VP2;
DE AltName: Full=Minor structural protein VP2;
OS Bovine polyomavirus (BPyV) (Bos taurus polyomavirus 1).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Epsilonpolyomavirus.
OX NCBI_TaxID=1891754;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2167926; DOI=10.1099/0022-1317-71-8-1723;
RA Schuurman R., Sol C., van der Noordaa J.;
RT "The complete nucleotide sequence of bovine polyomavirus.";
RL J. Gen. Virol. 71:1723-1735(1990).
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: Isoform VP2 is a structural protein that resides within the
CC core of the capsid surrounded by 72 VP1 pentamers. Participates in host
CC cell receptor binding together with VP1. Following virus endocytosis
CC and trafficking to the endoplasmic reticulum, VP2 and VP3 form
CC oligomers and integrate into the endoplasmic reticulum membrane.
CC Heterooligomer VP2-VP3 may create a viroporin for transporting the
CC viral genome across the endoplasmic reticulum membrane to the
CC cytoplasm. Nuclear entry of the viral DNA involves the selective
CC exposure and importin recognition of VP2 or Vp3 nuclear localization
CC signal (shared C-terminus). Plays a role in virion assembly within the
CC nucleus in particular through a DNA-binding domain located in the C-
CC terminal region. A N-terminal myristoylation suggests a scaffold
CC function for virion assembly (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Isoform VP3]: Structural protein that resides within the
CC core of the capsid surrounded by 72 VP1 pentamers. Following virus
CC endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3
CC form oligomers and integrate into the endoplasmic reticulum membrane.
CC Heterooligomer VP2-VP3 may create a viroporin for transporting the
CC viral genome across the endoplasmic reticulum membrane to the
CC cytoplasm. Nuclear entry of the viral DNA involves the selective
CC exposure and importin recognition of VP2 or Vp3 nuclear localization
CC signal (shared C-terminus). Isoform VP3 plays a role in virion assembly
CC within the nucleus (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: [Isoform VP2]: Forms homooligomers, and heterooligomers with
CC VP3 in the endoplasmic reticulum membrane. interacts (via D1 domain)
CC with VP1. {ECO:0000305}.
CC -!- SUBUNIT: [Isoform VP3]: Forms homooligomers, and heterooligomers with
CC VP2 in the endoplasmic reticulum membrane. Interacts (via D1 domain)
CC with VP1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host
CC endoplasmic reticulum. Host endoplasmic reticulum membrane
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host
CC endoplasmic reticulum. Host endoplasmic reticulum membrane
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P24849-1; Sequence=Displayed;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P24849-2; Sequence=VSP_018917;
CC Name=VP1;
CC IsoId=P24848-1; Sequence=External;
CC Name=Agno;
CC IsoId=P24850-1; Sequence=External;
CC -!- MISCELLANEOUS: [Isoform VP2]: Produced by alternative splicing of the
CC late mRNA.
CC -!- MISCELLANEOUS: [Isoform VP3]: Produced by alternative initiation at
CC Met-122 of isoform VP2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family.
CC {ECO:0000305}.
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DR EMBL; D13942; BAA03037.1; -; Genomic_DNA.
DR EMBL; D13942; BAA03038.1; -; Genomic_DNA.
DR PIR; JU0360; VVVPB2.
DR RefSeq; NP_040785.1; NC_001442.1. [P24849-1]
DR RefSeq; NP_040786.1; NC_001442.1. [P24849-2]
DR PRIDE; P24849; -.
DR GeneID; 29031003; -.
DR GeneID; 29031004; -.
DR KEGG; vg:29031003; -.
DR KEGG; vg:29031004; -.
DR Proteomes; UP000008476; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR InterPro; IPR001070; Polyoma_coat_VP2.
DR Pfam; PF00761; Polyoma_coat2; 1.
DR PIRSF; PIRSF003377; Polyoma_coat2; 1.
PE 3: Inferred from homology;
KW Alternative initiation; Alternative splicing; Capsid protein; DNA-binding;
KW Host endoplasmic reticulum; Host membrane; Host nucleus; Late protein;
KW Lipoprotein; Membrane; Myristate; Reference proteome; Transmembrane;
KW Transmembrane helix; Viral penetration into host nucleus; Virion;
KW Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..353
FT /note="Minor capsid protein VP2"
FT /id="PRO_0000039207"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 262..297
FT /note="D1"
FT /evidence="ECO:0000250"
FT REGION 301..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..353
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT MOTIF 318..327
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 331..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..121
FT /note="Missing (in isoform VP3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018917"
SQ SEQUENCE 353 AA; 39146 MW; B7472E4C4BBCC880 CRC64;
MGALLTILAE VFELATATGL SAEAILTGEA FTTAELLQAH IANLVEVGEL SVAEALAATE
VTSEAFEALQ SISSVLPTAF IGVAATEGAI LGSLITLTAT SSALYPSTWK HSTPSANLNQ
EMALVPYIGD LDIFFPGAET ISRFVYSIDP FRWASYLYNI VGRAVWEHLF RETRRQIAYH
TTDIAGRTAQ SIHHTIANFL ENVRWTVSHL GTNLYSGLHN YYRQLPPLNP PQSRELARRL
GVPQPDRQIF EKGEEGMKHP VSAEYVEKYG APGGAEQRVA PDWLLPLLLG LYGDLTPAWE
AEVEEEENEQ DEEEYEPPQK RIKRTAKSSS KVNNKRGDRS ARSPYRTRQH NHN
