VP2_POVWU
ID VP2_POVWU Reviewed; 415 AA.
AC A5HBE1; A5HBD3; A5HBD4; A5HBE2; A5HBF8; A5HBF9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 23-FEB-2022, entry version 48.
DE RecName: Full=Minor capsid protein VP2;
DE AltName: Full=Minor structural protein VP2;
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: 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 VP3
CC in the endoplasmic reticulum membrane. Isoform VP2 interacts (via D1
CC domain) with VP1. Isoform VP3 interacts (via D1 domain) with VP1 (By
CC 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=3;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=A5HBE1-1; Sequence=Displayed;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=A5HBE1-2; Sequence=VSP_027107;
CC Name=VP1;
CC IsoId=A5HBD5-1; 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-144 of isoform VP2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF444549; ABQ09290.1; -; Genomic_DNA.
DR EMBL; EF444549; ABQ09291.1; -; Genomic_DNA.
DR EMBL; EF444550; ABQ09294.1; -; Genomic_DNA.
DR EMBL; EF444550; ABQ09295.1; -; Genomic_DNA.
DR EMBL; EF444551; ABQ09299.1; -; Genomic_DNA.
DR EMBL; EF444551; ABQ09300.1; -; Genomic_DNA.
DR EMBL; EF444552; ABQ09304.1; -; Genomic_DNA.
DR EMBL; EF444552; ABQ09305.1; -; Genomic_DNA.
DR EMBL; EF444553; ABQ09309.1; -; Genomic_DNA.
DR EMBL; EF444553; ABQ09310.1; -; Genomic_DNA.
DR EMBL; EF444554; ABQ09314.1; -; Genomic_DNA.
DR EMBL; EF444554; ABQ09315.1; -; Genomic_DNA.
DR RefSeq; YP_001285485.1; NC_009539.1.
DR RefSeq; YP_001285486.1; NC_009539.1.
DR GeneID; 5309724; -.
DR GeneID; 5309725; -.
DR KEGG; vg:5309724; -.
DR KEGG; vg:5309725; -.
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:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
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;
KW Viral penetration into host nucleus; Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..415
FT /note="Minor capsid protein VP2"
FT /id="PRO_0000295818"
FT REGION 102..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..353
FT /note="D1"
FT /evidence="ECO:0000250"
FT REGION 358..409
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 365..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 377..384
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 373..415
FT /note="Basic 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..143
FT /note="Missing (in isoform VP3)"
FT /evidence="ECO:0000305"
FT /id="VSP_027107"
FT VARIANT 250
FT /note="Q -> E (in strain: Isolate B0)"
FT VARIANT 284
FT /note="D -> H (in strain: Isolate S5)"
SQ SEQUENCE 415 AA; 43604 MW; BA35930FAB36B1DA CRC64;
MGILLAVPEI IAASVAGGAE ALSIAGSGAA IATGEGLAAL GGLTESAALL GETVEISEAA
ATVLTKVPEL VTVTQGVTAA VQGGAGLVGG IYTALAADRP GDLPASTPTG SPSGLHPPAG
YNPQGGGLNI QSIHKPLHAP YPGMALAPIP EYNLETGIPG VPDWVFNFIA SHLPELPSLQ
DVFNRIAYGI WTSYYNTGRT VVNRAVSEEL QRLLGDLEYG FRTALATIGE SDPVNAIVEQ
VRSFVSGGRQ RELLQIAAGQ PVDISEGVSR GTATISNAVE AVRDATQRLS QATYNFVYDA
STLPRDGFNA LSDGVHRLGQ WISMPGATGG TPHYAAPDWI LYVLEELNSD ISKIPTQGIK
RKLQQNGLHS KASLHSKTRK VTKKSTHKSA KPSKTSQKRR GRRAGRRTTV RRNRV
