VP2_POVHA
ID VP2_POVHA Reviewed; 345 AA.
AC P03098; Q76V97;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 89.
DE RecName: Full=Minor capsid protein VP2;
DE AltName: Full=Minor structural protein VP2;
OS Hamster polyomavirus (HaPyV) (Mesocricetus auratus polyomavirus 1).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Alphapolyomavirus.
OX NCBI_TaxID=1891729;
OH NCBI_TaxID=10036; Mesocricetus auratus (Golden hamster).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2988942; DOI=10.1002/j.1460-2075.1985.tb03773.x;
RA Delmas V., Bastien C., Scherneck S., Feunteun J.;
RT "A new member of the polyomavirus family: the hamster papovavirus. Complete
RT nucleotide sequence and transformation properties.";
RL EMBO J. 4:1279-1286(1985).
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=3;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P03098-1; Sequence=Displayed;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P03098-2; Sequence=VSP_018918;
CC Name=VP1;
CC IsoId=P03092-1; 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-125 of isoform VP2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family.
CC {ECO:0000305}.
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DR EMBL; M26281; AAA67120.1; -; Genomic_DNA.
DR EMBL; M26281; AAA67121.1; -; Genomic_DNA.
DR EMBL; X02449; CAB59365.1; -; Genomic_DNA.
DR EMBL; X02449; CAB59366.1; -; Genomic_DNA.
DR PIR; A03636; VVVP2H.
DR Proteomes; UP000008477; 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: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;
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..345
FT /note="Minor capsid protein VP2"
FT /id="PRO_0000039209"
FT REGION 289..324
FT /note="D1"
FT /evidence="ECO:0000250"
FT REGION 329..345
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT MOTIF 336..344
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..124
FT /note="Missing (in isoform VP3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018918"
SQ SEQUENCE 345 AA; 38609 MW; 189C9187EA68332A CRC64;
MGSAISVIIE MISYLSEISS VTGISVEAIL SGEAFAAIDA QVTSLITMEG FLGAETALSS
IGLSEDMFIF MQAAPELTST VMTEFVRESV QTAFIFQTVA GSAAFSLGSL HGYLAHEVPI
VNRNMALIPR RPADYYDILF PGVQSFTHAL DVIHGWGHSL FQSVGEYIWD TLRRETQGAV
ESAVRDLSLQ TTHQFLDAIA RMMENSRWVV TNLPREAYSR IYGGLQNYYA ELPGINPAQR
RQIERALEYS NRPSIEDANS RQVLEAELGR PDVQRRSQQQ EDSSSWFESG ANIMRYFAPG
GAHQRVTPDW MLPLILGLYG DISPTWQTYI DEVEYGPKKK KRRFQ
