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VP2_POVSM
ID   VP2_POVSM               Reviewed;         332 AA.
AC   A8Y987;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   23-FEB-2022, entry version 49.
DE   RecName: Full=Minor capsid protein VP2;
DE   AltName: Full=Minor structural protein VP2;
GN   Name=VP2;
OS   Squirrel monkey polyomavirus.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX   NCBI_TaxID=452475;
OH   NCBI_TaxID=39432; Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Squi0106;
RX   PubMed=18089736; DOI=10.1099/vir.0.83287-0;
RA   Verschoor E.J., Groenewoud M.J., Fagrouch Z., Kewalapat A., van Gessel S.,
RA   Kik M.J., Heeney J.L.;
RT   "Molecular characterization of the first polyomavirus from a New World
RT   primate: squirrel monkey polyomavirus.";
RL   J. Gen. Virol. 89:130-137(2008).
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=5;
CC       Name=VP2; Synonyms=Minor capsid protein VP2;
CC         IsoId=A8Y987-1; Sequence=Displayed;
CC       Name=VP3; Synonyms=Minor capsid protein VP3;
CC         IsoId=A8Y987-2; Sequence=VSP_036018;
CC       Name=VP4;
CC         IsoId=A8Y987-3; Sequence=VSP_036017;
CC       Name=VP1; Synonyms=Major capsid protein VP1;
CC         IsoId=A8Y983-1; Sequence=External;
CC       Name=Agno;
CC         IsoId=A8Y986-1; 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-126 of isoform VP2. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform VP4]: Produced by alternative initiation at
CC       Met-239 of isoform VP2. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family.
CC       {ECO:0000305}.
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DR   EMBL; AM748741; CAO03080.1; -; Genomic_DNA.
DR   RefSeq; YP_001531346.1; NC_009951.1. [A8Y987-1]
DR   GeneID; 5714857; -.
DR   KEGG; vg:5714857; -.
DR   Proteomes; UP000135044; 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..332
FT                   /note="Minor capsid protein VP2"
FT                   /id="PRO_0000356259"
FT   REGION          265..300
FT                   /note="D1"
FT                   /evidence="ECO:0000250"
FT   REGION          305..332
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          306..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           315..323
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..238
FT                   /note="Missing (in isoform VP4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036017"
FT   VAR_SEQ         1..125
FT                   /note="Missing (in isoform VP3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036018"
SQ   SEQUENCE   332 AA;  36559 MW;  416F40742711B9C3 CRC64;
     MGALLAVLAE VVELASVTGL SVESFISGEA FATAELLEAH IANLVTVGGL TEAEALAATE
     VPAEAYAALT SLSSTFPQAF TAVAATELAT TGTLTVGATV AAALYPYYYD YSTPVANLNR
     GLNPEMALQL WFPEIDYEFP GLMPFVRFIN YIDPTQWATN LFETIGRYSW ESAQRYGQNL
     IAHEVRSASR ELATRTAQGF SEAVARYFEN ARWAVSTLPR SLYSGLQSYY EQLPSLNPMQ
     VRDLHRRLGQ PIPNRIALEE QAIKSAEYVQ KVDPPGGANQ RIAPDWLLPL ILGLYGDISP
     SWESTLEDIE EEEDAPQKKK RKRTKKNTPR SA
 
 
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