VP2_POVKI
ID VP2_POVKI Reviewed; 400 AA.
AC P0DOJ1; A3R4M6; A3R4M7; A3R4N1; A3R4N2; A3R4N6; A3R4N7;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 1.
DT 23-FEB-2022, entry version 11.
DE RecName: Full=Minor capsid protein VP2;
DE AltName: Full=Minor structural protein VP2;
OS KI polyomavirus (isolate Stockholm 350) (KIPyV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX NCBI_TaxID=423447;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17287263; DOI=10.1128/jvi.00028-07;
RA Allander T., Andreasson K., Gupta S., Bjerkner A., Bogdanovic G.,
RA Persson M.A., Dalianis T., Ramqvist T., Andersson B.;
RT "Identification of a third human polyomavirus.";
RL J. Virol. 81:4130-4136(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. {ECO:0000250|UniProtKB:P03093}.
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. {ECO:0000250|UniProtKB:P03093}.
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.
CC {ECO:0000250|UniProtKB:P03093}.
CC -!- SUBCELLULAR LOCATION: [Isoform VP2]: Virion
CC {ECO:0000250|UniProtKB:P03093}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P03093}. Host nucleus
CC {ECO:0000250|UniProtKB:P03093}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P03093}. Note=Following host cell entry, the
CC virion enters into the endoplasmic reticulum through a calveolar-
CC dependent pathway. Then, isoform VP2 integrates into the endoplasmic
CC reticulum membrane and participates in the translocation of viral DNA
CC to the nucleus. Shortly after synthesis, a nuclear localization signal
CC directs isoform VP2 to the cell nucleus where virion assembly occurs.
CC {ECO:0000250|UniProtKB:P03093}.
CC -!- SUBCELLULAR LOCATION: [Isoform VP3]: Virion
CC {ECO:0000250|UniProtKB:P03093}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P03093}. Host nucleus
CC {ECO:0000250|UniProtKB:P03093}. Host endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P03093}. Note=Following host cell entry, the
CC virion enters into the endoplasmic reticulum through a calveolar-
CC dependent pathway. Then, isoform VP3 integrates into the endoplasmic
CC reticulum membrane and participates in the translocation of viral DNA
CC to the nucleus. Shortly after synthesis, a nuclear localization signal
CC directs isoform VP3 to the cell nucleus where virion assembly occurs.
CC {ECO:0000250|UniProtKB:P03093}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P0DOJ1-1, A3R4N1-1;
CC Sequence=Displayed;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P0DOJ1-2, A3R4N1-2;
CC Sequence=VSP_027106;
CC Name=VP1;
CC IsoId=P0DOI2-1, A3R4N3-1;
CC 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}.
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DR EMBL; EF127907; ABN09923.1; -; Genomic_DNA.
DR EMBL; EF127907; ABN09924.1; -; Genomic_DNA.
DR Proteomes; UP000101503; 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: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;
KW Host endoplasmic reticulum; Host membrane; Host nucleus; Late protein;
KW Lipoprotein; Membrane; Myristate; Viral penetration into host nucleus;
KW Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P03093"
FT CHAIN 2..400
FT /note="Minor capsid protein VP2"
FT /id="PRO_0000295817"
FT REGION 99..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..342
FT /note="D1"
FT /evidence="ECO:0000250|UniProtKB:P03093"
FT REGION 347..394
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03093"
FT REGION 348..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 359..369
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P03093"
FT COMPBIAS 104..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..400
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|UniProtKB:P03093"
FT VAR_SEQ 1..143
FT /note="Missing (in isoform VP3)"
FT /evidence="ECO:0000305"
FT /id="VSP_027106"
SQ SEQUENCE 400 AA; 41819 MW; 42198DD7B330F768 CRC64;
MGIFLAVPEI IAASIAGGAE ALSIAGSGAA IATGEGLAAL GGITEGAALL GETIPISEAA
TTVLTKVPEL VQATQAVTAA VQGGAGLVGG IYTALASDHP GDLPPNTPTG SASGLHPTSG
YNPQGAGLNL QSVHKPIHAP YSGMALVPIP EYQLETGIPG IPDWLFNLVA SYLPELPSLQ
DVFNRIAFGI WSSYYNAGST VVNRVLSDEI QRLLRDLEYG FRATLASIGE SDPVNAIATQ
VRSLASTARE RELLQITAGQ PLDLSRPTSA LSAAAGALTE AAYNFIYDAS SLPKDGFNAL
SEGVHRLGQW ISFSGPTGGT PHYATPDWIL YVLEQLNADT YKIPTQAVKR KQDELHPVSP
TKKANKAKKS SSPGTNSGNR SKKRRGRSTS RSTTVRRNRI
