VP2_POVMK
ID VP2_POVMK Reviewed; 324 AA.
AC P24596; A2IBB4;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 5.
DT 23-FEB-2022, entry version 89.
DE RecName: Full=Minor capsid protein VP2;
DE AltName: Full=Minor structural protein VP2;
OS Murine polyomavirus (strain Kilham) (MPyV) (Murine pneumotropic virus).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX NCBI_TaxID=10638;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1849675; DOI=10.1016/0042-6822(91)90879-g;
RA Mayer M., Doerries K.;
RT "Nucleotide sequence and genome organization of the murine polyomavirus,
RT Kilham strain.";
RL Virology 181:469-480(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Libbey J.E., Kirkman N.J., Greenlee J.E., Fujinami R.S.;
RT "Amino acid sequence homology between murine pneumotropic virus and human
RT polyomaviruses.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
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=P24596-1; Sequence=Displayed;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P24596-2; Sequence=VSP_018924;
CC Name=VP1;
CC IsoId=P24595-1; 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-120 of isoform VP2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA46554.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA46555.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M55904; AAA46554.2; ALT_FRAME; Genomic_DNA.
DR EMBL; M55904; AAA46555.2; ALT_FRAME; Genomic_DNA.
DR EMBL; EF186666; ABM67408.1; -; Genomic_DNA.
DR PIR; D37945; VVVPK2.
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; 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"
FT CHAIN 2..324
FT /note="Minor capsid protein VP2"
FT /id="PRO_0000039221"
FT REGION 261..296
FT /note="D1"
FT /evidence="ECO:0000250"
FT REGION 301..324
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 302..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 311..321
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 302..316
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..119
FT /note="Missing (in isoform VP3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018924"
FT CONFLICT 58
FT /note="A -> R (in Ref. 1; AAA46554)"
FT /evidence="ECO:0000305"
FT CONFLICT 247..248
FT /note="RY -> SI (in Ref. 1; AAA46554/AAA46555)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 35563 MW; E9365524DEDDC0A3 CRC64;
MGAFLAVLAE VFDLASITGL SVESILSGEA LTTAELLQSH INNLVVYGGL TEAEALAAVE
VTPQAFAALT SLFPNFPQAL GALAATEFTA TGALTVGAAV SAALYPYYWD YRTPVADLNM
ALQIWYPDLD ILFPGALPFA RFVNYIDPAN WAADLYRAVG RYFWERVQAA GINFIEQQME
TGRELAMRSV TSLSETLSQY FENARWAVSG LSTSLYHGLE SYYSQLGLSP IQQRQLARNL
GHPQPYRYDL YDAPQLKGQV SATYVTKVDP PGGANQRSAP DWMLPLLLGL YGDLTPSWKD
TLEELEAEED GSHSQKAKRR KTKA
