VP2_POVBA
ID VP2_POVBA Reviewed; 351 AA.
AC P14997;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 95.
DE RecName: Full=Minor capsid protein VP2;
DE AltName: Full=Minor structural protein VP2;
OS BK polyomavirus (strain AS) (BKPyV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Betapolyomavirus.
OX NCBI_TaxID=10631;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2536111; DOI=10.1128/jvi.63.2.901-911.1989;
RA Tavis J.E., Walker D.L., Gardner S.D., Frisque R.J.;
RT "Nucleotide sequence of the human polyomavirus AS virus, an antigenic
RT variant of BK virus.";
RL J. Virol. 63:901-911(1989).
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. May participate in host cell lysis when associated
CC with VP4 (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Isoform VP4 is a viroporin inducing perforation of cellular
CC membranes to trigger virus progeny release. Forms pores of 3 nm inner
CC diameter. VP4 is expressed about 24 hours after the late structural
CC proteins and is not incorporated into the mature virion (By
CC 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 -!- SUBCELLULAR LOCATION: [Isoform VP4]: Host nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=5;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P14997-1; Sequence=Displayed;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P14997-2; Sequence=VSP_018915;
CC Name=VP4; Synonyms=Viroporin VP4;
CC IsoId=P14997-3; Sequence=VSP_036013;
CC Name=VP1;
CC IsoId=P14996-1; Sequence=External;
CC Name=Agno;
CC IsoId=P14998-1; 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 -!- MISCELLANEOUS: [Isoform VP4]: Produced by alternative initiation at
CC Met-229 of isoform VP2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family.
CC {ECO:0000305}.
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DR EMBL; M23122; AAA46880.1; -; Genomic_DNA.
DR EMBL; M23122; AAA46881.1; -; Genomic_DNA.
DR PIR; E33278; VVVPAS.
DR PRIDE; P14997; -.
DR Proteomes; UP000008166; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044385; C:integral to membrane of host cell; 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:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0099008; P:viral entry via permeabilization of inner membrane; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; 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;
KW Host-virus interaction; Ion channel; Ion transport; Late protein;
KW Lipoprotein; Membrane; Myristate; Transmembrane; Transmembrane helix;
KW Transport; Viral attachment to host cell; Viral ion channel;
KW Viral penetration into host cytoplasm; Viral penetration into host nucleus;
KW Viral penetration via permeabilization of host membrane;
KW Viral release from host cell; Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..351
FT /note="Minor capsid protein VP2"
FT /id="PRO_0000039203"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 272..307
FT /note="D1"
FT /evidence="ECO:0000250"
FT REGION 312..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..351
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT MOTIF 315..323
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 337..351
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..228
FT /note="Missing (in isoform VP4)"
FT /evidence="ECO:0000305"
FT /id="VSP_036013"
FT VAR_SEQ 1..119
FT /note="Missing (in isoform VP3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018915"
SQ SEQUENCE 351 AA; 38303 MW; D926105B0D1A4130 CRC64;
MGAALALLGD LVASVSEAAA ATGFSVAEIA AGEAAAAIEV QIASLATVEG ITTTSEAIAA
IGLTPQTYAV IAGAPGAIAG FAALIQTVTG ISSLAQVGYR FFSDWDHKVS TVGLYQQSGM
ALELFNPDEY YDILFPGVNT FVNNIQYLDP RHWGPSLFAT ISQALWHVIR DDIPAITSQE
LQRRTERFFR DSLARFLEET TWTIVNAPIN FYNYIQDYYS NLSPIRPSMV RQVAEREGTH
VNFGHTYSID NADSIEEVTQ RMDLRNKESV HSGEFIEKTI APGGANQRTA PQWMLPLLLG
LYGTVTPALE AYEDGPNQKK RRVSRGSSQK AKGTRASAKT TNKRRSRSSR S
