VP2_BFPYV
ID VP2_BFPYV Reviewed; 341 AA.
AC P13892; O89837; Q84249; Q9WG00; Q9WG01;
DT 01-JAN-1990, 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 Budgerigar fledgling disease virus (BFPyV) (Aves polyomavirus 1).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Gammapolyomavirus.
OX NCBI_TaxID=1891747;
OH NCBI_TaxID=9224; Psittacidae (parrots).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2838972; DOI=10.1016/0042-6822(88)90660-5;
RA Rott O., Kroeger M., Mueller H., Hobom G.;
RT "The genome of budgerigar fledgling disease virus, an avian polyomavirus.";
RL Virology 165:74-86(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lafferty S.L., Fudge A.M., Schmidt R.E., Wilson V.G., Phalen D.N.;
RT "Avian polyomavirus infection and disease in a green aracaris (Pteroglossus
RT viridis).";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate MCFL87;
RX PubMed=10396633; DOI=10.2307/1592610;
RA Phalen D.N., Wilson V.G., Gaskin J.M., Derr J.N., Graham D.L.;
RT "Genetic diversity in twenty variants of the avian polyomavirus.";
RL Avian Dis. 43:207-218(1999).
RN [4]
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=7;
CC Name=VP2; Synonyms=Minor capsid protein VP2;
CC IsoId=P13892-1; Sequence=Displayed;
CC Name=VP3; Synonyms=Minor capsid protein VP3;
CC IsoId=P13892-2; Sequence=VSP_018914;
CC Name=VP1;
CC IsoId=P13891-1; Sequence=External;
CC Name=Agno-1a;
CC IsoId=A6QL29-1; Sequence=External;
CC Name=Agno-1b;
CC IsoId=A6QL29-2; Sequence=External;
CC Name=Agno-2b;
CC IsoId=P13893-1; Sequence=External;
CC Name=Agno-2a;
CC IsoId=P13893-2; 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-107 of isoform VP2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family.
CC {ECO:0000305}.
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DR EMBL; M20775; AAB59757.1; -; Genomic_DNA.
DR EMBL; M20775; AAB59758.1; -; Genomic_DNA.
DR EMBL; AF118150; AAD30958.1; -; Genomic_DNA.
DR EMBL; AF118150; AAD30959.1; -; Genomic_DNA.
DR EMBL; AF054335; AAC33658.1; -; Genomic_DNA.
DR PIR; B29194; VVVPBF.
DR TCDB; 1.A.83.1.6; the sv40 virus viroporin vp2 (sv40 vp2) family.
DR Proteomes; UP000134051; Genome.
DR Proteomes; UP000180851; 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..341
FT /note="Minor capsid protein VP2"
FT /id="PRO_0000039200"
FT REGION 262..297
FT /note="D1"
FT /evidence="ECO:0000250"
FT REGION 302..341
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 310..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 309..317
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..106
FT /note="Missing (in isoform VP3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018914"
FT VARIANT 205
FT /note="Q -> H (in strain: Isolate MCFL87)"
FT VARIANT 221
FT /note="V -> G (in strain: Isolate MCFL87)"
SQ SEQUENCE 341 AA; 37358 MW; E5055C44A70AE845 CRC64;
MGAIISAIAG LFELGALGGL AVDAAVNTAE IEAFIGELVL QDFSVAEIFD AIETSGIPLA
NTAVPVAELQ QTAATSGLIG QALSAPSLIA ASVKAFAGDP VAAGNNMALQ VWRDQMDILF
PGAEWFSNAV HNINPLAWAQ SLYEQVGQSI WNYMTGNIGQ AVIHQIEERT TALIVYQSRG
IYDILARALE TARWTLTTAA VDTYQTLKSY YGELPAVSGR VEAFRRYHEV AQGRSFFEDS
DIQDVLEGKK AQKRIEGPQE MTGQTIEQQT PPGGAMQRHA NDWLLPLILG LYGDLTPEWR
YQLKERLNVP KRKRKLPTTS AGTSPPSKRR YRGVRRKVRS R
