CAPSD_ADVG
ID CAPSD_ADVG Reviewed; 690 AA.
AC P24029; G1E7B4;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 3.
DT 23-FEB-2022, entry version 87.
DE RecName: Full=Capsid protein VP1;
OS Aleutian mink disease parvovirus (strain G) (ADV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Amdoparvovirus.
OX NCBI_TaxID=10783;
OH NCBI_TaxID=9665; Mustela.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2839709; DOI=10.1128/jvi.62.8.2903-2915.1988;
RA Bloom M.E., Alexandersen S., Perryman S., Lechner D., Wolfinbarger J.B.;
RT "Nucleotide sequence and genomic organization of Aleutian mink disease
RT parvovirus (ADV): sequence comparisons between a nonpathogenic and a
RT pathogenic strain of ADV.";
RL J. Virol. 62:2903-2915(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=22361476; DOI=10.1016/j.virol.2012.01.031;
RA Huang Q., Deng X., Best S.M., Bloom M.E., Li Y., Qiu J.;
RT "Internal polyadenylation of parvoviral precursor mRNA limits progeny virus
RT production.";
RL Virology 426:167-177(2012).
RN [3]
RP FUNCTION.
RX PubMed=2842956; DOI=10.1016/0042-6822(88)90145-6;
RA Willwand K., Kaaden O.R.;
RT "Capsid protein VP1 (p85) of Aleutian disease virus is a major DNA-binding
RT protein.";
RL Virology 166:52-57(1988).
RN [4]
RP FUNCTION.
RX PubMed=8380073; DOI=10.1128/jvi.67.1.229-238.1993;
RA Christensen J., Storgaard T., Bloch B., Alexandersen S., Aasted B.;
RT "Expression of Aleutian mink disease parvovirus proteins in a baculovirus
RT vector system.";
RL J. Virol. 67:229-238(1993).
RN [5]
RP FUNCTION.
RX PubMed=11602751; DOI=10.1128/jvi.75.22.11116-11127.2001;
RA Bloom M.E., Best S.M., Hayes S.F., Wells R.D., Wolfinbarger J.B.,
RA McKenna R., Agbandje-McKenna M.;
RT "Identification of aleutian mink disease parvovirus capsid sequences
RT mediating antibody-dependent enhancement of infection, virus
RT neutralization, and immune complex formation.";
RL J. Virol. 75:11116-11127(2001).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12692232; DOI=10.1128/jvi.77.9.5305-5312.2003;
RA Best S.M., Shelton J.F., Pompey J.M., Wolfinbarger J.B., Bloom M.E.;
RT "Caspase cleavage of the nonstructural protein NS1 mediates replication of
RT Aleutian mink disease parvovirus.";
RL J. Virol. 77:5305-5312(2003).
CC -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid
CC with a T=1 symmetry, about 25 nm in diameter, and consisting of 60
CC copies of two size variants of the capsid proteins, VP1 (10% abundance)
CC and VP2 (90% abundance), which differ by the presence of an N-terminal
CC extension in the minor protein VP1. Capsid proteins are responsible for
CC the attachment to host cell receptors. This attachment induces virion
CC internalization predominantly through clathrin-dependent endocytosis.
CC VP1 binds DNA and may therefore play a role in viral DNA encapsidation.
CC {ECO:0000269|PubMed:11602751, ECO:0000269|PubMed:2842956,
CC ECO:0000269|PubMed:8380073}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:12692232}. Host
CC nucleus {ECO:0000269|PubMed:12692232}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=VP1;
CC IsoId=P24029-1; Sequence=Displayed;
CC Name=VP2;
CC IsoId=P24029-2; Sequence=VSP_054580;
CC -!- SIMILARITY: Belongs to the parvoviridae capsid protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA66615.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEK27534.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M20036; AAA66615.1; ALT_SEQ; Genomic_DNA.
DR EMBL; JN040434; AEK27534.1; ALT_SEQ; Genomic_DNA.
DR PIR; B36760; VCPVAP.
DR RefSeq; NP_042875.1; NC_001662.1.
DR GeneID; 1494587; -.
DR KEGG; vg:1494587; -.
DR Proteomes; UP000008470; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039615; C:T=1 icosahedral viral capsid; IDA:CACAO.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0099008; P:viral entry via permeabilization of inner membrane; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.170.30.10; -; 1.
DR InterPro; IPR016184; Capsid/spike_ssDNA_virus.
DR InterPro; IPR001403; Parvovirus_coat.
DR InterPro; IPR036952; VP1/VP2.
DR Pfam; PF00740; Parvo_coat; 1.
DR SUPFAM; SSF88645; SSF88645; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Capsid protein;
KW Clathrin-mediated endocytosis of virus by host; Host nucleus;
KW Host-virus interaction; Reference proteome; T=1 icosahedral capsid protein;
KW Viral attachment to host cell; Viral penetration into host cytoplasm;
KW Viral penetration via permeabilization of host membrane; Virion;
KW Virus endocytosis by host; Virus entry into host cell.
FT CHAIN 1..690
FT /note="Capsid protein VP1"
FT /id="PRO_0000428998"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform VP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054580"
SQ SEQUENCE 690 AA; 78502 MW; B3571236583EE4FE CRC64;
MSKIPQHYPG KKRSAPRHVF IQQAKKKKQT NPAVYHGEDT IEEMDSTEAE QMDTEQATNQ
TAEAGGGGGG GGGGGGGGGG VGNSTGGFNN TTEFKVINNE VYITCHATRM VHINQADTDE
YLIFNAGRTT DTKTHQQKLN LEFFVYDDFH QQVMTPWYIV DSNAWGVWMS PKDFQQMKTL
CSEISLVTLE QEIDNVTIKT VTETNQGNAS TKQFNNDLTA SLQVALDTNN ILPYTPAAPL
GETLGFVPWR ATKPTQYRYY HPCYIYNRYP NIQKVATETL TWDAVQDDYL SVDEQYFNFI
TIENNIPINI LRTGDNFHTG LYEFNSKPCK LTLSYQSTRC LGLPPLCKPK TDTTHKVTSK
ENGADLIYIQ GQDNTRLGHF WGEERGKKNA EMNRIRPYNI GYQYPEWIIP AGLQGSYFAG
GPRQWSDTTK GAGTHSQHLQ QNFSTRYIYD RNHGGDNEVD LLDGIPIHER SNYYSDNEIE
QHTAKQPKLR TPPIHHSKID SWEEEGWPAA SGTHFEDEVI YLDYFNFSGE QELNFPHEVL
DDAAQMKKLL NSYQPTVAQD NVGPVYPWGQ IWDKKPHMDH KPSMNNNAPF VCKNNPPGQL
FVKLTENLTD TFNYDENPDR IKTYGYFTWR GKLVLKGKLS QVTCWNPVKR ELIGEPGVFT
KDKYHKQIPN NKGNFEIGLQ YGRSTIKYIY
