CAPSD_PCV1
ID CAPSD_PCV1 Reviewed; 230 AA.
AC Q80QL5; O90239; Q6DMP2;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 23-FEB-2022, entry version 74.
DE RecName: Full=Capsid protein;
GN Name=Cap; ORFNames=ORF2;
OS Porcine circovirus 1 (PCV1).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC Cirlivirales; Circoviridae; Circovirus.
OX NCBI_TaxID=133704;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate ATCC CCL-33/PK15;
RX PubMed=9787657; DOI=10.1007/s007050050412;
RA Niagro F.D., Forsthoefel A.N., Lawther R.P., Kamalanathan L., Ritchie B.W.,
RA Latimer K.S., Lukert P.D.;
RT "Beak and feather disease virus and porcine circovirus genomes:
RT intermediates between the geminiviruses and plant circoviruses.";
RL Arch. Virol. 143:1723-1744(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate ATCC CCL-33/PK15;
RX PubMed=12788629; DOI=10.1016/s0042-6822(03)00096-5;
RA Cheung A.K.;
RT "Comparative analysis of the transcriptional patterns of pathogenic and
RT nonpathogenic porcine circoviruses.";
RL Virology 310:41-49(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate IBRS-2;
RA Cao S., Chen H., Ju C.;
RT "Genomic sequence of porcine circovirus type 1 isolated from IBRS-2 cell
RT line.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEAR LOCALIZATION SIGNALS.
RX PubMed=18180855; DOI=10.1111/j.1745-7270.2008.00377.x;
RA Shuai J., Wei W., Jiang L., Li X., Chen N., Fang W.;
RT "Mapping of the nuclear localization signals in open reading frame 2
RT protein from porcine circovirus type 1.";
RL Acta Biochim. Biophys. Sin. 40:71-77(2008).
CC -!- FUNCTION: Self-assembles to form the virion icosahedral capsid with a
CC T=1 symmetry. This very small capsid (17-22 nm in diameter) allows the
CC virus to be very stable in the environment and resistant to some
CC disinfectants, including detergents. Essential for the initial
CC attachment to heparan sulfate moieties and chondroitin sulfate B of the
CC host cell surface proteoglycans. After attachment, the virus is
CC endocytosed and traffics to the nucleus. The capsid protein binds and
CC transports the viral genome and Rep across the nuclear envelope.
CC {ECO:0000250|UniProtKB:Q9YUC8}.
CC -!- SUBUNIT: Homomultimer. Assembles in the nucleus, presumably in an
CC immature form, then migrates to the cytoplasm once assembled as mature
CC virion. Interacts with Rep; this interaction relocates Rep into the
CC nucleus. {ECO:0000250|UniProtKB:Q9YUC8}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:Q9YUC8}.
CC Virion {ECO:0000250|UniProtKB:Q9YUC8}.
CC -!- SIMILARITY: Belongs to the circoviridae capsid protein family.
CC {ECO:0000305}.
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DR EMBL; AF071879; AAC34820.1; -; Genomic_DNA.
DR EMBL; AY184287; AAN77864.1; -; Genomic_DNA.
DR EMBL; AY660574; AAT72756.1; -; Genomic_DNA.
DR RefSeq; NP_065679.1; NC_001792.2.
DR SMR; Q80QL5; -.
DR GeneID; 7693232; -.
DR KEGG; vg:7693232; -.
DR Proteomes; UP000007023; Genome.
DR Proteomes; UP000136520; Genome.
DR Proteomes; UP000180335; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019069; P:viral capsid assembly; IEA:InterPro.
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 Gene3D; 2.60.120.950; -; 1.
DR InterPro; IPR003383; Circovirus_capsid.
DR InterPro; IPR038652; Circovirus_capsid_sf.
DR Pfam; PF02443; Circo_capsid; 1.
PE 3: Inferred from homology;
KW Capsid protein; DNA-binding; Host nucleus; Host-virus interaction;
KW Reference proteome; T=1 icosahedral capsid protein;
KW Viral attachment to host cell; Viral penetration into host cytoplasm;
KW Viral penetration into host nucleus; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT CHAIN 1..230
FT /note="Capsid protein"
FT /id="PRO_0000133084"
FT REGION 1..47
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 5..43
FT /note="Nuclear localization signals"
FT /evidence="ECO:0000250|UniProtKB:O56129"
FT VARIANT 53..55
FT /note="TEL -> REF (in strain: Isolate IBRS-2)"
FT VARIANT 78
FT /note="G -> S (in strain: Isolate IBRS-2)"
FT CONFLICT 49
FT /note="S -> C (in Ref. 2; AAN77864)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="L -> F (in Ref. 2; AAN77864)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="Y -> F (in Ref. 2; AAN77864)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="N -> H (in Ref. 2; AAN77864)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..74
FT /note="YLK -> HLR (in Ref. 2; AAN77864)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="N -> K (in Ref. 2; AAN77864)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="E -> Q (in Ref. 1; AAC34820)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="P -> L (in Ref. 1; AAC34820)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 230 AA; 27479 MW; F3CC66F6DEE8D587 CRC64;
MTWPRRRYRR RRTRPRSHLG NILRRRPYLA HPAFRNRYRW RRKTGIFNSR LSTELVLTIK
GGYSQPSWNV NYLKFNIGQF LPPSGGTNPL PLPFQYYRIR KAKYEFYPRD PITSNERGVG
STVVILDANF VTPSTNLAYD PYINYSSRHT IRQPFTYHSR YFTPKPELDQ TIDWFHPNNK
RNQLWLHLNT HTNVEHTGLG YALQNAATAQ NYVVRLTIYV QFREFILKDP
