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Capsid protein

 CAPSD_PCV2              Reviewed;         233 AA.
O56129; Q8BB11;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-APR-2018, entry version 71.
RecName: Full=Capsid protein;
Name=Cap; ORFNames=ORF2;
Porcine circovirus 2 (PCV2).
Viruses; ssDNA viruses; Circoviridae; Circovirus.
NCBI_TaxID=85708;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=pmws;
PubMed=9573301;
Hamel A.L., Lin L.L., Nayar G.P.;
"Nucleotide sequence of porcine circovirus associated with postweaning
multisystemic wasting syndrome in pigs.";
J. Virol. 72:5262-5267(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Isolate PCV/688;
PubMed=12504550; DOI=10.1006/viro.2002.1733;
Cheung A.K.;
"Transcriptional analysis of porcine circovirus type 2.";
Virology 305:168-180(2003).
[3]
FUNCTION, AND SUBUNIT.
PubMed=10950986;
Nawagitgul P., Morozov I., Bolin S.R., Harms P.A., Sorden S.D.,
Paul P.S.;
"Open reading frame 2 of porcine circovirus type 2 encodes a major
capsid protein.";
J. Gen. Virol. 81:2281-2287(2000).
[4]
SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNALS.
PubMed=11414809; DOI=10.1006/viro.2001.0922;
Liu Q., Tikoo S.K., Babiuk L.A.;
"Nuclear localization of the ORF2 protein encoded by porcine
circovirus type 2.";
Virology 285:91-99(2001).
[5]
MUTAGENESIS OF PRO-110 AND ARG-191.
PubMed=15564454; DOI=10.1128/JVI.78.24.13440-13446.2004;
Fenaux M., Opriessnig T., Halbur P.G., Elvinger F., Meng X.J.;
"Two amino acid mutations in the capsid protein of type 2 porcine
circovirus (PCV2) enhanced PCV2 replication in vitro and attenuated
the virus in vivo.";
J. Virol. 78:13440-13446(2004).
[6]
FUNCTION.
PubMed=16537616; DOI=10.1128/JVI.80.7.3487-3494.2006;
Misinzo G., Delputte P.L., Meerts P., Lefebvre D.J., Nauwynck H.J.;
"Porcine circovirus 2 uses heparan sulfate and chondroitin sulfate B
glycosaminoglycans as receptors for its attachment to host cells.";
J. Virol. 80:3487-3494(2006).
[7]
FUNCTION.
PubMed=18952130; DOI=10.1016/j.virusres.2008.09.005;
Misinzo G., Delputte P.L., Lefebvre D.J., Nauwynck H.J.;
"Porcine circovirus 2 infection of epithelial cells is clathrin-,
caveolae-and dynamin-independent, actin and Rho-GTPase-mediated, and
enhanced by cholesterol depletion.";
Virus Res. 139:1-9(2009).
-!- FUNCTION: Self-assembles to form the virion icosahedral capsid
with a T=1 symmetry. This very small capsid (17 - 22 nm in
diameter) allows the virus to be very stable in the environment
and resistant to some disinfectants, including detergents.
Essential for the initial attachment to heparan sulfate moities
and chondroitin sulfate B of the host cell surface proteoglycans.
After attachment, the virus is internalized in a clathrin-,
caveolae- and dynamin-independent, actin and Rho-GTPase-mediated
pathway and traffics to the nucleus. The capsid protein binds and
transports the viral genome and Rep across the nuclear envelope
(By similarity). {ECO:0000250, ECO:0000269|PubMed:10950986,
ECO:0000269|PubMed:16537616, ECO:0000269|PubMed:18952130}.
-!- SUBUNIT: Homomultimer. Assembles in the nucleus, presumably in an
immature form, then migrates to the cytoplasm once assembled as
mature virion (Probable). Interacts with Rep; this interaction
relocates Rep into the nucleus (By similarity). {ECO:0000250,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:11414809}.
Virion {ECO:0000305}.
-!- SIMILARITY: Belongs to the circoviridae capsid protein family.
{ECO:0000305}.
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EMBL; AF027217; AAC59463.1; -; Genomic_DNA.
EMBL; AY094619; AAM21849.1; -; Genomic_DNA.
ProteinModelPortal; O56129; -.
SMR; O56129; -.
DIP; DIP-61914N; -.
OrthoDB; VOG090001MC; -.
Proteomes; UP000000470; Genome.
Proteomes; UP000150239; Genome.
GO; GO:0030430; C:host cell cytoplasm; IDA:AgBase.
GO; GO:0044174; C:host cell endosome; IDA:AgBase.
GO; GO:0042025; C:host cell nucleus; IDA:AgBase.
GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0071929; P:alpha-tubulin acetylation; IMP:AgBase.
GO; GO:0039506; P:modulation by virus of host molecular function; IMP:AgBase.
GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0019069; P:viral capsid assembly; IEA:InterPro.
GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
Gene3D; 2.60.120.950; -; 1.
InterPro; IPR003383; Circovirus_capsid.
InterPro; IPR038652; Circovirus_capsid_sf.
Pfam; PF02443; Circo_capsid; 1.
1: Evidence at protein level;
Capsid protein;
Clathrin- and caveolin-independent endocytosis of virus by host;
Complete proteome; DNA-binding; Host nucleus; Host-virus interaction;
T=1 icosahedral capsid protein; Viral attachment to host cell;
Viral penetration into host cytoplasm;
Viral penetration into host nucleus; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 233 Capsid protein.
/FTId=PRO_0000133085.
REGION 1 47 DNA-binding. {ECO:0000250}.
REGION 9 41 Nuclear localization signals.
{ECO:0000255}.
VARIANT 59 59 A -> R (in strain: Isolate PCV/688).
VARIANT 63 63 R -> T (in strain: Isolate PCV/688).
VARIANT 75 76 NI -> KF (in strain: Isolate PCV/688).
VARIANT 131 131 T -> P (in strain: Isolate PCV/688).
VARIANT 134 134 T -> N (in strain: Isolate PCV/688).
VARIANT 181 181 T -> N (in strain: Isolate PCV/688).
VARIANT 206 206 I -> K (in strain: Isolate PCV/688).
VARIANT 215 215 V -> I (in strain: Isolate PCV/688).
VARIANT 232 232 K -> N (in strain: Isolate PCV/688).
MUTAGEN 110 110 P->A: Complete loss of virulence in host
and increased replication in PK15 cell
culture; when associated with S-191.
{ECO:0000269|PubMed:15564454}.
MUTAGEN 191 191 R->S: Complete loss of virulence in host
and increased replication in PK15 cell
culture; when associated with A-110.
{ECO:0000269|PubMed:15564454}.
SEQUENCE 233 AA; 27897 MW; 3C664C4B4E83AB58 CRC64;
MTYPRRRYRR RRHRPRSHLG QILRRRPWLV HPRHRYRWRR KNGIFNTRLS RTFGYTVKAT
TVRTPSWAVD MMRFNIDDFV PPGGGTNKIS IPFEYYRIRK VKVEFWPCSP ITQGDRGVGS
TAVILDDNFV TKATALTYDP YVNYSSRHTI PQPFSYHSRY FTPKPVLDST IDYFQPNNKR
TQLWLRLQTS RNVDHVGLGT AFENSIYDQD YNIRVTMYVQ FREFNLKDPP LKP


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