CAPSD_PCV2
ID CAPSD_PCV2 Reviewed; 233 AA.
AC O56129; Q8BB11;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Capsid protein;
GN Name=Cap; ORFNames=ORF2;
OS Porcine circovirus 2 (PCV2).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC Cirlivirales; Circoviridae; Circovirus.
OX NCBI_TaxID=85708;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=pmws;
RX PubMed=9573301; DOI=10.1128/jvi.72.6.5262-5267.1998;
RA Hamel A.L., Lin L.L., Nayar G.P.;
RT "Nucleotide sequence of porcine circovirus associated with postweaning
RT multisystemic wasting syndrome in pigs.";
RL J. Virol. 72:5262-5267(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate PCV/688;
RX PubMed=12504550; DOI=10.1006/viro.2002.1733;
RA Cheung A.K.;
RT "Transcriptional analysis of porcine circovirus type 2.";
RL Virology 305:168-180(2003).
RN [3]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10950986; DOI=10.1099/0022-1317-81-9-2281;
RA Nawagitgul P., Morozov I., Bolin S.R., Harms P.A., Sorden S.D., Paul P.S.;
RT "Open reading frame 2 of porcine circovirus type 2 encodes a major capsid
RT protein.";
RL J. Gen. Virol. 81:2281-2287(2000).
RN [4]
RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNALS.
RX PubMed=11414809; DOI=10.1006/viro.2001.0922;
RA Liu Q., Tikoo S.K., Babiuk L.A.;
RT "Nuclear localization of the ORF2 protein encoded by porcine circovirus
RT type 2.";
RL Virology 285:91-99(2001).
RN [5]
RP MUTAGENESIS OF PRO-110 AND ARG-191.
RX PubMed=15564454; DOI=10.1128/jvi.78.24.13440-13446.2004;
RA Fenaux M., Opriessnig T., Halbur P.G., Elvinger F., Meng X.J.;
RT "Two amino acid mutations in the capsid protein of type 2 porcine
RT circovirus (PCV2) enhanced PCV2 replication in vitro and attenuated the
RT virus in vivo.";
RL J. Virol. 78:13440-13446(2004).
RN [6]
RP FUNCTION.
RX PubMed=16537616; DOI=10.1128/jvi.80.7.3487-3494.2006;
RA Misinzo G., Delputte P.L., Meerts P., Lefebvre D.J., Nauwynck H.J.;
RT "Porcine circovirus 2 uses heparan sulfate and chondroitin sulfate B
RT glycosaminoglycans as receptors for its attachment to host cells.";
RL J. Virol. 80:3487-3494(2006).
RN [7]
RP FUNCTION.
RX PubMed=18952130; DOI=10.1016/j.virusres.2008.09.005;
RA Misinzo G., Delputte P.L., Lefebvre D.J., Nauwynck H.J.;
RT "Porcine circovirus 2 infection of epithelial cells is clathrin-,
RT caveolae- and dynamin-independent, actin and Rho-GTPase-mediated, and
RT enhanced by cholesterol depletion.";
RL Virus Res. 139:1-9(2009).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=29292065; DOI=10.1016/j.virusres.2017.12.012;
RA Hou Q., Hou S., Chen Q., Jia H., Xin T., Jiang Y., Guo X., Zhu H.;
RT "Nuclear localization signal regulates porcine circovirus type 2 capsid
RT protein nuclear export through phosphorylation.";
RL Virus Res. 246:12-22(2018).
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
CC the 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 internalized in a clathrin-, caveolae- and dynamin-independent, actin
CC and Rho-GTPase-mediated pathway and traffics to the nucleus. The capsid
CC protein binds and transports the viral genome and Rep across the
CC nuclear envelope (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10950986, ECO:0000269|PubMed:16537616,
CC ECO:0000269|PubMed:18952130}.
CC -!- SUBUNIT: Homomultimer. Assembles in the nucleus, presumably in an
CC immature form, then migrates to the cytoplasm once assembled as mature
CC virion (Probable). Interacts with Rep; this interaction relocates Rep
CC into the nucleus (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:11414809,
CC ECO:0000269|PubMed:29292065}. Virion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the circoviridae capsid protein family.
CC {ECO:0000305}.
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DR EMBL; AF027217; AAC59463.1; -; Genomic_DNA.
DR EMBL; AY094619; AAM21849.1; -; Genomic_DNA.
DR SMR; O56129; -.
DR DIP; DIP-61914N; -.
DR ABCD; O56129; 21 sequenced antibodies.
DR Proteomes; UP000000470; Genome.
DR Proteomes; UP000150239; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:AgBase.
DR GO; GO:0044174; C:host cell endosome; IDA:AgBase.
DR GO; GO:0042025; C:host cell nucleus; IDA:AgBase.
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:0071929; P:alpha-tubulin acetylation; IMP:AgBase.
DR GO; GO:0039506; P:modulation by virus of host molecular function; IMP:AgBase.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by 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 1: Evidence at protein level;
KW Capsid protein;
KW Clathrin- and caveolin-independent endocytosis of virus by host;
KW DNA-binding; Host nucleus; Host-virus interaction;
KW T=1 icosahedral capsid protein; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Viral penetration into host nucleus;
KW Virion; Virus endocytosis by host; Virus entry into host cell.
FT CHAIN 1..233
FT /note="Capsid protein"
FT /id="PRO_0000133085"
FT REGION 1..47
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 5..41
FT /note="Nuclear localization signals"
FT /evidence="ECO:0000269|PubMed:29292065"
FT VARIANT 59
FT /note="A -> R (in strain: Isolate PCV/688)"
FT VARIANT 63
FT /note="R -> T (in strain: Isolate PCV/688)"
FT VARIANT 75..76
FT /note="NI -> KF (in strain: Isolate PCV/688)"
FT VARIANT 131
FT /note="T -> P (in strain: Isolate PCV/688)"
FT VARIANT 134
FT /note="T -> N (in strain: Isolate PCV/688)"
FT VARIANT 181
FT /note="T -> N (in strain: Isolate PCV/688)"
FT VARIANT 206
FT /note="I -> K (in strain: Isolate PCV/688)"
FT VARIANT 215
FT /note="V -> I (in strain: Isolate PCV/688)"
FT VARIANT 232
FT /note="K -> N (in strain: Isolate PCV/688)"
FT MUTAGEN 110
FT /note="P->A: Complete loss of virulence in host and
FT increased replication in PK15 cell culture; when associated
FT with S-191."
FT /evidence="ECO:0000269|PubMed:15564454"
FT MUTAGEN 191
FT /note="R->S: Complete loss of virulence in host and
FT increased replication in PK15 cell culture; when associated
FT with A-110."
FT /evidence="ECO:0000269|PubMed:15564454"
SQ 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
