VCP_VACCW
ID VCP_VACCW Reviewed; 263 AA.
AC P68638; P10998; Q76ZY4;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Complement control protein C3;
DE AltName: Full=28 kDa protein;
DE AltName: Full=Secretory protein 35;
DE Short=Protein C3;
DE AltName: Full=VCP;
DE Flags: Precursor;
GN OrderedLocusNames=VACWR025; ORFNames=C3L;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 20-37.
RX PubMed=3412473; DOI=10.1038/335176a0;
RA Kotwal G.J., Moss B.;
RT "Vaccinia virus encodes a secretory polypeptide structurally related to
RT complement control proteins.";
RL Nature 335:176-178(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2849238; DOI=10.1016/s0042-6822(88)90115-8;
RA Kotwal G.J., Moss B.;
RT "Analysis of a large cluster of nonessential genes deleted from a vaccinia
RT virus terminal transposition mutant.";
RL Virology 167:524-537(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=1731333; DOI=10.1073/pnas.89.2.628;
RA Isaacs S.N., Kotwal G.J., Moss B.;
RT "Vaccinia virus complement-control protein prevents antibody-dependent
RT complement-enhanced neutralization of infectivity and contributes to
RT virulence.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:628-632(1992).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18287241; DOI=10.1128/jvi.02426-07;
RA Girgis N.M., Dehaven B.C., Fan X., Viner K.M., Shamim M., Isaacs S.N.;
RT "Cell surface expression of the vaccinia virus complement control protein
RT is mediated by interaction with the viral A56 protein and protects infected
RT cells from complement attack.";
RL J. Virol. 82:4205-4214(2008).
RN [6]
RP INTERMOLECULAR DISULFIDE BOND.
RX PubMed=20719953; DOI=10.1128/jvi.00372-10;
RA DeHaven B.C., Girgis N.M., Xiao Y., Hudson P.N., Olson V.A., Damon I.K.,
RA Isaacs S.N.;
RT "Poxvirus complement control proteins are expressed on the cell surface
RT through an intermolecular disulfide bridge with the viral A56 protein.";
RL J. Virol. 84:11245-11254(2010).
RN [7]
RP INTERACTION WITH A56, AND SUBCELLULAR LOCATION.
RX PubMed=21715594; DOI=10.1099/vir.0.030460-0;
RA Dehaven B.C., Gupta K., Isaacs S.N.;
RT "The vaccinia virus A56 protein: a multifunctional transmembrane
RT glycoprotein that anchors two secreted viral proteins.";
RL J. Gen. Virol. 92:1971-1980(2011).
RN [8]
RP STRUCTURE BY NMR OF 146-263, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=9299352; DOI=10.1006/jmbi.1997.1241;
RA Wiles A.P., Shaw G., Bright J., Perczel A., Campbell I.D., Barlow P.N.;
RT "NMR studies of a viral protein that mimics the regulators of complement
RT activation.";
RL J. Mol. Biol. 272:253-265(1997).
CC -!- FUNCTION: Serves to protect the virus against complement attack by
CC inhibiting both classical and alternative pathways of complement
CC activation. Binds C3b and C4b. {ECO:0000269|PubMed:1731333,
CC ECO:0000269|PubMed:18287241}.
CC -!- SUBUNIT: Heterodimer with A56 protein; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}; Extracellular side
CC {ECO:0000305}. Secreted {ECO:0000305}. Note=Component of extracellular
CC enveloped virus (EEV) but not intracellular mature virus (IMV).
CC Anchored to the surface of the outermost membrane of EEV via its
CC interaction with A56 protein.
CC -!- SIMILARITY: Belongs to the receptors of complement activation (RCA)
CC family. {ECO:0000305}.
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DR EMBL; X13166; CAA31564.1; -; Genomic_DNA.
DR EMBL; M22812; AAA69605.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89304.1; -; Genomic_DNA.
DR PIR; A31005; WMVZSP.
DR RefSeq; YP_232907.1; NC_006998.1.
DR PDB; 1VVC; NMR; -; A=146-263.
DR PDB; 1VVD; NMR; -; A=146-263.
DR PDB; 1VVE; NMR; -; A=146-263.
DR PDBsum; 1VVC; -.
DR PDBsum; 1VVD; -.
DR PDBsum; 1VVE; -.
DR SMR; P68638; -.
DR IntAct; P68638; 1.
DR MINT; P68638; -.
DR DrugBank; DB03959; N,O6-Disulfo-Glucosamine.
DR DrugBank; DB02264; O2-Sulfo-Glucuronic Acid.
DR DrugBank; DB04786; Suramin.
DR ABCD; P68638; 4 sequenced antibodies.
DR DNASU; 3707640; -.
DR GeneID; 3707640; -.
DR KEGG; vg:3707640; -.
DR EvolutionaryTrace; P68638; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001848; F:complement binding; IEA:InterPro.
DR GO; GO:0045916; P:negative regulation of complement activation; IEA:InterPro.
DR GO; GO:0039573; P:suppression by virus of host complement activation; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 4.
DR InterPro; IPR011176; CCP_VACV_C3/B5.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 4.
DR PIRSF; PIRSF002486; CIP_VAC_C3L; 1.
DR SMART; SM00032; CCP; 4.
DR SUPFAM; SSF57535; SSF57535; 4.
DR PROSITE; PS50923; SUSHI; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Host cell membrane; Host membrane; Host-virus interaction;
KW Inhibition of host complement factors by virus; Membrane;
KW Reference proteome; Repeat; Secreted; Signal; Sushi; Viral immunoevasion;
KW Virion.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:3412473"
FT CHAIN 20..263
FT /note="Complement control protein C3"
FT /id="PRO_0000006024"
FT DOMAIN 20..83
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 84..145
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 146..203
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 204..263
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 20
FT /note="Interchain (with C-162 in protein A56)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 21..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 54..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 86..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 112..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 148..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 176..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 206..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 234..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1VVC"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1VVC"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1VVC"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:1VVC"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1VVE"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1VVD"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1VVC"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1VVC"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1VVC"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:1VVC"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1VVC"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:1VVC"
SQ SEQUENCE 263 AA; 28629 MW; E4322CC9A6EF8997 CRC64;
MKVESVTFLT LLGIGCVLSC CTIPSRPINM KFKNSVETDA NANYNIGDTI EYLCLPGYRK
QKMGPIYAKC TGTGWTLFNQ CIKRRCPSPR DIDNGQLDIG GVDFGSSITY SCNSGYHLIG
ESKSYCELGS TGSMVWNPEA PICESVKCQS PPSISNGRHN GYEDFYTDGS VVTYSCNSGY
SLIGNSGVLC SGGEWSDPPT CQIVKCPHPT ISNGYLSSGF KRSYSYNDNV DFKCKYGYKL
SGSSSSTCSP GNTWKPELPK CVR
