VCP_VACCC
ID VCP_VACCC Reviewed; 263 AA.
AC P68639; P10998;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 65.
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 ORFNames=C3L;
OS Vaccinia virus (strain Copenhagen) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10249;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "The complete DNA sequence of vaccinia virus.";
RL Virology 179:247-266(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA Paoletti E.;
RT "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL Virology 179:517-563(1990).
RN [3]
RP STRUCTURE BY NMR OF 84-203, AND DISULFIDE BONDS.
RX PubMed=11243823; DOI=10.1006/jmbi.2000.4477;
RA Henderson C.E., Bromek K., Mullin N.P., Smith B.O., Uhrin D., Barlow P.N.;
RT "Solution structure and dynamics of the central CCP module pair of a
RT poxvirus complement control protein.";
RL J. Mol. Biol. 307:323-339(2001).
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.
CC -!- SUBUNIT: Heterodimer with A56 protein; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Extracellular side
CC {ECO:0000250}. Secreted {ECO:0000250}. 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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the receptors of complement activation (RCA)
CC family. {ECO:0000305}.
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DR EMBL; M35027; AAA47997.1; -; Genomic_DNA.
DR PIR; A31005; WMVZSP.
DR PDB; 1E5G; NMR; -; A=84-203.
DR PDBsum; 1E5G; -.
DR SMR; P68639; -.
DR EvolutionaryTrace; P68639; -.
DR Proteomes; UP000008269; 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; Disulfide bond; Host cell membrane; Host membrane;
KW Host-virus interaction; Inhibition of host complement factors by virus;
KW Membrane; Reference proteome; Repeat; Secreted; Signal; Sushi;
KW Viral immunoevasion; Virion.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..263
FT /note="Complement control protein C3"
FT /id="PRO_0000006023"
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 ECO:0000269|PubMed:11243823"
FT DISULFID 176..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:11243823"
FT DISULFID 206..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:11243823"
FT DISULFID 234..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:11243823"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1E5G"
FT STRAND 107..117
FT /evidence="ECO:0007829|PDB:1E5G"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1E5G"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1E5G"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1E5G"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1E5G"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1E5G"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1E5G"
FT STRAND 170..179
FT /evidence="ECO:0007829|PDB:1E5G"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:1E5G"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1E5G"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1E5G"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1E5G"
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
