ID CO2_PANTR Reviewed; 752 AA.
AC Q8SQ74;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 24-JAN-2024, entry version 114.
DE RecName: Full=Complement C2;
DE EC=3.4.21.43;
DE AltName: Full=C3/C5 convertase;
DE Contains:
DE RecName: Full=Complement C2b fragment;
DE Contains:
DE RecName: Full=Complement C2a fragment;
DE Flags: Precursor;
GN Name=C2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schneider P.M., Tantalaki E., Stradmann-Bellinghausen B., Rittner C.;
RT "Comparative analysis of human and primate complement C2 and factor B
RT genes.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component C2 which is part of the classical pathway of the
CC complement system is cleaved by activated factor C1 into two fragments:
CC C2b and C2a. C2a, a serine protease, then combines with complement
CC factor C4b to generate the C3 or C5 convertase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Ser bond in complement component
CC C3 alpha-chain to form C3a and C3b, and Arg-|-Xaa bond in complement
CC component C5 alpha-chain to form C5a and C5b.; EC=3.4.21.43;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AY074703; AAL82821.1; -; Genomic_DNA.
DR EMBL; AY074691; AAL82821.1; JOINED; Genomic_DNA.
DR EMBL; AY074692; AAL82821.1; JOINED; Genomic_DNA.
DR EMBL; AY074693; AAL82821.1; JOINED; Genomic_DNA.
DR EMBL; AY074694; AAL82821.1; JOINED; Genomic_DNA.
DR EMBL; AY074695; AAL82821.1; JOINED; Genomic_DNA.
DR EMBL; AY074696; AAL82821.1; JOINED; Genomic_DNA.
DR EMBL; AY074697; AAL82821.1; JOINED; Genomic_DNA.
DR EMBL; AY074698; AAL82821.1; JOINED; Genomic_DNA.
DR EMBL; AY074699; AAL82821.1; JOINED; Genomic_DNA.
DR EMBL; AY074700; AAL82821.1; JOINED; Genomic_DNA.
DR EMBL; AY074701; AAL82821.1; JOINED; Genomic_DNA.
DR EMBL; AY074702; AAL82821.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q8SQ74; -.
DR SMR; Q8SQ74; -.
DR MEROPS; S01.194; -.
DR GlyCosmos; Q8SQ74; 8 sites, No reported glycans.
DR PaxDb; 9598-ENSPTRP00000030714; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q8SQ74; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005601; C:classical-complement-pathway C3/C5 convertase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006956; P:complement activation; IBA:GO_Central.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IBA:GO_Central.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR CDD; cd01470; vWA_complement_factors; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 3.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR011360; Compl_C2_B.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR46393:SF2; COMPLEMENT C2; 1.
DR PANTHER; PTHR46393; SUSHI DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR Pfam; PF00092; VWA; 1.
DR PIRSF; PIRSF001154; Compl_C2_B; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50923; SUSHI; 3.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW Complement pathway; Disulfide bond; Glycoprotein; Hydrolase; Immunity;
KW Innate immunity; Metal-binding; Protease; Reference proteome; Repeat;
KW Secreted; Serine protease; Signal; Sushi.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..752
FT /note="Complement C2"
FT /id="PRO_0000027616"
FT CHAIN 21..243
FT /note="Complement C2b fragment"
FT /id="PRO_0000027617"
FT CHAIN 244..752
FT /note="Complement C2a fragment"
FT /id="PRO_0000027618"
FT DOMAIN 22..86
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 87..146
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 149..206
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 254..452
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 464..744
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MOTIF 260..264
FT /note="MIDAS-like motif"
FT /evidence="ECO:0000250"
FT ACT_SITE 507
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 561
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 679
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..64
FT /evidence="ECO:0000250"
FT DISULFID 51..84
FT /evidence="ECO:0000250"
FT DISULFID 89..131
FT /evidence="ECO:0000250"
FT DISULFID 117..144
FT /evidence="ECO:0000250"
FT DISULFID 151..191
FT /evidence="ECO:0000250"
FT DISULFID 177..204
FT /evidence="ECO:0000250"
FT DISULFID 492..508
FT /evidence="ECO:0000250"
FT DISULFID 675..705
FT /evidence="ECO:0000250"
SQ SEQUENCE 752 AA; 83280 MW; 54026575E7F1F763 CRC64;
MGPLMVLFCL LFLYPGLADS APSCPQNVNI SGGTFTLSHG WAPGSLLTYS CPQGLYPSPA
SRLCKSSGQW QTPGATRSLS KAVCKPVRCP APVSFENGIY TPRLGSYPVG GNVSFECEDG
FILRGSPVRH CCPNGMWDGE TAVCDNGAGH CPNPGISLGA VRTGFRFGHG DKVRYRCSSN
LVLTGSSERE CQGNGVWSGT EPICRQPYSY DFPEDVAPAL GTSFSHMLGA TNPTQKTKES
LGRKIQIQRS GHLNLYLLLD CSQSVSENDF LIFKESASLM VDRIFSFEIN VSVAIITFAS
EPRVLMSVLN DNSRDMTEVI SSLENANYKD HENGTGTNTY AALNSVYLMM NNQMRLLGME
TMAWQEIRHA IILLTDGKSN MGGSPKTAVD HIREILNINQ KRNDYLDIYA IGVGKLDVDW
RELNELGSKK DGERHAFILQ DTKALHQVFE HMLDVSKLTD TICGVGNMSA NASDQERTPW
HVTIKPKSQE TCRGALISDQ WVLTAAHCFR DGNDHSLWRV NVGDPKSRWG KEFLIEKAVI
SPGFDVFAKK NQGILEFYGD DIALLKLAQK VKMSTHARPI CLPCTMEANL ALRRPQGSTC
RDHENELLNK QSVPAHFVAL NGSKLNINLK MGVEWTSCAE VVSQEKTMFP NLTDVREVVT
DQFLCSGTQE DESPCKGESG GAVFLERRFR FFQVGLVSWG LYNPCLGSAD KNSRKRAPRS
KVPPPRDFHI NLFRMQPWLR QHLGDVLNFL PL
//
