CO2_BOVIN
ID CO2_BOVIN Reviewed; 750 AA.
AC Q3SYW2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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 (By similarity).
CC {ECO:0000250}.
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 {ECO:0000250}.
CC -!- DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent metal
CC cations. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; BC103357; AAI03358.1; -; mRNA.
DR RefSeq; NP_001029664.1; NM_001034492.1.
DR AlphaFoldDB; Q3SYW2; -.
DR SMR; Q3SYW2; -.
DR STRING; 9913.ENSBTAP00000042824; -.
DR MEROPS; S01.194; -.
DR PaxDb; Q3SYW2; -.
DR PRIDE; Q3SYW2; -.
DR Ensembl; ENSBTAT00000009798; ENSBTAP00000009798; ENSBTAG00000007450.
DR GeneID; 515440; -.
DR KEGG; bta:515440; -.
DR CTD; 717; -.
DR VEuPathDB; HostDB:ENSBTAG00000007450; -.
DR VGNC; VGNC:53959; C2.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162934; -.
DR InParanoid; Q3SYW2; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000007450; Expressed in liver and 102 other tissues.
DR ExpressionAtlas; Q3SYW2; baseline and differential.
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; 3.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR011360; Compl_C2_B.
DR InterPro; IPR037568; Complement_C2.
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; PTHR46393; 1.
DR PANTHER; PTHR46393:SF2; PTHR46393:SF2; 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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF57535; SSF57535; 3.
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 2: Evidence at transcript level;
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..750
FT /note="Complement C2"
FT /id="PRO_0000236266"
FT CHAIN 21..244
FT /note="Complement C2b fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000236267"
FT CHAIN 245..750
FT /note="Complement C2a fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000236268"
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 255..453
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 465..742
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MOTIF 261..265
FT /note="MIDAS-like motif"
FT /evidence="ECO:0000250"
FT ACT_SITE 508
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 562
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 680
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 338
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 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..65
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 493..509
FT /evidence="ECO:0000250"
FT DISULFID 676..706
FT /evidence="ECO:0000250"
SQ SEQUENCE 750 AA; 82906 MW; 25D199DB5CB43B21 CRC64;
MDPLMAVLCL LPLYPGLATA ALSCPKNVNI SGGSFTLSNG WNPGSILTYS CPLGHYPYPV
VTRLCKSNGQ WQIPRSTRST KAICKPVRCP APVSFENGVY IPRLGSHPVG GNLSFECEDG
FTLRGSAVRQ CRPNGMWDGE TAVCDNGASH CPNPGISVGA VRTGSRFGLG DKVRYRCSSN
LVLTGSAERE CQDDGVWSGT EAICRQPYSY DFPEDVAPAL GTSFSHLLAT TNPIQQKKKQ
NLGRKIQIQR SGHLNLYLLL DASQSVSKDD FEIFKDSASR MVDRIFSFEI KVSVAIITFA
SKPKIIMSVL EDRSRDVTEV ENSLRNINYK DHENGTGTNI YEALHAVYIM MNNQMNRPHM
NPGAWQEIRH AIILLTDGKS NMGGSPKVAV DNIKEVLNIN QKRKDYLDIY AIGVGSLHVD
WKELNNLGSK KDGERHAFIL KDVQALSQVF EHMLDVSQLT DPICGVGNMS ANASAQERTP
WHVTIKPKSQ ETCRGALISD QWVLTAAHCF RNAEDRTLWR VSVGDPNFQG SKEFQIEEAV
ISPGFNVFSK KSQGIPEFYG DDIALLKLTQ KVKMSTHARP ICLPCTVGAN LALRKLPGST
CRDHEKELLN QVSIPAHFVA LNGDKLNINL KTGSEWTNCV KVVLKDKTTF PNLTDVREVV
TDQFLCSGTQ GDDSPCKGES GGAVFLERRL RFFQVGLVSW GLYNPCGGSS KNSRKPAPHG
KVPRDFHINL FRLQPWLRQH LEGILNFVPL
