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CO2_GORGO
ID   CO2_GORGO               Reviewed;         752 AA.
AC   Q863A0;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
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   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
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 (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; AY074677; AAM10001.1; -; Genomic_DNA.
DR   EMBL; AY074665; AAM10001.1; JOINED; Genomic_DNA.
DR   EMBL; AY074666; AAM10001.1; JOINED; Genomic_DNA.
DR   EMBL; AY074667; AAM10001.1; JOINED; Genomic_DNA.
DR   EMBL; AY074669; AAM10001.1; JOINED; Genomic_DNA.
DR   EMBL; AY074671; AAM10001.1; JOINED; Genomic_DNA.
DR   EMBL; AY074673; AAM10001.1; JOINED; Genomic_DNA.
DR   EMBL; AY074675; AAM10001.1; JOINED; Genomic_DNA.
DR   EMBL; AY074676; AAM10001.1; JOINED; Genomic_DNA.
DR   EMBL; AY074674; AAM10001.1; JOINED; Genomic_DNA.
DR   EMBL; AY074672; AAM10001.1; JOINED; Genomic_DNA.
DR   EMBL; AY074670; AAM10001.1; JOINED; Genomic_DNA.
DR   EMBL; AY074668; AAM10001.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q863A0; -.
DR   SMR; Q863A0; -.
DR   MEROPS; S01.194; -.
DR   InParanoid; Q863A0; -.
DR   Proteomes; UP000001519; 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; 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   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_0000027607"
FT   CHAIN           21..243
FT                   /note="Complement C2b fragment"
FT                   /id="PRO_0000027608"
FT   CHAIN           244..752
FT                   /note="Complement C2a fragment"
FT                   /id="PRO_0000027609"
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;  83276 MW;  4ADCD2B96AABB167 CRC64;
     MGPLMVLFCL LFVYTGLADS APSCPQNVNI SGGTFTLSHG WAPGSLLTYS CPQGLYPSPA
     SRLCKSSGQW QTPGATRSLS KAVCKPVRCP APVSFENGIY TPRLGSYPVG GNVSFECEDG
     FILRGSPVRQ CRPNGMWDGE TAVCDNGAGH CPNPGISLGA VRTGFRFGHG DKVRYRCSSN
     LVLTGSSERE CQGNGVWSGT EPICRQPYSY DFPEDVAPAL GTSFSHMLGA TNPTQKTKES
     LGRKIQIQRS GHLNLYLLLD CSQSVSENDF LIFKESASLM VDRIFSFEIN VSVAIITFAS
     KPKVLMSVLN DNSRDMTEVI SSLENANYKD HENGTGTNTY AALNSVYLMM NNQMRILGME
     TMAWQEIRHA IILLTDGKSN MGGSPKTAVD RIREILNINQ KRNDYLDIYA IGVGKLDVDW
     RELNELGSKK DGERHAFILQ DTKALHQVFE HMLDVSKLTD TICGVGNMSA NASDQERTPW
     HVTIKPKSQE TCRGALISDQ WVLTAAHCFR DGNDHSLWRV NVGDPKSQWG KEFLIEKAVI
     SPGFDVFAKK NQGILEFYGD DIALLKLAQK VKMSTHARPI CLPCTMEANL ALRRPQGSTC
     RDHENELLNK QSVPAHFVAL NGSKLNINLK MGVEWTSCAE VVSQEKTMFP NLTDVREVVT
     DQFLCSGTQE DESPCKGESG GAVFLERRFR FFQVGLVSWG LYNPCLGSAD KNSRKRAPRS
     KVPPPRDFHI NLFRMQPWLR QHLGDVLNFL PL
 
 
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