ID   CFBL_CHICK              Reviewed;         250 AA.
AC   P81475;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Complement factor B-like protease;
DE            EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=Complement factor B-like protease Ba fragment;
DE   Contains:
DE     RecName: Full=Complement factor B-like protease Bb fragment;
DE   Flags: Fragment;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Plasma;
RX   PubMed=8409391;
RA   Kjalke M., Welinder K.G., Koch C.;
RT   "Structural analysis of chicken factor B-like protease and comparison with
RT   mammalian complement proteins factor B and C2.";
RL   J. Immunol. 151:4147-4152(1993).
CC   -!- FUNCTION: Required in both the classical and alternate pathways of the
CC       complement system.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   MEROPS; S01.196; -.
DR   VEuPathDB; HostDB:geneid_419574; -.
DR   PhylomeDB; P81475; -.
DR   Reactome; R-GGA-2132263; Creation of classical C3 convertase.
DR   Reactome; R-GGA-2132273; Formation of membrane-bound convertase C3.
DR   Reactome; R-GGA-2132281; Regulation of complement cascades.
DR   Reactome; R-GGA-2132285; Complement Cascade.
DR   Reactome; R-GGA-2132293; Formation of fluid-phase convertase C3.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005601; C:classical-complement-pathway C3/C5 convertase complex; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006956; P:complement activation; IBA:GO_Central.
DR   GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006958; P:complement activation, classical pathway; 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   InterPro; IPR011360; Compl_C2_B.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   PANTHER; PTHR46393; PTHR46393; 1.
DR   Pfam; PF00084; Sushi; 2.
DR   SMART; SM00032; CCP; 2.
DR   SUPFAM; SSF57535; SSF57535; 2.
DR   PROSITE; PS50923; SUSHI; 3.
PE   1: Evidence at protein level;
KW   Complement alternate pathway; Complement pathway;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Immunity; Innate immunity; Protease; Reference proteome; Repeat; Secreted;
KW   Serine protease; Sushi.
FT   CHAIN           1..>250
FT                   /note="Complement factor B-like protease"
FT                   /id="PRO_0000027557"
FT   CHAIN           1..232
FT                   /note="Complement factor B-like protease Ba fragment"
FT                   /id="PRO_0000027558"
FT   CHAIN           233..>250
FT                   /note="Complement factor B-like protease Bb fragment"
FT                   /id="PRO_0000027559"
FT   DOMAIN          3..73
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          74..133
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          136..193
FT                   /note="Sushi 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        5..44
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..71
FT                   /evidence="ECO:0000250"
FT   DISULFID        76..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        104..131
FT                   /evidence="ECO:0000250"
FT   DISULFID        138..178
FT                   /evidence="ECO:0000250"
FT   DISULFID        164..191
FT                   /evidence="ECO:0000250"
FT   NON_TER         250
SQ   SEQUENCE   250 AA;  27059 MW;  8DEFE8454838C923 CRC64;
     ATTRCDPTLI PIAGGWFELL EGGEALRYRC PPGHIPTPLA RRSCGPDGQX EPLXXXXXXX
     XXXXXXXXXK CRAVWCPPPQ DMEHGSFWPR LPRYPPGSRL HFQCFQGFNL RGAPNRTCGE
     GGRWSGVTPV CDDGSGDCPA PPVXXXXXKE GSRYLLEDTV RFRCGPGLVL LGSAVRQCLE
     GGVWSGTEPQ CRAPLSFDTP SDVAASFMAS LSQSVERADS NSSHGPTEKL PRXIRVDGSA
     XLNVFLLXDA