CFAB_BOVIN
ID CFAB_BOVIN Reviewed; 761 AA.
AC P81187; Q2KIU6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Complement factor B;
DE EC=3.4.21.47;
DE AltName: Full=C3/C5 convertase;
DE AltName: Full=EC-VMFB;
DE Contains:
DE RecName: Full=Complement factor B Ba fragment;
DE Contains:
DE RecName: Full=Complement factor B Bb fragment;
DE Flags: Precursor;
GN Name=CFB; Synonyms=BF;
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=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 260-275.
RC TISSUE=Blood;
RX PubMed=9281322; DOI=10.1006/abbi.1997.0234;
RA Cai G., Satoh T., Hoshi H.;
RT "Isolation from fetal bovine serum of a fragment b of complement factor B-
RT like protein improving a long-term survival of human endothelial cells.";
RL Arch. Biochem. Biophys. 345:150-155(1997).
CC -!- FUNCTION: Factor B which is part of the alternate pathway of the
CC complement system is cleaved by factor D into 2 fragments: Ba and Bb.
CC Bb, a serine protease, then combines with complement factor 3b to
CC generate the C3 or C5 convertase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of Arg-|-Ser bond in complement component C3 alpha-
CC chain to yield C3a and C3b, and Arg-|-Xaa bond in complement
CC component C5 alpha-chain to yield C5a and C5b.; EC=3.4.21.47;
CC -!- SUBUNIT: Monomer (By similarity). Part of the C3-convertase enzyme
CC complex comprised of Complement C3 beta chain (C3b) and Complement
CC factor B Bb fragment (Bb) and CFP (By similarity). Interacts to C3b;
CC this interaction is dependent on the presence of Mg2+ (By similarity).
CC Interacts to CFP; this interaction contributes to the stabilization of
CC the active C3-convertase enzyme complex (By similarity).
CC {ECO:0000250|UniProtKB:P00751}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: The unliganded VWA domain has an inactive 'locked' conformation
CC whereby the scissile Arg-259|Lys-260 bond is protected from proteolytic
CC activation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; BC112504; AAI12505.1; -; mRNA.
DR RefSeq; NP_001035616.1; NM_001040526.1.
DR AlphaFoldDB; P81187; -.
DR SMR; P81187; -.
DR STRING; 9913.ENSBTAP00000009800; -.
DR MEROPS; S01.196; -.
DR PaxDb; P81187; -.
DR PeptideAtlas; P81187; -.
DR PRIDE; P81187; -.
DR Ensembl; ENSBTAT00000009800; ENSBTAP00000009800; ENSBTAG00000046158.
DR GeneID; 514076; -.
DR KEGG; bta:514076; -.
DR CTD; 629; -.
DR VEuPathDB; HostDB:ENSBTAG00000046158; -.
DR VGNC; VGNC:107285; CFB.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000158605; -.
DR HOGENOM; CLU_022004_1_0_1; -.
DR InParanoid; P81187; -.
DR OMA; QKGHENC; -.
DR OrthoDB; 172139at2759; -.
DR TreeFam; TF330194; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000046158; Expressed in liver and 102 other tissues.
DR ExpressionAtlas; P81187; baseline and differential.
DR GO; GO:0005601; C:classical-complement-pathway C3/C5 convertase complex; IBA:GO_Central.
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:0006957; P:complement activation, alternative 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; 3.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR011360; Compl_C2_B.
DR InterPro; IPR028341; Complement_B.
DR InterPro; IPR009003; Peptidase_S1_PA.
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:SF1; PTHR46393:SF1; 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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Complement alternate pathway;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Immunity; Innate immunity; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal; Sushi; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..761
FT /note="Complement factor B"
FT /id="PRO_0000285857"
FT CHAIN 26..259
FT /note="Complement factor B Ba fragment"
FT /id="PRO_0000285858"
FT CHAIN 260..761
FT /note="Complement factor B Bb fragment"
FT /id="PRO_0000027541"
FT DOMAIN 35..100
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 101..160
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 163..220
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 270..469
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 477..754
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 526
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 576
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 699
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..76
FT /evidence="ECO:0000250"
FT DISULFID 62..98
FT /evidence="ECO:0000250"
FT DISULFID 103..145
FT /evidence="ECO:0000250"
FT DISULFID 131..158
FT /evidence="ECO:0000250"
FT DISULFID 165..205
FT /evidence="ECO:0000250"
FT DISULFID 191..218
FT /evidence="ECO:0000250"
FT DISULFID 511..527
FT /evidence="ECO:0000250"
FT DISULFID 695..725
FT /evidence="ECO:0000250"
SQ SEQUENCE 761 AA; 85366 MW; 9802026064256687 CRC64;
MGIGHNPRLC LVPLILGLLC GGVGMTPLPE AGPQSPCSLE GVEIKGGSFR LLKAGQVLEY
LCPSGFYPYP TQIRTCRSTG SWSTLQTQDR KIVKRAECKA IRCPRPQDFE NGEYWPRAAY
YNLSDEISFR CYDGYTLRGS ANRTCQGNGR WDGETAICDD GATYCPNPGI PLGTRKVGSQ
YRLEDRVTYY CNRGLTLRGS EQRTCLEGGS WSGTEPSCQD SFMYDTPAEV AEAFLSSLTE
TIEGVDAEDG HSPGEQQKRK IVLDPSGSMN IYLVLDGSDS VGAHNFTGAK NCLRDFIEKV
ASYGVKPKYG LVTYATEPKV LIRVSDPKSS EADWVTDQLN QINYADHKLK AGTNTKRALL
EVYNMMSREV NQFKETWNRT RHVIIIMTDG LHNMGGDPVT VIHDIRYLLD IGRNRKNPRE
DYLDIYVFGV GPLVNQENIN ALASKKDKEK HVFKLQGMEN LEDVFVQMLD ESRTLGLCGM
VWEHKDGTAY HKQPWQAKIS VTRPSKGHES CMGAIVSEYF VLTAAHCFTV DDEKHSIKVS
LGGQRKEWEV KEILFHPKYD LNAKKAKGIP EFYDYDVALV RLKEKLKYET TIRPICLPCT
EGSIQALRLP RSTTCQQQMQ ELLPAKDIEA LFVSESKKTL TRKAVYIKNG DKKASCERDA
LRAPGYEKVK DVSEVVTPRF LCTGGVDPYA DPNTCKGDSG GPLIIHKRSR FIQVGVISWG
VVDVCKRPQQ VPGYARDFHI NLYQVLPWLK EKLQNEDLGF L
