ID CFAB_GORGO Reviewed; 764 AA.
AC Q864V9;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 108.
DE RecName: Full=Complement factor B;
DE EC=3.4.21.47;
DE AltName: Full=C3/C5 convertase;
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 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: 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. It has also been implicated in
CC proliferation and differentiation of preactivated B-lymphocytes, rapid
CC spreading of peripheral blood monocytes, stimulation of lymphocyte
CC blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation
CC of preactivated B-lymphocytes (By similarity). {ECO:0000250}.
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; AY074664; AAM10005.1; -; Genomic_DNA.
DR RefSeq; XP_004043760.1; XM_004043712.2.
DR AlphaFoldDB; Q864V9; -.
DR SMR; Q864V9; -.
DR STRING; 9593.ENSGGOP00000027366; -.
DR MEROPS; S01.196; -.
DR GlyCosmos; Q864V9; 4 sites, No reported glycans.
DR Ensembl; ENSGGOT00000002275.3; ENSGGOP00000002227.2; ENSGGOG00000002254.3.
DR GeneID; 101141641; -.
DR KEGG; ggo:101141641; -.
DR CTD; 629; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000158605; -.
DR HOGENOM; CLU_022004_1_0_1; -.
DR InParanoid; Q864V9; -.
DR OrthoDB; 3594820at2759; -.
DR Proteomes; UP000001519; Chromosome 6.
DR Bgee; ENSGGOG00000002254; Expressed in liver and 6 other cell types or tissues.
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 CDD; cd01470; vWA_complement_factors; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 3.
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; 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:SF1; COMPLEMENT FACTOR B; 1.
DR PANTHER; PTHR46393; SUSHI DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00084; Sushi; 3.
DR Pfam; PF00089; Trypsin; 1.
DR Pfam; PF00092; VWA; 1.
DR PIRSF; PIRSF001154; Compl_C2_B; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00453; VWFADOMAIN.
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 Cleavage on pair of basic residues; Complement alternate pathway;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunity; Innate immunity;
KW Protease; Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW Sushi; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..764
FT /note="Complement factor B"
FT /id="PRO_0000027542"
FT CHAIN 26..259
FT /note="Complement factor B Ba fragment"
FT /id="PRO_0000027543"
FT CHAIN 260..764
FT /note="Complement factor B Bb fragment"
FT /id="PRO_0000027544"
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..757
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 764 AA; 85526 MW; 2C6E9FFC2846D847 CRC64;
MGSNLSPQLC LMPFILGLLS GGVTTTPWSL ARPQGSCSLE GVEIKGGSFR LLQEGQALEY
VCPSGFYPYP VQTRTCRSTG SWSTLKTQDQ KTVRKAECRA IHCPRPHDFE NGEYWPRSPY
YNVSDEISFH CYDGYTLRGS ANRTCQVNGR WSGQTAICDN GAGYCSNPGI PIGTRKVGSQ
YRLEDSVTYH CSRGLTLRGS QRRTCQEGGS WSGTEPSCQD SFMYDTPQEV AEAFLSSLTE
TIEGVDAEDG HGPGEQQKRK IVLDPSGSMN IYLVLDGSDS IGASNFTGAK KCLVNLIEKV
ASYGVKPRYG LVTYATYPKI WVKVSDPDSS NADWVTKQLN EINYEDHKLK SGTNTKKALQ
AVYSMMSWPD DVPPEGWNRT RHVIILMTDG LHNMGGDPIT VIDEIRDLLY IGKDHKNPRE
DYLDVYVFGV GPLVNQVNIN ALASKKDNEQ HVFKVKDMEN LEDVFYQMID ESQSLSLCGM
VWEHRKGTDY HKQPWQAKIS VIRPSKGHES CMGAVVSEYF VLTAAHCFTV DDKEHSIKVS
VGGEKRDLEI EVVLFHPNYN INGKKEAGIP EFYDYDVALI KLKNKLKYGQ TIRPICLPCT
EGTTRALRLP PTTTCQQQKE ELLPAQDIKA LFVSEEEKKL TRKEVYIKNG DKKGSCERDA
QYAPGYDKVK DISEVVTPRF LCTGGVSPYA DPNTCRGDSG GPLIVHKRSR FIQVGVISWG
VVDVCKNQKR QKQVPAHARD FHINLFQVLP WLKEKLQDED LGFL
//
