CFAB_MOUSE
ID CFAB_MOUSE Reviewed; 761 AA.
AC P04186;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 190.
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, H2-Bf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2229060; DOI=10.1016/s0021-9258(17)30621-x;
RA Ishikawa N., Nonaka M., Wetsel R.A., Colten H.R.;
RT "Murine complement C2 and factor B genomic and cDNA cloning reveals
RT different mechanisms for multiple transcripts of C2 and B.";
RL J. Biol. Chem. 265:19040-19046(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 285-761.
RX PubMed=6689022; DOI=10.1016/s0021-9258(17)43918-4;
RA Sackstein R., Colten H.R., Woods D.E.;
RT "Phylogenetic conservation of a class III major histocompatibility complex
RT antigen, factor B. Isolation and nucleotide sequencing of mouse factor B
RT cDNA clones.";
RL J. Biol. Chem. 258:14693-14697(1983).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-282.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
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-256|Lys-257 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; M60646; AAA37379.1; -; Genomic_DNA.
DR EMBL; M60629; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60630; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60631; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60632; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60633; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60634; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60635; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60636; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60637; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60638; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60639; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60640; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60641; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60642; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60643; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60644; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; M60645; AAA37379.1; JOINED; Genomic_DNA.
DR EMBL; AF049850; AAC05283.1; -; Genomic_DNA.
DR EMBL; AF109906; AAC84160.1; -; Genomic_DNA.
DR EMBL; BC005451; AAH05451.1; -; mRNA.
DR EMBL; K01496; AAA39549.1; -; mRNA.
DR EMBL; K01497; AAA39550.1; -; mRNA.
DR EMBL; K01498; AAA39551.1; -; mRNA.
DR EMBL; M57890; AAA63293.1; -; mRNA.
DR PIR; A38875; BBMS.
DR AlphaFoldDB; P04186; -.
DR SMR; P04186; -.
DR ComplexPortal; CPX-5893; Alternative pathway fluid-phase C3 convertase complex C3(H2O)Bb.
DR ComplexPortal; CPX-5894; Alternative pathway C3 convertase complex C3bBb.
DR IntAct; P04186; 1.
DR MINT; P04186; -.
DR STRING; 10090.ENSMUSP00000025229; -.
DR BindingDB; P04186; -.
DR ChEMBL; CHEMBL4630808; -.
DR MEROPS; S01.196; -.
DR GlyGen; P04186; 4 sites.
DR iPTMnet; P04186; -.
DR PhosphoSitePlus; P04186; -.
DR SwissPalm; P04186; -.
DR CPTAC; non-CPTAC-3901; -.
DR jPOST; P04186; -.
DR PaxDb; P04186; -.
DR PeptideAtlas; P04186; -.
DR PRIDE; P04186; -.
DR Ensembl; ENSMUST00000128767; ENSMUSP00000119977; ENSMUSG00000090231.
DR MGI; MGI:105975; Cfb.
DR VEuPathDB; HostDB:ENSMUSG00000090231; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000158605; -.
DR HOGENOM; CLU_022004_1_0_1; -.
DR InParanoid; P04186; -.
DR OMA; QKGHENC; -.
DR PhylomeDB; P04186; -.
DR BRENDA; 3.4.21.47; 3474.
DR Reactome; R-MMU-173736; Alternative complement activation.
DR Reactome; R-MMU-174577; Activation of C3 and C5.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR ChiTaRS; Cfb; mouse.
DR PRO; PR:P04186; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P04186; protein.
DR Bgee; ENSMUSG00000090231; Expressed in proximal tubule and 64 other tissues.
DR ExpressionAtlas; P04186; baseline and differential.
DR Genevisible; P04186; MM.
DR GO; GO:0005601; C:classical-complement-pathway C3/C5 convertase complex; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042100; P:B cell proliferation; TAS:MGI.
DR GO; GO:0006956; P:complement activation; IBA:GO_Central.
DR GO; GO:0006957; P:complement activation, alternative pathway; IMP:MGI.
DR GO; GO:0050778; P:positive regulation of immune response; IC:ComplexPortal.
DR GO; GO:1903028; P:positive regulation of opsonization; IC:ComplexPortal.
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 PIRSF; PIRSF500181; Complement_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 Disulfide bond; Glycoprotein; Hydrolase; Immunity; Innate immunity;
KW Protease; Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW Sushi; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..761
FT /note="Complement factor B"
FT /id="PRO_0000027548"
FT CHAIN 23..256
FT /note="Complement factor B Ba fragment"
FT /id="PRO_0000027549"
FT CHAIN 257..761
FT /note="Complement factor B Bb fragment"
FT /id="PRO_0000027550"
FT DOMAIN 32..97
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 98..157
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 160..217
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 267..466
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 474..754
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 523
FT /note="Charge relay system"
FT ACT_SITE 573
FT /note="Charge relay system"
FT ACT_SITE 696
FT /note="Charge relay system"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..73
FT /evidence="ECO:0000250"
FT DISULFID 59..95
FT /evidence="ECO:0000250"
FT DISULFID 100..142
FT /evidence="ECO:0000250"
FT DISULFID 128..155
FT /evidence="ECO:0000250"
FT DISULFID 162..202
FT /evidence="ECO:0000250"
FT DISULFID 188..215
FT /evidence="ECO:0000250"
FT DISULFID 508..524
FT /evidence="ECO:0000250"
FT DISULFID 692..722
FT /evidence="ECO:0000250"
FT CONFLICT 730
FT /note="L -> P (in Ref. 4; AAA39549)"
FT /evidence="ECO:0000305"
FT CONFLICT 745
FT /note="V -> E (in Ref. 4; AAA39549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 85004 MW; 9E9015448A61020E CRC64;
MESPQLCLVL LVLGFSSGGV SATPVLEARP QVSCSLEGVE IKGGSFQLLQ GGQALEYLCP
SGFYPYPVQT RTCRSTGSWS DLQTRDQKIV QKAECRAIRC PRPQDFENGE FWPRSPFYNL
SDQISFQCYD GYVLRGSANR TCQENGRWDG QTAICDDGAG YCPNPGIPIG TRKVGSQYRL
EDIVTYHCSR GLVLRGSQKR KCQEGGSWSG TEPSCQDSFM YDSPQEVAEA FLSSLTETIE
GADAEDGHSP GEQQKRKIVL DPSGSMNIYL VLDGSDSIGS SNFTGAKRCL TNLIEKVASY
GVRPRYGLLT YATVPKVLVR VSDERSSDAD WVTEKLNQIS YEDHKLKSGT NTKRALQAVY
SMMSWAGDAP PEGWNRTRHV IIIMTDGLHN MGGNPVTVIQ DIRALLDIGR DPKNPREDYL
DVYVFGVGPL VDSVNINALA SKKDNEHHVF KVKDMEDLEN VFYQMIDETK SLSLCGMVWE
HKKGNDYHKQ PWQAKISVTR PLKGHETCMG AVVSEYFVLT AAHCFMVDDQ KHSIKVSVGG
QRRDLEIEEV LFHPKYNING KKAEGIPEFY DYDVALVKLK NKLKYGQTLR PICLPCTEGT
TRALRLPQTA TCKQHKEQLL PVKDVKALFV SEQGKSLTRK EVYIKNGDKK ASCERDATKA
QGYEKVKDAS EVVTPRFLCT GGVDPYADPN TCKGDSGGPL IVHKRSRFIQ VGVISWGVVD
VCRDQRRQQL VPSYARDFHI NLFQVLPWLK DKLKDEDLGF L
