ID CFAB_HUMAN Reviewed; 764 AA.
AC P00751; B0QZQ6; O15006; Q29944; Q5JP67; Q5ST50; Q96HX6; Q9BTF5;
AC Q9BX92;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 01-MAY-2013, entry version 181.
DE RecName: Full=Complement factor B;
DE EC=3.4.21.47;
DE AltName: Full=C3/C5 convertase;
DE AltName: Full=Glycine-rich beta glycoprotein;
DE Short=GBG;
DE AltName: Full=PBF2;
DE AltName: Full=Properdin factor B;
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, BFD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28; GLN-28;
RP GLN-32 AND SER-736.
RX PubMed=2249879; DOI=10.1007/BF00211644;
RA Davrinche C., Abbal M., Clerc A.;
RT "Molecular characterization of human complement factor B subtypes.";
RL Immunogenetics 32:309-312(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28 AND
RP GLN-32.
RC TISSUE=Liver;
RX PubMed=8181962; DOI=10.1016/0198-8859(94)90100-7;
RA Mejia J.E., Jahn I., de la Salle H., Hauptmann G.;
RT "Human factor B. Complete cDNA sequence of the BF*S allele.";
RL Hum. Immunol. 39:49-53(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28 AND
RP GLN-32.
RC TISSUE=Liver;
RX PubMed=8225386;
RA Schwaeble W., Luettig B., Sokolowski T., Estaller C., Weiss E.H.,
RA Meyer Zum Bueschenfelde K.-H., Whaley K., Dippold W.;
RT "Human complement factor B: functional properties of a recombinant
RT zymogen of the alternative activation pathway convertase.";
RL Immunobiology 188:221-232(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28 AND
RP GLN-32.
RX PubMed=8247029; DOI=10.1016/0161-5890(93)90450-P;
RA Horiuchi T., Kim S., Matsumoto M., Watanabe I., Fujita S.,
RA Volanakis J.E.;
RT "Human complement factor B: cDNA cloning, nucleotide sequencing,
RT phenotypic conversion by site-directed mutagenesis and expression.";
RL Mol. Immunol. 30:1587-1592(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Jaatinen T., Kanerva J., Poutanen K.E., Saarinen-Pihkala U.,
RA Lokki M.-L.;
RT "Expression and alternative splicing of human factor B gene in
RT leukemic mononuclear cells.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA Campbell R.D., 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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-9; GLN-32; TRP-32;
RP SER-252; GLU-565 AND GLU-651.
RG SeattleSNPs variation discovery resource;
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-565.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP TRP-32.
RC TISSUE=Colon;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 26-764, PARTIAL NUCLEOTIDE SEQUENCE [MRNA], AND
RP GLYCOSYLATION AT ASN-122; ASN-142; ASN-285 AND ASN-378.
RX PubMed=6546754;
RA Mole J.E., Anderson J.K., Davison E.A., Woods D.E.;
RT "Complete primary structure for the zymogen of human complement factor
RT B.";
RL J. Biol. Chem. 259:3407-3412(1984).
RN [11]
RP PROTEIN SEQUENCE OF 260-764.
RX PubMed=6342610;
RA Christie D.L., Gagnon J.;
RT "Amino acid sequence of the Bb fragment from complement Factor B.
RT Sequence of the major cyanogen bromide-cleavage peptide (CB-II) and
RT completion of the sequence of the Bb fragment.";
RL Biochem. J. 209:61-70(1983).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 339-764.
RX PubMed=6308626; DOI=10.1073/pnas.80.14.4464;
RA Campbell R.D., Porter R.R.;
RT "Molecular cloning and characterization of the gene coding for human
RT complement protein factor B.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4464-4468(1983).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 467-595 AND 752-764.
RX PubMed=6957884; DOI=10.1073/pnas.79.18.5661;
RA Woods D.E., Markham A.F., Ricker A.T., Goldberger G., Colten H.R.;
RT "Isolation of cDNA clones for the human complement protein factor B, a
RT class III major histocompatibility complex gene product.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:5661-5665(1982).
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-259.
RX PubMed=6323161;
RA Morley B.J., Campbell R.D.;
RT "Internal homologies of the Ba fragment from human complement
RT component Factor B, a class III MHC antigen.";
RL EMBO J. 3:153-157(1984).
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99.
RC TISSUE=Blood;
RX PubMed=3643061; DOI=10.1016/0092-8674(87)90436-3;
RA Wu L.C., Morley B.J., Campbell R.D.;
RT "Cell-specific expression of the human complement protein factor B
RT gene: evidence for the role of two distinct 5'-flanking elements.";
RL Cell 48:331-342(1987).
RN [16]
RP GLYCATION AT LYS-291.
RX PubMed=2006911;
RA Niemann M.A., Bhown A.S., Miller E.J.;
RT "The principal site of glycation of human complement factor B.";
RL Biochem. J. 274:473-480(1991).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-122; ASN-285 AND ASN-378,
RP AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-122 AND ASN-285, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 467-764.
RX PubMed=10637221; DOI=10.1093/emboj/19.2.164;
RA Jing H., Xu Y., Carson M., Moore D., Macon K.J., Volanakis J.E.,
RA Narayana S.V.L.;
RT "New structural motifs on the chymotrypsin fold and their potential
RT roles in complement factor B.";
RL EMBO J. 19:164-173(2000).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 26-764 IN COMPLEX WITH COBRA
RP VENOM FACTOR, GLYCOSYLATION AT ASN-142 AND ASN-378, AND DISULFIDE
RP BONDS.
RX PubMed=19574954; DOI=10.1038/emboj.2009.184;
RA Janssen B.J., Gomes L., Koning R.I., Svergun D.I., Koster A.J.,
RA Fritzinger D.C., Vogel C.-W., Gros P.;
RT "Insights into complement convertase formation based on the structure
RT of the factor B-cobra venom factor complex.";
RL EMBO J. 28:2469-2478(2009).
RN [21]
RP VARIANTS HIS-9 AND GLN-32, AND INVOLVEMENT IN REDUCED RISK OF ARMD.
RX PubMed=16518403; DOI=10.1038/ng1750;
RA Gold B., Merriam J.E., Zernant J., Hancox L.S., Taiber A.J., Gehrs K.,
RA Cramer K., Neel J., Bergeron J., Barile G.R., Smith R.T.,
RA Hageman G.S., Dean M., Allikmets R.;
RT "Variation in factor B (BF) and complement component 2 (C2) genes is
RT associated with age-related macular degeneration.";
RL Nat. Genet. 38:458-462(2006).
RN [22]
RP VARIANTS AHUS4 LEU-286 AND GLU-323, AND CHARACTERIZATION OF VARIANTS
RP AHUS4 LEU-286 AND GLU-323.
RX PubMed=17182750; DOI=10.1073/pnas.0603420103;
RA Goicoechea de Jorge E., Harris C.L., Esparza-Gordillo J., Carreras L.,
RA Arranz E.A., Garrido C.A., Lopez-Trascasa M., Sanchez-Corral P.,
RA Morgan B.P., Rodriguez de Cordoba S.;
RT "Gain-of-function mutations in complement factor B are associated with
RT atypical hemolytic uremic syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:240-245(2007).
RN [23]
RP VARIANTS AHUS4 PRO-166; GLN-203; LEU-242; GLN-323; ILE-458 AND
RP ARG-533.
RX PubMed=20513133; DOI=10.1002/humu.21256;
RA Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.;
RT "Mutations in alternative pathway complement proteins in American
RT patients with atypical hemolytic uremic syndrome.";
RL Hum. Mutat. 31:E1445-E1460(2010).
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
CC Bb. Bb, a serine protease, then combines with complement factor 3b
CC to generate the C3 or C5 convertase. It has also been implicated
CC in proliferation and differentiation of preactivated B-
CC lymphocytes, rapid spreading of peripheral blood monocytes,
CC stimulation of lymphocyte blastogenesis and lysis of erythrocytes.
CC Ba inhibits the proliferation of preactivated B-lymphocytes.
CC -!- CATALYTIC ACTIVITY: Cleavage of Arg-|-Ser bond in complement
CC component C3 alpha-chain to yield C3a and C3b, and Arg-|-Xaa bond
CC in complement component C5 alpha-chain to yield C5a and C5b.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P00751-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P00751-2; Sequence=VSP_005380, VSP_005381;
CC -!- POLYMORPHISM: Two major variants, F and S, and 2 minor variants,
CC as well as at least 14 very rare variants, have been identified.
CC The variants His-9 and Gln-32 are associated with a reduced risk
CC of age-related macular degeneration (ARMD) [MIM:603075]. ARMD is a
CC multifactorial eye disease and the most common cause of
CC irreversible vision loss in the developed world.
CC -!- DISEASE: Hemolytic uremic syndrome atypical 4 (AHUS4)
CC [MIM:612924]: An atypical form of hemolytic uremic syndrome. It is
CC a complex genetic disease characterized by microangiopathic
CC hemolytic anemia, thrombocytopenia, renal failure and absence of
CC episodes of enterocolitis and diarrhea. In contrast to typical
CC hemolytic uremic syndrome, atypical forms have a poorer prognosis,
CC with higher death rates and frequent progression to end-stage
CC renal disease. Note=Disease susceptibility is associated with
CC variations affecting the gene represented in this entry.
CC Susceptibility to the development of atypical hemolytic uremic
CC syndrome can be conferred by mutations in various components of or
CC regulatory factors in the complement cascade system. Other genes
CC may play a role in modifying the phenotype.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC -!- SIMILARITY: Contains 3 Sushi (CCP/SCR) domains.
CC -!- SIMILARITY: Contains 1 VWFA domain.
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/CFB";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/bf/";
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DR EMBL; X72875; CAA51389.1; -; mRNA.
DR EMBL; S67310; AAD13989.1; -; mRNA.
DR EMBL; L15702; AAA16820.1; -; mRNA.
DR EMBL; X00284; CAA25077.1; -; mRNA.
DR EMBL; AF349679; AAK30167.1; -; mRNA.
DR EMBL; AF019413; AAB67977.1; -; Genomic_DNA.
DR EMBL; AF551848; AAN71991.1; -; Genomic_DNA.
DR EMBL; AL844853; CAI41860.1; -; Genomic_DNA.
DR EMBL; AL662849; CAI17456.1; -; Genomic_DNA.
DR EMBL; BX005143; CAM25864.1; -; Genomic_DNA.
DR EMBL; CR759782; CAQ07113.1; -; Genomic_DNA.
DR EMBL; CR388219; CAQ07483.1; -; Genomic_DNA.
DR EMBL; AL645922; CAQ09274.1; -; Genomic_DNA.
DR EMBL; BC004143; AAH04143.1; -; mRNA.
DR EMBL; BC007990; AAH07990.1; -; mRNA.
DR EMBL; K01566; AAA36225.2; -; mRNA.
DR EMBL; J00125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; J00126; AAA36226.1; -; mRNA.
DR EMBL; J00185; AAA36219.1; ALT_SEQ; mRNA.
DR EMBL; J00186; AAA36220.1; -; mRNA.
DR EMBL; M15082; AAA59625.1; -; Genomic_DNA.
DR IPI; IPI00218508; -.
DR IPI; IPI00921523; -.
DR PIR; S34075; BBHU.
DR RefSeq; NP_001701.2; NM_001710.5.
DR UniGene; Hs.69771; -.
DR PDB; 1DLE; X-ray; 2.10 A; A/B=470-764.
DR PDB; 1Q0P; X-ray; 1.80 A; A=254-476.
DR PDB; 1RRK; X-ray; 2.00 A; A=268-764.
DR PDB; 1RS0; X-ray; 2.60 A; A=268-764.
DR PDB; 1RTK; X-ray; 2.30 A; A=268-764.
DR PDB; 2OK5; X-ray; 2.30 A; A=26-764.
DR PDB; 2WIN; X-ray; 3.90 A; I/J/K/L=260-764.
DR PDB; 2XWB; X-ray; 3.49 A; F/H=35-764.
DR PDB; 2XWJ; X-ray; 4.00 A; I/J/K/L=26-764.
DR PDB; 3HRZ; X-ray; 2.20 A; D=26-764.
DR PDB; 3HS0; X-ray; 3.00 A; D/I=26-764.
DR PDBsum; 1DLE; -.
DR PDBsum; 1Q0P; -.
DR PDBsum; 1RRK; -.
DR PDBsum; 1RS0; -.
DR PDBsum; 1RTK; -.
DR PDBsum; 2OK5; -.
DR PDBsum; 2WIN; -.
DR PDBsum; 2XWB; -.
DR PDBsum; 2XWJ; -.
DR PDBsum; 3HRZ; -.
DR PDBsum; 3HS0; -.
DR ProteinModelPortal; P00751; -.
DR DIP; DIP-38319N; -.
DR IntAct; P00751; 3.
DR STRING; 9606.ENSP00000388516; -.
DR MEROPS; S01.196; -.
DR PhosphoSite; P00751; -.
DR DMDM; 584908; -.
DR DOSAC-COBS-2DPAGE; P00751; -.
DR REPRODUCTION-2DPAGE; P00751; -.
DR SWISS-2DPAGE; P00751; -.
DR PaxDb; P00751; -.
DR PeptideAtlas; P00751; -.
DR PRIDE; P00751; -.
DR DNASU; 629; -.
DR Ensembl; ENST00000399981; ENSP00000382862; ENSG00000241253.
DR Ensembl; ENST00000417261; ENSP00000414889; ENSG00000239754.
DR Ensembl; ENST00000419411; ENSP00000391902; ENSG00000242335.
DR Ensembl; ENST00000419920; ENSP00000411474; ENSG00000241253.
DR Ensembl; ENST00000424727; ENSP00000401719; ENSG00000243570.
DR Ensembl; ENST00000425368; ENSP00000416561; ENSG00000243649.
DR Ensembl; ENST00000426239; ENSP00000413351; ENSG00000242335.
DR Ensembl; ENST00000427888; ENSP00000411515; ENSG00000239754.
DR Ensembl; ENST00000433503; ENSP00000388352; ENSG00000241534.
DR Ensembl; ENST00000436692; ENSP00000389604; ENSG00000243570.
DR Ensembl; ENST00000455591; ENSP00000414341; ENSG00000241534.
DR GeneID; 629; -.
DR KEGG; hsa:629; -.
DR UCSC; uc003nyi.2; human.
DR UCSC; uc003nyj.4; human.
DR CTD; 629; -.
DR GeneCards; GC06P031917; -.
DR H-InvDB; HIX0038706; -.
DR HGNC; HGNC:1037; CFB.
DR HPA; CAB016381; -.
DR HPA; HPA001817; -.
DR HPA; HPA001832; -.
DR MIM; 138470; gene.
DR MIM; 603075; phenotype.
DR MIM; 612924; phenotype.
DR neXtProt; NX_P00751; -.
DR Orphanet; 279; Age-related macular degeneration.
DR Orphanet; 93578; Atypical hemolytic uremic syndrome with B factor anomaly.
DR PharmGKB; PA25341; -.
DR eggNOG; NOG304026; -.
DR HOVERGEN; HBG002567; -.
DR InParanoid; P00751; -.
DR KO; K01335; -.
DR OrthoDB; EOG4DV5KF; -.
DR PhylomeDB; P00751; -.
DR BRENDA; 3.4.21.47; 2681.
DR Reactome; REACT_6900; Immune System.
DR BindingDB; P00751; -.
DR ChEMBL; CHEMBL5731; -.
DR ChiTaRS; CFB; human.
DR EvolutionaryTrace; P00751; -.
DR GenomeRNAi; 629; -.
DR NextBio; 2546; -.
DR ArrayExpress; P00751; -.
DR Bgee; P00751; -.
DR CleanEx; HS_CFB; -.
DR Genevestigator; P00751; -.
DR GermOnline; ENSG00000204359; Homo sapiens.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0001848; F:complement binding; TAS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
DR GO; GO:0006957; P:complement activation, alternative pathway; NAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
DR InterPro; IPR011360; Compl_C2_B.
DR InterPro; IPR001254; Peptidase_S1.
DR InterPro; IPR018114; Peptidase_S1_AS.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR000436; Sushi_SCR_CCP.
DR InterPro; IPR009003; Trypsin-like_Pept_dom.
DR InterPro; IPR002035; VWF_A.
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 SMART; SM00032; CCP; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF57535; Complement_control_module; 3.
DR SUPFAM; SSF50494; Pept_Ser_Cys; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing;
KW Cleavage on pair of basic residues; Complement alternate pathway;
KW Complete proteome; Direct protein sequencing; Disease mutation;
KW Disulfide bond; Glycation; Glycoprotein; Hemolytic uremic syndrome;
KW Hydrolase; Immunity; Innate immunity; Polymorphism; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal; Sushi;
KW Zymogen.
FT SIGNAL 1 25
FT CHAIN 26 764 Complement factor B.
FT /FTId=PRO_0000027545.
FT CHAIN 26 259 Complement factor B Ba fragment.
FT /FTId=PRO_0000027546.
FT CHAIN 260 764 Complement factor B Bb fragment.
FT /FTId=PRO_0000027547.
FT DOMAIN 35 100 Sushi 1.
FT DOMAIN 101 160 Sushi 2.
FT DOMAIN 163 220 Sushi 3.
FT DOMAIN 270 469 VWFA.
FT DOMAIN 477 757 Peptidase S1.
FT ACT_SITE 526 526 Charge relay system.
FT ACT_SITE 576 576 Charge relay system.
FT ACT_SITE 699 699 Charge relay system.
FT CARBOHYD 122 122 N-linked (GlcNAc...).
FT CARBOHYD 142 142 N-linked (GlcNAc...).
FT CARBOHYD 285 285 N-linked (GlcNAc...).
FT CARBOHYD 291 291 N-linked (Glc) (glycation).
FT CARBOHYD 378 378 N-linked (GlcNAc...).
FT DISULFID 37 76
FT DISULFID 62 98
FT DISULFID 103 145
FT DISULFID 131 158
FT DISULFID 165 205
FT DISULFID 191 218
FT DISULFID 478 596
FT DISULFID 511 527
FT DISULFID 599 615
FT DISULFID 656 682
FT DISULFID 695 725
FT VAR_SEQ 543 621 GEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLK
FT NKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEE ->
FT KDATEGPGLHLCSPGNTSHFLQILHSTHPQCSPIPCTPDQS
FT GMGEDVKLGMTRGQRQEAAHKEVVPTLLLQEGRSGTWR
FT (in isoform 2).
FT /FTId=VSP_005380.
FT VAR_SEQ 622 764 Missing (in isoform 2).
FT /FTId=VSP_005381.
FT VARIANT 9 9 L -> H (in dbSNP:rs4151667).
FT /FTId=VAR_016274.
FT VARIANT 28 28 W -> Q (in allele FA; requires 2
FT nucleotide substitutions).
FT /FTId=VAR_006493.
FT VARIANT 28 28 W -> R (in allele S).
FT /FTId=VAR_006492.
FT VARIANT 32 32 R -> Q (in allele S; dbSNP:rs641153).
FT /FTId=VAR_006494.
FT VARIANT 32 32 R -> W (in dbSNP:rs12614).
FT /FTId=VAR_016275.
FT VARIANT 166 166 S -> P (in AHUS4).
FT /FTId=VAR_063659.
FT VARIANT 203 203 R -> Q (in AHUS4).
FT /FTId=VAR_063660.
FT VARIANT 242 242 I -> L (in AHUS4).
FT /FTId=VAR_063661.
FT VARIANT 252 252 G -> S (in dbSNP:rs4151651).
FT /FTId=VAR_016276.
FT VARIANT 286 286 F -> L (in AHUS4; gain-of-function
FT mutation that results in enhanced
FT formation of the C3bBb).
FT /FTId=VAR_063221.
FT VARIANT 323 323 K -> E (in AHUS4; gain-of-function
FT mutation that results in enhanced
FT formation of the C3bBb).
FT /FTId=VAR_063222.
FT VARIANT 323 323 K -> Q (in AHUS4).
FT /FTId=VAR_063662.
FT VARIANT 458 458 M -> I (in AHUS4).
FT /FTId=VAR_063663.
FT VARIANT 533 533 K -> R (in AHUS4).
FT /FTId=VAR_063664.
FT VARIANT 565 565 K -> E (in dbSNP:rs4151659).
FT /FTId=VAR_016277.
FT VARIANT 651 651 D -> E (in dbSNP:rs4151660).
FT /FTId=VAR_016278.
FT VARIANT 736 736 A -> S (in allele FA).
FT /FTId=VAR_006495.
FT CONFLICT 297 297 I -> T (in Ref. 11; AA sequence).
FT CONFLICT 300 300 V -> L (in Ref. 10; AAA36225).
FT CONFLICT 328 328 D -> V (in Ref. 10; AAA36225).
FT CONFLICT 356 357 KK -> EE (in Ref. 10; AAA36225).
FT CONFLICT 537 537 I -> T (in Ref. 13; AAA36219).
FT CONFLICT 764 764 L -> H (in Ref. 13; AAA36220).
FT STRAND 47 51
FT HELIX 53 55
FT STRAND 56 61
FT STRAND 66 70
FT STRAND 72 76
FT STRAND 80 82
FT STRAND 88 90
FT STRAND 92 94
FT STRAND 97 100
FT STRAND 112 115
FT STRAND 119 122
FT STRAND 126 131
FT STRAND 136 139
FT STRAND 141 145
FT STRAND 151 153
FT STRAND 157 159
FT STRAND 163 165
FT STRAND 174 177
FT STRAND 186 191
FT STRAND 195 199
FT STRAND 201 205
FT STRAND 209 213
FT STRAND 217 219
FT HELIX 227 238
FT HELIX 240 243
FT STRAND 269 276
FT TURN 279 281
FT HELIX 283 301
FT TURN 302 304
FT STRAND 308 322
FT STRAND 324 326
FT HELIX 327 330
FT HELIX 332 340
FT HELIX 344 346
FT STRAND 348 350
FT HELIX 355 366
FT STRAND 369 372
FT HELIX 377 379
FT STRAND 381 388
FT STRAND 394 396
FT HELIX 399 408
FT STRAND 412 414
FT HELIX 420 422
FT STRAND 423 429
FT STRAND 431 433
FT HELIX 436 442
FT STRAND 452 454
FT STRAND 455 457
FT HELIX 458 468
FT HELIX 471 474
FT HELIX 489 492
FT STRAND 496 501
FT TURN 504 506
FT STRAND 509 515
FT STRAND 517 523
FT HELIX 525 527
FT HELIX 534 536
FT STRAND 537 541
FT STRAND 548 555
FT TURN 561 564
FT HELIX 565 567
FT STRAND 578 584
FT STRAND 598 600
FT HELIX 601 606
FT HELIX 615 622
FT STRAND 625 638
FT STRAND 640 648
FT HELIX 653 658
FT HELIX 659 662
FT HELIX 666 668
FT HELIX 672 674
FT STRAND 680 689
FT HELIX 696 698
FT STRAND 702 707
FT STRAND 710 721
FT HELIX 725 727
FT TURN 728 730
FT HELIX 735 737
FT STRAND 739 744
FT HELIX 745 748
FT HELIX 749 755
FT TURN 756 758
SQ SEQUENCE 764 AA; 85533 MW; 8BB6C101CC6AC200 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 WVKVSEADSS NADWVTKQLN EINYEDHKLK SGTNTKKALQ
AVYSMMSWPD DVPPEGWNRT RHVIILMTDG LHNMGGDPIT VIDEIRDLLY IGKDRKNPRE
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
//
