GenomeNet

Database: UniProt
Entry: P00751
LinkDB: P00751
Original site: P00751 
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   19-MAR-2014, entry version 190.
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.
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.
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/books/NBK1116/?term=CFB[genesymbol]";
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   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   SMR; P00751; 35-764.
DR   BioGrid; 107098; 6.
DR   DIP; DIP-38319N; -.
DR   IntAct; P00751; 4.
DR   MINT; MINT-3003542; -.
DR   STRING; 9606.ENSP00000388516; -.
DR   BindingDB; P00751; -.
DR   ChEMBL; CHEMBL5731; -.
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. [P00751-1]
DR   Ensembl; ENST00000419411; ENSP00000391902; ENSG00000242335. [P00751-1]
DR   Ensembl; ENST00000419920; ENSP00000411474; ENSG00000241253.
DR   Ensembl; ENST00000424727; ENSP00000401719; ENSG00000243570. [P00751-1]
DR   Ensembl; ENST00000425368; ENSP00000416561; ENSG00000243649. [P00751-1]
DR   Ensembl; ENST00000426239; ENSP00000413351; ENSG00000242335. [P00751-1]
DR   Ensembl; ENST00000427888; ENSP00000411515; ENSG00000239754. [P00751-1]
DR   Ensembl; ENST00000433503; ENSP00000388352; ENSG00000241534. [P00751-1]
DR   Ensembl; ENST00000436692; ENSP00000389604; ENSG00000243570. [P00751-1]
DR   Ensembl; ENST00000455591; ENSP00000414341; ENSG00000241534. [P00751-1]
DR   GeneID; 629; -.
DR   KEGG; hsa:629; -.
DR   UCSC; uc003nyi.2; human. [P00751-2]
DR   UCSC; uc003nyj.4; human. [P00751-1]
DR   CTD; 629; -.
DR   GeneCards; GC06P031917; -.
DR   GeneCards; GC06Pj31900; -.
DR   GeneCards; GC06Pk31895; -.
DR   GeneCards; GC06Pm31989; -.
DR   GeneCards; GC06Pn31885; -.
DR   GeneCards; GC06Po31905; -.
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   PhylomeDB; P00751; -.
DR   TreeFam; TF330194; -.
DR   BRENDA; 3.4.21.47; 2681.
DR   Reactome; REACT_6900; Immune System.
DR   ChiTaRS; CFB; human.
DR   EvolutionaryTrace; P00751; -.
DR   GeneWiki; Complement_factor_B; -.
DR   GenomeRNAi; 629; -.
DR   NextBio; 2546; -.
DR   PRO; PR:P00751; -.
DR   ArrayExpress; P00751; -.
DR   Bgee; P00751; -.
DR   CleanEx; HS_CFB; -.
DR   Genevestigator; P00751; -.
DR   GO; GO:0072562; C:blood microparticle; IDA:UniProt.
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   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR011360; Compl_C2_B.
DR   InterPro; IPR028341; Complement_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   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; 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   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       78     81
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       461    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       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
//
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