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UniProtKB/Swiss-Prot entry P00751


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CFAB_HUMAN
Primary accession number P00751
Secondary accession numbers O15006 Q29944 Q5ST50 Q96HX6 Q9BTF5 Q9BX92
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on October 1, 1994 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 131)
Name and origin of the protein
Protein name Complement factor B [Precursor]
Synonyms EC 3.4.21.47
C3/C5 convertase
Properdin factor B
Glycine-rich beta glycoprotein
GBG
PBF2
Contains Complement factor B Ba fragment
Complement factor B Bb fragment
Gene name
Name: CFB
Synonyms: BF, BFD
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28; GLN-28; GLN-32 AND SER-736.
DOI=10.1007/BF00211644; PubMed=2249879 [NCBI, ExPASy, EBI, Israel, Japan]
Davrinche C., Abbal M., Clerc A.;
"Molecular characterization of human complement factor B subtypes.";
Immunogenetics 32:309-312(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28 AND GLN-32.
TISSUE=Liver;
DOI=10.1016/0198-8859(94)90100-7; PubMed=8181962 [NCBI, ExPASy, EBI, Israel, Japan]
Mejia J.E., Jahn I., de la Salle H., Hauptmann G.;
"Human factor B. Complete cDNA sequence of the BF*S allele.";
Hum. Immunol. 39:49-53(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28 AND GLN-32.
TISSUE=Liver;
PubMed=8225386 [NCBI, ExPASy, EBI, Israel, Japan]
Schwaeble W., Luettig B., Sokolowski T., Estaller C., Weiss E.H., Meyer Zum Bueschenfelde K.-H., Whaley K., Dippold W.;
"Human complement factor B: functional properties of a recombinant zymogen of the alternative activation pathway convertase.";
Immunobiology 188:221-232(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28 AND GLN-32.
DOI=10.1016/0161-5890(93)90450-P; PubMed=8247029 [NCBI, ExPASy, EBI, Israel, Japan]
Horiuchi T., Kim S., Matsumoto M., Watanabe I., Fujita S., Volanakis J.E.;
"Human complement factor B: cDNA cloning, nucleotide sequencing, phenotypic conversion by site-directed mutagenesis and expression.";
Mol. Immunol. 30:1587-1592(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Jaatinen T., Kanerva J., Poutanen K.E., Saarinen-Pihkala U., Lokki M.-L.;
"Expression and alternative splicing of human factor B gene in leukemic mononuclear cells.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1101/gr.1736803; PubMed=14656967 [NCBI, ExPASy, EBI, Israel, Japan]
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-9; GLN-32; TRP-32; SER-252; GLU-565 AND GLU-651.
SeattleSNPs program for genomic applications;
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TRP-32.
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 26-764, PARTIAL NUCLEOTIDE SEQUENCE [MRNA], AND GLYCOSYLATION AT ASN-122; ASN-142; ASN-285 AND ASN-378.
PubMed=6546754 [NCBI, ExPASy, EBI, Israel, Japan]
Mole J.E., Anderson J.K., Davison E.A., Woods D.E.;
"Complete primary structure for the zymogen of human complement factor B.";
J. Biol. Chem. 259:3407-3412(1984).
[11]
PROTEIN SEQUENCE OF 260-764.
PubMed=6342610 [NCBI, ExPASy, EBI, Israel, Japan]
Christie D.L., Gagnon J.;
"Amino acid sequence of the Bb fragment from complement Factor B. Sequence of the major cyanogen bromide-cleavage peptide (CB-II) and completion of the sequence of the Bb fragment.";
Biochem. J. 209:61-70(1983).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 339-764.
PubMed=6308626 [NCBI, ExPASy, EBI, Israel, Japan]
Campbell R.D., Porter R.R.;
"Molecular cloning and characterization of the gene coding for human complement protein factor B.";
Proc. Natl. Acad. Sci. U.S.A. 80:4464-4468(1983).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 467-595 AND 752-764.
PubMed=6957884 [NCBI, ExPASy, EBI, Israel, Japan]
Woods D.E., Markham A.F., Ricker A.T., Goldberger G., Colten H.R.;
"Isolation of cDNA clones for the human complement protein factor B, a class III major histocompatibility complex gene product.";
Proc. Natl. Acad. Sci. U.S.A. 79:5661-5665(1982).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 16-259.
PubMed=6323161 [NCBI, ExPASy, EBI, Israel, Japan]
Morley B.J., Campbell R.D.;
"Internal homologies of the Ba fragment from human complement component Factor B, a class III MHC antigen.";
EMBO J. 3:153-157(1984).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99.
TISSUE=Blood;
DOI=10.1016/0092-8674(87)90436-3; PubMed=3643061 [NCBI, ExPASy, EBI, Israel, Japan]
Wu L.C., Morley B.J., Campbell R.D.;
"Cell-specific expression of the human complement protein factor B gene: evidence for the role of two distinct 5'-flanking elements.";
Cell 48:331-342(1987).
[16]
GLYCATION AT LYS-291.
PubMed=2006911 [NCBI, ExPASy, EBI, Israel, Japan]
Niemann M.A., Bhown A.S., Miller E.J.;
"The principal site of glycation of human complement factor B.";
Biochem. J. 274:473-480(1991).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-122; ASN-285 AND ASN-378, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[18]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 467-764.
DOI=10.1093/emboj/19.2.164; PubMed=10637221 [NCBI, ExPASy, EBI, Israel, Japan]
Jing H., Xu Y., Carson M., Moore D., Macon K.J., Volanakis J.E., Narayana S.V.L.;
"New structural motifs on the chymotrypsin fold and their potential roles in complement factor B.";
EMBO J. 19:164-173(2000).
[19]
VARIANTS HIS-9 AND GLN-32, AND INVOLVEMENT IN REDUCED RISK OF ARMD.
DOI=10.1038/ng1750; PubMed=16518403 [NCBI, ExPASy, EBI, Israel, Japan]
Gold B., Merriam J.E., Zernant J., Hancox L.S., Taiber A.J., Gehrs K., Cramer K., Neel J., Bergeron J., Barile G.R., Smith R.T., Hageman G.S., Dean M., Allikmets R.;
"Variation in factor B (BF) and complement component 2 (C2) genes is associated with age-related macular degeneration.";
Nat. Genet. 38:458-462(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X72875; CAA51389.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S67310; AAD13989.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L15702; AAA16820.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00284; CAA25077.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF349679; AAK30167.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF019413; AAB67977.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF551848; AAN71991.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL662849; CAI17456.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL645922; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BX005143; CAM25864.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004143; AAH04143.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007990; AAH07990.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K01566; AAA36225.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J00125; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
J00126; AAA36226.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J00185; AAA36219.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J00186; AAA36220.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M15082; AAA59625.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S34075; BBHU.
RefSeq NP_001701.2; -.
UniGene Hs.69771
3D structure databases
PDB
1DLE; X-ray; 2.10 A; A/B=470-764.[ExPASy / RCSB / EBI]
1Q0P; X-ray; 1.80 A; A=254-476.[ExPASy / RCSB / EBI]
1RRK; X-ray; 2.00 A; A=268-764.[ExPASy / RCSB / EBI]
1RS0; X-ray; 2.60 A; A=268-764.[ExPASy / RCSB / EBI]
1RTK; X-ray; 2.30 A; A=268-764.[ExPASy / RCSB / EBI]
2OK5; X-ray; 2.30 A; A=25-764.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DLE; -.
1Q0P; -.
1RRK; -.
1RS0; -.
1RTK; -.
2OK5; -.
SMR P00751; 34-764.
ModBase P00751.
Protein family/group databases
MEROPS S01.196; -.
Enzyme and pathway databases
Reactome REACT_6900; Signaling in Immune System.
2D gel databases
SWISS-2DPAGE P00751; -.
DOSAC-COBS-2DPAGE P00751; -.
REPRODUCTION-2DPAGE P00751; -.
Siena-2DPAGE P00751; -.
Organism-specific databases
H-InvDB HIX0005740; -.
HIX0038706; -.
HIX0057938; -.
HIX0058144; -.
HIX0067201; -.
HGNC HGNC:1037; CFB.
GenAtlas CFB.
HPA CAB016381; -.
HPA000951; -.
HPA000952; -.
HPA001817; -.
HPA001832; -.
MIM 138470; gene. [NCBI / EBI]
603075; phenotype. [NCBI / EBI]
Orphanet 90038; Haemolytic-uremic syndrome, typical.
GeneCards P00751.
Gene expression databases
CleanEx HS_CFB; -.
GermOnline ENSG00000204359; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from experiment from Reactome).
GO:0005886; Cellular component: plasma membrane (inferred from experiment from Reactome).
GO:0003812; Molecular function: alternative-complement-pathway C3/C5 convertase activity (inferred from experiment from Reactome).
GO:0001848; Molecular function: complement binding (traceable author statement from UniProtKB).
GO:0006957; Biological process: complement activation, alternative pathway (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR011360; Compl_C2_B.
IPR016060; Complement_control_module.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
IPR000436; Sushi_SCR_CCP.
IPR002035; VWF_A.
Graphical view of domain structure.
Gene3D G3DSA:2.10.70.10; Complement_control_module; 2.
Pfam PF00084; Sushi; 2.
PF00089; Trypsin; 1.
PF00092; VWA; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001154; Compl_C2_B; 1.
PRINTS PR00722; CHYMOTRYPSIN.
PR00453; VWFADOMAIN.
SMART SM00032; CCP; 3.
SM00020; Tryp_SPc; 1.
SM00327; VWA; 1.
SMART graphical view of domain structure.
PROSITE PS50923; SUSHI; 3.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PS50234; VWFA; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00751.
ProtoNet P00751.
Proteomic databases
PeptideAtlas P00751; -.
Genome annotation databases
Ensembl ENSG00000166285; Homo sapiens. [Contig view]
ENSG00000204359; Homo sapiens. [Contig view]
GeneID 629; -.
KEGG hsa:629; -.
Phylogenomic databases
HOVERGEN P00751; -.
Other
NextBio 2546; -.
SOURCE CFB; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cleavage on pair of basic residues; Complement alternate pathway; Direct protein sequencing; Glycation; Glycoprotein; Hydrolase; Immune response; Innate immunity; Polymorphism; Protease; Repeat; Secreted; Serine protease; Signal; Sushi; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    25  25      
CHAIN   26   764  739     Complement factor B. PRO_0000027545
CHAIN   26   259  234     Complement factor B Ba fragment. PRO_0000027546
CHAIN   260   764  505     Complement factor B Bb fragment. PRO_0000027547
DOMAIN   35   100  66     Sushi 1. 
DOMAIN   101   160  60     Sushi 2. 
DOMAIN   163   220  58     Sushi 3. 
DOMAIN   270   469  200     VWFA. 
DOMAIN   477   757  281     Peptidase S1. 
ACT_SITE   526   526        Charge relay system. 
ACT_SITE   576   576        Charge relay system. 
ACT_SITE   699   699        Charge relay system. 
CARBOHYD   122   122        N-linked (GlcNAc...). 
CARBOHYD   142   142        N-linked (GlcNAc...). 
CARBOHYD   285   285        N-linked (GlcNAc...). 
CARBOHYD   291   291        N-linked (Glc) (glycation). 
CARBOHYD   378   378        N-linked (GlcNAc...). 
DISULFID   37    76        By similarity. 
DISULFID   62    98        By similarity. 
DISULFID   103   145        By similarity. 
DISULFID   131   158        By similarity. 
DISULFID   165   205        By similarity. 
DISULFID   191   218        By similarity. 
DISULFID   478   596         
DISULFID   511   527         
DISULFID   599   615         
DISULFID   656   682         
DISULFID   695   725         
VAR_SEQ   543   621        GEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKL KNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEE -> KDATEGPGLHLCSPGNTSHFLQILHSTHPQCSPIPCTPDQ SGMGEDVKLGMTRGQRQEAAHKEVVPTLLLQEGRSGTWR (in isoform 2). VSP_005380
VAR_SEQ   622   764        Missing (in isoform 2). VSP_005381
VARIANT   9     9  1     L -> H. VAR_016274 
VARIANT   28    28  1     W -> Q (in allele FA; requires 2 nucleotide substitutions). VAR_006493 
VARIANT   28    28  1     W -> R (in allele S). VAR_006492 
VARIANT   32    32  1     R -> Q (in allele S). VAR_006494 
VARIANT   32    32  1     R -> W. VAR_016275 
VARIANT   252   252  1     G -> S. VAR_016276 [3D]
VARIANT   565   565  1     K -> E. VAR_016277 [3D]
VARIANT   651   651  1     D -> E. VAR_016278 [3D]
VARIANT   736   736  1     A -> S (in allele FA). VAR_006495 [3D]
CONFLICT   297   297        I -> T (in Ref. 11; AA sequence). 
CONFLICT   300   300        V -> L (in Ref. 10; AAA36225). 
CONFLICT   328   328        D -> V (in Ref. 10; AAA36225). 
CONFLICT   356   357        KK -> EE (in Ref. 10; AAA36225). 
CONFLICT   537   537        I -> T (in Ref. 13; AAA36219). 
CONFLICT   764   764        L -> H (in Ref. 13). 
STRAND   269   276  8      
TURN   279   281  3      
HELIX   283   301  19      
TURN   302   304  3      
STRAND   308   322  15      
HELIX   327   330  4      
HELIX   332   340  9      
HELIX   355   366  12      
HELIX   377   379  3      
STRAND   381   388  8      
STRAND   394   396  3      
HELIX   399   408  10