CFAB_HUMAN
ID CFAB_HUMAN Reviewed; 764 AA.
AC P00751; B0QZQ6; O15006; Q29944; Q53F89; Q5JP67; Q5ST50; Q96HX6; Q9BTF5;
AC Q9BX92;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 254.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28; GLN-28; GLN-32
RP 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 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 GLN-32.
RC TISSUE=Liver;
RX PubMed=8225386; DOI=10.1016/s0171-2985(11)80231-7;
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 zymogen
RT 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 GLN-32.
RX PubMed=8247029; DOI=10.1016/0161-5890(93)90450-p;
RA Horiuchi T., Kim S., Matsumoto M., Watanabe I., Fujita S., Volanakis J.E.;
RT "Human complement factor B: cDNA cloning, nucleotide sequencing, phenotypic
RT 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., Lokki M.-L.;
RT "Expression and alternative splicing of human factor B gene in leukemic
RT 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., 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 [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 MRNA] (ISOFORM 1), AND VARIANT TRP-32.
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TRP-32.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
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; DOI=10.1016/s0021-9258(17)43108-5;
RA Mole J.E., Anderson J.K., Davison E.A., Woods D.E.;
RT "Complete primary structure for the zymogen of human complement factor B.";
RL J. Biol. Chem. 259:3407-3412(1984).
RN [13]
RP PROTEIN SEQUENCE OF 260-764.
RX PubMed=6342610; DOI=10.1042/bj2090061;
RA Christie D.L., Gagnon J.;
RT "Amino acid sequence of the Bb fragment from complement Factor B. Sequence
RT of the major cyanogen bromide-cleavage peptide (CB-II) and completion of
RT the sequence of the Bb fragment.";
RL Biochem. J. 209:61-70(1983).
RN [14]
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 [15]
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 [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-259.
RX PubMed=6323161; DOI=10.1002/j.1460-2075.1984.tb01776.x;
RA Morley B.J., Campbell R.D.;
RT "Internal homologies of the Ba fragment from human complement component
RT Factor B, a class III MHC antigen.";
RL EMBO J. 3:153-157(1984).
RN [17]
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 gene:
RT evidence for the role of two distinct 5'-flanking elements.";
RL Cell 48:331-342(1987).
RN [18]
RP GLYCATION AT LYS-291.
RX PubMed=2006911; DOI=10.1042/bj2740473;
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 [19]
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., Moore R.J.,
RA 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 [20]
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 multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [21]
RP INVOLVEMENT IN CFBD.
RX PubMed=24152280; DOI=10.1056/nejmc1306326;
RA Slade C., Bosco J., Unglik G., Bleasel K., Nagel M., Winship I.;
RT "Deficiency in complement factor B.";
RL N. Engl. J. Med. 369:1667-1669(2013).
RN [22]
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 roles
RT in complement factor B.";
RL EMBO J. 19:164-173(2000).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 26-764, DOMAIN ARCHITECTURE, AND
RP GLYCOSYLATION AT ASN-122; ASN-142; ASN-285 AND ASN-378.
RX PubMed=17310251; DOI=10.1038/nsmb1210;
RA Milder F.J., Gomes L., Schouten A., Janssen B.J., Huizinga E.G.,
RA Romijn R.A., Hemrika W., Roos A., Daha M.R., Gros P.;
RT "Factor B structure provides insights into activation of the central
RT protease of the complement system.";
RL Nat. Struct. Mol. Biol. 14:224-228(2007).
RN [24]
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 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 of
RT the factor B-cobra venom factor complex.";
RL EMBO J. 28:2469-2478(2009).
RN [25] {ECO:0007744|PDB:6RUR}
RP X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS) OF 260-764 IN COMPLEX WITH COMPLEMENT
RP C3 BETA CHAIN; CFP AND STAPHYLOCOCCUS AUREUS PROTEIN SCN, AND INTERACTION
RP WITH COMPLEMENT C3 BETA CHAIN.
RX PubMed=28264884; DOI=10.15252/embj.201696173;
RA Pedersen D.V., Roumenina L., Jensen R.K., Gadeberg T.A., Marinozzi C.,
RA Picard C., Rybkine T., Thiel S., Soerensen U.B., Stover C.,
RA Fremeaux-Bacchi V., Andersen G.R.;
RT "Functional and structural insight into properdin control of complement
RT alternative pathway amplification.";
RL EMBO J. 36:1084-1099(2017).
RN [26] {ECO:0007744|PDB:6RUV}
RP X-RAY CRYSTALLOGRAPHY (6.15 ANGSTROMS) OF 260-764 IN COMPLEX WITH
RP COMPLEMENT C3 BETA CHAIN; CFP AND STAPHYLOCOCCUS AUREUS PROTEIN SCN,
RP INTERACTION WITH COMPLEMENT C3 BETA CHAIN AND CFP, AND MUTAGENESIS OF
RP 348-LYS--LYS-350.
RX PubMed=31507604; DOI=10.3389/fimmu.2019.02007;
RA Pedersen D.V., Gadeberg T.A.F., Thomas C., Wang Y., Joram N., Jensen R.K.,
RA Mazarakis S.M.M., Revel M., El Sissy C., Petersen S.V., Lindorff-Larsen K.,
RA Thiel S., Laursen N.S., Fremeaux-Bacchi V., Andersen G.R.;
RT "Structural Basis for Properdin Oligomerization and Convertase Stimulation
RT in the Human Complement System.";
RL Front. Immunol. 10:2007-2007(2019).
RN [27]
RP VARIANTS HIS-9 AND GLN-32, AND INVOLVEMENT IN ARMD14.
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., Hageman G.S.,
RA 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 [28]
RP VARIANTS AHUS4 LEU-286 AND GLU-323, AND CHARACTERIZATION OF VARIANTS AHUS4
RP 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 [29]
RP VARIANTS AHUS4 PRO-166; GLN-203; LEU-242; GLN-323; ILE-458 AND 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 patients
RT 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 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.
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 (PubMed:19574954). 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 (PubMed:28264884, PubMed:31507604).
CC Interacts to C3b; this interaction is dependent on the presence of Mg2+
CC (PubMed:28264884, PubMed:31507604). Interacts to CFP; this interaction
CC contributes to the stabilization of the active C3-convertase enzyme
CC complex (PubMed:31507604). {ECO:0000269|PubMed:19574954,
CC ECO:0000269|PubMed:28264884, ECO:0000269|PubMed:31507604}.
CC -!- INTERACTION:
CC P00751; P01024: C3; NbExp=3; IntAct=EBI-1223668, EBI-905851;
CC P00751; Q92496-1: CFHR4; NbExp=2; IntAct=EBI-1223668, EBI-22033617;
CC P00751; Q92496-3: CFHR4; NbExp=2; IntAct=EBI-1223668, EBI-22033638;
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 -!- 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:0000269|PubMed:17310251}.
CC -!- POLYMORPHISM: Two major variants, F and S, and 2 minor variants, as
CC well as at least 14 very rare variants, have been identified.
CC {ECO:0000269|PubMed:2249879, ECO:0000269|PubMed:8181962}.
CC -!- DISEASE: Macular degeneration, age-related, 14 (ARMD14) [MIM:615489]: A
CC form of age-related macular degeneration, a multifactorial eye disease
CC and the most common cause of irreversible vision loss in the developed
CC world. In most patients, the disease is manifest as ophthalmoscopically
CC visible yellowish accumulations of protein and lipid that lie beneath
CC the retinal pigment epithelium and within an elastin-containing
CC structure known as Bruch membrane. {ECO:0000269|PubMed:16518403}.
CC Note=Disease susceptibility may be associated with variants affecting
CC the gene represented in this entry. Haplotype analyses have identified
CC a statistically significant common risk haplotype and two protective
CC haplotypes. CFB variant His-9 and C2 variant Asp-318, as well as CFB
CC variant Gln-32 and a variant in intron 10 of C2, confer a significantly
CC reduced risk of AMD. {ECO:0000269|PubMed:16518403}.
CC -!- DISEASE: Hemolytic uremic syndrome atypical 4 (AHUS4) [MIM:612924]: An
CC atypical form of hemolytic uremic syndrome. It is a complex genetic
CC disease characterized by microangiopathic hemolytic anemia,
CC thrombocytopenia, renal failure and absence of episodes of
CC enterocolitis and diarrhea. In contrast to typical hemolytic uremic
CC syndrome, atypical forms have a poorer prognosis, with higher death
CC rates and frequent progression to end-stage renal disease.
CC {ECO:0000269|PubMed:17182750, ECO:0000269|PubMed:20513133}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry. Susceptibility to the development of
CC atypical hemolytic uremic syndrome can be conferred by mutations in
CC various components of or regulatory factors in the complement cascade
CC system. Other genes may play a role in modifying the phenotype.
CC -!- DISEASE: Complement factor B deficiency (CFBD) [MIM:615561]: An
CC immunologic disorder characterized by increased susceptibility to
CC bacterial infections, particularly Neisseria infections, due to a
CC defect in the alternative complement pathway.
CC {ECO:0000269|PubMed:24152280}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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; AL662849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX005143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR388219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK223400; BAD97120.1; -; mRNA.
DR EMBL; AL645922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03550.1; -; 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 CCDS; CCDS4729.1; -. [P00751-1]
DR PIR; S34075; BBHU.
DR RefSeq; NP_001701.2; NM_001710.5. [P00751-1]
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 PDB; 6QSW; X-ray; 1.64 A; AAA/BBB/CCC=474-764.
DR PDB; 6QSX; X-ray; 1.77 A; AAA/BBB=474-764.
DR PDB; 6RAV; X-ray; 1.70 A; AAA/BBB=474-764.
DR PDB; 6RUR; X-ray; 6.00 A; J/L=260-764.
DR PDB; 6RUV; X-ray; 6.15 A; J/L=260-764.
DR PDB; 6T8U; X-ray; 2.84 A; AAA/BBB/CCC=474-764.
DR PDB; 6T8V; X-ray; 2.29 A; AAA/BBB=474-764.
DR PDB; 6T8W; X-ray; 1.70 A; AAA/BBB=474-764.
DR PDB; 7JTN; X-ray; 3.10 A; A/C=1-764.
DR PDB; 7JTQ; X-ray; 3.50 A; A/C=1-764.
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 PDBsum; 6QSW; -.
DR PDBsum; 6QSX; -.
DR PDBsum; 6RAV; -.
DR PDBsum; 6RUR; -.
DR PDBsum; 6RUV; -.
DR PDBsum; 6T8U; -.
DR PDBsum; 6T8V; -.
DR PDBsum; 6T8W; -.
DR PDBsum; 7JTN; -.
DR PDBsum; 7JTQ; -.
DR AlphaFoldDB; P00751; -.
DR SMR; P00751; -.
DR BioGRID; 107098; 43.
DR ComplexPortal; CPX-5381; Alternative pathway fluid-phase C3 convertase complex C3(H2O)Bb.
DR ComplexPortal; CPX-5601; Alternative pathway C3 convertase complex C3bBb.
DR DIP; DIP-38319N; -.
DR IntAct; P00751; 17.
DR MINT; P00751; -.
DR STRING; 9606.ENSP00000416561; -.
DR BindingDB; P00751; -.
DR ChEMBL; CHEMBL5731; -.
DR DrugBank; DB02459; 4-guanidinobenzoic acid.
DR DrugBank; DB04491; Diisopropylphosphono Group.
DR DrugBank; DB06503; MLN2222.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR GuidetoPHARMACOLOGY; 2339; -.
DR MEROPS; S01.196; -.
DR CarbonylDB; P00751; -.
DR GlyConnect; 753; 11 N-Linked glycans (4 sites).
DR GlyGen; P00751; 7 sites, 19 N-linked glycans (4 sites), 3 O-linked glycans (3 sites).
DR iPTMnet; P00751; -.
DR PhosphoSitePlus; P00751; -.
DR BioMuta; CFB; -.
DR DMDM; 584908; -.
DR DOSAC-COBS-2DPAGE; P00751; -.
DR REPRODUCTION-2DPAGE; P00751; -.
DR SWISS-2DPAGE; P00751; -.
DR CPTAC; non-CPTAC-1112; -.
DR EPD; P00751; -.
DR jPOST; P00751; -.
DR MassIVE; P00751; -.
DR MaxQB; P00751; -.
DR PaxDb; P00751; -.
DR PeptideAtlas; P00751; -.
DR PRIDE; P00751; -.
DR ProteomicsDB; 51285; -. [P00751-1]
DR ProteomicsDB; 51286; -. [P00751-2]
DR ABCD; P00751; 1 sequenced antibody.
DR Antibodypedia; 35050; 863 antibodies from 38 providers.
DR DNASU; 629; -.
DR Ensembl; ENST00000399981.5; ENSP00000382862.1; ENSG00000241253.8.
DR Ensembl; ENST00000417261.5; ENSP00000414889.1; ENSG00000239754.9. [P00751-1]
DR Ensembl; ENST00000419411.6; ENSP00000391902.2; ENSG00000242335.8. [P00751-1]
DR Ensembl; ENST00000419920.2; ENSP00000411474.2; ENSG00000241253.8.
DR Ensembl; ENST00000424727.5; ENSP00000401719.1; ENSG00000243570.9. [P00751-1]
DR Ensembl; ENST00000425368.7; ENSP00000416561.2; ENSG00000243649.9. [P00751-1]
DR Ensembl; ENST00000426239.1; ENSP00000413351.1; ENSG00000242335.8. [P00751-1]
DR Ensembl; ENST00000427888.2; ENSP00000411515.2; ENSG00000239754.9. [P00751-1]
DR Ensembl; ENST00000433503.2; ENSP00000388352.2; ENSG00000241534.9. [P00751-1]
DR Ensembl; ENST00000436692.2; ENSP00000389604.2; ENSG00000243570.9. [P00751-1]
DR Ensembl; ENST00000455591.5; ENSP00000414341.1; ENSG00000241534.9. [P00751-1]
DR GeneID; 629; -.
DR KEGG; hsa:629; -.
DR MANE-Select; ENST00000425368.7; ENSP00000416561.2; NM_001710.6; NP_001701.2.
DR UCSC; uc003nyj.5; human. [P00751-1]
DR CTD; 629; -.
DR DisGeNET; 629; -.
DR GeneCards; CFB; -.
DR GeneReviews; CFB; -.
DR HGNC; HGNC:1037; CFB.
DR HPA; ENSG00000243649; Tissue enriched (liver).
DR MalaCards; CFB; -.
DR MIM; 138470; gene.
DR MIM; 612924; phenotype.
DR MIM; 615489; phenotype.
DR MIM; 615561; phenotype.
DR neXtProt; NX_P00751; -.
DR OpenTargets; ENSG00000243649; -.
DR Orphanet; 544472; Atypical hemolytic uremic syndrome with complement gene abnormality.
DR Orphanet; 279; NON RARE IN EUROPE: Age-related macular degeneration.
DR PharmGKB; PA25341; -.
DR VEuPathDB; HostDB:ENSG00000243649; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000158605; -.
DR HOGENOM; CLU_022004_1_0_1; -.
DR InParanoid; P00751; -.
DR OMA; QKGHENC; -.
DR PhylomeDB; P00751; -.
DR TreeFam; TF330194; -.
DR BRENDA; 3.4.21.47; 2681.
DR PathwayCommons; P00751; -.
DR Reactome; R-HSA-173736; Alternative complement activation.
DR Reactome; R-HSA-174577; Activation of C3 and C5.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SignaLink; P00751; -.
DR SIGNOR; P00751; -.
DR BioGRID-ORCS; 629; 14 hits in 1073 CRISPR screens.
DR ChiTaRS; CFB; human.
DR EvolutionaryTrace; P00751; -.
DR GeneWiki; Complement_factor_B; -.
DR GenomeRNAi; 629; -.
DR Pharos; P00751; Tchem.
DR PRO; PR:P00751; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P00751; protein.
DR Bgee; ENSG00000243649; Expressed in right lobe of liver and 98 other tissues.
DR ExpressionAtlas; P00751; baseline and differential.
DR Genevisible; P00751; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005601; C:classical-complement-pathway C3/C5 convertase complex; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IPI:ComplexPortal.
DR GO; GO:0001848; F:complement binding; TAS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
DR GO; GO:0006956; P:complement activation; IBA:GO_Central.
DR GO; GO:0006957; P:complement activation, alternative pathway; TAS:Reactome.
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; 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; 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 3D-structure; Age-related macular degeneration; Alternative splicing;
KW Cleavage on pair of basic residues; Complement alternate pathway;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycation;
KW Glycoprotein; Hemolytic uremic syndrome; Hydrolase; Immunity;
KW Innate immunity; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal; Sushi; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:6546754"
FT CHAIN 26..764
FT /note="Complement factor B"
FT /id="PRO_0000027545"
FT CHAIN 26..259
FT /note="Complement factor B Ba fragment"
FT /id="PRO_0000027546"
FT CHAIN 260..764
FT /note="Complement factor B Bb fragment"
FT /id="PRO_0000027547"
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 ACT_SITE 576
FT /note="Charge relay system"
FT ACT_SITE 699
FT /note="Charge relay system"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:6546754"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17310251,
FT ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:6546754"
FT CARBOHYD 291
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:2006911"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954,
FT ECO:0000269|PubMed:6546754"
FT DISULFID 37..76
FT /evidence="ECO:0000269|PubMed:19574954"
FT DISULFID 62..98
FT /evidence="ECO:0000269|PubMed:19574954"
FT DISULFID 103..145
FT /evidence="ECO:0000269|PubMed:19574954"
FT DISULFID 131..158
FT /evidence="ECO:0000269|PubMed:19574954"
FT DISULFID 165..205
FT /evidence="ECO:0000269|PubMed:19574954"
FT DISULFID 191..218
FT /evidence="ECO:0000269|PubMed:19574954"
FT DISULFID 478..596
FT /evidence="ECO:0000269|PubMed:19574954"
FT DISULFID 511..527
FT /evidence="ECO:0000269|PubMed:19574954"
FT DISULFID 599..615
FT /evidence="ECO:0000269|PubMed:19574954"
FT DISULFID 656..682
FT /evidence="ECO:0000269|PubMed:19574954"
FT DISULFID 695..725
FT /evidence="ECO:0000269|PubMed:19574954"
FT VAR_SEQ 543..621
FT /note="GEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRP
FT ICLPCTEGTTRALRLPPTTTCQQQKEE -> KDATEGPGLHLCSPGNTSHFLQILHSTH
FT PQCSPIPCTPDQSGMGEDVKLGMTRGQRQEAAHKEVVPTLLLQEGRSGTWR (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_005380"
FT VAR_SEQ 622..764
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_005381"
FT VARIANT 9
FT /note="L -> H (may be associated with a reduced risk for
FT age-related macular degeneration; dbSNP:rs4151667)"
FT /evidence="ECO:0000269|PubMed:16518403, ECO:0000269|Ref.7"
FT /id="VAR_016274"
FT VARIANT 28
FT /note="W -> Q (in allele FA; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:2249879"
FT /id="VAR_006493"
FT VARIANT 28
FT /note="W -> R (in allele S)"
FT /evidence="ECO:0000269|PubMed:2249879,
FT ECO:0000269|PubMed:8181962, ECO:0000269|PubMed:8225386,
FT ECO:0000269|PubMed:8247029"
FT /id="VAR_006492"
FT VARIANT 32
FT /note="R -> Q (in allele S; may be associated with a
FT reduced risk for age-related macular degeneration;
FT dbSNP:rs641153)"
FT /evidence="ECO:0000269|PubMed:16518403,
FT ECO:0000269|PubMed:2249879, ECO:0000269|PubMed:8181962,
FT ECO:0000269|PubMed:8225386, ECO:0000269|PubMed:8247029,
FT ECO:0000269|Ref.7"
FT /id="VAR_006494"
FT VARIANT 32
FT /note="R -> W (in dbSNP:rs12614)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.8"
FT /id="VAR_016275"
FT VARIANT 166
FT /note="S -> P (in AHUS4)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063659"
FT VARIANT 203
FT /note="R -> Q (in AHUS4; dbSNP:rs745794224)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063660"
FT VARIANT 242
FT /note="I -> L (in AHUS4; dbSNP:rs144812066)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063661"
FT VARIANT 252
FT /note="G -> S (in dbSNP:rs4151651)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_016276"
FT VARIANT 286
FT /note="F -> L (in AHUS4; gain-of-function mutation that
FT results in enhanced formation of the C3bBb;
FT dbSNP:rs117905900)"
FT /evidence="ECO:0000269|PubMed:17182750"
FT /id="VAR_063221"
FT VARIANT 323
FT /note="K -> E (in AHUS4; gain-of-function mutation that
FT results in enhanced formation of the C3bBb;
FT dbSNP:rs121909748)"
FT /evidence="ECO:0000269|PubMed:17182750"
FT /id="VAR_063222"
FT VARIANT 323
FT /note="K -> Q (in AHUS4)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063662"
FT VARIANT 458
FT /note="M -> I (in AHUS4; dbSNP:rs200837114)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063663"
FT VARIANT 533
FT /note="K -> R (in AHUS4; benign variant;
FT dbSNP:rs149101394)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063664"
FT VARIANT 565
FT /note="K -> E (in dbSNP:rs4151659)"
FT /evidence="ECO:0000269|PubMed:14574404, ECO:0000269|Ref.7"
FT /id="VAR_016277"
FT VARIANT 651
FT /note="D -> E (in dbSNP:rs4151660)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_016278"
FT VARIANT 736
FT /note="A -> S (in allele FA)"
FT /evidence="ECO:0000269|PubMed:2249879"
FT /id="VAR_006495"
FT MUTAGEN 348..350
FT /note="KLK->AAA: Decreases binding to the pro-C3-convertase
FT complex. Does not affect Complement C3 beta chain binding."
FT /evidence="ECO:0000269|PubMed:31507604"
FT CONFLICT 297
FT /note="I -> T (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="V -> L (in Ref. 12; AAA36225)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="D -> V (in Ref. 12; AAA36225)"
FT /evidence="ECO:0000305"
FT CONFLICT 356..357
FT /note="KK -> EE (in Ref. 12; AAA36225)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="I -> T (in Ref. 15; AAA36219)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="L -> H (in Ref. 15; AAA36220)"
FT /evidence="ECO:0000305"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2OK5"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2XWB"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:3HRZ"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:7JTN"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:1Q0P"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:1Q0P"
FT HELIX 283..301
FT /evidence="ECO:0007829|PDB:1Q0P"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1Q0P"
FT STRAND 308..322
FT /evidence="ECO:0007829|PDB:1Q0P"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:3HS0"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:1Q0P"
FT HELIX 332..340
FT /evidence="ECO:0007829|PDB:1Q0P"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 355..366
FT /evidence="ECO:0007829|PDB:1Q0P"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:3HS0"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:1Q0P"
FT STRAND 381..388
FT /evidence="ECO:0007829|PDB:1Q0P"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:1Q0P"
FT HELIX 399..408
FT /evidence="ECO:0007829|PDB:1Q0P"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:1RTK"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:1Q0P"
FT STRAND 423..429
FT /evidence="ECO:0007829|PDB:1Q0P"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:1RRK"
FT HELIX 436..442
FT /evidence="ECO:0007829|PDB:1Q0P"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:1Q0P"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:3HRZ"
FT HELIX 458..468
FT /evidence="ECO:0007829|PDB:1RRK"
FT HELIX 471..474
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:7JTN"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:1DLE"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 496..501
FT /evidence="ECO:0007829|PDB:1RRK"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:2XWB"
FT STRAND 509..515
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 517..523
FT /evidence="ECO:0007829|PDB:1RRK"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:7JTN"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 548..555
FT /evidence="ECO:0007829|PDB:1RRK"
FT TURN 561..564
FT /evidence="ECO:0007829|PDB:1RRK"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 578..584
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:7JTN"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:1DLE"
FT HELIX 601..606
FT /evidence="ECO:0007829|PDB:1RRK"
FT HELIX 615..622
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 625..638
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 640..648
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 650..652
FT /evidence="ECO:0007829|PDB:7JTN"
FT HELIX 653..658
FT /evidence="ECO:0007829|PDB:1RRK"
FT HELIX 659..662
FT /evidence="ECO:0007829|PDB:1RRK"
FT HELIX 666..668
FT /evidence="ECO:0007829|PDB:3HS0"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 680..689
FT /evidence="ECO:0007829|PDB:1RRK"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 702..707
FT /evidence="ECO:0007829|PDB:1RRK"
FT STRAND 710..721
FT /evidence="ECO:0007829|PDB:1RRK"
FT HELIX 725..727
FT /evidence="ECO:0007829|PDB:2OK5"
FT TURN 728..730
FT /evidence="ECO:0007829|PDB:2OK5"
FT HELIX 735..737
FT /evidence="ECO:0007829|PDB:1DLE"
FT STRAND 739..744
FT /evidence="ECO:0007829|PDB:1RRK"
FT HELIX 745..748
FT /evidence="ECO:0007829|PDB:1RRK"
FT HELIX 749..755
FT /evidence="ECO:0007829|PDB:1RRK"
FT TURN 756..758
FT /evidence="ECO:0007829|PDB:1RRK"
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
