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 27-MAR-2024, entry version 263. 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]: CC An 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7NOZ; X-ray; 3.90 A; F=35-764. DR PDB; 8ENU; EM; 3.22 A; D=2-764. DR PDB; 8EOK; EM; 3.53 A; D=2-764. 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 PDBsum; 7NOZ; -. DR PDBsum; 8ENU; -. DR PDBsum; 8EOK; -. DR AlphaFoldDB; P00751; -. DR EMDB; EMD-2403; -. DR EMDB; EMD-28279; -. DR EMDB; EMD-28378; -. DR SMR; P00751; -. DR BioGRID; 107098; 49. 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; 16. 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 GlyCosmos; P00751; 7 sites, 15 glycans. DR GlyGen; P00751; 7 sites, 19 N-linked glycans (4 sites), 4 O-linked glycans (3 sites). DR iPTMnet; P00751; -. DR PhosphoSitePlus; P00751; -. DR SwissPalm; P00751; -. DR BioMuta; CFB; -. DR DMDM; 584908; -. DR DOSAC-COBS-2DPAGE; P00751; -. DR REPRODUCTION-2DPAGE; P00751; -. DR CPTAC; non-CPTAC-1112; -. DR EPD; P00751; -. DR jPOST; P00751; -. DR MassIVE; P00751; -. DR MaxQB; P00751; -. DR PaxDb; 9606-ENSP00000416561; -. DR PeptideAtlas; P00751; -. DR ProteomicsDB; 51285; -. [P00751-1] DR ProteomicsDB; 51286; -. [P00751-2] DR ABCD; P00751; 1 sequenced antibody. DR Antibodypedia; 35050; 961 antibodies from 39 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; ENSG00000243649.10. [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 AGR; HGNC:1037; -. 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 OrthoDB; 3594820at2759; -. 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; 18 hits in 1149 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 99 other cell types or tissues. DR ExpressionAtlas; P00751; baseline and differential. 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; 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:0006956; P:complement activation; IBA:GO_Central. DR GO; GO:0006957; P:complement activation, alternative pathway; TAS:Reactome. 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 CDD; cd01470; vWA_complement_factors; 1. DR Gene3D; 2.40.10.120; -; 1. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 3. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 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:SF1; COMPLEMENT FACTOR B; 1. DR PANTHER; PTHR46393; SUSHI DOMAIN-CONTAINING PROTEIN; 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 PRINTS; PR00453; VWFADOMAIN. DR SMART; SM00032; CCP; 3. DR SMART; SM00020; Tryp_SPc; 1. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF57535; Complement control module/SCR domain; 3. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR SUPFAM; SSF53300; vWA-like; 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. DR SWISS-2DPAGE; P00751; -. DR Genevisible; P00751; HS. 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; 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 //