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Database: UniProt
Entry: P00751
LinkDB: P00751
Original site: P00751 
ID   CFAB_HUMAN              Reviewed;         764 AA.
AC   P00751; B0QZQ6; O15006; Q29944; Q53F89; Q5JP67; Q5ST50; Q96HX6;
AC   Q9BTF5; Q9BX92;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   26-NOV-2014, entry version 198.
DE   RecName: Full=Complement factor B;
DE            EC=3.4.21.47;
DE   AltName: Full=C3/C5 convertase;
DE   AltName: Full=Glycine-rich beta glycoprotein;
DE            Short=GBG;
DE   AltName: Full=PBF2;
DE   AltName: Full=Properdin factor B;
DE   Contains:
DE     RecName: Full=Complement factor B Ba fragment;
DE   Contains:
DE     RecName: Full=Complement factor B Bb fragment;
DE   Flags: Precursor;
GN   Name=CFB; Synonyms=BF, BFD;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28; GLN-28;
RP   GLN-32 AND SER-736.
RX   PubMed=2249879; DOI=10.1007/BF00211644;
RA   Davrinche C., Abbal M., Clerc A.;
RT   "Molecular characterization of human complement factor B subtypes.";
RL   Immunogenetics 32:309-312(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28 AND
RP   GLN-32.
RC   TISSUE=Liver;
RX   PubMed=8181962; DOI=10.1016/0198-8859(94)90100-7;
RA   Mejia J.E., Jahn I., de la Salle H., Hauptmann G.;
RT   "Human factor B. Complete cDNA sequence of the BF*S allele.";
RL   Hum. Immunol. 39:49-53(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28 AND
RP   GLN-32.
RC   TISSUE=Liver;
RX   PubMed=8225386;
RA   Schwaeble W., Luettig B., Sokolowski T., Estaller C., Weiss E.H.,
RA   Meyer Zum Bueschenfelde K.-H., Whaley K., Dippold W.;
RT   "Human complement factor B: functional properties of a recombinant
RT   zymogen of the alternative activation pathway convertase.";
RL   Immunobiology 188:221-232(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28 AND
RP   GLN-32.
RX   PubMed=8247029; DOI=10.1016/0161-5890(93)90450-P;
RA   Horiuchi T., Kim S., Matsumoto M., Watanabe I., Fujita S.,
RA   Volanakis J.E.;
RT   "Human complement factor B: cDNA cloning, nucleotide sequencing,
RT   phenotypic conversion by site-directed mutagenesis and expression.";
RL   Mol. Immunol. 30:1587-1592(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Jaatinen T., Kanerva J., Poutanen K.E., Saarinen-Pihkala U.,
RA   Lokki M.-L.;
RT   "Expression and alternative splicing of human factor B gene in
RT   leukemic mononuclear cells.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA   Campbell R.D., Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-9; GLN-32; TRP-32;
RP   SER-252; GLU-565 AND GLU-651.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   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.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RP   TRP-32.
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [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;
RA   Mole J.E., Anderson J.K., Davison E.A., Woods D.E.;
RT   "Complete primary structure for the zymogen of human complement factor
RT   B.";
RL   J. Biol. Chem. 259:3407-3412(1984).
RN   [13]
RP   PROTEIN SEQUENCE OF 260-764.
RX   PubMed=6342610;
RA   Christie D.L., Gagnon J.;
RT   "Amino acid sequence of the Bb fragment from complement Factor B.
RT   Sequence of the major cyanogen bromide-cleavage peptide (CB-II) and
RT   completion of the sequence of the Bb fragment.";
RL   Biochem. J. 209:61-70(1983).
RN   [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;
RA   Morley B.J., Campbell R.D.;
RT   "Internal homologies of the Ba fragment from human complement
RT   component Factor B, a class III MHC antigen.";
RL   EMBO J. 3:153-157(1984).
RN   [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
RT   gene: 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;
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.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [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
RT   multiple 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
RT   roles 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,
RP   AND 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
RP   BONDS.
RX   PubMed=19574954; DOI=10.1038/emboj.2009.184;
RA   Janssen B.J., Gomes L., Koning R.I., Svergun D.I., Koster A.J.,
RA   Fritzinger D.C., Vogel C.-W., Gros P.;
RT   "Insights into complement convertase formation based on the structure
RT   of the factor B-cobra venom factor complex.";
RL   EMBO J. 28:2469-2478(2009).
RN   [25]
RP   VARIANTS HIS-9 AND GLN-32, AND INVOLVEMENT IN REDUCED RISK OF ARMD.
RX   PubMed=16518403; DOI=10.1038/ng1750;
RA   Gold B., Merriam J.E., Zernant J., Hancox L.S., Taiber A.J., Gehrs K.,
RA   Cramer K., Neel J., Bergeron J., Barile G.R., Smith R.T.,
RA   Hageman G.S., Dean M., Allikmets R.;
RT   "Variation in factor B (BF) and complement component 2 (C2) genes is
RT   associated with age-related macular degeneration.";
RL   Nat. Genet. 38:458-462(2006).
RN   [26]
RP   VARIANTS AHUS4 LEU-286 AND GLU-323, AND CHARACTERIZATION OF VARIANTS
RP   AHUS4 LEU-286 AND GLU-323.
RX   PubMed=17182750; DOI=10.1073/pnas.0603420103;
RA   Goicoechea de Jorge E., Harris C.L., Esparza-Gordillo J., Carreras L.,
RA   Arranz E.A., Garrido C.A., Lopez-Trascasa M., Sanchez-Corral P.,
RA   Morgan B.P., Rodriguez de Cordoba S.;
RT   "Gain-of-function mutations in complement factor B are associated with
RT   atypical hemolytic uremic syndrome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:240-245(2007).
RN   [27]
RP   VARIANTS AHUS4 PRO-166; GLN-203; LEU-242; GLN-323; ILE-458 AND
RP   ARG-533.
RX   PubMed=20513133; DOI=10.1002/humu.21256;
RA   Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.;
RT   "Mutations in alternative pathway complement proteins in American
RT   patients with atypical hemolytic uremic syndrome.";
RL   Hum. Mutat. 31:E1445-E1460(2010).
CC   -!- FUNCTION: Factor B which is part of the alternate pathway of the
CC       complement system is cleaved by factor D into 2 fragments: Ba and
CC       Bb. Bb, a serine protease, then combines with complement factor 3b
CC       to generate the C3 or C5 convertase. It has also been implicated
CC       in proliferation and differentiation of preactivated B-
CC       lymphocytes, rapid spreading of peripheral blood monocytes,
CC       stimulation of lymphocyte blastogenesis and lysis of erythrocytes.
CC       Ba inhibits the proliferation of preactivated B-lymphocytes.
CC   -!- CATALYTIC ACTIVITY: Cleavage of Arg-|-Ser bond in complement
CC       component C3 alpha-chain to yield C3a and C3b, and Arg-|-Xaa bond
CC       in complement component C5 alpha-chain to yield C5a and C5b.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19574954}.
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'
CC       conformation whereby the scissile Arg-259|Lys-260 bond is
CC       protected from proteolytic activation.
CC       {ECO:0000269|PubMed:17310251}.
CC   -!- POLYMORPHISM: Two major variants, F and S, and 2 minor variants,
CC       as well as at least 14 very rare variants, have been identified.
CC       The variants His-9 and Gln-32 are associated with a reduced risk
CC       of age-related macular degeneration (ARMD) [MIM:603075]. ARMD is a
CC       multifactorial eye disease and the most common cause of
CC       irreversible vision loss in the developed world.
CC   -!- DISEASE: Hemolytic uremic syndrome atypical 4 (AHUS4)
CC       [MIM:612924]: An atypical form of hemolytic uremic syndrome. It is
CC       a complex genetic disease characterized by microangiopathic
CC       hemolytic anemia, thrombocytopenia, renal failure and absence of
CC       episodes of enterocolitis and diarrhea. In contrast to typical
CC       hemolytic uremic syndrome, atypical forms have a poorer prognosis,
CC       with higher death rates and frequent progression to end-stage
CC       renal disease. {ECO:0000269|PubMed:17182750,
CC       ECO:0000269|PubMed:20513133}. Note=Disease susceptibility is
CC       associated with variations affecting the gene represented in this
CC       entry. Susceptibility to the development of atypical hemolytic
CC       uremic syndrome can be conferred by mutations in various
CC       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
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- SIMILARITY: Contains 3 Sushi (CCP/SCR) domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00302}.
CC   -!- SIMILARITY: Contains 1 VWFA domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00219}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/bf/";
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DR   EMBL; X72875; CAA51389.1; -; mRNA.
DR   EMBL; S67310; AAD13989.1; -; mRNA.
DR   EMBL; L15702; AAA16820.1; -; mRNA.
DR   EMBL; X00284; CAA25077.1; -; mRNA.
DR   EMBL; AF349679; AAK30167.1; -; mRNA.
DR   EMBL; AF019413; AAB67977.1; -; Genomic_DNA.
DR   EMBL; AF551848; AAN71991.1; -; Genomic_DNA.
DR   EMBL; AL844853; CAI41860.1; -; Genomic_DNA.
DR   EMBL; AL662849; CAI17456.1; -; Genomic_DNA.
DR   EMBL; BX005143; CAM25864.1; -; Genomic_DNA.
DR   EMBL; CR759782; CAQ07113.1; -; Genomic_DNA.
DR   EMBL; CR388219; CAQ07483.1; -; Genomic_DNA.
DR   EMBL; AK223400; BAD97120.1; -; mRNA.
DR   EMBL; AL645922; CAQ09274.1; -; 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   UniGene; Hs.69771; -.
DR   PDB; 1DLE; X-ray; 2.10 A; A/B=470-764.
DR   PDB; 1Q0P; X-ray; 1.80 A; A=254-476.
DR   PDB; 1RRK; X-ray; 2.00 A; A=268-764.
DR   PDB; 1RS0; X-ray; 2.60 A; A=268-764.
DR   PDB; 1RTK; X-ray; 2.30 A; A=268-764.
DR   PDB; 2OK5; X-ray; 2.30 A; A=26-764.
DR   PDB; 2WIN; X-ray; 3.90 A; I/J/K/L=260-764.
DR   PDB; 2XWB; X-ray; 3.49 A; F/H=35-764.
DR   PDB; 2XWJ; X-ray; 4.00 A; I/J/K/L=26-764.
DR   PDB; 3HRZ; X-ray; 2.20 A; D=26-764.
DR   PDB; 3HS0; X-ray; 3.00 A; D/I=26-764.
DR   PDBsum; 1DLE; -.
DR   PDBsum; 1Q0P; -.
DR   PDBsum; 1RRK; -.
DR   PDBsum; 1RS0; -.
DR   PDBsum; 1RTK; -.
DR   PDBsum; 2OK5; -.
DR   PDBsum; 2WIN; -.
DR   PDBsum; 2XWB; -.
DR   PDBsum; 2XWJ; -.
DR   PDBsum; 3HRZ; -.
DR   PDBsum; 3HS0; -.
DR   ProteinModelPortal; P00751; -.
DR   SMR; P00751; 35-764.
DR   BioGrid; 107098; 8.
DR   DIP; DIP-38319N; -.
DR   IntAct; P00751; 4.
DR   MINT; MINT-3003542; -.
DR   STRING; 9606.ENSP00000388516; -.
DR   BindingDB; P00751; -.
DR   ChEMBL; CHEMBL5731; -.
DR   MEROPS; S01.196; -.
DR   PhosphoSite; P00751; -.
DR   DMDM; 584908; -.
DR   DOSAC-COBS-2DPAGE; P00751; -.
DR   REPRODUCTION-2DPAGE; P00751; -.
DR   SWISS-2DPAGE; P00751; -.
DR   MaxQB; P00751; -.
DR   PaxDb; P00751; -.
DR   PeptideAtlas; P00751; -.
DR   PRIDE; P00751; -.
DR   DNASU; 629; -.
DR   Ensembl; ENST00000399981; ENSP00000382862; ENSG00000241253.
DR   Ensembl; ENST00000417261; ENSP00000414889; ENSG00000239754. [P00751-1]
DR   Ensembl; ENST00000419411; ENSP00000391902; ENSG00000242335. [P00751-1]
DR   Ensembl; ENST00000419920; ENSP00000411474; ENSG00000241253.
DR   Ensembl; ENST00000424727; ENSP00000401719; ENSG00000243570. [P00751-1]
DR   Ensembl; ENST00000425368; ENSP00000416561; ENSG00000243649. [P00751-1]
DR   Ensembl; ENST00000426239; ENSP00000413351; ENSG00000242335. [P00751-1]
DR   Ensembl; ENST00000427888; ENSP00000411515; ENSG00000239754. [P00751-1]
DR   Ensembl; ENST00000433503; ENSP00000388352; ENSG00000241534. [P00751-1]
DR   Ensembl; ENST00000436692; ENSP00000389604; ENSG00000243570. [P00751-1]
DR   Ensembl; ENST00000455591; ENSP00000414341; ENSG00000241534. [P00751-1]
DR   GeneID; 629; -.
DR   KEGG; hsa:629; -.
DR   UCSC; uc003nyi.2; human. [P00751-2]
DR   UCSC; uc003nyj.4; human. [P00751-1]
DR   CTD; 629; -.
DR   GeneCards; GC06P031931; -.
DR   GeneCards; GC06Pj31900; -.
DR   GeneCards; GC06Pk31895; -.
DR   GeneCards; GC06Pm31989; -.
DR   GeneCards; GC06Pn31885; -.
DR   GeneCards; GC06Po31905; -.
DR   GeneReviews; CFB; -.
DR   H-InvDB; HIX0038706; -.
DR   HGNC; HGNC:1037; CFB.
DR   HPA; CAB016381; -.
DR   HPA; HPA001817; -.
DR   HPA; HPA001832; -.
DR   MIM; 138470; gene.
DR   MIM; 603075; phenotype.
DR   MIM; 612924; phenotype.
DR   MIM; 615561; phenotype.
DR   neXtProt; NX_P00751; -.
DR   Orphanet; 279; Age-related macular degeneration.
DR   Orphanet; 93578; Atypical hemolytic-uremic syndrome with B factor anomaly.
DR   PharmGKB; PA25341; -.
DR   eggNOG; NOG304026; -.
DR   GeneTree; ENSGT00530000063826; -.
DR   HOVERGEN; HBG002567; -.
DR   InParanoid; P00751; -.
DR   KO; K01335; -.
DR   OMA; FMYDTPA; -.
DR   PhylomeDB; P00751; -.
DR   TreeFam; TF330194; -.
DR   BRENDA; 3.4.21.47; 2681.
DR   Reactome; REACT_118707; Regulation of Complement cascade.
DR   Reactome; REACT_7972; Activation of C3 and C5.
DR   Reactome; REACT_8001; Alternative complement activation.
DR   ChiTaRS; CFB; human.
DR   EvolutionaryTrace; P00751; -.
DR   GeneWiki; Complement_factor_B; -.
DR   GenomeRNAi; 629; -.
DR   NextBio; 2546; -.
DR   PRO; PR:P00751; -.
DR   Bgee; P00751; -.
DR   CleanEx; HS_CFB; -.
DR   ExpressionAtlas; P00751; baseline and differential.
DR   Genevestigator; P00751; -.
DR   GO; GO:0072562; C:blood microparticle; IDA:UniProt.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProt.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA: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; TAS:Reactome.
DR   GO; GO:0006957; P:complement activation, alternative pathway; NAS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR011360; Compl_C2_B.
DR   InterPro; IPR028341; Complement_B.
DR   InterPro; IPR001254; Peptidase_S1.
DR   InterPro; IPR018114; Peptidase_S1_AS.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR000436; Sushi_SCR_CCP.
DR   InterPro; IPR009003; Trypsin-like_Pept_dom.
DR   InterPro; IPR002035; VWF_A.
DR   Pfam; PF00084; Sushi; 3.
DR   Pfam; PF00089; Trypsin; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PIRSF; PIRSF001154; Compl_C2_B; 1.
DR   PIRSF; PIRSF500181; Complement_B; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00032; CCP; 3.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; 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; Alternative splicing;
KW   Cleavage on pair of basic residues; Complement alternate pathway;
KW   Complete proteome; Direct protein sequencing; Disease mutation;
KW   Disulfide bond; Glycation; Glycoprotein; Hemolytic uremic syndrome;
KW   Hydrolase; Immunity; Innate immunity; Polymorphism; Protease;
KW   Reference proteome; Repeat; Secreted; Serine protease; Signal; Sushi;
KW   Zymogen.
FT   SIGNAL        1     25       {ECO:0000269|PubMed:6546754}.
FT   CHAIN        26    764       Complement factor B.
FT                                /FTId=PRO_0000027545.
FT   CHAIN        26    259       Complement factor B Ba fragment.
FT                                /FTId=PRO_0000027546.
FT   CHAIN       260    764       Complement factor B Bb fragment.
FT                                /FTId=PRO_0000027547.
FT   DOMAIN       35    100       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      101    160       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      163    220       Sushi 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      270    469       VWFA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN      477    757       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    526    526       Charge relay system.
FT   ACT_SITE    576    576       Charge relay system.
FT   ACT_SITE    699    699       Charge relay system.
FT   CARBOHYD    122    122       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:17310251,
FT                                ECO:0000269|PubMed:19159218,
FT                                ECO:0000269|PubMed:6546754}.
FT   CARBOHYD    142    142       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:17310251,
FT                                ECO:0000269|PubMed:19574954,
FT                                ECO:0000269|PubMed:6546754}.
FT   CARBOHYD    285    285       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:17310251,
FT                                ECO:0000269|PubMed:19159218,
FT                                ECO:0000269|PubMed:6546754}.
FT   CARBOHYD    291    291       N-linked (Glc) (glycation).
FT                                {ECO:0000269|PubMed:6546754}.
FT   CARBOHYD    378    378       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:16335952,
FT                                ECO:0000269|PubMed:17310251,
FT                                ECO:0000269|PubMed:19574954,
FT                                ECO:0000269|PubMed:6546754}.
FT   DISULFID     37     76       {ECO:0000269|PubMed:19574954}.
FT   DISULFID     62     98       {ECO:0000269|PubMed:19574954}.
FT   DISULFID    103    145       {ECO:0000269|PubMed:19574954}.
FT   DISULFID    131    158       {ECO:0000269|PubMed:19574954}.
FT   DISULFID    165    205       {ECO:0000269|PubMed:19574954}.
FT   DISULFID    191    218       {ECO:0000269|PubMed:19574954}.
FT   DISULFID    478    596       {ECO:0000269|PubMed:19574954}.
FT   DISULFID    511    527       {ECO:0000269|PubMed:19574954}.
FT   DISULFID    599    615       {ECO:0000269|PubMed:19574954}.
FT   DISULFID    656    682       {ECO:0000269|PubMed:19574954}.
FT   DISULFID    695    725       {ECO:0000269|PubMed:19574954}.
FT   VAR_SEQ     543    621       GEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLK
FT                                NKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEE ->
FT                                KDATEGPGLHLCSPGNTSHFLQILHSTHPQCSPIPCTPDQS
FT                                GMGEDVKLGMTRGQRQEAAHKEVVPTLLLQEGRSGTWR
FT                                (in isoform 2). {ECO:0000303|Ref.5}.
FT                                /FTId=VSP_005380.
FT   VAR_SEQ     622    764       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.5}.
FT                                /FTId=VSP_005381.
FT   VARIANT       9      9       L -> H (in dbSNP:rs4151667).
FT                                {ECO:0000269|PubMed:16518403,
FT                                ECO:0000269|Ref.7}.
FT                                /FTId=VAR_016274.
FT   VARIANT      28     28       W -> Q (in allele FA; requires 2
FT                                nucleotide substitutions).
FT                                {ECO:0000269|PubMed:2249879}.
FT                                /FTId=VAR_006493.
FT   VARIANT      28     28       W -> R (in allele S).
FT                                {ECO:0000269|PubMed:2249879,
FT                                ECO:0000269|PubMed:8181962,
FT                                ECO:0000269|PubMed:8225386,
FT                                ECO:0000269|PubMed:8247029}.
FT                                /FTId=VAR_006492.
FT   VARIANT      32     32       R -> Q (in allele S; dbSNP:rs641153).
FT                                {ECO:0000269|PubMed:16518403,
FT                                ECO:0000269|PubMed:2249879,
FT                                ECO:0000269|PubMed:8181962,
FT                                ECO:0000269|PubMed:8225386,
FT                                ECO:0000269|PubMed:8247029,
FT                                ECO:0000269|Ref.7}.
FT                                /FTId=VAR_006494.
FT   VARIANT      32     32       R -> W (in dbSNP:rs12614).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.10, ECO:0000269|Ref.7,
FT                                ECO:0000269|Ref.8}.
FT                                /FTId=VAR_016275.
FT   VARIANT     166    166       S -> P (in AHUS4).
FT                                {ECO:0000269|PubMed:20513133}.
FT                                /FTId=VAR_063659.
FT   VARIANT     203    203       R -> Q (in AHUS4).
FT                                {ECO:0000269|PubMed:20513133}.
FT                                /FTId=VAR_063660.
FT   VARIANT     242    242       I -> L (in AHUS4).
FT                                {ECO:0000269|PubMed:20513133}.
FT                                /FTId=VAR_063661.
FT   VARIANT     252    252       G -> S (in dbSNP:rs4151651).
FT                                {ECO:0000269|Ref.7}.
FT                                /FTId=VAR_016276.
FT   VARIANT     286    286       F -> L (in AHUS4; gain-of-function
FT                                mutation that results in enhanced
FT                                formation of the C3bBb).
FT                                {ECO:0000269|PubMed:17182750}.
FT                                /FTId=VAR_063221.
FT   VARIANT     323    323       K -> E (in AHUS4; gain-of-function
FT                                mutation that results in enhanced
FT                                formation of the C3bBb).
FT                                {ECO:0000269|PubMed:17182750}.
FT                                /FTId=VAR_063222.
FT   VARIANT     323    323       K -> Q (in AHUS4).
FT                                {ECO:0000269|PubMed:20513133}.
FT                                /FTId=VAR_063662.
FT   VARIANT     458    458       M -> I (in AHUS4).
FT                                {ECO:0000269|PubMed:20513133}.
FT                                /FTId=VAR_063663.
FT   VARIANT     533    533       K -> R (in AHUS4).
FT                                {ECO:0000269|PubMed:20513133}.
FT                                /FTId=VAR_063664.
FT   VARIANT     565    565       K -> E (in dbSNP:rs4151659).
FT                                {ECO:0000269|PubMed:14574404,
FT                                ECO:0000269|Ref.7}.
FT                                /FTId=VAR_016277.
FT   VARIANT     651    651       D -> E (in dbSNP:rs4151660).
FT                                {ECO:0000269|Ref.7}.
FT                                /FTId=VAR_016278.
FT   VARIANT     736    736       A -> S (in allele FA).
FT                                {ECO:0000269|PubMed:2249879}.
FT                                /FTId=VAR_006495.
FT   CONFLICT    297    297       I -> T (in Ref. 13; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    300    300       V -> L (in Ref. 12; AAA36225).
FT                                {ECO:0000305}.
FT   CONFLICT    328    328       D -> V (in Ref. 12; AAA36225).
FT                                {ECO:0000305}.
FT   CONFLICT    356    357       KK -> EE (in Ref. 12; AAA36225).
FT                                {ECO:0000305}.
FT   CONFLICT    537    537       I -> T (in Ref. 15; AAA36219).
FT                                {ECO:0000305}.
FT   CONFLICT    764    764       L -> H (in Ref. 15; AAA36220).
FT                                {ECO:0000305}.
FT   STRAND       47     51       {ECO:0000244|PDB:3HRZ}.
FT   HELIX        53     55       {ECO:0000244|PDB:3HRZ}.
FT   STRAND       56     61       {ECO:0000244|PDB:3HRZ}.
FT   STRAND       66     70       {ECO:0000244|PDB:3HRZ}.
FT   STRAND       72     76       {ECO:0000244|PDB:3HRZ}.
FT   STRAND       80     82       {ECO:0000244|PDB:2OK5}.
FT   STRAND       88     90       {ECO:0000244|PDB:2XWB}.
FT   STRAND       92     94       {ECO:0000244|PDB:3HRZ}.
FT   STRAND       97    100       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      112    115       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      119    122       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      126    131       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      136    139       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      141    145       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      151    153       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      157    159       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      163    165       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      174    177       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      186    191       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      195    199       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      201    205       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      209    213       {ECO:0000244|PDB:3HRZ}.
FT   STRAND      217    219       {ECO:0000244|PDB:3HRZ}.
FT   HELIX       227    238       {ECO:0000244|PDB:3HRZ}.
FT   HELIX       240    243       {ECO:0000244|PDB:2XWB}.
FT   STRAND      269    276       {ECO:0000244|PDB:1Q0P}.
FT   TURN        279    281       {ECO:0000244|PDB:1Q0P}.
FT   HELIX       283    301       {ECO:0000244|PDB:1Q0P}.
FT   TURN        302    304       {ECO:0000244|PDB:1Q0P}.
FT   STRAND      308    322       {ECO:0000244|PDB:1Q0P}.
FT   STRAND      324    326       {ECO:0000244|PDB:3HS0}.
FT   HELIX       327    330       {ECO:0000244|PDB:1Q0P}.
FT   HELIX       332    340       {ECO:0000244|PDB:1Q0P}.
FT   HELIX       344    346       {ECO:0000244|PDB:1RRK}.
FT   STRAND      348    350       {ECO:0000244|PDB:3HRZ}.
FT   HELIX       355    366       {ECO:0000244|PDB:1Q0P}.
FT   STRAND      369    372       {ECO:0000244|PDB:3HS0}.
FT   HELIX       377    379       {ECO:0000244|PDB:1Q0P}.
FT   STRAND      381    388       {ECO:0000244|PDB:1Q0P}.
FT   STRAND      394    396       {ECO:0000244|PDB:1Q0P}.
FT   HELIX       399    408       {ECO:0000244|PDB:1Q0P}.
FT   STRAND      412    414       {ECO:0000244|PDB:1RTK}.
FT   HELIX       420    422       {ECO:0000244|PDB:1Q0P}.
FT   STRAND      423    429       {ECO:0000244|PDB:1Q0P}.
FT   STRAND      431    433       {ECO:0000244|PDB:1RRK}.
FT   HELIX       436    442       {ECO:0000244|PDB:1Q0P}.
FT   STRAND      452    454       {ECO:0000244|PDB:1Q0P}.
FT   STRAND      455    457       {ECO:0000244|PDB:3HRZ}.
FT   HELIX       461    468       {ECO:0000244|PDB:1RRK}.
FT   HELIX       471    474       {ECO:0000244|PDB:1RRK}.
FT   HELIX       489    492       {ECO:0000244|PDB:1RRK}.
FT   STRAND      496    501       {ECO:0000244|PDB:1RRK}.
FT   TURN        504    506       {ECO:0000244|PDB:2XWB}.
FT   STRAND      509    515       {ECO:0000244|PDB:1RRK}.
FT   STRAND      517    523       {ECO:0000244|PDB:1RRK}.
FT   HELIX       525    527       {ECO:0000244|PDB:1RRK}.
FT   HELIX       534    536       {ECO:0000244|PDB:1RRK}.
FT   STRAND      537    541       {ECO:0000244|PDB:1RRK}.
FT   STRAND      548    555       {ECO:0000244|PDB:1RRK}.
FT   TURN        561    564       {ECO:0000244|PDB:1RRK}.
FT   HELIX       565    567       {ECO:0000244|PDB:1RRK}.
FT   STRAND      578    584       {ECO:0000244|PDB:1RRK}.
FT   STRAND      598    600       {ECO:0000244|PDB:1DLE}.
FT   HELIX       601    606       {ECO:0000244|PDB:1RRK}.
FT   HELIX       615    622       {ECO:0000244|PDB:1RRK}.
FT   STRAND      625    638       {ECO:0000244|PDB:1RRK}.
FT   STRAND      640    648       {ECO:0000244|PDB:1RRK}.
FT   HELIX       653    658       {ECO:0000244|PDB:1RRK}.
FT   HELIX       659    662       {ECO:0000244|PDB:1RRK}.
FT   HELIX       666    668       {ECO:0000244|PDB:3HS0}.
FT   HELIX       672    674       {ECO:0000244|PDB:1RRK}.
FT   STRAND      680    689       {ECO:0000244|PDB:1RRK}.
FT   HELIX       696    698       {ECO:0000244|PDB:1RRK}.
FT   STRAND      702    707       {ECO:0000244|PDB:1RRK}.
FT   STRAND      710    721       {ECO:0000244|PDB:1RRK}.
FT   HELIX       725    727       {ECO:0000244|PDB:2OK5}.
FT   TURN        728    730       {ECO:0000244|PDB:2OK5}.
FT   HELIX       735    737       {ECO:0000244|PDB:1DLE}.
FT   STRAND      739    744       {ECO:0000244|PDB:1RRK}.
FT   HELIX       745    748       {ECO:0000244|PDB:1RRK}.
FT   HELIX       749    755       {ECO:0000244|PDB:1RRK}.
FT   TURN        756    758       {ECO:0000244|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
//
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