CFAH_HUMAN
ID CFAH_HUMAN Reviewed; 1231 AA.
AC P08603; A5PL14; P78435; Q14570; Q2TAZ5; Q38G77; Q5TFM3; Q8N708; Q9NU86;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 4.
DT 03-AUG-2022, entry version 242.
DE RecName: Full=Complement factor H;
DE AltName: Full=H factor 1;
DE Flags: Precursor;
GN Name=CFH; Synonyms=HF, HF1, HF2;
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] (ISOFORMS 1 AND 2), GLYCOSYLATION AT ASN-529,
RP AND VARIANTS HIS-402 AND ARG-493.
RC TISSUE=Liver;
RX PubMed=2963625; DOI=10.1042/bj2490593;
RA Ripoche J., Day A.J., Harris T.J.R., Sim R.B.;
RT "The complete amino acid sequence of human complement factor H.";
RL Biochem. J. 249:593-602(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-62; THR-551; ILE-890;
RP ASP-936; ILE-1007; ILE-1017; TYR-1050 AND THR-1059.
RG SeattleSNPs variation discovery resource;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-402.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ILE-62.
RC TISSUE=Testis, and Urinary bladder;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-445.
RX PubMed=2946589; DOI=10.1002/eji.1830161107;
RA Schulz T.F., Schwaeble W., Stanley K.K., Weiss E., Dierich M.P.;
RT "Human complement factor H: isolation of cDNA clones and partial cDNA
RT sequence of the 38-kDa tryptic fragment containing the binding site for
RT C3b.";
RL Eur. J. Immunol. 16:1351-1355(1986).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 226-449, AND PROTEIN SEQUENCE OF 205-216;
RP 237-246; 320-331; 425-435; 508-518; 645-662; 667-717; 858-885; 907-972;
RP 1163-1182 AND 1193-1203.
RX PubMed=2937845;
RA Kristensen T., Wetsel R.A., Tack B.F.;
RT "Structural analysis of human complement protein H: homology with C4b
RT binding protein, beta 2-glycoprotein I, and the Ba fragment of B2.";
RL J. Immunol. 136:3407-3411(1986).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1047-1231.
RX PubMed=1826708;
RA Estaller C., Koistinen V., Schwaeble W., Dierich M.P., Weiss E.H.;
RT "Cloning of the 1.4-kb mRNA species of human complement factor H reveals a
RT novel member of the short consensus repeat family related to the carboxy
RT terminal of the classical 150-kDa molecule.";
RL J. Immunol. 146:3190-3196(1991).
RN [8]
RP PROTEIN SEQUENCE OF 19-35.
RX PubMed=6215918; DOI=10.1042/bj2050285;
RA Sim R.B., Discipio R.G.;
RT "Purification and structural studies on the complement-system control
RT protein beta 1H (Factor H).";
RL Biochem. J. 205:285-293(1982).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RA Vik D.P., Williams S.A.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RA Dominguez O.;
RL Thesis (1993), Hospital Trias I Pujol, Spain.
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=6444659; DOI=10.1084/jem.151.3.501;
RA Whaley K.;
RT "Biosynthesis of the complement components and the regulatory proteins of
RT the alternative complement pathway by human peripheral blood monocytes.";
RL J. Exp. Med. 151:501-516(1980).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=2968404;
RA Katz Y., Strunk R.C.;
RT "Synthesis and regulation of complement protein factor H in human skin
RT fibroblasts.";
RL J. Immunol. 141:559-563(1988).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=2139673;
RA Brooimans R.A., van der Ark A.A., Buurman W.A., van Es L.A., Daha M.R.;
RT "Differential regulation of complement factor H and C3 production in human
RT umbilical vein endothelial cells by IFN-gamma and IL-1.";
RL J. Immunol. 144:3835-3840(1990).
RN [14]
RP FUNCTION, AND INTERACTION WITH ITGAM.
RX PubMed=9558116;
RA DiScipio R.G., Daffern P.J., Schraufstaetter I.U., Sriramarao P.;
RT "Human polymorphonuclear leukocytes adhere to complement factor H through
RT an interaction that involves alphaMbeta2 (CD11b/CD18).";
RL J. Immunol. 160:4057-4066(1998).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-882.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-529 AND ASN-911.
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 [17]
RP GLYCOSYLATION AT ASN-529; ASN-718; ASN-802; ASN-822; ASN-882; ASN-911;
RP ASN-1029 AND ASN-1095.
RX PubMed=17591618; DOI=10.1093/glycob/cwm060;
RA Fenaille F., Le Mignon M., Groseil C., Ramon C., Riande S., Siret L.,
RA Bihoreau N.;
RT "Site-specific N-glycan characterization of human complement factor H.";
RL Glycobiology 17:932-944(2007).
RN [18]
RP INTERACTION WITH STAPHYLOCOCCUS AUREUS PROTEIN SBI (MICROBIAL INFECTION).
RX PubMed=19112495; DOI=10.1371/journal.ppat.1000250;
RA Haupt K., Reuter M., van den Elsen J., Burman J., Haelbich S., Richter J.,
RA Skerka C., Zipfel P.F.;
RT "The Staphylococcus aureus protein Sbi acts as a complement inhibitor and
RT forms a tripartite complex with host complement Factor H and C3b.";
RL PLoS Pathog. 4:E1000250-E1000250(2008).
RN [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-529; ASN-802; ASN-882; ASN-911
RP AND ASN-1029.
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 [20]
RP GLYCOSYLATION AT ASN-217; ASN-882; ASN-911 AND ASN-1029.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [21]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-882, AND STRUCTURE OF
RP CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [22]
RP FUNCTION, AND INTERACTION WITH ITGAM.
RX PubMed=20008295; DOI=10.4049/jimmunol.0901702;
RA Losse J., Zipfel P.F., Jozsi M.;
RT "Factor H and factor H-related protein 1 bind to human neutrophils via
RT complement receptor 3, mediate attachment to Candida albicans, and enhance
RT neutrophil antimicrobial activity.";
RL J. Immunol. 184:912-921(2010).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP TISSUE SPECIFICITY, AND SULFATION.
RX PubMed=25136834; DOI=10.1371/journal.pone.0105409;
RA Kanan Y., Siefert J.C., Kinter M., Al-Ubaidi M.R.;
RT "Complement factor H, vitronectin, and opticin are tyrosine-sulfated
RT proteins of the retinal pigment epithelium.";
RL PLoS ONE 9:E105409-E105409(2014).
RN [25]
RP FUNCTION, AND INTERACTION WITH P.FALCIPARUM PF92 (MICROBIAL INFECTION).
RX PubMed=26700768; DOI=10.4049/jimmunol.1501581;
RA Kennedy A.T., Schmidt C.Q., Thompson J.K., Weiss G.E.,
RA Taechalertpaisarn T., Gilson P.R., Barlow P.N., Crabb B.S., Cowman A.F.,
RA Tham W.H.;
RT "Recruitment of Factor H as a Novel Complement Evasion Strategy for Blood-
RT Stage Plasmodium falciparum Infection.";
RL J. Immunol. 196:1239-1248(2016).
RN [26]
RP STRUCTURE BY NMR OF 927-985 (SUSHI 16), AND DISULFIDE BOND.
RX PubMed=1829116; DOI=10.1016/0022-2836(91)90666-t;
RA Norman D.G., Barlow P.N., Baron M., Day A.J., Sim B., Campbell I.D.;
RT "Three-dimensional structure of a complement control protein module in
RT solution.";
RL J. Mol. Biol. 219:717-725(1991).
RN [27]
RP STRUCTURE BY NMR OF 264-322 (SUSHI 5).
RX PubMed=1533152; DOI=10.1021/bi00129a011;
RA Barlow P.N., Norman D.G., Steinkasserer A., Horne T.J., Pearce J.,
RA Driscoll P.C., Sim B., Campbell I.D.;
RT "Solution structure of the fifth repeat of factor H: a second example of
RT the complement control protein module.";
RL Biochemistry 31:3626-3634(1992).
RN [28]
RP STRUCTURE BY NMR OF 866-985 (SUSHIS 15 AND 16), AND DISULFIDE BOND.
RX PubMed=8331663; DOI=10.1006/jmbi.1993.1381;
RA Barlow P.N., Steinkasserer A., Norman D.G., Kieffer B., Wiles A.P., Sim B.,
RA Campbell I.D.;
RT "Solution structure of a pair of complement modules by nuclear magnetic
RT resonance.";
RL J. Mol. Biol. 232:268-284(1993).
RN [29]
RP VARIANTS CFHD ARG-536 AND TYR-959.
RX PubMed=9312129; DOI=10.1074/jbc.272.40.25168;
RA Ault B.H., Schmidt B.Z., Fowler N.L., Kashtan C.E., Ahmed A.E., Vogt B.A.,
RA Colten H.R.;
RT "Human factor H deficiency. Mutations in framework cysteine residues and
RT block in H protein secretion and intracellular catabolism.";
RL J. Biol. Chem. 272:25168-25175(1997).
RN [30]
RP VARIANT AHUS1 GLY-1215.
RX PubMed=9551389; DOI=10.1111/j.1523-1755.1998.00824.x;
RA Warwicker P., Goodship T.H.J., Donne R.L., Pirson Y., Nicholls A.,
RA Ward R.M., Turnpenny P., Goodship J.A.;
RT "Genetic studies into inherited and sporadic hemolytic uremic syndrome.";
RL Kidney Int. 53:836-844(1998).
RN [31]
RP VARIANT AHUS1 LEU-1191.
RX PubMed=10577907; DOI=10.1086/302673;
RA Ying L., Katz Y., Schlesinger M., Carmi R., Shalev H., Haider N., Beck G.,
RA Sheffield V.C., Landau D.;
RT "Complement factor H gene mutation associated with autosomal recessive
RT atypical hemolytic uremic syndrome.";
RL Am. J. Hum. Genet. 65:1538-1546(1999).
RN [32]
RP VARIANT AHUS1 1225-TYR--ARG-1231 DELINS PHE-GLN-SER.
RX PubMed=10762557; DOI=10.1086/302877;
RA Buddles M.R.H., Donne R.L., Richards A., Goodship J., Goodship T.H.J.;
RT "Complement factor H gene mutation associated with autosomal recessive
RT atypical hemolytic uremic syndrome.";
RL Am. J. Hum. Genet. 66:1721-1722(2000).
RN [33]
RP INVOLVEMENT IN CFHD.
RX PubMed=10803850; DOI=10.1007/s002510050631;
RA Sanchez-Corral P., Bellavia D., Amico L., Brai M., Rodriguez de Cordoba S.;
RT "Molecular basis for factor H and FHL-1 deficiency in an Italian family.";
RL Immunogenetics 51:366-369(2000).
RN [34]
RP VARIANTS CFHD MET-956; LEU-1183; ARG-1189 AND ALA-1197.
RX PubMed=11170895; DOI=10.1086/318201;
RA Perez-Caballero D., Gonzalez-Rubio C., Gallardo M.E., Vera M.,
RA Lopez-Trascasa M., Rodriguez de Cordoba S., Sanchez-Corral P.;
RT "Clustering of missense mutations in the C-terminal region of factor H in
RT atypical hemolytic uremic syndrome.";
RL Am. J. Hum. Genet. 68:478-484(2001).
RN [35]
RP VARIANTS CFHD GLU-1076; GLY-1119 AND ARG-1184.
RX PubMed=11170896; DOI=10.1086/318203;
RA Richards A., Buddles M.R., Donne R.L., Kaplan B.S., Kirk E., Venning M.C.,
RA Tielemans C.L., Goodship J.A., Goodship T.H.J.;
RT "Factor H mutations in hemolytic uremic syndrome cluster in exons 18-20, a
RT domain important for host cell recognition.";
RL Am. J. Hum. Genet. 68:485-490(2001).
RN [36]
RP VARIANTS CFHD CYS-1210 AND GLN-1215.
RX PubMed=11158219; DOI=10.1681/asn.v122297;
RG Italian registry of familial and recurrent HUS/TTP;
RA Caprioli J., Bettinaglio P., Zipfel P.F., Amadei B., Daina E., Gamba S.,
RA Skerka C., Marziliano N., Remuzzi G., Noris M.;
RT "The molecular basis of familial hemolytic uremic syndrome: mutation
RT analysis of factor H gene reveals a hot spot in short consensus repeat
RT 20.";
RL J. Am. Soc. Nephrol. 12:297-307(2001).
RN [37]
RP VARIANTS AHUS1 MET-956; GLU-1076; GLY-1119; LEU-1183; ARG-1184; ARG-1189;
RP LEU-1191; ASP-1194; ALA-1197; CYS-1210; GLY-1215 AND GLN-1215.
RX PubMed=11851332; DOI=10.1006/jmbi.2001.5337;
RA Perkins S.J., Goodship T.H.J.;
RT "Molecular modelling of the C-terminal domains of factor H of human
RT complement: a correlation between haemolytic uraemic syndrome and a
RT predicted heparin binding site.";
RL J. Mol. Biol. 316:217-224(2002).
RN [38]
RP VARIANT CFHD ARG-1183.
RX PubMed=12020532; DOI=10.1016/s0140-6736(02)08560-4;
RA Remuzzi G., Ruggenenti P., Codazzi D., Noris M., Caprioli J., Locatelli G.,
RA Gridelli B.;
RT "Combined kidney and liver transplantation for familial haemolytic uraemic
RT syndrome.";
RL Lancet 359:1671-1672(2002).
RN [39]
RP VARIANTS AHUS1 GLY-78; HIS-950; HIS-951; TRP-1163 AND ALA-1198, AND VARIANT
RP ASP-936.
RX PubMed=14583443; DOI=10.1093/hmg/ddg363;
RG International registry of recurrent and familial HUS/TTP;
RA Caprioli J., Castelletti F., Bucchioni S., Bettinaglio P., Bresin E.,
RA Pianetti G., Gamba S., Brioschi S., Daina E., Remuzzi G., Noris M.;
RT "Complement factor H mutations and gene polymorphisms in haemolytic uraemic
RT syndrome: the C-257T, the A2089G and the G2881T polymorphisms are strongly
RT associated with the disease.";
RL Hum. Mol. Genet. 12:3385-3395(2003).
RN [40]
RP VARIANTS AHUS1 TRP-630; LYS-850; CYS-978; PHE-1021; ARG-1043; GLY-1134;
RP ASP-1142; ARG-1157; ARG-1183 AND SER-1226.
RX PubMed=12960213; DOI=10.1136/jmg.40.9.676;
RA Neumann H.P.H., Salzmann M., Bohnert-Iwan B., Mannuelian T., Skerka C.,
RA Lenk D., Bender B.U., Cybulla M., Riegler P., Koenigsrainer A., Neyer U.,
RA Bock A., Widmer U., Male D.A., Franke G., Zipfel P.F.;
RT "Haemolytic uraemic syndrome and mutations of the factor H gene: a
RT registry-based study of German speaking countries.";
RL J. Med. Genet. 40:676-681(2003).
RN [41]
RP VARIANTS CFHD LEU-127; SER-431 AND SER-673, AND VARIANTS AHUS1 LYS-400;
RP TYR-673; ARG-893; SER-915; LEU-1183 AND SER-1199.
RX PubMed=14978182; DOI=10.1097/01.asn.0000115702.28859.a7;
RA Dragon-Durey M.-A., Fremeaux-Bacchi V., Loirat C., Blouin J., Niaudet P.,
RA Deschenes G., Coppo P., Herman Fridman W., Weiss L.;
RT "Heterozygous and homozygous factor H deficiencies associated with
RT hemolytic uremic syndrome or membranoproliferative glomerulonephritis:
RT report and genetic analysis of 16 cases.";
RL J. Am. Soc. Nephrol. 15:787-795(2004).
RN [42]
RP VARIANT HIS-402.
RX PubMed=15895326; DOI=10.1086/431426;
RA Zareparsi S., Branham K.E.H., Li M., Shah S., Klein R.J., Ott J., Hoh J.,
RA Abecasis G.R., Swaroop A.;
RT "Strong association of the Y402H variant in complement factor H at 1q32
RT with susceptibility to age-related macular degeneration.";
RL Am. J. Hum. Genet. 77:149-153(2005).
RN [43]
RP VARIANTS ILE-62 AND HIS-402, AND ASSOCIATION WITH ARMD.
RX PubMed=15870199; DOI=10.1073/pnas.0501536102;
RA Hageman G.S., Anderson D.H., Johnson L.V., Hancox L.S., Taiber A.J.,
RA Hardisty L.I., Hageman J.L., Stockman H.A., Borchardt J.D., Gehrs K.M.,
RA Smith R.J.H., Silvestri G., Russell S.R., Klaver C.C.W., Barbazetto I.,
RA Chang S., Yannuzzi L.A., Barile G.R., Merriam J.C., Smith R.T., Olsh A.K.,
RA Bergeron J., Zernant J., Merriam J.E., Gold B., Dean M., Allikmets R.;
RT "A common haplotype in the complement regulatory gene factor H (HF1/CFH)
RT predisposes individuals to age-related macular degeneration.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7227-7232(2005).
RN [44]
RP ASSOCIATION OF VARIANT HIS-402 WITH ARMD.
RX PubMed=15761122; DOI=10.1126/science.1109557;
RA Klein R.J., Zeiss C., Chew E.Y., Tsai J.-Y., Sackler R.S., Haynes C.,
RA Henning A.K., SanGiovanni J.P., Mane S.M., Mayne S.T., Bracken M.B.,
RA Ferris F.L., Ott J., Barnstable C., Hoh J.;
RT "Complement factor H polymorphism in age-related macular degeneration.";
RL Science 308:385-389(2005).
RN [45]
RP ASSOCIATION OF VARIANT HIS-402 WITH ARMD.
RX PubMed=15761120; DOI=10.1126/science.1110359;
RA Haines J.L., Hauser M.A., Schmidt S., Scott W.K., Olson L.M., Gallins P.,
RA Spencer K.L., Kwan S.Y., Noureddine M., Gilbert J.R., Schnetz-Boutaud N.,
RA Agarwal A., Postel E.A., Pericak-Vance M.A.;
RT "Complement factor H variant increases the risk of age-related macular
RT degeneration.";
RL Science 308:419-421(2005).
RN [46]
RP ASSOCIATION OF VARIANT HIS-402 WITH ARMD.
RX PubMed=15761121; DOI=10.1126/science.1110189;
RA Edwards A.O., Ritter R. III, Abel K.J., Manning A., Panhuysen C.,
RA Farrer L.A.;
RT "Complement factor H polymorphism and age-related macular degeneration.";
RL Science 308:421-424(2005).
RN [47]
RP VARIANT CFHD LYS-224 DEL, AND CHARACTERIZATION OF VARIANT CFHD LYS-224 DEL.
RX PubMed=16612335; DOI=10.1038/sj.ki.5000269;
RA Licht C., Heinen S., Jozsi M., Loeschmann I., Saunders R.E., Perkins S.J.,
RA Waldherr R., Skerka C., Kirschfink M., Hoppe B., Zipfel P.F.;
RT "Deletion of Lys224 in regulatory domain 4 of factor H reveals a novel
RT pathomechanism for dense deposit disease (MPGN II).";
RL Kidney Int. 70:42-50(2006).
RN [48]
RP INTERACTION WITH WEST NILE VIRUS NON-STRUCTURAL PROTEIN 1.
RX PubMed=17132743; DOI=10.1073/pnas.0605668103;
RA Chung K.M., Liszewski M.K., Nybakken G., Davis A.E., Townsend R.R.,
RA Fremont D.H., Atkinson J.P., Diamond M.S.;
RT "West Nile virus nonstructural protein NS1 inhibits complement activation
RT by binding the regulatory protein factor H.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19111-19116(2006).
RN [49]
RP INVOLVEMENT IN BASAL LAMINAR DRUSEN, AND VARIANTS HIS-402; GLY-567;
RP ASP-936; TYR-1050 AND SER-1078.
RX PubMed=18252232; DOI=10.1016/j.ajhg.2007.11.007;
RA Boon C.J.F., Klevering B.J., Hoyng C.B., Zonneveld-Vrieling M.N.,
RA Nabuurs S.B., Blokland E., Cremers F.P.M., den Hollander A.I.;
RT "Basal laminar drusen caused by compound heterozygous variants in the CFH
RT gene.";
RL Am. J. Hum. Genet. 82:516-523(2008).
RN [50]
RP VARIANTS AHUS1 TYR-325; ILE-609; LEU-1169 AND CYS-1183, AND VARIANT
RP ASP-936.
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).
RN [51]
RP VARIANTS ILE-62; LYS-850; TYR-959 AND GLU-1143, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=22028381; DOI=10.1093/jmcb/mjr024;
RA Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X.,
RA Zeng R., Wu J.R.;
RT "Quantitative detection of single amino acid polymorphisms by targeted
RT proteomics.";
RL J. Mol. Cell Biol. 3:309-315(2011).
RN [52]
RP VARIANT ARMD4 CYS-1210.
RX PubMed=22019782; DOI=10.1038/ng.976;
RA Raychaudhuri S., Iartchouk O., Chin K., Tan P.L., Tai A.K., Ripke S.,
RA Gowrisankar S., Vemuri S., Montgomery K., Yu Y., Reynolds R., Zack D.J.,
RA Campochiaro B., Campochiaro P., Katsanis N., Daly M.J., Seddon J.M.;
RT "A rare penetrant mutation in CFH confers high risk of age-related macular
RT degeneration.";
RL Nat. Genet. 43:1232-1236(2011).
RN [53]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1107-1231, INTERACTION WITH C3B
RP AND GLYCOSAMINOGLYCANS, MUTAGENESIS OF ARG-1182; TRP-1183; LYS-1186;
RP LYS-1188 AND GLU-1198, AND DISULFIDE BOND.
RX PubMed=16601698; DOI=10.1038/sj.emboj.7601052;
RA Jokiranta T.S., Jaakola V.P., Lehtinen M.J., Paerepalo M., Meri S.,
RA Goldman A.;
RT "Structure of complement factor H carboxyl-terminus reveals molecular basis
RT of atypical haemolytic uremic syndrome.";
RL EMBO J. 25:1784-1794(2006).
RN [54]
RP STRUCTURE BY NMR OF 386-446, AND DISULFIDE BONDS.
RX PubMed=17360715; DOI=10.1074/jbc.m609636200;
RA Herbert A.P., Deakin J.A., Schmidt C.Q., Blaum B.S., Egan C.,
RA Ferreira V.P., Pangburn M.K., Lyon M., Uhrin D., Barlow P.N.;
RT "Structure shows that a glycosaminoglycan and protein recognition site in
RT factor H is perturbed by age-related macular degeneration-linked single
RT nucleotide polymorphism.";
RL J. Biol. Chem. 282:18960-18968(2007).
RN [55]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 322-506, INTERACTION WITH
RP GLYCOSAMINOGLYCANS, MUTAGENESIS OF HIS-337 AND ARG-341, AND DISULFIDE BOND.
RX PubMed=17893204; DOI=10.1084/jem.20071069;
RA Prosser B.E., Johnson S., Roversi P., Herbert A.P., Blaum B.S., Tyrrell J.,
RA Jowitt T.A., Clark S.J., Tarelli E., Uhrin D., Barlow P.N., Sim R.B.,
RA Day A.J., Lea S.M.;
RT "Structural basis for complement factor H linked age-related macular
RT degeneration.";
RL J. Exp. Med. 204:2277-2283(2007).
RN [56]
RP STRUCTURE BY NMR OF 20-206, FUNCTION, DOMAIN, AND DISULFIDE BOND.
RX PubMed=18252712; DOI=10.1074/jbc.m709587200;
RA Hocking H.G., Herbert A.P., Kavanagh D., Soares D.C., Ferreira V.P.,
RA Pangburn M.K., Uhrin D., Barlow P.N.;
RT "Structure of the N-terminal region of complement factor H and
RT conformational implications of disease-linked sequence variations.";
RL J. Biol. Chem. 283:9475-9487(2008).
RN [57]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 322-506, AND SUBUNIT.
RX PubMed=18005991; DOI=10.1016/j.jmb.2007.09.026;
RA Okemefuna A.I., Gilbert H.E., Griggs K.M., Ormsby R.J., Gordon D.L.,
RA Perkins S.J.;
RT "The regulatory SCR-1/5 and cell surface-binding SCR-16/20 fragments of
RT factor H reveal partially folded-back solution structures and different
RT self-associative properties.";
RL J. Mol. Biol. 375:80-101(2008).
RN [58]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 18-264, AND SUBUNIT.
RX PubMed=19505476; DOI=10.1016/j.jmb.2009.06.010;
RA Okemefuna A.I., Nan R., Gor J., Perkins S.J.;
RT "Electrostatic interactions contribute to the folded-back conformation of
RT wild type human factor H.";
RL J. Mol. Biol. 391:98-118(2009).
RN [59]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 18-264, INTERACTION WITH PROTEIN
RP C3B, FUNCTION, AND DISULFIDE BOND.
RX PubMed=19503104; DOI=10.1038/ni.1755;
RA Wu J., Wu Y.Q., Ricklin D., Janssen B.J., Lambris J.D., Gros P.;
RT "Structure of complement fragment C3b-factor H and implications for host
RT protection by complement regulators.";
RL Nat. Immunol. 10:728-733(2009).
RN [60]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 321-443, INTERACTION WITH
RP NEISSERIA MENINGITIDIS PROTEIN FHBP (MICROBIAL INFECTION), AND DISULFIDE
RP BOND.
RX PubMed=19225461; DOI=10.1038/nature07769;
RA Schneider M.C., Prosser B.E., Caesar J.J., Kugelberg E., Li S., Zhang Q.,
RA Quoraishi S., Lovett J.E., Deane J.E., Sim R.B., Roversi P., Johnson S.,
RA Tang C.M., Lea S.M.;
RT "Neisseria meningitidis recruits factor H using protein mimicry of host
RT carbohydrates.";
RL Nature 458:890-893(2009).
RN [61]
RP STRUCTURE BY NMR OF 690-804, AND DISULFIDE BONDS.
RX PubMed=19835885; DOI=10.1016/j.jmb.2009.10.010;
RA Schmidt C.Q., Herbert A.P., Mertens H.D., Guariento M., Soares D.C.,
RA Uhrin D., Rowe A.J., Svergun D.I., Barlow P.N.;
RT "The central portion of factor H (modules 10-15) is compact and contains a
RT structurally deviant CCP module.";
RL J. Mol. Biol. 395:105-122(2010).
RN [62]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1103-1231, INTERACTION WITH C3B
RP AND C3D, AND DISULFIDE BOND.
RX PubMed=20378178; DOI=10.1016/j.molimm.2010.03.007;
RA Bhattacharjee A., Lehtinen M.J., Kajander T., Goldman A., Jokiranta T.S.;
RT "Both domain 19 and domain 20 of factor H are involved in binding to
RT complement C3b and C3d.";
RL Mol. Immunol. 47:1686-1691(2010).
RN [63]
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 1103-1231, INTERACTION WITH C3B
RP AND C3D, FUNCTION, DOMAIN, AND DISULFIDE BOND.
RX PubMed=21285368; DOI=10.1073/pnas.1017087108;
RA Kajander T., Lehtinen M.J., Hyvaerinen S., Bhattacharjee A., Leung E.,
RA Isenman D.E., Meri S., Goldman A., Jokiranta T.S.;
RT "Dual interaction of factor H with C3d and glycosaminoglycans in host-
RT nonhost discrimination by complement.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2897-2902(2011).
RN [64]
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 321-443, INTERACTION WITH
RP NEISSERIA MENINGITIDIS PROTEIN FHBP (MICROBIAL INFECTION), AND DISULFIDE
RP BOND.
RX PubMed=23133374; DOI=10.1371/journal.ppat.1002981;
RA Johnson S., Tan L., van der Veen S., Caesar J., Goicoechea De Jorge E.,
RA Harding R.J., Bai X., Exley R.M., Ward P.N., Ruivo N., Trivedi K.,
RA Cumber E., Jones R., Newham L., Staunton D., Ufret-Vincenty R., Borrow R.,
RA Pickering M.C., Lea S.M., Tang C.M.;
RT "Design and evaluation of meningococcal vaccines through structure-based
RT modification of host and pathogen molecules.";
RL PLoS Pathog. 8:E1002981-E1002981(2012).
RN [65]
RP STRUCTURE BY NMR OF 566-687, AND DISULFIDE BONDS.
RX PubMed=23017427; DOI=10.1016/j.jmb.2012.09.013;
RA Makou E., Mertens H.D., Maciejewski M., Soares D.C., Matis I.,
RA Schmidt C.Q., Herbert A.P., Svergun D.I., Barlow P.N.;
RT "Solution structure of CCP modules 10-12 illuminates functional
RT architecture of the complement regulator, factor H.";
RL J. Mol. Biol. 424:295-312(2012).
RN [66]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1046-1231, AND DISULFIDE BONDS.
RX PubMed=22389686; DOI=10.1371/journal.pone.0032187;
RA Morgan H.P., Mertens H.D., Guariento M., Schmidt C.Q., Soares D.C.,
RA Svergun D.I., Herbert A.P., Barlow P.N., Hannan J.P.;
RT "Structural analysis of the C-terminal region (modules 18-20) of complement
RT regulator factor H (FH).";
RL PLoS ONE 7:e32187-e32187(2012).
RN [67]
RP X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 1103-1231, INTERACTION WITH
RP BORRELIA BURGDORFERI OUTER SURFACE PROTEIN E/OSPE (MICROBIA INFECTION), AND
RP DISULFIDE BOND.
RX PubMed=23658013; DOI=10.1074/jbc.m113.459040;
RA Bhattacharjee A., Oeemig J.S., Kolodziejczyk R., Meri T., Kajander T.,
RA Lehtinen M.J., Iwai H., Jokiranta T.S., Goldman A.;
RT "Structural basis for complement evasion by Lyme disease pathogen Borrelia
RT burgdorferi.";
RL J. Biol. Chem. 288:18685-18695(2013).
RN [68]
RP INTERACTION WITH C.ALBICANS GPD2 (MICROBIAL INFECTION).
RX PubMed=23204165; DOI=10.1093/infdis/jis718;
RA Luo S., Hoffmann R., Skerka C., Zipfel P.F.;
RT "Glycerol-3-phosphate dehydrogenase 2 is a novel factor H-, factor H-like
RT protein 1-, and plasminogen-binding surface protein of Candida albicans.";
RL J. Infect. Dis. 207:594-603(2013).
RN [69]
RP X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF 508-567, INTERACTION WITH
RP STREPTOCOCCUS PNEUMONIAE PROTEIN VIRULENCE FACTOR CHOLINE-BINDING PROTEIN
RP A/CBPAN (MICROBIAL INFECTION), AND DISULFIDE BOND.
RX PubMed=25330773; DOI=10.1042/bj20141069;
RA Achila D., Liu A., Banerjee R., Li Y., Martinez-Hackert E., Zhang J.R.,
RA Yan H.;
RT "Structural determinants of host specificity of complement Factor H
RT recruitment by Streptococcus pneumoniae.";
RL Biochem. J. 465:325-335(2015).
RN [70]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1107-1231, FUNCTION, AND
RP DISULFIDE BOND.
RX PubMed=25402769; DOI=10.1038/nchembio.1696;
RA Blaum B.S., Hannan J.P., Herbert A.P., Kavanagh D., Uhrin D., Stehle T.;
RT "Structural basis for sialic acid-mediated self-recognition by complement
RT factor H.";
RL Nat. Chem. Biol. 11:77-82(2015).
RN [71]
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1206-1226, AND INTERACTION WITH
RP STAPHYLOCOCCUS AUREUS SURFACE PROTEIN SERINE-ASPARTATE REPEAT PROTEIN
RP E/SDRE (MICROBIAL INFECTION).
RX PubMed=28258151; DOI=10.1042/bcj20170085;
RA Zhang Y., Wu M., Hang T., Wang C., Yang Y., Pan W., Zang J., Zhang M.,
RA Zhang X.;
RT "Staphylococcus aureus SdrE captures complement factor H's C-terminus via a
RT novel 'close, dock, lock and latch' mechanism for complement evasion.";
RL Biochem. J. 474:1619-1631(2017).
RN [72]
RP X-RAY CRYSTALLOGRAPHY (4.20 ANGSTROMS) OF 19-388 IN COMPLEX WITH CFH AND
RP C3B, DISULFIDE BONDS, AND FUNCTION.
RX PubMed=28671664; DOI=10.1038/nsmb.3427;
RA Xue X., Wu J., Ricklin D., Forneris F., Di Crescenzio P., Schmidt C.Q.,
RA Granneman J., Sharp T.H., Lambris J.D., Gros P.;
RT "Regulator-dependent mechanisms of C3b processing by factor I allow
RT differentiation of immune responses.";
RL Nat. Struct. Mol. Biol. 24:643-651(2017).
RN [73]
RP X-RAY CRYSTALLOGRAPHY (3.18 ANGSTROMS) OF 1104-1230, INTERACTION WITH CD3D
RP AND BORRELIA BURGDORFERI OUTER SURFACE PROTEIN E/OSPE (MICROBIA INFECTION),
RP AND DISULFIDE BOND.
RX PubMed=29190743; DOI=10.1371/journal.pone.0188127;
RA Kolodziejczyk R., Mikula K.M., Kotila T., Postis V.L.G., Jokiranta T.S.,
RA Goldman A., Meri T.;
RT "Crystal structure of a tripartite complex between C3dg, C-terminal domains
RT of factor H and OspE of Borrelia burgdorferi.";
RL PLoS ONE 12:E0188127-E0188127(2017).
RN [74]
RP INTERACTION WITH C.ALBICANS GPD2 (MICROBIAL INFECTION).
RX PubMed=34986357; DOI=10.1016/j.celrep.2021.110183;
RA Kumwenda P., Cottier F., Hendry A.C., Kneafsey D., Keevan B., Gallagher H.,
RA Tsai H.J., Hall R.A.;
RT "Estrogen promotes innate immune evasion of Candida albicans through
RT inactivation of the alternative complement system.";
RL Cell Rep. 38:110183-110183(2022).
CC -!- FUNCTION: Glycoprotein that plays an essential role in maintaining a
CC well-balanced immune response by modulating complement activation. Acts
CC as a soluble inhibitor of complement, where its binding to self markers
CC such as glycan structures prevents complement activation and
CC amplification on cell surfaces (PubMed:21285368, PubMed:25402769).
CC Accelerates the decay of the complement alternative pathway (AP) C3
CC convertase C3bBb, thus preventing local formation of more C3b, the
CC central player of the complement amplification loop (PubMed:19503104,
CC PubMed:26700768). As a cofactor of the serine protease factor I, CFH
CC also regulates proteolytic degradation of already-deposited C3b
CC (PubMed:18252712, PubMed:28671664). In addition, mediates several
CC cellular responses through interaction with specific receptors. For
CC example, interacts with CR3/ITGAM receptor and thereby mediates the
CC adhesion of human neutrophils to different pathogens. In turn, these
CC pathogens are phagocytosed and destroyed (PubMed:9558116,
CC PubMed:20008295). {ECO:0000269|PubMed:18252712,
CC ECO:0000269|PubMed:19503104, ECO:0000269|PubMed:20008295,
CC ECO:0000269|PubMed:21285368, ECO:0000269|PubMed:25402769,
CC ECO:0000269|PubMed:26700768, ECO:0000269|PubMed:28671664,
CC ECO:0000269|PubMed:9558116}.
CC -!- SUBUNIT: Homodimer (PubMed:18005991, PubMed:19505476). Forms also
CC homooligomers (PubMed:19505476). Interacts with complement protein C3b;
CC this interaction inhibits complement activation (PubMed:16601698,
CC PubMed:19503104, PubMed:20378178, PubMed:21285368, PubMed:28671664).
CC Interacts with complement protein C3d (PubMed:20378178,
CC PubMed:21285368, PubMed:29190743). Interacts with CR3/ITGAM; this
CC interaction mediates adhesion of neutrophils to pathogens leading to
CC pathogen clearance (PubMed:9558116, PubMed:20008295). Interacts with
CC complement factor I (PubMed:28671664). {ECO:0000269|PubMed:16601698,
CC ECO:0000269|PubMed:18005991, ECO:0000269|PubMed:19503104,
CC ECO:0000269|PubMed:19505476, ECO:0000269|PubMed:20008295,
CC ECO:0000269|PubMed:20378178, ECO:0000269|PubMed:21285368,
CC ECO:0000269|PubMed:28671664, ECO:0000269|PubMed:29190743,
CC ECO:0000269|PubMed:9558116}.
CC -!- SUBUNIT: (Microbial infection) Interacts with West nile virus non-
CC structural protein 1 (NS1); this interaction leads to the degradation
CC of C3. {ECO:0000269|PubMed:17132743}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.albicans GPD2; the
CC interaction is direct and leads to the degradation of C3 which enables
CC the pathogen to evade the host innate immune system.
CC {ECO:0000269|PubMed:23204165, ECO:0000269|PubMed:34986357}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Neisseria meningitidis
CC protein fHbp. {ECO:0000269|PubMed:19225461,
CC ECO:0000269|PubMed:23133374}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Borrelia burgdorferi
CC outer surface protein E/OspE; this interaction recruits complement
CC regulator factor H onto the bacterial surface to evade complement-
CC mediated cell lysis. {ECO:0000269|PubMed:23658013,
CC ECO:0000269|PubMed:29190743}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Streptococcus pneumoniae
CC protein virulence factor choline-binding protein A/CbpAN; this
CC interaction enables Streptococcus pneumoniae to evade surveillance by
CC human complement system. {ECO:0000269|PubMed:25330773}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC surface protein serine-aspartate repeat protein E/SdrE; this
CC interaction sequesters CFH on the surface of S. aureus for complement
CC evasion. {ECO:0000269|PubMed:28258151}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC protein Sbi; this interaction inhibits the complement activation of the
CC alternative pathway. {ECO:0000269|PubMed:19112495}.
CC -!- SUBUNIT: [Isoform 1]: (Microbial infection) Interacts (via sushi 4-6
CC domains) with P.falciparum surface protein PF92; the interaction
CC recruits CFH onto the merozoite surface preventing complement-mediated
CC cell lysis (PubMed:26700768). The interaction does not affect CFH
CC activity (PubMed:26700768). {ECO:0000269|PubMed:26700768}.
CC -!- SUBUNIT: [Isoform 2]: (Microbial infection) Interacts (via sushi 4-6
CC domains) with P.falciparum surface protein PF92; the interaction
CC recruits FHL-1 isoform onto the merozoite surface preventing
CC complement-mediated cell lysis (PubMed:26700768). The interaction does
CC not affect FHL-1 isoform activity (PubMed:26700768).
CC {ECO:0000269|PubMed:26700768}.
CC -!- INTERACTION:
CC P08603; P02649: APOE; NbExp=8; IntAct=EBI-1223708, EBI-1222467;
CC P08603; P01024: C3; NbExp=6; IntAct=EBI-1223708, EBI-905851;
CC P08603; PRO_0000005908 [P01024]: C3; NbExp=4; IntAct=EBI-1223708, EBI-6863145;
CC P08603; PRO_0000005915 [P01024]: C3; NbExp=2; IntAct=EBI-1223708, EBI-6863106;
CC P08603; P08603: CFH; NbExp=5; IntAct=EBI-1223708, EBI-1223708;
CC P08603; P02741: CRP; NbExp=39; IntAct=EBI-1223708, EBI-1395983;
CC P08603; PRO_0000023526 [P02741]: CRP; NbExp=3; IntAct=EBI-1223708, EBI-22033103;
CC P08603; P26022: PTX3; NbExp=15; IntAct=EBI-1223708, EBI-11574553;
CC P08603; PRO_0000023545 [P26022]: PTX3; NbExp=8; IntAct=EBI-1223708, EBI-22114950;
CC P08603; P02769: ALB; Xeno; NbExp=10; IntAct=EBI-1223708, EBI-2296927;
CC P08603; P16946: ennX; Xeno; NbExp=2; IntAct=EBI-1223708, EBI-6403567;
CC P08603; P13605: FMOD; Xeno; NbExp=4; IntAct=EBI-1223708, EBI-5281124;
CC P08603; A0A024A2C9: lph; Xeno; NbExp=6; IntAct=EBI-1223708, EBI-12498321;
CC P08603; Q9JXV4: NMB1870; Xeno; NbExp=6; IntAct=EBI-1223708, EBI-15758684;
CC P08603; Q932F7: sdrE; Xeno; NbExp=4; IntAct=EBI-1223708, EBI-26369465;
CC P08603-1; P02741: CRP; NbExp=3; IntAct=EBI-22027829, EBI-1395983;
CC P08603-2; P02741: CRP; NbExp=8; IntAct=EBI-12684810, EBI-1395983;
CC P08603-2; P26022: PTX3; NbExp=2; IntAct=EBI-12684810, EBI-11574553;
CC P08603-2; PRO_0000023545 [P26022]: PTX3; NbExp=2; IntAct=EBI-12684810, EBI-22114950;
CC PRO_0000005894; P02741: CRP; NbExp=5; IntAct=EBI-22114230, EBI-1395983;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P08603-1; Sequence=Displayed;
CC Name=2; Synonyms=FHL-1;
CC IsoId=P08603-2; Sequence=VSP_001190, VSP_001191;
CC -!- TISSUE SPECIFICITY: Expressed in the retinal pigment epithelium (at
CC protein level) (PubMed:25136834). CFH is one of the most abundant
CC complement components in blood where the liver is the major source of
CC CFH protein in vivo. in addition, CFH is secreted by additional cell
CC types including monocytes, fibroblasts, or endothelial cells
CC (PubMed:6444659, PubMed:2968404, PubMed:2139673, PubMed:25136834).
CC {ECO:0000269|PubMed:2139673, ECO:0000269|PubMed:25136834,
CC ECO:0000269|PubMed:2968404, ECO:0000269|PubMed:6444659}.
CC -!- DOMAIN: Sushi 1-3 domain represents the minimal unit capable of
CC cofactor activity (PubMed:18252712). The property to discriminate self
CC surfaces from non-self surfaces depends on the C-terminal region made
CC of Sushis 19-20 (PubMed:21285368). {ECO:0000269|PubMed:18252712,
CC ECO:0000269|PubMed:21285368}.
CC -!- PTM: Sulfated on tyrosine residues. {ECO:0000269|PubMed:25136834}.
CC -!- DISEASE: Basal laminar drusen (BLD) [MIM:126700]: Drusen are
CC extracellular deposits that accumulate below the retinal pigment
CC epithelium on Bruch membrane. Basal laminar drusen refers to an early
CC adult-onset drusen phenotype that shows a pattern of uniform small,
CC slightly raised yellow subretinal nodules randomly scattered in the
CC macula. In later stages, these drusen often become more numerous, with
CC clustered groups of drusen scattered throughout the retina. In time
CC these small basal laminar drusen may expand and ultimately lead to a
CC serous pigment epithelial detachment of the macula that may result in
CC vision loss. {ECO:0000269|PubMed:18252232}. Note=The gene represented
CC in this entry is involved in disease pathogenesis.
CC -!- DISEASE: Complement factor H deficiency (CFHD) [MIM:609814]: A disorder
CC that can manifest as several different phenotypes, including
CC asymptomatic, recurrent bacterial infections, and renal failure.
CC Laboratory features usually include decreased serum levels of factor H,
CC complement component C3, and a decrease in other terminal complement
CC components, indicating activation of the alternative complement
CC pathway. It is associated with a number of renal diseases with variable
CC clinical presentation and progression, including membranoproliferative
CC glomerulonephritis and atypical hemolytic uremic syndrome.
CC {ECO:0000269|PubMed:10803850, ECO:0000269|PubMed:11158219,
CC ECO:0000269|PubMed:11170895, ECO:0000269|PubMed:11170896,
CC ECO:0000269|PubMed:12020532, ECO:0000269|PubMed:14978182,
CC ECO:0000269|PubMed:16612335, ECO:0000269|PubMed:9312129}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Hemolytic uremic syndrome atypical 1 (AHUS1) [MIM:235400]: 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:10577907, ECO:0000269|PubMed:10762557,
CC ECO:0000269|PubMed:11851332, ECO:0000269|PubMed:12960213,
CC ECO:0000269|PubMed:14583443, ECO:0000269|PubMed:14978182,
CC ECO:0000269|PubMed:20513133, ECO:0000269|PubMed:9551389}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry. Other genes may play a role in modifying the
CC phenotype.
CC -!- DISEASE: Macular degeneration, age-related, 4 (ARMD4) [MIM:610698]: 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:22019782}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- CAUTION: According to a report, Asn-217 is not glycosylated
CC (PubMed:17591618). Another study observed glycosylation at this
CC position (PubMed:19139490). {ECO:0000305|PubMed:17591618,
CC ECO:0000305|PubMed:19139490}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41739.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=CFHbase; Note=CFH mutation db;
CC URL="http://structure.bmc.lu.se/idbase/CFHbase/";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/cfh/";
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; Y00716; CAA68704.1; -; mRNA.
DR EMBL; DQ233256; ABB02180.1; -; Genomic_DNA.
DR EMBL; AL049744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037285; AAH37285.1; -; mRNA.
DR EMBL; BC110643; AAI10644.1; -; mRNA.
DR EMBL; BC142699; AAI42700.1; -; mRNA.
DR EMBL; X04697; CAB41739.1; ALT_FRAME; mRNA.
DR EMBL; X07523; CAA30403.1; -; mRNA.
DR EMBL; M12383; AAA52013.1; -; mRNA.
DR EMBL; M65294; AAA35948.1; -; mRNA.
DR EMBL; U56979; AAB01987.1; -; Genomic_DNA.
DR EMBL; Z29665; CAA82763.1; -; Genomic_DNA.
DR CCDS; CCDS1385.1; -. [P08603-1]
DR CCDS; CCDS53452.1; -. [P08603-2]
DR PIR; S00254; NBHUH.
DR PIR; S03013; NBHUHS.
DR RefSeq; NP_000177.2; NM_000186.3.
DR PDB; 1HAQ; X-ray; -; A=19-1231.
DR PDB; 1HCC; NMR; -; A=927-985.
DR PDB; 1HFH; NMR; -; A=866-985.
DR PDB; 1HFI; NMR; -; A=866-927.
DR PDB; 2BZM; NMR; -; A=1107-1231.
DR PDB; 2G7I; X-ray; 1.75 A; A=1107-1231.
DR PDB; 2IC4; X-ray; -; A=321-506.
DR PDB; 2JGW; NMR; -; A=386-446.
DR PDB; 2JGX; NMR; -; A=386-446.
DR PDB; 2KMS; NMR; -; A=690-804.
DR PDB; 2QFG; X-ray; -; A=19-322.
DR PDB; 2QFH; X-ray; -; A=928-1231.
DR PDB; 2RLP; NMR; -; A=20-142.
DR PDB; 2RLQ; NMR; -; A=84-206.
DR PDB; 2UWN; X-ray; 2.35 A; A=322-506.
DR PDB; 2V8E; X-ray; 2.50 A; A=322-506.
DR PDB; 2W80; X-ray; 2.35 A; A/B/E/G=321-443.
DR PDB; 2W81; X-ray; 2.35 A; A/B/E=321-443.
DR PDB; 2WII; X-ray; 2.70 A; C=18-264.
DR PDB; 2XQW; X-ray; 2.31 A; C=1103-1231.
DR PDB; 3GAU; X-ray; -; A=19-1231.
DR PDB; 3GAV; X-ray; -; A=19-1231.
DR PDB; 3GAW; X-ray; -; A=19-1231.
DR PDB; 3KXV; X-ray; 2.00 A; A=1103-1231.
DR PDB; 3KZJ; X-ray; 1.65 A; A=1103-1231.
DR PDB; 3OXU; X-ray; 2.10 A; D/E/F=1107-1231.
DR PDB; 3R62; X-ray; 1.52 A; A/B=1107-1231.
DR PDB; 3RJ3; X-ray; 2.35 A; D/E/F=1107-1231.
DR PDB; 3SW0; X-ray; 1.80 A; X=1046-1231.
DR PDB; 4AYD; X-ray; 2.40 A; A/B/E=321-443.
DR PDB; 4AYE; X-ray; 2.80 A; A/B/E=321-443.
DR PDB; 4AYI; X-ray; 2.31 A; A/E=321-443.
DR PDB; 4AYM; X-ray; 3.00 A; A/B/E/F=321-443.
DR PDB; 4B2R; NMR; -; A=566-687.
DR PDB; 4B2S; NMR; -; A=627-747.
DR PDB; 4J38; X-ray; 2.83 A; B=1103-1231.
DR PDB; 4K12; X-ray; 1.08 A; A=508-567.
DR PDB; 4ONT; X-ray; 2.15 A; D/E/F=1107-1231.
DR PDB; 4ZH1; X-ray; 2.24 A; D/E/F=1107-1231.
DR PDB; 5NBQ; X-ray; 3.18 A; D/E/F=1104-1230.
DR PDB; 5O32; X-ray; 4.21 A; C/G=19-387.
DR PDB; 5O35; X-ray; 4.20 A; C=19-388.
DR PDB; 5WTB; X-ray; 3.30 A; E/F/G/H=1206-1226.
DR PDB; 6ATG; X-ray; 1.80 A; A/D=388-446.
DR PDB; 6ZH1; X-ray; 2.20 A; B=1104-1231.
DR PDBsum; 1HAQ; -.
DR PDBsum; 1HCC; -.
DR PDBsum; 1HFH; -.
DR PDBsum; 1HFI; -.
DR PDBsum; 2BZM; -.
DR PDBsum; 2G7I; -.
DR PDBsum; 2IC4; -.
DR PDBsum; 2JGW; -.
DR PDBsum; 2JGX; -.
DR PDBsum; 2KMS; -.
DR PDBsum; 2QFG; -.
DR PDBsum; 2QFH; -.
DR PDBsum; 2RLP; -.
DR PDBsum; 2RLQ; -.
DR PDBsum; 2UWN; -.
DR PDBsum; 2V8E; -.
DR PDBsum; 2W80; -.
DR PDBsum; 2W81; -.
DR PDBsum; 2WII; -.
DR PDBsum; 2XQW; -.
DR PDBsum; 3GAU; -.
DR PDBsum; 3GAV; -.
DR PDBsum; 3GAW; -.
DR PDBsum; 3KXV; -.
DR PDBsum; 3KZJ; -.
DR PDBsum; 3OXU; -.
DR PDBsum; 3R62; -.
DR PDBsum; 3RJ3; -.
DR PDBsum; 3SW0; -.
DR PDBsum; 4AYD; -.
DR PDBsum; 4AYE; -.
DR PDBsum; 4AYI; -.
DR PDBsum; 4AYM; -.
DR PDBsum; 4B2R; -.
DR PDBsum; 4B2S; -.
DR PDBsum; 4J38; -.
DR PDBsum; 4K12; -.
DR PDBsum; 4ONT; -.
DR PDBsum; 4ZH1; -.
DR PDBsum; 5NBQ; -.
DR PDBsum; 5O32; -.
DR PDBsum; 5O35; -.
DR PDBsum; 5WTB; -.
DR PDBsum; 6ATG; -.
DR PDBsum; 6ZH1; -.
DR AlphaFoldDB; P08603; -.
DR SMR; P08603; -.
DR BioGRID; 109324; 40.
DR ComplexPortal; CPX-6163; Complement factor H complex.
DR ComplexPortal; CPX-6164; Complement factor I-H-C3b complex.
DR DIP; DIP-38303N; -.
DR IntAct; P08603; 31.
DR MINT; P08603; -.
DR STRING; 9606.ENSP00000356399; -.
DR BindingDB; P08603; -.
DR ChEMBL; CHEMBL4629; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR CarbonylDB; P08603; -.
DR GlyConnect; 722; 37 N-Linked glycans (9 sites).
DR GlyGen; P08603; 9 sites, 62 N-linked glycans (9 sites).
DR iPTMnet; P08603; -.
DR PhosphoSitePlus; P08603; -.
DR BioMuta; CFH; -.
DR DMDM; 158517847; -.
DR CPTAC; non-CPTAC-2658; -.
DR EPD; P08603; -.
DR jPOST; P08603; -.
DR MassIVE; P08603; -.
DR MaxQB; P08603; -.
DR PaxDb; P08603; -.
DR PeptideAtlas; P08603; -.
DR PRIDE; P08603; -.
DR ProteomicsDB; 52135; -. [P08603-1]
DR ProteomicsDB; 52136; -. [P08603-2]
DR ABCD; P08603; 11 sequenced antibodies.
DR Antibodypedia; 3393; 950 antibodies from 47 providers.
DR DNASU; 3075; -.
DR Ensembl; ENST00000367429.9; ENSP00000356399.4; ENSG00000000971.16.
DR GeneID; 3075; -.
DR KEGG; hsa:3075; -.
DR UCSC; uc001gtj.4; human. [P08603-1]
DR CTD; 3075; -.
DR DisGeNET; 3075; -.
DR GeneCards; CFH; -.
DR GeneReviews; CFH; -.
DR HGNC; HGNC:4883; CFH.
DR HPA; ENSG00000000971; Tissue enriched (liver).
DR MalaCards; CFH; -.
DR MIM; 126700; phenotype.
DR MIM; 134370; gene.
DR MIM; 235400; phenotype.
DR MIM; 609814; phenotype.
DR MIM; 610698; phenotype.
DR neXtProt; NX_P08603; -.
DR Orphanet; 544472; Atypical hemolytic uremic syndrome with complement gene abnormality.
DR Orphanet; 244275; De novo thrombotic microangiopathy after kidney transplantation.
DR Orphanet; 93571; Dense deposit disease.
DR Orphanet; 75376; Familial drusen.
DR Orphanet; 244242; HELLP syndrome.
DR Orphanet; 200421; Immunodeficiency with factor H anomaly.
DR Orphanet; 329903; Immunoglobulin-mediated membranoproliferative glomerulonephritis.
DR Orphanet; 279; NON RARE IN EUROPE: Age-related macular degeneration.
DR PharmGKB; PA29261; -.
DR VEuPathDB; HostDB:ENSG00000000971; -.
DR eggNOG; ENOG502QVSB; Eukaryota.
DR HOGENOM; CLU_003511_0_0_1; -.
DR InParanoid; P08603; -.
DR OrthoDB; 296899at2759; -.
DR PhylomeDB; P08603; -.
DR TreeFam; TF326157; -.
DR PathwayCommons; P08603; -.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SignaLink; P08603; -.
DR SIGNOR; P08603; -.
DR BioGRID-ORCS; 3075; 9 hits in 1073 CRISPR screens.
DR ChiTaRS; CFH; human.
DR EvolutionaryTrace; P08603; -.
DR GeneWiki; Factor_H; -.
DR GenomeRNAi; 3075; -.
DR Pharos; P08603; Tbio.
DR PRO; PR:P08603; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P08603; protein.
DR Bgee; ENSG00000000971; Expressed in urethra and 189 other tissues.
DR ExpressionAtlas; P08603; baseline and differential.
DR Genevisible; P08603; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IPI:ComplexPortal.
DR GO; GO:0001851; F:complement component C3b binding; IBA:GO_Central.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006956; P:complement activation; IDA:AgBase.
DR GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
DR GO; GO:0030449; P:regulation of complement activation; IDA:MGI.
DR GO; GO:0030451; P:regulation of complement activation, alternative pathway; IDA:ComplexPortal.
DR GO; GO:1903659; P:regulation of complement-dependent cytotoxicity; IDA:MGI.
DR CDD; cd00033; CCP; 16.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 19.
DR SMART; SM00032; CCP; 20.
DR SUPFAM; SSF57535; SSF57535; 18.
DR PROSITE; PS50923; SUSHI; 19.
PE 1: Evidence at protein level;
KW 3D-structure; Age-related macular degeneration; Alternative splicing;
KW Complement alternate pathway; Direct protein sequencing; Disease variant;
KW Disulfide bond; Glycoprotein; Hemolytic uremic syndrome;
KW Host-virus interaction; Immunity; Innate immunity; Reference proteome;
KW Repeat; Secreted; Signal; Sulfation; Sushi.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:6215918"
FT CHAIN 19..1231
FT /note="Complement factor H"
FT /id="PRO_0000005894"
FT DOMAIN 19..82
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 83..143
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 144..207
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 208..264
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 265..322
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 324..386
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 387..444
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 446..507
FT /note="Sushi 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 515..566
FT /note="Sushi 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 567..625
FT /note="Sushi 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 628..686
FT /note="Sushi 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 689..746
FT /note="Sushi 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 751..805
FT /note="Sushi 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 809..866
FT /note="Sushi 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 868..928
FT /note="Sushi 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 929..986
FT /note="Sushi 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 987..1045
FT /note="Sushi 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1046..1104
FT /note="Sushi 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1107..1165
FT /note="Sushi 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1170..1230
FT /note="Sushi 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:17591618, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:2963625"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17591618"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17591618,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17591618"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:17591618, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169"
FT CARBOHYD 911
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:17591618, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 1029
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:17591618,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218"
FT CARBOHYD 1095
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17591618"
FT DISULFID 21..66
FT /evidence="ECO:0000269|PubMed:18252712,
FT ECO:0000269|PubMed:19503104, ECO:0000269|PubMed:28671664"
FT DISULFID 52..80
FT /evidence="ECO:0000269|PubMed:18252712,
FT ECO:0000269|PubMed:19503104, ECO:0000269|PubMed:28671664"
FT DISULFID 85..129
FT /evidence="ECO:0000269|PubMed:18252712,
FT ECO:0000269|PubMed:19503104, ECO:0000269|PubMed:28671664"
FT DISULFID 114..141
FT /evidence="ECO:0000269|PubMed:18252712,
FT ECO:0000269|PubMed:19503104, ECO:0000269|PubMed:28671664"
FT DISULFID 146..192
FT /evidence="ECO:0000269|PubMed:19503104,
FT ECO:0000269|PubMed:28671664"
FT DISULFID 178..205
FT /evidence="ECO:0000269|PubMed:19503104,
FT ECO:0000269|PubMed:28671664"
FT DISULFID 210..251
FT /evidence="ECO:0000269|PubMed:19503104,
FT ECO:0000269|PubMed:28671664"
FT DISULFID 237..262
FT /evidence="ECO:0000269|PubMed:19503104,
FT ECO:0000269|PubMed:28671664"
FT DISULFID 267..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 294..320
FT /evidence="ECO:0000269|PubMed:28671664"
FT DISULFID 325..374
FT /evidence="ECO:0000269|PubMed:17893204,
FT ECO:0000269|PubMed:19225461, ECO:0000269|PubMed:23133374,
FT ECO:0000269|PubMed:28671664"
FT DISULFID 357..385
FT /evidence="ECO:0000269|PubMed:17893204,
FT ECO:0000269|PubMed:19225461, ECO:0000269|PubMed:23133374,
FT ECO:0000269|PubMed:28671664"
FT DISULFID 389..431
FT /evidence="ECO:0000269|PubMed:17360715,
FT ECO:0000269|PubMed:17893204, ECO:0000269|PubMed:19225461,
FT ECO:0000269|PubMed:23133374"
FT DISULFID 416..442
FT /evidence="ECO:0000269|PubMed:17360715,
FT ECO:0000269|PubMed:17893204, ECO:0000269|PubMed:19225461,
FT ECO:0000269|PubMed:23133374"
FT DISULFID 448..494
FT /evidence="ECO:0000269|PubMed:17893204"
FT DISULFID 477..505
FT /evidence="ECO:0000269|PubMed:17893204"
FT DISULFID 509..553
FT /evidence="ECO:0000269|PubMed:25330773"
FT DISULFID 536..564
FT /evidence="ECO:0000269|PubMed:25330773"
FT DISULFID 569..611
FT /evidence="ECO:0000269|PubMed:23017427"
FT DISULFID 597..623
FT /evidence="ECO:0000269|PubMed:23017427"
FT DISULFID 630..673
FT /evidence="ECO:0000269|PubMed:23017427"
FT DISULFID 659..684
FT /evidence="ECO:0000269|PubMed:23017427"
FT DISULFID 691..733
FT /evidence="ECO:0000269|PubMed:19835885,
FT ECO:0000269|PubMed:23017427"
FT DISULFID 719..744
FT /evidence="ECO:0000269|PubMed:19835885,
FT ECO:0000269|PubMed:23017427"
FT DISULFID 753..792
FT /evidence="ECO:0000269|PubMed:19835885"
FT DISULFID 781..803
FT /evidence="ECO:0000269|PubMed:19835885"
FT DISULFID 811..853
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 839..864
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 870..915
FT /evidence="ECO:0000269|PubMed:8331663"
FT DISULFID 901..926
FT /evidence="ECO:0000269|PubMed:8331663"
FT DISULFID 931..973
FT /evidence="ECO:0000269|PubMed:1829116,
FT ECO:0000269|PubMed:8331663"
FT DISULFID 959..984
FT /evidence="ECO:0000269|PubMed:1829116,
FT ECO:0000269|PubMed:8331663"
FT DISULFID 989..1032
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1018..1043
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1048..1091
FT /evidence="ECO:0000269|PubMed:22389686"
FT DISULFID 1077..1102
FT /evidence="ECO:0000269|PubMed:22389686"
FT DISULFID 1109..1152
FT /evidence="ECO:0000269|PubMed:16601698,
FT ECO:0000269|PubMed:20378178, ECO:0000269|PubMed:21285368,
FT ECO:0000269|PubMed:22389686, ECO:0000269|PubMed:23658013,
FT ECO:0000269|PubMed:25402769, ECO:0000269|PubMed:29190743"
FT DISULFID 1138..1163
FT /evidence="ECO:0000269|PubMed:16601698,
FT ECO:0000269|PubMed:20378178, ECO:0000269|PubMed:21285368,
FT ECO:0000269|PubMed:22389686, ECO:0000269|PubMed:23658013,
FT ECO:0000269|PubMed:25402769, ECO:0000269|PubMed:29190743"
FT DISULFID 1167..1218
FT /evidence="ECO:0000269|PubMed:16601698,
FT ECO:0000269|PubMed:20378178, ECO:0000269|PubMed:21285368,
FT ECO:0000269|PubMed:22389686, ECO:0000269|PubMed:23658013,
FT ECO:0000269|PubMed:25402769, ECO:0000269|PubMed:29190743"
FT DISULFID 1201..1228
FT /evidence="ECO:0000269|PubMed:16601698,
FT ECO:0000269|PubMed:20378178, ECO:0000269|PubMed:21285368,
FT ECO:0000269|PubMed:22389686, ECO:0000269|PubMed:23658013,
FT ECO:0000269|PubMed:25402769, ECO:0000269|PubMed:29190743"
FT VAR_SEQ 446..449
FT /note="KTCS -> SFTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2963625"
FT /id="VSP_001190"
FT VAR_SEQ 450..1231
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2963625"
FT /id="VSP_001191"
FT VARIANT 62
FT /note="V -> I (confirmed at protein level; dbSNP:rs800292)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15870199, ECO:0000269|PubMed:22028381,
FT ECO:0000269|Ref.2"
FT /id="VAR_023836"
FT VARIANT 78
FT /note="R -> G (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:14583443"
FT /id="VAR_025864"
FT VARIANT 127
FT /note="R -> L (in CFHD; with membranoproliferative
FT glomerulonephritis; dbSNP:rs121913058)"
FT /evidence="ECO:0000269|PubMed:14978182"
FT /id="VAR_031978"
FT VARIANT 224
FT /note="Missing (in CFHD; with membranoproliferative
FT glomerulonephritis; affects binding of factor H to C3b and
FT shows defective complement regulation)"
FT /evidence="ECO:0000269|PubMed:16612335"
FT /id="VAR_031979"
FT VARIANT 325
FT /note="C -> Y (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063648"
FT VARIANT 400
FT /note="Q -> K (in AHUS1; dbSNP:rs201671665)"
FT /evidence="ECO:0000269|PubMed:14978182"
FT /id="VAR_031980"
FT VARIANT 402
FT /note="Y -> H (associated with ARMD4; dbSNP:rs1061170)"
FT /evidence="ECO:0000269|PubMed:15870199,
FT ECO:0000269|PubMed:15895326, ECO:0000269|PubMed:16710414,
FT ECO:0000269|PubMed:18252232, ECO:0000269|PubMed:2963625"
FT /id="VAR_001979"
FT VARIANT 431
FT /note="C -> S (in CFHD; with membranoproliferative
FT glomerulonephritis; dbSNP:rs121913056)"
FT /evidence="ECO:0000269|PubMed:14978182"
FT /id="VAR_031981"
FT VARIANT 493
FT /note="T -> R (in dbSNP:rs1061171)"
FT /evidence="ECO:0000269|PubMed:2963625"
FT /id="VAR_043892"
FT VARIANT 536
FT /note="C -> R (in CFHD; dbSNP:rs121913052)"
FT /evidence="ECO:0000269|PubMed:9312129"
FT /id="VAR_019405"
FT VARIANT 551
FT /note="I -> T (in dbSNP:rs35453854)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025092"
FT VARIANT 567
FT /note="R -> G (associated with basal laminar drusen;
FT dbSNP:rs757756991)"
FT /evidence="ECO:0000269|PubMed:18252232"
FT /id="VAR_043893"
FT VARIANT 609
FT /note="V -> I (in AHUS1; dbSNP:rs148165372)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063649"
FT VARIANT 630
FT /note="C -> W (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:12960213"
FT /id="VAR_025865"
FT VARIANT 673
FT /note="C -> S (in CFHD; with membranoproliferative
FT glomerulonephritis)"
FT /evidence="ECO:0000269|PubMed:14978182"
FT /id="VAR_031982"
FT VARIANT 673
FT /note="C -> Y (in AHUS1; dbSNP:rs1391815797)"
FT /evidence="ECO:0000269|PubMed:14978182"
FT /id="VAR_031983"
FT VARIANT 850
FT /note="E -> K (in AHUS1; variant confirmed at protein
FT level; dbSNP:rs762443267)"
FT /evidence="ECO:0000269|PubMed:12960213,
FT ECO:0000269|PubMed:22028381"
FT /id="VAR_025866"
FT VARIANT 890
FT /note="S -> I (in dbSNP:rs515299)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025093"
FT VARIANT 893
FT /note="H -> R (in AHUS1; dbSNP:rs1573076722)"
FT /evidence="ECO:0000269|PubMed:14978182"
FT /id="VAR_031984"
FT VARIANT 915
FT /note="C -> S (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:14978182"
FT /id="VAR_031985"
FT VARIANT 936
FT /note="E -> D (associated with hemolytic uremic syndrome
FT and basal laminar drusen; dbSNP:rs1065489)"
FT /evidence="ECO:0000269|PubMed:14583443,
FT ECO:0000269|PubMed:18252232, ECO:0000269|PubMed:20513133,
FT ECO:0000269|Ref.2"
FT /id="VAR_020261"
FT VARIANT 950
FT /note="Q -> H (in AHUS1; dbSNP:rs149474608)"
FT /evidence="ECO:0000269|PubMed:14583443"
FT /id="VAR_025867"
FT VARIANT 951
FT /note="Y -> H (in AHUS1; dbSNP:rs777049051)"
FT /evidence="ECO:0000269|PubMed:14583443"
FT /id="VAR_025868"
FT VARIANT 956
FT /note="T -> M (in AHUS1; dbSNP:rs145975787)"
FT /evidence="ECO:0000269|PubMed:11170895,
FT ECO:0000269|PubMed:11851332"
FT /id="VAR_025869"
FT VARIANT 959
FT /note="C -> Y (in CFHD; variant confirmed at protein level;
FT dbSNP:rs121913053)"
FT /evidence="ECO:0000269|PubMed:22028381,
FT ECO:0000269|PubMed:9312129"
FT /id="VAR_019406"
FT VARIANT 978
FT /note="W -> C (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:12960213"
FT /id="VAR_025870"
FT VARIANT 997
FT /note="N -> T (in dbSNP:rs17575212)"
FT /id="VAR_055683"
FT VARIANT 1007
FT /note="V -> I"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025094"
FT VARIANT 1007
FT /note="V -> L (in dbSNP:rs534399)"
FT /id="VAR_043894"
FT VARIANT 1010
FT /note="A -> T (in dbSNP:rs11539862)"
FT /id="VAR_055684"
FT VARIANT 1017
FT /note="T -> I (in dbSNP:rs34362004)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025095"
FT VARIANT 1021
FT /note="Y -> F (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:12960213"
FT /id="VAR_025871"
FT VARIANT 1043
FT /note="C -> R (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:12960213"
FT /id="VAR_025872"
FT VARIANT 1050
FT /note="N -> Y (associated with basal laminar drusen;
FT dbSNP:rs35274867)"
FT /evidence="ECO:0000269|PubMed:18252232, ECO:0000269|Ref.2"
FT /id="VAR_025096"
FT VARIANT 1059
FT /note="I -> T (in dbSNP:rs35343172)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_025097"
FT VARIANT 1076
FT /note="Q -> E (in CFHD; dbSNP:rs62625015)"
FT /evidence="ECO:0000269|PubMed:11170896,
FT ECO:0000269|PubMed:11851332"
FT /id="VAR_025873"
FT VARIANT 1078
FT /note="R -> S (associated with basal laminar drusen;
FT dbSNP:rs121913062)"
FT /evidence="ECO:0000269|PubMed:18252232"
FT /id="VAR_043895"
FT VARIANT 1119
FT /note="D -> G (in CFHD; dbSNP:rs575109631)"
FT /evidence="ECO:0000269|PubMed:11170896,
FT ECO:0000269|PubMed:11851332"
FT /id="VAR_025874"
FT VARIANT 1134
FT /note="V -> G (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:12960213"
FT /id="VAR_025875"
FT VARIANT 1142
FT /note="Y -> D (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:12960213"
FT /id="VAR_025876"
FT VARIANT 1143
FT /note="Q -> E (confirmed at protein level; dbSNP:rs15809)"
FT /evidence="ECO:0000269|PubMed:22028381"
FT /id="VAR_043896"
FT VARIANT 1157
FT /note="W -> R (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:12960213"
FT /id="VAR_025877"
FT VARIANT 1163
FT /note="C -> W (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:14583443"
FT /id="VAR_025878"
FT VARIANT 1169
FT /note="I -> L (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063650"
FT VARIANT 1183
FT /note="W -> C (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063651"
FT VARIANT 1183
FT /note="W -> L (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:11170895,
FT ECO:0000269|PubMed:11851332, ECO:0000269|PubMed:14978182"
FT /id="VAR_025879"
FT VARIANT 1183
FT /note="W -> R (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:12020532,
FT ECO:0000269|PubMed:12960213"
FT /id="VAR_025880"
FT VARIANT 1184
FT /note="T -> R (in CFHD)"
FT /evidence="ECO:0000269|PubMed:11170896,
FT ECO:0000269|PubMed:11851332"
FT /id="VAR_025881"
FT VARIANT 1189
FT /note="L -> R (in AHUS1; dbSNP:rs121913055)"
FT /evidence="ECO:0000269|PubMed:11170895,
FT ECO:0000269|PubMed:11851332"
FT /id="VAR_019407"
FT VARIANT 1191
FT /note="S -> L (in AHUS1; dbSNP:rs460897)"
FT /evidence="ECO:0000269|PubMed:10577907,
FT ECO:0000269|PubMed:11851332"
FT /id="VAR_019408"
FT VARIANT 1194
FT /note="G -> D (in AHUS1; dbSNP:rs761877050)"
FT /evidence="ECO:0000269|PubMed:11851332"
FT /id="VAR_025882"
FT VARIANT 1197
FT /note="V -> A (in AHUS1; dbSNP:rs460184)"
FT /evidence="ECO:0000269|PubMed:11170895,
FT ECO:0000269|PubMed:11851332"
FT /id="VAR_025883"
FT VARIANT 1198
FT /note="E -> A (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:14583443"
FT /id="VAR_025884"
FT VARIANT 1199
FT /note="F -> S (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:14978182"
FT /id="VAR_031986"
FT VARIANT 1210
FT /note="R -> C (in CFHD and ARMD4; rare penetrant mutation
FT that confers high risk of age-related macular degeneration;
FT dbSNP:rs121913059)"
FT /evidence="ECO:0000269|PubMed:11158219,
FT ECO:0000269|PubMed:11851332, ECO:0000269|PubMed:22019782"
FT /id="VAR_025885"
FT VARIANT 1215
FT /note="R -> G (in AHUS1; dbSNP:rs121913051)"
FT /evidence="ECO:0000269|PubMed:11851332,
FT ECO:0000269|PubMed:9551389"
FT /id="VAR_025886"
FT VARIANT 1215
FT /note="R -> Q (in CFHD)"
FT /evidence="ECO:0000269|PubMed:11158219,
FT ECO:0000269|PubMed:11851332"
FT /id="VAR_025887"
FT VARIANT 1225..1231
FT /note="YPTCAKR -> FQS (in AHUS1)"
FT /evidence="ECO:0000269|PubMed:10762557"
FT /id="VAR_019409"
FT VARIANT 1226
FT /note="P -> S (in AHUS1; atypical)"
FT /evidence="ECO:0000269|PubMed:12960213"
FT /id="VAR_025888"
FT MUTAGEN 337
FT /note="H->A: About 10% loss of heparin-binding."
FT /evidence="ECO:0000269|PubMed:17893204"
FT MUTAGEN 341
FT /note="R->A: About 20% loss of heparin-binding."
FT /evidence="ECO:0000269|PubMed:17893204"
FT MUTAGEN 1182
FT /note="R->A: About 50% loss of C3b binding."
FT /evidence="ECO:0000269|PubMed:16601698"
FT MUTAGEN 1183
FT /note="W->L: About 40% loss of C3b binding."
FT /evidence="ECO:0000269|PubMed:16601698"
FT MUTAGEN 1186
FT /note="K->A: About 20% loss of C3b binding."
FT /evidence="ECO:0000269|PubMed:16601698"
FT MUTAGEN 1188
FT /note="K->A: About 50% loss of C3b binding."
FT /evidence="ECO:0000269|PubMed:16601698"
FT MUTAGEN 1198
FT /note="E->A: About 30% loss of C3b binding."
FT /evidence="ECO:0000269|PubMed:16601698"
FT CONFLICT 21
FT /note="C -> Q (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="T -> V (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="T -> Q (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53..54
FT /note="RP -> IL (in Ref. 5; CAB41739)"
FT /evidence="ECO:0000305"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2RLP"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 94..105
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:2RLQ"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:2WII"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:4AYI"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:4AYI"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:4AYI"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:4AYI"
FT STRAND 366..375
FT /evidence="ECO:0007829|PDB:4AYI"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:4AYI"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:4AYI"
FT TURN 400..403
FT /evidence="ECO:0007829|PDB:6ATG"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:4AYI"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:6ATG"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:2JGW"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:2JGW"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:6ATG"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:6ATG"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:6ATG"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:2UWN"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:2UWN"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:2UWN"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:2UWN"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:2UWN"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:2UWN"
FT STRAND 488..495
FT /evidence="ECO:0007829|PDB:2UWN"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:2UWN"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:4K12"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:4K12"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:4K12"
FT STRAND 531..536
FT /evidence="ECO:0007829|PDB:4K12"
FT STRAND 547..554
FT /evidence="ECO:0007829|PDB:4K12"
FT STRAND 557..560
FT /evidence="ECO:0007829|PDB:4K12"
FT STRAND 578..582
FT /evidence="ECO:0007829|PDB:4B2R"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:4B2R"
FT STRAND 592..597
FT /evidence="ECO:0007829|PDB:4B2R"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:4B2R"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:4B2R"
FT STRAND 615..618
FT /evidence="ECO:0007829|PDB:4B2R"
FT STRAND 622..625
FT /evidence="ECO:0007829|PDB:4B2R"
FT STRAND 637..641
FT /evidence="ECO:0007829|PDB:4B2R"
FT STRAND 654..659
FT /evidence="ECO:0007829|PDB:4B2R"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:4B2R"
FT STRAND 669..674
FT /evidence="ECO:0007829|PDB:4B2R"
FT STRAND 675..678
FT /evidence="ECO:0007829|PDB:4B2S"
FT STRAND 684..686
FT /evidence="ECO:0007829|PDB:4B2R"
FT STRAND 700..703
FT /evidence="ECO:0007829|PDB:2KMS"
FT STRAND 714..718
FT /evidence="ECO:0007829|PDB:2KMS"
FT STRAND 723..727
FT /evidence="ECO:0007829|PDB:4B2S"
FT STRAND 729..732
FT /evidence="ECO:0007829|PDB:2KMS"
FT STRAND 737..739
FT /evidence="ECO:0007829|PDB:4B2S"
FT STRAND 743..746
FT /evidence="ECO:0007829|PDB:4B2S"
FT STRAND 757..760
FT /evidence="ECO:0007829|PDB:2KMS"
FT HELIX 765..767
FT /evidence="ECO:0007829|PDB:2KMS"
FT STRAND 769..771
FT /evidence="ECO:0007829|PDB:2KMS"
FT STRAND 790..792
FT /evidence="ECO:0007829|PDB:2KMS"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:2KMS"
FT STRAND 870..872
FT /evidence="ECO:0007829|PDB:1HFI"
FT STRAND 879..881
FT /evidence="ECO:0007829|PDB:1HFH"
FT STRAND 883..887
FT /evidence="ECO:0007829|PDB:1HFH"
FT STRAND 889..891
FT /evidence="ECO:0007829|PDB:1HFI"
FT STRAND 895..904
FT /evidence="ECO:0007829|PDB:1HFH"
FT STRAND 906..909
FT /evidence="ECO:0007829|PDB:1HFH"
FT STRAND 911..916
FT /evidence="ECO:0007829|PDB:1HFH"
FT STRAND 925..927
FT /evidence="ECO:0007829|PDB:1HFH"
FT STRAND 940..943
FT /evidence="ECO:0007829|PDB:1HCC"
FT STRAND 950..952
FT /evidence="ECO:0007829|PDB:1HFH"
FT STRAND 957..959
FT /evidence="ECO:0007829|PDB:1HCC"
FT STRAND 965..967
FT /evidence="ECO:0007829|PDB:1HCC"
FT STRAND 971..974
FT /evidence="ECO:0007829|PDB:1HCC"
FT STRAND 977..979
FT /evidence="ECO:0007829|PDB:1HCC"
FT STRAND 1057..1059
FT /evidence="ECO:0007829|PDB:3SW0"
FT STRAND 1065..1067
FT /evidence="ECO:0007829|PDB:3SW0"
FT STRAND 1072..1077
FT /evidence="ECO:0007829|PDB:3SW0"
FT STRAND 1082..1085
FT /evidence="ECO:0007829|PDB:3SW0"
FT STRAND 1087..1092
FT /evidence="ECO:0007829|PDB:3SW0"
FT STRAND 1101..1103
FT /evidence="ECO:0007829|PDB:3SW0"
FT STRAND 1118..1122
FT /evidence="ECO:0007829|PDB:3R62"
FT STRAND 1126..1128
FT /evidence="ECO:0007829|PDB:3R62"
FT STRAND 1133..1138
FT /evidence="ECO:0007829|PDB:3R62"
FT STRAND 1143..1146
FT /evidence="ECO:0007829|PDB:3R62"
FT STRAND 1148..1153
FT /evidence="ECO:0007829|PDB:3R62"
FT STRAND 1154..1157
FT /evidence="ECO:0007829|PDB:4ONT"
FT STRAND 1162..1164
FT /evidence="ECO:0007829|PDB:3R62"
FT STRAND 1167..1169
FT /evidence="ECO:0007829|PDB:4ONT"
FT HELIX 1171..1177
FT /evidence="ECO:0007829|PDB:3R62"
FT STRAND 1179..1181
FT /evidence="ECO:0007829|PDB:3R62"
FT TURN 1182..1186
FT /evidence="ECO:0007829|PDB:3R62"
FT STRAND 1189..1191
FT /evidence="ECO:0007829|PDB:3R62"
FT STRAND 1196..1201
FT /evidence="ECO:0007829|PDB:3R62"
FT TURN 1202..1204
FT /evidence="ECO:0007829|PDB:2BZM"
FT STRAND 1205..1207
FT /evidence="ECO:0007829|PDB:3R62"
FT STRAND 1214..1217
FT /evidence="ECO:0007829|PDB:3R62"
FT STRAND 1228..1230
FT /evidence="ECO:0007829|PDB:3R62"
SQ SEQUENCE 1231 AA; 139096 MW; 3C26D62A2BF9BFEE CRC64;
MRLLAKIICL MLWAICVAED CNELPPRRNT EILTGSWSDQ TYPEGTQAIY KCRPGYRSLG
NVIMVCRKGE WVALNPLRKC QKRPCGHPGD TPFGTFTLTG GNVFEYGVKA VYTCNEGYQL
LGEINYRECD TDGWTNDIPI CEVVKCLPVT APENGKIVSS AMEPDREYHF GQAVRFVCNS
GYKIEGDEEM HCSDDGFWSK EKPKCVEISC KSPDVINGSP ISQKIIYKEN ERFQYKCNMG
YEYSERGDAV CTESGWRPLP SCEEKSCDNP YIPNGDYSPL RIKHRTGDEI TYQCRNGFYP
ATRGNTAKCT STGWIPAPRC TLKPCDYPDI KHGGLYHENM RRPYFPVAVG KYYSYYCDEH
FETPSGSYWD HIHCTQDGWS PAVPCLRKCY FPYLENGYNQ NYGRKFVQGK SIDVACHPGY
ALPKAQTTVT CMENGWSPTP RCIRVKTCSK SSIDIENGFI SESQYTYALK EKAKYQCKLG
YVTADGETSG SITCGKDGWS AQPTCIKSCD IPVFMNARTK NDFTWFKLND TLDYECHDGY
ESNTGSTTGS IVCGYNGWSD LPICYERECE LPKIDVHLVP DRKKDQYKVG EVLKFSCKPG
FTIVGPNSVQ CYHFGLSPDL PICKEQVQSC GPPPELLNGN VKEKTKEEYG HSEVVEYYCN
PRFLMKGPNK IQCVDGEWTT LPVCIVEEST CGDIPELEHG WAQLSSPPYY YGDSVEFNCS
ESFTMIGHRS ITCIHGVWTQ LPQCVAIDKL KKCKSSNLII LEEHLKNKKE FDHNSNIRYR
CRGKEGWIHT VCINGRWDPE VNCSMAQIQL CPPPPQIPNS HNMTTTLNYR DGEKVSVLCQ
ENYLIQEGEE ITCKDGRWQS IPLCVEKIPC SQPPQIEHGT INSSRSSQES YAHGTKLSYT
CEGGFRISEE NETTCYMGKW SSPPQCEGLP CKSPPEISHG VVAHMSDSYQ YGEEVTYKCF
EGFGIDGPAI AKCLGEKWSH PPSCIKTDCL SLPSFENAIP MGEKKDVYKA GEQVTYTCAT
YYKMDGASNV TCINSRWTGR PTCRDTSCVN PPTVQNAYIV SRQMSKYPSG ERVRYQCRSP
YEMFGDEEVM CLNGNWTEPP QCKDSTGKCG PPPPIDNGDI TSFPLSVYAP ASSVEYQCQN
LYQLEGNKRI TCRNGQWSEP PKCLHPCVIS REIMENYNIA LRWTAKQKLY SRTGESVEFV
CKRGYRLSSR SHTLRTTCWD GKLEYPTCAK R
