CFAI_HUMAN
ID CFAI_HUMAN Reviewed; 583 AA.
AC P05156; O60442;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Complement factor I;
DE EC=3.4.21.45;
DE AltName: Full=C3B/C4B inactivator;
DE Contains:
DE RecName: Full=Complement factor I heavy chain;
DE Contains:
DE RecName: Full=Complement factor I light chain;
DE Flags: Precursor;
GN Name=CFI; Synonyms=IF;
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], AND VARIANT ALA-300.
RC TISSUE=Liver;
RX PubMed=2954545; DOI=10.1042/bj2420849;
RA Catterall C.F., Lyons A., Sim R.M., Day A.J., Harris T.J.R.;
RT "Characterization of primary amino acid sequence of human complement
RT control protein factor I from an analysis of cDNA clones.";
RL Biochem. J. 242:849-856(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-300.
RX PubMed=2956252; DOI=10.1016/s0021-9258(18)61076-2;
RA Goldberger G., Bruns G.A.P., Rits M., Edge M.D., Kwiatkowski D.J.;
RT "Human complement factor I: analysis of cDNA-derived primary structure and
RT assignment of its gene to chromosome 4.";
RL J. Biol. Chem. 262:10065-10071(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RC TISSUE=Liver;
RX PubMed=9479036; DOI=10.1016/s0378-1119(97)00632-x;
RA Minta J.O., Fung M., Turner S., Eren R., Zemach L., Rits M., Goldberger G.;
RT "Cloning and characterization of the promoter for the human complement
RT factor I (C3b/C4b inactivator) gene.";
RL Gene 208:17-24(1998).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=7360115; DOI=10.1016/0161-5890(80)90119-4;
RA Harrison R.A., Lachmann P.J.;
RT "The physiological breakdown of the third component of human complement.";
RL Mol. Immunol. 17:9-20(1980).
RN [7]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=6327681; DOI=10.1016/s0021-9258(20)82168-1;
RA Goldberger G., Arnaout M.A., Aden D., Kay R., Rits M., Colten H.R.;
RT "Biosynthesis and postsynthetic processing of human C3b/C4b inactivator
RT (factor I) in three hepatoma cell lines.";
RL J. Biol. Chem. 259:6492-6497(1984).
RN [8]
RP FUNCTION.
RX PubMed=2141838; DOI=10.1093/oxfordjournals.jbchem.a123044;
RA Seya T., Okada M., Nishino H., Atkinson J.P.;
RT "Regulation of proteolytic activity of complement factor I by pH: C3b/C4b
RT receptor (CR1) and membrane cofactor protein (MCP) have different pH optima
RT for factor I-mediated cleavage of C3b.";
RL J. Biochem. 107:310-315(1990).
RN [9]
RP PROTEIN SEQUENCE OF 258-269.
RX PubMed=7672128; DOI=10.1016/0014-5793(95)00916-w;
RA Ullman C.G., Haris P.I., Smith K.F., Sim R.B., Emery V.C., Perkins S.J.;
RT "Beta-sheet secondary structure of an LDL receptor domain from complement
RT factor I by consensus structure predictions and spectroscopy.";
RL FEBS Lett. 371:199-203(1995).
RN [10]
RP INTERACTION WITH CFH AND C3B.
RX PubMed=9291131; DOI=10.1042/bj3260553;
RA Soames C.J., Sim R.B.;
RT "Interactions between human complement components factor H, factor I and
RT C3b.";
RL Biochem. J. 326:553-561(1997).
RN [11]
RP FUNCTION.
RX PubMed=9605165;
RA Sahu A., Isaacs S.N., Soulika A.M., Lambris J.D.;
RT "Interaction of vaccinia virus complement control protein with human
RT complement proteins: factor I-mediated degradation of C3b to iC3b1
RT inactivates the alternative complement pathway.";
RL J. Immunol. 160:5596-5604(1998).
RN [12]
RP FUNCTION.
RX PubMed=12055245; DOI=10.4049/jimmunol.168.12.6298;
RA Barilla-LaBarca M.L., Liszewski M.K., Lambris J.D., Hourcade D.,
RA Atkinson J.P.;
RT "Role of membrane cofactor protein (CD46) in regulation of C4b and C3b
RT deposited on cells.";
RL J. Immunol. 168:6298-6304(2002).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464.
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 [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-103; ASN-177; ASN-464
RP AND ASN-536.
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 [15]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=17320177; DOI=10.1016/j.molimm.2007.01.007;
RA Timar K.K., Junnikkala S., Dallos A., Jarva H., Bhuiyan Z.A., Meri S.,
RA Bos J.D., Asghar S.S.;
RT "Human keratinocytes produce the complement inhibitor factor I: Synthesis
RT is regulated by interferon-gamma.";
RL Mol. Immunol. 44:2943-2949(2007).
RN [16]
RP INTERACTION WITH STAPHYLOCOCCUS AUREUS CLUMPING FACTOR A/CLFA (MICROBIAL
RP INFECTION).
RX PubMed=18544012; DOI=10.1086/588825;
RA Hair P.S., Ward M.D., Semmes O.J., Foster T.J., Cunnion K.M.;
RT "Staphylococcus aureus clumping factor A binds to complement regulator
RT factor I and increases factor I cleavage of C3b.";
RL J. Infect. Dis. 198:125-133(2008).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103.
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 [18]
RP GLYCOSYLATION AT ASN-103.
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 [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103, 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 [20] {ECO:0007744|PDB:2XRC}
RP X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 19-583 IN COMPLEX WITH CALCIUM,
RP GLYCOSYLATION AT ASN-70; ASN-103; ASN-177; ASN-464; ASN-494 AND ASN-536,
RP AND DISULFIDE BONDS.
RX PubMed=21768352; DOI=10.1073/pnas.1102167108;
RA Roversi P., Johnson S., Caesar J.J., McLean F., Leath K.J.,
RA Tsiftsoglou S.A., Morgan B.P., Harris C.L., Sim R.B., Lea S.M.;
RT "Structural basis for complement factor I control and its disease-
RT associated sequence polymorphisms.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12839-12844(2011).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 19-339 AND 340-583, INTERACTION
RP WITH C3B AND CFH, DISULFIDE BOND, 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 [22]
RP VARIANT CFI DEFICIENCY LEU-418.
RX PubMed=8613545; DOI=10.1172/jci118515;
RA Vyse T.J., Morley B.J., Bartok I., Theodoridis E.L., Davies K.A.,
RA Webster A.D.B., Walport M.J.;
RT "The molecular basis of hereditary complement factor I deficiency.";
RL J. Clin. Invest. 97:925-933(1996).
RN [23]
RP INVOLVEMENT IN CFI DEFICIENCY.
RX PubMed=12562389; DOI=10.1046/j.1365-2249.2003.02077.x;
RA Baracho G.V., Nudelman V., Isaac L.;
RT "Molecular characterization of homozygous hereditary factor I deficiency.";
RL Clin. Exp. Immunol. 131:280-286(2003).
RN [24]
RP VARIANT AHUS3 VAL-524.
RX PubMed=15173250; DOI=10.1136/jmg.2004.019083;
RA Fremeaux-Bacchi V., Dragon-Durey M.-A., Blouin J., Vigneau C., Kuypers D.,
RA Boudailliez B., Loirat C., Rondeau E., Fridman W.H.;
RT "Complement factor I: a susceptibility gene for atypical haemolytic uraemic
RT syndrome.";
RL J. Med. Genet. 41:E84-E84(2004).
RN [25]
RP VARIANTS AHUS3 TRP-317 AND ASN-519.
RX PubMed=16621965; DOI=10.1182/blood-2005-10-007252;
RG The international registry of recurrent and familial HUS/TTP;
RA Caprioli J., Noris M., Brioschi S., Pianetti G., Castelletti F.,
RA Bettinaglio P., Mele C., Bresin E., Cassis L., Gamba S., Porrati F.,
RA Bucchioni S., Monteferrante G., Fang C.J., Liszewski M.K., Kavanagh D.,
RA Atkinson J.P., Remuzzi G.;
RT "Genetics of HUS: the impact of MCP, CFH, and IF mutations on clinical
RT presentation, response to treatment, and outcome.";
RL Blood 108:1267-1279(2006).
RN [26]
RP VARIANT CFI DEFICIENCY ASP-243.
RX PubMed=17018561; DOI=10.1136/jmg.2006.045328;
RA Servais A., Fremeaux-Bacchi V., Lequintrec M., Salomon R., Blouin J.,
RA Knebelmann B., Gruenfeld J.-P., Lesavre P., Noeel L.-H., Fakhouri F.;
RT "Primary glomerulonephritis with isolated C3 deposits: a new entity which
RT shares common genetic risk factors with haemolytic uraemic syndrome.";
RL J. Med. Genet. 44:193-199(2007).
RN [27]
RP VARIANT AHUS3 THR-340.
RX PubMed=17106690; DOI=10.1007/s00467-006-0320-2;
RA Geelen J., van den Dries K., Roos A., van de Kar N., de Kat Angelino C.,
RA Klasen I., Monnens L., van den Heuvel L.;
RT "A missense mutation in factor I (IF) predisposes to atypical haemolytic
RT uraemic syndrome.";
RL Pediatr. Nephrol. 22:371-375(2007).
RN [28]
RP VARIANTS AHUS3 LEU-64; ARG-119; ARG-183; ARG-287; LEU-416 AND THR-522.
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 [29]
RP VARIANT ARMD13 ARG-119, VARIANT ALA-188, AND CHARACTERIZATION OF VARIANT
RP ARMD13 ARG-119.
RX PubMed=23685748; DOI=10.1038/ng.2640;
RA van de Ven J.P., Nilsson S.C., Tan P.L., Buitendijk G.H., Ristau T.,
RA Mohlin F.C., Nabuurs S.B., Schoenmaker-Koller F.E., Smailhodzic D.,
RA Campochiaro P.A., Zack D.J., Duvvari M.R., Bakker B., Paun C.C., Boon C.J.,
RA Uitterlinden A.G., Liakopoulos S., Klevering B.J., Fauser S., Daha M.R.,
RA Katsanis N., Klaver C.C., Blom A.M., Hoyng C.B., den Hollander A.I.;
RT "A functional variant in the CFI gene confers a high risk of age-related
RT macular degeneration.";
RL Nat. Genet. 45:813-817(2013).
RN [30]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-300, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Trypsin-like serine protease that plays an essential role in
CC regulating the immune response by controlling all complement pathways.
CC Inhibits these pathways by cleaving three peptide bonds in the alpha-
CC chain of C3b and two bonds in the alpha-chain of C4b thereby
CC inactivating these proteins (PubMed:7360115, PubMed:17320177).
CC Essential cofactors for these reactions include factor H and C4BP in
CC the fluid phase and membrane cofactor protein/CD46 and CR1 on cell
CC surfaces (PubMed:2141838, PubMed:9605165, PubMed:12055245). The
CC presence of these cofactors on healthy cells allows degradation of
CC deposited C3b by CFI in order to prevent undesired complement
CC activation, while in apoptotic cells or microbes, the absence of such
CC cofactors leads to C3b-mediated complement activation and subsequent
CC opsonization (PubMed:28671664). {ECO:0000269|PubMed:12055245,
CC ECO:0000269|PubMed:17320177, ECO:0000269|PubMed:2141838,
CC ECO:0000269|PubMed:28671664, ECO:0000269|PubMed:7360115,
CC ECO:0000269|PubMed:9605165}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Inactivates complement subcomponents C3b, iC3b and C4b by
CC proteolytic cleavage.; EC=3.4.21.45;
CC -!- SUBUNIT: Heterodimer of a light and heavy chains; disulfide-linked. The
CC fully processed and mature protein circulates as a zymogen, and is
CC allosterically activated by substrate-induced remodeling of the active
CC site (PubMed:21768352). Interacts with C3b (PubMed:9291131,
CC PubMed:28671664). Interacts with complement factor H (PubMed:9291131,
CC PubMed:28671664). {ECO:0000269|PubMed:21768352,
CC ECO:0000269|PubMed:28671664, ECO:0000269|PubMed:9291131}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC clumping factor A/ClfA; this interaction enhances cleavage of C3b into
CC iC3b by CFI. {ECO:0000269|PubMed:18544012}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Secreted
CC {ECO:0000269|PubMed:6327681}.
CC -!- TISSUE SPECIFICITY: Expressed in the liver by hepatocytes
CC (PubMed:6327681). Also present in other cells such as monocytes,
CC fibroblasts or keratinocytes (PubMed:6444659, PubMed:17320177).
CC {ECO:0000269|PubMed:17320177, ECO:0000269|PubMed:6327681,
CC ECO:0000269|PubMed:6444659}.
CC -!- DISEASE: Hemolytic uremic syndrome atypical 3 (AHUS3) [MIM:612923]: 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:15173250, ECO:0000269|PubMed:16621965,
CC ECO:0000269|PubMed:17106690, ECO:0000269|PubMed:20513133}. 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: Complement factor I deficiency (CFI deficiency) [MIM:610984]:
CC Autosomal recessive condition associated with a propensity to pyogenic
CC infections. {ECO:0000269|PubMed:12562389, ECO:0000269|PubMed:17018561,
CC ECO:0000269|PubMed:8613545}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Macular degeneration, age-related, 13 (ARMD13) [MIM:615439]: 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:23685748}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA68416.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=CFIbase; Note=CFI mutation db;
CC URL="http://structure.bmc.lu.se/idbase/CFIbase/";
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DR EMBL; Y00318; CAA68416.1; ALT_INIT; mRNA.
DR EMBL; J02770; AAA52455.1; -; mRNA.
DR EMBL; AC126283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF005095; AAC08733.2; -; Genomic_DNA.
DR CCDS; CCDS34049.1; -.
DR PIR; A29154; A29154.
DR RefSeq; NP_000195.2; NM_000204.4.
DR RefSeq; NP_001317964.1; NM_001331035.1.
DR PDB; 2XRC; X-ray; 2.69 A; A/B/C/D=19-583.
DR PDB; 5O32; X-ray; 2.69 A; D/H=19-339, I/J=340-583.
DR PDBsum; 2XRC; -.
DR PDBsum; 5O32; -.
DR AlphaFoldDB; P05156; -.
DR SMR; P05156; -.
DR BioGRID; 109652; 10.
DR ComplexPortal; CPX-6165; Complement factor I complex.
DR IntAct; P05156; 11.
DR MINT; P05156; -.
DR STRING; 9606.ENSP00000378130; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR MEROPS; S01.199; -.
DR GlyConnect; 742; 21 N-Linked glycans (6 sites).
DR GlyGen; P05156; 6 sites, 33 N-linked glycans (6 sites).
DR iPTMnet; P05156; -.
DR PhosphoSitePlus; P05156; -.
DR BioMuta; CFI; -.
DR DMDM; 317373341; -.
DR SWISS-2DPAGE; P05156; -.
DR CPTAC; non-CPTAC-1113; -.
DR CPTAC; non-CPTAC-2659; -.
DR CPTAC; non-CPTAC-2660; -.
DR EPD; P05156; -.
DR jPOST; P05156; -.
DR MassIVE; P05156; -.
DR MaxQB; P05156; -.
DR PaxDb; P05156; -.
DR PeptideAtlas; P05156; -.
DR PRIDE; P05156; -.
DR ProteomicsDB; 51807; -.
DR Antibodypedia; 695; 722 antibodies from 33 providers.
DR DNASU; 3426; -.
DR Ensembl; ENST00000394634.7; ENSP00000378130.2; ENSG00000205403.14.
DR GeneID; 3426; -.
DR KEGG; hsa:3426; -.
DR MANE-Select; ENST00000394634.7; ENSP00000378130.2; NM_000204.5; NP_000195.3.
DR UCSC; uc003hzr.5; human.
DR CTD; 3426; -.
DR DisGeNET; 3426; -.
DR GeneCards; CFI; -.
DR GeneReviews; CFI; -.
DR HGNC; HGNC:5394; CFI.
DR HPA; ENSG00000205403; Tissue enriched (liver).
DR MalaCards; CFI; -.
DR MIM; 217030; gene.
DR MIM; 610984; phenotype.
DR MIM; 612923; phenotype.
DR MIM; 615439; phenotype.
DR neXtProt; NX_P05156; -.
DR OpenTargets; ENSG00000205403; -.
DR Orphanet; 544472; Atypical hemolytic uremic syndrome with complement gene abnormality.
DR Orphanet; 244275; De novo thrombotic microangiopathy after kidney transplantation.
DR Orphanet; 75376; Familial drusen.
DR Orphanet; 244242; HELLP syndrome.
DR Orphanet; 200418; Immunodeficiency with factor I anomaly.
DR Orphanet; 279; NON RARE IN EUROPE: Age-related macular degeneration.
DR PharmGKB; PA29641; -.
DR VEuPathDB; HostDB:ENSG00000205403; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00930000151042; -.
DR InParanoid; P05156; -.
DR PhylomeDB; P05156; -.
DR TreeFam; TF330647; -.
DR BRENDA; 3.4.21.45; 2681.
DR PathwayCommons; P05156; -.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SignaLink; P05156; -.
DR SIGNOR; P05156; -.
DR BioGRID-ORCS; 3426; 8 hits in 1069 CRISPR screens.
DR ChiTaRS; CFI; human.
DR EvolutionaryTrace; P05156; -.
DR GeneWiki; Complement_factor_I; -.
DR GenomeRNAi; 3426; -.
DR Pharos; P05156; Tbio.
DR PRO; PR:P05156; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P05156; protein.
DR Bgee; ENSG00000205403; Expressed in germinal epithelium of ovary and 156 other tissues.
DR ExpressionAtlas; P05156; baseline and differential.
DR Genevisible; P05156; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IPI:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
DR GO; GO:0030451; P:regulation of complement activation, alternative pathway; IDA:ComplexPortal.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 3.10.250.10; -; 1.
DR Gene3D; 4.10.400.10; -; 2.
DR InterPro; IPR003884; FacI_MAC.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF00530; SRCR; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00057; FIMAC; 1.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR SUPFAM; SSF57424; SSF57424; 2.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50287; SRCR_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Age-related macular degeneration; Calcium;
KW Cleavage on pair of basic residues; Complement pathway;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Hemolytic uremic syndrome; Host-virus interaction; Hydrolase; Immunity;
KW Innate immunity; Metal-binding; Protease; Reference proteome; Repeat;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..18
FT CHAIN 19..583
FT /note="Complement factor I"
FT /id="PRO_0000027568"
FT CHAIN 19..335
FT /note="Complement factor I heavy chain"
FT /id="PRO_0000027569"
FT CHAIN 340..583
FT /note="Complement factor I light chain"
FT /id="PRO_0000027570"
FT DOMAIN 55..108
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 114..212
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 213..257
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 258..294
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 340..574
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 380
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00750"
FT ACT_SITE 429
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00750"
FT ACT_SITE 525
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00750"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC"
FT DISULFID 33..255
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 43..54
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 48..59
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 61..93
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 67..86
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 75..106
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 141..181
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 154..214
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 186..196
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 229..247
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 241..256
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 259..271
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 266..284
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 278..293
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 327..453
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0007744|PDB:2XRC"
FT DISULFID 365..381
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 373..444
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 453
FT /note="Interchain (with C-327)"
FT /evidence="ECO:0000269|PubMed:28671664,
FT ECO:0007744|PDB:5O32"
FT DISULFID 467..531
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 495..510
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT DISULFID 521..550
FT /evidence="ECO:0000269|PubMed:21768352,
FT ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
FT ECO:0007744|PDB:5O32"
FT VARIANT 64
FT /note="P -> L (in AHUS3; dbSNP:rs773187287)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063665"
FT VARIANT 119
FT /note="G -> R (in AHUS3 and ARMD13; the mutant is both
FT expressed and secreted at lower levels than wild-type
FT protein; mediates C3 degradation to a lesser extent than
FT that of controls; dbSNP:rs141853578)"
FT /evidence="ECO:0000269|PubMed:20513133,
FT ECO:0000269|PubMed:23685748"
FT /id="VAR_063666"
FT VARIANT 183
FT /note="H -> R (in AHUS3; dbSNP:rs75612300)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063667"
FT VARIANT 188
FT /note="G -> A"
FT /evidence="ECO:0000269|PubMed:23685748"
FT /id="VAR_070843"
FT VARIANT 243
FT /note="G -> D (in CFI deficiency; dbSNP:rs121964916)"
FT /evidence="ECO:0000269|PubMed:17018561"
FT /id="VAR_034907"
FT VARIANT 287
FT /note="G -> R (in AHUS3; dbSNP:rs182078921)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063668"
FT VARIANT 300
FT /note="T -> A (in dbSNP:rs11098044)"
FT /evidence="ECO:0000269|PubMed:2954545,
FT ECO:0000269|PubMed:2956252, ECO:0007744|PubMed:24275569"
FT /id="VAR_034908"
FT VARIANT 317
FT /note="R -> W (in AHUS3; dbSNP:rs121964917)"
FT /evidence="ECO:0000269|PubMed:16621965"
FT /id="VAR_063669"
FT VARIANT 340
FT /note="I -> T (in AHUS3; dbSNP:rs769419740)"
FT /evidence="ECO:0000269|PubMed:17106690"
FT /id="VAR_030343"
FT VARIANT 416
FT /note="I -> L (in AHUS3; dbSNP:rs61733901)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063670"
FT VARIANT 418
FT /note="H -> L (in CFI deficiency; dbSNP:rs121964912)"
FT /evidence="ECO:0000269|PubMed:8613545"
FT /id="VAR_026757"
FT VARIANT 519
FT /note="D -> N (in AHUS3; dbSNP:rs121964918)"
FT /evidence="ECO:0000269|PubMed:16621965"
FT /id="VAR_063671"
FT VARIANT 522
FT /note="K -> T (in AHUS3)"
FT /evidence="ECO:0000269|PubMed:20513133"
FT /id="VAR_063672"
FT VARIANT 524
FT /note="D -> V (in AHUS3; dbSNP:rs121964914)"
FT /evidence="ECO:0000269|PubMed:15173250"
FT /id="VAR_030344"
FT CONFLICT 558
FT /note="V -> F (in Ref. 2; AAA52455)"
FT /evidence="ECO:0000305"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2XRC"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:2XRC"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2XRC"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2XRC"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2XRC"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2XRC"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:2XRC"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 247..258
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:2XRC"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2XRC"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:2XRC"
FT HELIX 312..319
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:2XRC"
FT HELIX 379..382
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 409..417
FT /evidence="ECO:0007829|PDB:2XRC"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 486..491
FT /evidence="ECO:0007829|PDB:2XRC"
FT HELIX 496..499
FT /evidence="ECO:0007829|PDB:2XRC"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 528..532
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 538..546
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 549..551
FT /evidence="ECO:0007829|PDB:2XRC"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:2XRC"
FT HELIX 562..565
FT /evidence="ECO:0007829|PDB:2XRC"
FT HELIX 566..572
FT /evidence="ECO:0007829|PDB:2XRC"
SQ SEQUENCE 583 AA; 65750 MW; F06070EFE6B572A1 CRC64;
MKLLHVFLLF LCFHLRFCKV TYTSQEDLVE KKCLAKKYTH LSCDKVFCQP WQRCIEGTCV
CKLPYQCPKN GTAVCATNRR SFPTYCQQKS LECLHPGTKF LNNGTCTAEG KFSVSLKHGN
TDSEGIVEVK LVDQDKTMFI CKSSWSMREA NVACLDLGFQ QGADTQRRFK LSDLSINSTE
CLHVHCRGLE TSLAECTFTK RRTMGYQDFA DVVCYTQKAD SPMDDFFQCV NGKYISQMKA
CDGINDCGDQ SDELCCKACQ GKGFHCKSGV CIPSQYQCNG EVDCITGEDE VGCAGFASVT
QEETEILTAD MDAERRRIKS LLPKLSCGVK NRMHIRRKRI VGGKRAQLGD LPWQVAIKDA
SGITCGGIYI GGCWILTAAH CLRASKTHRY QIWTTVVDWI HPDLKRIVIE YVDRIIFHEN
YNAGTYQNDI ALIEMKKDGN KKDCELPRSI PACVPWSPYL FQPNDTCIVS GWGREKDNER
VFSLQWGEVK LISNCSKFYG NRFYEKEMEC AGTYDGSIDA CKGDSGGPLV CMDANNVTYV
WGVVSWGENC GKPEFPGVYT KVANYFDWIS YHVGRPFISQ YNV
