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Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain]

 CFAI_HUMAN              Reviewed;         583 AA.
P05156; O60442;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
25-APR-2018, entry version 195.
RecName: Full=Complement factor I;
EC=3.4.21.45;
AltName: Full=C3B/C4B inactivator;
Contains:
RecName: Full=Complement factor I heavy chain;
Contains:
RecName: Full=Complement factor I light chain;
Flags: Precursor;
Name=CFI; Synonyms=IF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-300.
TISSUE=Liver;
PubMed=2954545; DOI=10.1042/bj2420849;
Catterall C.F., Lyons A., Sim R.M., Day A.J., Harris T.J.R.;
"Characterization of primary amino acid sequence of human complement
control protein factor I from an analysis of cDNA clones.";
Biochem. J. 242:849-856(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-300.
PubMed=2956252;
Goldberger G., Bruns G.A.P., Rits M., Edge M.D., Kwiatkowski D.J.;
"Human complement factor I: analysis of cDNA-derived primary structure
and assignment of its gene to chromosome 4.";
J. Biol. Chem. 262:10065-10071(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
TISSUE=Liver;
PubMed=9479036; DOI=10.1016/S0378-1119(97)00632-X;
Minta J.O., Fung M., Turner S., Eren R., Zemach L., Rits M.,
Goldberger G.;
"Cloning and characterization of the promoter for the human complement
factor I (C3b/C4b inactivator) gene.";
Gene 208:17-24(1998).
[5]
PROTEIN SEQUENCE OF 258-269.
PubMed=7672128; DOI=10.1016/0014-5793(95)00916-W;
Ullman C.G., Haris P.I., Smith K.F., Sim R.B., Emery V.C.,
Perkins S.J.;
"Beta-sheet secondary structure of an LDL receptor domain from
complement factor I by consensus structure predictions and
spectroscopy.";
FEBS Lett. 371:199-203(1995).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-103; ASN-177;
ASN-464 AND ASN-536.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[9]
GLYCOSYLATION AT ASN-103.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103, AND STRUCTURE OF
CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[11]
X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 19-583, CALCIUM-BINDING,
SUBUNIT, AND DISULFIDE BONDS.
PubMed=21768352; DOI=10.1073/pnas.1102167108;
Roversi P., Johnson S., Caesar J.J., McLean F., Leath K.J.,
Tsiftsoglou S.A., Morgan B.P., Harris C.L., Sim R.B., Lea S.M.;
"Structural basis for complement factor I control and its disease-
associated sequence polymorphisms.";
Proc. Natl. Acad. Sci. U.S.A. 108:12839-12844(2011).
[12]
VARIANT CFI DEFICIENCY LEU-418.
PubMed=8613545; DOI=10.1172/JCI118515;
Vyse T.J., Morley B.J., Bartok I., Theodoridis E.L., Davies K.A.,
Webster A.D.B., Walport M.J.;
"The molecular basis of hereditary complement factor I deficiency.";
J. Clin. Invest. 97:925-933(1996).
[13]
INVOLVEMENT IN CFI DEFICIENCY.
PubMed=12562389; DOI=10.1046/j.1365-2249.2003.02077.x;
Baracho G.V., Nudelman V., Isaac L.;
"Molecular characterization of homozygous hereditary factor I
deficiency.";
Clin. Exp. Immunol. 131:280-286(2003).
[14]
VARIANT AHUS3 VAL-524.
PubMed=15173250; DOI=10.1136/jmg.2004.019083;
Fremeaux-Bacchi V., Dragon-Durey M.-A., Blouin J., Vigneau C.,
Kuypers D., Boudailliez B., Loirat C., Rondeau E., Fridman W.H.;
"Complement factor I: a susceptibility gene for atypical haemolytic
uraemic syndrome.";
J. Med. Genet. 41:E84-E84(2004).
[15]
VARIANTS AHUS3 TRP-317 AND ASN-519.
PubMed=16621965; DOI=10.1182/blood-2005-10-007252;
The international registry of recurrent and familial HUS/TTP;
Caprioli J., Noris M., Brioschi S., Pianetti G., Castelletti F.,
Bettinaglio P., Mele C., Bresin E., Cassis L., Gamba S., Porrati F.,
Bucchioni S., Monteferrante G., Fang C.J., Liszewski M.K.,
Kavanagh D., Atkinson J.P., Remuzzi G.;
"Genetics of HUS: the impact of MCP, CFH, and IF mutations on clinical
presentation, response to treatment, and outcome.";
Blood 108:1267-1279(2006).
[16]
VARIANT CFI DEFICIENCY ASP-243.
PubMed=17018561; DOI=10.1136/jmg.2006.045328;
Servais A., Fremeaux-Bacchi V., Lequintrec M., Salomon R., Blouin J.,
Knebelmann B., Gruenfeld J.-P., Lesavre P., Noeel L.-H., Fakhouri F.;
"Primary glomerulonephritis with isolated C3 deposits: a new entity
which shares common genetic risk factors with haemolytic uraemic
syndrome.";
J. Med. Genet. 44:193-199(2007).
[17]
VARIANT AHUS3 THR-340.
PubMed=17106690; DOI=10.1007/s00467-006-0320-2;
Geelen J., van den Dries K., Roos A., van de Kar N.,
de Kat Angelino C., Klasen I., Monnens L., van den Heuvel L.;
"A missense mutation in factor I (IF) predisposes to atypical
haemolytic uraemic syndrome.";
Pediatr. Nephrol. 22:371-375(2007).
[18]
VARIANTS AHUS3 LEU-64; ARG-119; ARG-183; ARG-287; LEU-416 AND THR-522.
PubMed=20513133; DOI=10.1002/humu.21256;
Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.;
"Mutations in alternative pathway complement proteins in American
patients with atypical hemolytic uremic syndrome.";
Hum. Mutat. 31:E1445-E1460(2010).
[19]
VARIANT ARMD13 ARG-119, VARIANT ALA-188, AND CHARACTERIZATION VARIANT
ARMD13 ARG-119.
PubMed=23685748; DOI=10.1038/ng.2640;
van de Ven J.P., Nilsson S.C., Tan P.L., Buitendijk G.H., Ristau T.,
Mohlin F.C., Nabuurs S.B., Schoenmaker-Koller F.E., Smailhodzic D.,
Campochiaro P.A., Zack D.J., Duvvari M.R., Bakker B., Paun C.C.,
Boon C.J., Uitterlinden A.G., Liakopoulos S., Klevering B.J.,
Fauser S., Daha M.R., Katsanis N., Klaver C.C., Blom A.M., Hoyng C.B.,
den Hollander A.I.;
"A functional variant in the CFI gene confers a high risk of age-
related macular degeneration.";
Nat. Genet. 45:813-817(2013).
[20]
VARIANT [LARGE SCALE ANALYSIS] ALA-300, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Responsible for cleaving the alpha-chains of C4b and C3b
in the presence of the cofactors C4-binding protein and factor H
respectively.
-!- CATALYTIC ACTIVITY: Inactivates complement subcomponents C3b, iC3b
and C4b by proteolytic cleavage.
-!- SUBUNIT: Heterodimer of a light and heavy chains; disulfide-
linked. The fully processed and mature protein circulates as a
zymogen, and is allosterically activated by substrate-induced
remodeling of the active site. {ECO:0000269|PubMed:21768352}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- TISSUE SPECIFICITY: Plasma.
-!- DISEASE: Hemolytic uremic syndrome atypical 3 (AHUS3)
[MIM:612923]: An atypical form of hemolytic uremic syndrome. It is
a complex genetic disease characterized by microangiopathic
hemolytic anemia, thrombocytopenia, renal failure and absence of
episodes of enterocolitis and diarrhea. In contrast to typical
hemolytic uremic syndrome, atypical forms have a poorer prognosis,
with higher death rates and frequent progression to end-stage
renal disease. {ECO:0000269|PubMed:15173250,
ECO:0000269|PubMed:16621965, ECO:0000269|PubMed:17106690,
ECO:0000269|PubMed:20513133}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry. Other genes may play a role in modifying the phenotype.
-!- DISEASE: Complement factor I deficiency (CFI deficiency)
[MIM:610984]: Autosomal recessive condition associated with a
propensity to pyogenic infections. {ECO:0000269|PubMed:12562389,
ECO:0000269|PubMed:17018561, ECO:0000269|PubMed:8613545}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Macular degeneration, age-related, 13 (ARMD13)
[MIM:615439]: A form of age-related macular degeneration, a
multifactorial eye disease and the most common cause of
irreversible vision loss in the developed world. In most patients,
the disease is manifest as ophthalmoscopically visible yellowish
accumulations of protein and lipid that lie beneath the retinal
pigment epithelium and within an elastin-containing structure
known as Bruch membrane. {ECO:0000269|PubMed:23685748}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- SEQUENCE CAUTION:
Sequence=CAA68416.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=CFIbase; Note=CFI mutation db;
URL="http://structure.bmc.lu.se/idbase/CFIbase/";
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EMBL; Y00318; CAA68416.1; ALT_INIT; mRNA.
EMBL; J02770; AAA52455.1; -; mRNA.
EMBL; AC126283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF005095; AAC08733.2; -; Genomic_DNA.
CCDS; CCDS34049.1; -.
PIR; A29154; A29154.
RefSeq; NP_000195.2; NM_000204.4.
RefSeq; NP_001317964.1; NM_001331035.1.
UniGene; Hs.312485; -.
PDB; 2XRC; X-ray; 2.69 A; A/B/C/D=19-583.
PDB; 5O32; X-ray; 2.69 A; D/H=19-339, I/J=340-583.
PDBsum; 2XRC; -.
PDBsum; 5O32; -.
ProteinModelPortal; P05156; -.
SMR; P05156; -.
BioGrid; 109652; 4.
IntAct; P05156; 1.
STRING; 9606.ENSP00000378130; -.
MEROPS; S01.199; -.
GlyConnect; 742; -.
iPTMnet; P05156; -.
PhosphoSitePlus; P05156; -.
UniCarbKB; P05156; -.
BioMuta; CFI; -.
DMDM; 317373341; -.
SWISS-2DPAGE; P05156; -.
MaxQB; P05156; -.
PaxDb; P05156; -.
PeptideAtlas; P05156; -.
PRIDE; P05156; -.
Ensembl; ENST00000394634; ENSP00000378130; ENSG00000205403.
GeneID; 3426; -.
KEGG; hsa:3426; -.
UCSC; uc003hzr.5; human.
CTD; 3426; -.
DisGeNET; 3426; -.
EuPathDB; HostDB:ENSG00000205403.12; -.
GeneCards; CFI; -.
GeneReviews; CFI; -.
HGNC; HGNC:5394; CFI.
HPA; CAB016777; -.
HPA; HPA001143; -.
HPA; HPA024061; -.
MalaCards; CFI; -.
MIM; 217030; gene.
MIM; 610984; phenotype.
MIM; 612923; phenotype.
MIM; 615439; phenotype.
neXtProt; NX_P05156; -.
OpenTargets; ENSG00000205403; -.
Orphanet; 279; Age-related macular degeneration.
Orphanet; 93580; Atypical hemolytic-uremic syndrome with I factor anomaly.
Orphanet; 244275; De novo thrombotic microangiopathy after kidney transplantation.
Orphanet; 244242; HELLP syndrome.
Orphanet; 200418; Immunodeficiency with factor I anomaly.
PharmGKB; PA29641; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00900000140784; -.
HOGENOM; HOG000060288; -.
HOVERGEN; HBG005311; -.
InParanoid; P05156; -.
KO; K01333; -.
PhylomeDB; P05156; -.
TreeFam; TF330647; -.
BRENDA; 3.4.21.45; 2681.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SIGNOR; P05156; -.
EvolutionaryTrace; P05156; -.
GeneWiki; Complement_factor_I; -.
GenomeRNAi; 3426; -.
PRO; PR:P05156; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000205403; -.
CleanEx; HS_CFI; -.
ExpressionAtlas; P05156; baseline and differential.
Genevisible; P05156; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
CDD; cd00112; LDLa; 2.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 3.10.250.10; -; 1.
InterPro; IPR003884; FacI_MAC.
InterPro; IPR002350; Kazal_dom.
InterPro; IPR036058; Kazal_dom_sf.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001190; SRCR.
InterPro; IPR017448; SRCR-like_dom.
InterPro; IPR036772; SRCR-like_dom_sf.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00057; Ldl_recept_a; 2.
Pfam; PF00530; SRCR; 1.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00057; FIMAC; 1.
SMART; SM00192; LDLa; 2.
SMART; SM00202; SR; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF100895; SSF100895; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF56487; SSF56487; 1.
SUPFAM; SSF57424; SSF57424; 2.
PROSITE; PS51465; KAZAL_2; 1.
PROSITE; PS01209; LDLRA_1; 1.
PROSITE; PS50068; LDLRA_2; 2.
PROSITE; PS50287; SRCR_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Age-related macular degeneration; Calcium;
Cleavage on pair of basic residues; Complement pathway;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycoprotein; Hemolytic uremic syndrome; Hydrolase;
Immunity; Innate immunity; Metal-binding; Polymorphism; Protease;
Reference proteome; Repeat; Secreted; Serine protease; Signal.
SIGNAL 1 18
CHAIN 19 583 Complement factor I.
/FTId=PRO_0000027568.
CHAIN 19 335 Complement factor I heavy chain.
/FTId=PRO_0000027569.
CHAIN 340 583 Complement factor I light chain.
/FTId=PRO_0000027570.
DOMAIN 55 108 Kazal-like. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 114 212 SRCR. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 213 257 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 258 294 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 340 574 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
CA_BIND 239 253 1.
CA_BIND 276 290 2.
ACT_SITE 380 380 Charge relay system. {ECO:0000250}.
ACT_SITE 429 429 Charge relay system. {ECO:0000250}.
ACT_SITE 525 525 Charge relay system. {ECO:0000250}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 103 103 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 464 464 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952}.
CARBOHYD 494 494 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 536 536 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 33 255 {ECO:0000269|PubMed:21768352}.
DISULFID 43 54 {ECO:0000269|PubMed:21768352}.
DISULFID 48 59 {ECO:0000269|PubMed:21768352}.
DISULFID 61 93 {ECO:0000269|PubMed:21768352}.
DISULFID 67 86 {ECO:0000269|PubMed:21768352}.
DISULFID 75 106 {ECO:0000269|PubMed:21768352}.
DISULFID 141 181 {ECO:0000269|PubMed:21768352}.
DISULFID 154 214 {ECO:0000269|PubMed:21768352}.
DISULFID 186 196 {ECO:0000269|PubMed:21768352}.
DISULFID 229 247 {ECO:0000269|PubMed:21768352}.
DISULFID 259 271 {ECO:0000269|PubMed:21768352}.
DISULFID 266 284 {ECO:0000269|PubMed:21768352}.
DISULFID 278 293 {ECO:0000269|PubMed:21768352}.
DISULFID 327 453 Interchain (between heavy and light
chains). {ECO:0000255|PROSITE-
ProRule:PRU00124, ECO:0000255|PROSITE-
ProRule:PRU00196, ECO:0000255|PROSITE-
ProRule:PRU00274, ECO:0000255|PROSITE-
ProRule:PRU00798,
ECO:0000269|PubMed:21768352}.
DISULFID 365 381 {ECO:0000269|PubMed:21768352}.
DISULFID 373 444 {ECO:0000269|PubMed:21768352}.
DISULFID 467 531 {ECO:0000269|PubMed:21768352}.
DISULFID 495 510 {ECO:0000269|PubMed:21768352}.
DISULFID 521 550 {ECO:0000269|PubMed:21768352}.
VARIANT 64 64 P -> L (in AHUS3; dbSNP:rs773187287).
{ECO:0000269|PubMed:20513133}.
/FTId=VAR_063665.
VARIANT 119 119 G -> R (in AHUS3 and ARMD13; the mutant
is both expressed and secreted at lower
levels than wild-type protein; mediates
C3 degradation to a lesser extent than
that of controls; dbSNP:rs141853578).
{ECO:0000269|PubMed:20513133,
ECO:0000269|PubMed:23685748}.
/FTId=VAR_063666.
VARIANT 183 183 H -> R (in AHUS3; dbSNP:rs75612300).
{ECO:0000269|PubMed:20513133}.
/FTId=VAR_063667.
VARIANT 188 188 G -> A. {ECO:0000269|PubMed:23685748}.
/FTId=VAR_070843.
VARIANT 243 243 G -> D (in CFI deficiency;
dbSNP:rs121964916).
{ECO:0000269|PubMed:17018561}.
/FTId=VAR_034907.
VARIANT 287 287 G -> R (in AHUS3; dbSNP:rs182078921).
{ECO:0000269|PubMed:20513133}.
/FTId=VAR_063668.
VARIANT 300 300 T -> A (in dbSNP:rs11098044).
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:2954545,
ECO:0000269|PubMed:2956252}.
/FTId=VAR_034908.
VARIANT 317 317 R -> W (in AHUS3; dbSNP:rs121964917).
{ECO:0000269|PubMed:16621965}.
/FTId=VAR_063669.
VARIANT 340 340 I -> T (in AHUS3; dbSNP:rs769419740).
{ECO:0000269|PubMed:17106690}.
/FTId=VAR_030343.
VARIANT 416 416 I -> L (in AHUS3; dbSNP:rs61733901).
{ECO:0000269|PubMed:20513133}.
/FTId=VAR_063670.
VARIANT 418 418 H -> L (in CFI deficiency;
dbSNP:rs121964912).
{ECO:0000269|PubMed:8613545}.
/FTId=VAR_026757.
VARIANT 519 519 D -> N (in AHUS3; dbSNP:rs121964918).
{ECO:0000269|PubMed:16621965}.
/FTId=VAR_063671.
VARIANT 522 522 K -> T (in AHUS3).
{ECO:0000269|PubMed:20513133}.
/FTId=VAR_063672.
VARIANT 524 524 D -> V (in AHUS3; dbSNP:rs121964914).
{ECO:0000269|PubMed:15173250}.
/FTId=VAR_030344.
CONFLICT 558 558 V -> F (in Ref. 2; AAA52455).
{ECO:0000305}.
STRAND 31 33 {ECO:0000244|PDB:2XRC}.
TURN 34 36 {ECO:0000244|PDB:2XRC}.
HELIX 43 45 {ECO:0000244|PDB:2XRC}.
STRAND 52 55 {ECO:0000244|PDB:2XRC}.
STRAND 58 61 {ECO:0000244|PDB:2XRC}.
HELIX 64 66 {ECO:0000244|PDB:2XRC}.
STRAND 74 76 {ECO:0000244|PDB:2XRC}.
TURN 77 79 {ECO:0000244|PDB:2XRC}.
STRAND 80 84 {ECO:0000244|PDB:2XRC}.
HELIX 85 94 {ECO:0000244|PDB:2XRC}.
STRAND 100 105 {ECO:0000244|PDB:2XRC}.
STRAND 113 118 {ECO:0000244|PDB:2XRC}.
STRAND 124 130 {ECO:0000244|PDB:2XRC}.
STRAND 138 140 {ECO:0000244|PDB:2XRC}.
HELIX 147 156 {ECO:0000244|PDB:2XRC}.
STRAND 173 175 {ECO:0000244|PDB:2XRC}.
STRAND 182 185 {ECO:0000244|PDB:2XRC}.
HELIX 193 195 {ECO:0000244|PDB:2XRC}.
STRAND 196 199 {ECO:0000244|PDB:2XRC}.
STRAND 211 214 {ECO:0000244|PDB:2XRC}.
STRAND 242 244 {ECO:0000244|PDB:2XRC}.
STRAND 247 258 {ECO:0000244|PDB:2XRC}.
STRAND 260 262 {ECO:0000244|PDB:2XRC}.
STRAND 264 266 {ECO:0000244|PDB:2XRC}.
TURN 267 269 {ECO:0000244|PDB:2XRC}.
STRAND 270 272 {ECO:0000244|PDB:2XRC}.
HELIX 274 276 {ECO:0000244|PDB:2XRC}.
STRAND 279 281 {ECO:0000244|PDB:2XRC}.
STRAND 284 286 {ECO:0000244|PDB:2XRC}.
STRAND 290 292 {ECO:0000244|PDB:2XRC}.
HELIX 312 319 {ECO:0000244|PDB:2XRC}.
STRAND 346 348 {ECO:0000244|PDB:2XRC}.
STRAND 356 362 {ECO:0000244|PDB:2XRC}.
STRAND 368 371 {ECO:0000244|PDB:2XRC}.
STRAND 374 377 {ECO:0000244|PDB:2XRC}.
HELIX 379 382 {ECO:0000244|PDB:2XRC}.
STRAND 390 393 {ECO:0000244|PDB:2XRC}.
STRAND 409 417 {ECO:0000244|PDB:2XRC}.
TURN 423 425 {ECO:0000244|PDB:2XRC}.
STRAND 431 435 {ECO:0000244|PDB:2XRC}.
STRAND 439 442 {ECO:0000244|PDB:2XRC}.
STRAND 466 470 {ECO:0000244|PDB:2XRC}.
STRAND 486 491 {ECO:0000244|PDB:2XRC}.
HELIX 496 499 {ECO:0000244|PDB:2XRC}.
TURN 505 507 {ECO:0000244|PDB:2XRC}.
STRAND 508 513 {ECO:0000244|PDB:2XRC}.
STRAND 528 532 {ECO:0000244|PDB:2XRC}.
STRAND 538 546 {ECO:0000244|PDB:2XRC}.
STRAND 549 551 {ECO:0000244|PDB:2XRC}.
STRAND 557 561 {ECO:0000244|PDB:2XRC}.
HELIX 562 565 {ECO:0000244|PDB:2XRC}.
HELIX 566 572 {ECO:0000244|PDB:2XRC}.
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


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