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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.
23-FEB-2022, entry version 218.
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]
TISSUE SPECIFICITY.
PubMed=6444659; DOI=10.1084/jem.151.3.501;
Whaley K.;
"Biosynthesis of the complement components and the regulatory proteins of
the alternative complement pathway by human peripheral blood monocytes.";
J. Exp. Med. 151:501-516(1980).
[6]
FUNCTION.
PubMed=7360115; DOI=10.1016/0161-5890(80)90119-4;
Harrison R.A., Lachmann P.J.;
"The physiological breakdown of the third component of human complement.";
Mol. Immunol. 17:9-20(1980).
[7]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=6327681;
Goldberger G., Arnaout M.A., Aden D., Kay R., Rits M., Colten H.R.;
"Biosynthesis and postsynthetic processing of human C3b/C4b inactivator
(factor I) in three hepatoma cell lines.";
J. Biol. Chem. 259:6492-6497(1984).
[8]
FUNCTION.
PubMed=2141838; DOI=10.1093/oxfordjournals.jbchem.a123044;
Seya T., Okada M., Nishino H., Atkinson J.P.;
"Regulation of proteolytic activity of complement factor I by pH: C3b/C4b
receptor (CR1) and membrane cofactor protein (MCP) have different pH optima
for factor I-mediated cleavage of C3b.";
J. Biochem. 107:310-315(1990).
[9]
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).
[10]
INTERACTION WITH CFH AND C3B.
PubMed=9291131; DOI=10.1042/bj3260553;
Soames C.J., Sim R.B.;
"Interactions between human complement components factor H, factor I and
C3b.";
Biochem. J. 326:553-561(1997).
[11]
FUNCTION.
PubMed=9605165;
Sahu A., Isaacs S.N., Soulika A.M., Lambris J.D.;
"Interaction of vaccinia virus complement control protein with human
complement proteins: factor I-mediated degradation of C3b to iC3b1
inactivates the alternative complement pathway.";
J. Immunol. 160:5596-5604(1998).
[12]
FUNCTION.
PubMed=12055245; DOI=10.4049/jimmunol.168.12.6298;
Barilla-LaBarca M.L., Liszewski M.K., Lambris J.D., Hourcade D.,
Atkinson J.P.;
"Role of membrane cofactor protein (CD46) in regulation of C4b and C3b
deposited on cells.";
J. Immunol. 168:6298-6304(2002).
[13]
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).
[14]
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).
[15]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=17320177; DOI=10.1016/j.molimm.2007.01.007;
Timar K.K., Junnikkala S., Dallos A., Jarva H., Bhuiyan Z.A., Meri S.,
Bos J.D., Asghar S.S.;
"Human keratinocytes produce the complement inhibitor factor I: Synthesis
is regulated by interferon-gamma.";
Mol. Immunol. 44:2943-2949(2007).
[16]
INTERACTION WITH STAPHYLOCOCCUS AUREUS CLUMPING FACTOR A/CLFA (MICROBIAL
INFECTION).
PubMed=18544012; DOI=10.1086/588825;
Hair P.S., Ward M.D., Semmes O.J., Foster T.J., Cunnion K.M.;
"Staphylococcus aureus clumping factor A binds to complement regulator
factor I and increases factor I cleavage of C3b.";
J. Infect. Dis. 198:125-133(2008).
[17]
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).
[18]
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).
[19]
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).
[20]
X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 19-583 IN COMPLEX WITH CALCIUM,
GLYCOSYLATION AT ASN-70; ASN-103; ASN-177; ASN-464; ASN-494 AND ASN-536,
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).
[21]
X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 19-339 AND 340-583, INTERACTION
WITH C3B AND CFH, DISULFIDE BOND, AND FUNCTION.
PubMed=28671664; DOI=10.1038/nsmb.3427;
Xue X., Wu J., Ricklin D., Forneris F., Di Crescenzio P., Schmidt C.Q.,
Granneman J., Sharp T.H., Lambris J.D., Gros P.;
"Regulator-dependent mechanisms of C3b processing by factor I allow
differentiation of immune responses.";
Nat. Struct. Mol. Biol. 24:643-651(2017).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
VARIANT ARMD13 ARG-119, VARIANT ALA-188, AND CHARACTERIZATION OF 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).
[30]
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: Trypsin-like serine protease that plays an essential role in
regulating the immune response by controlling all complement pathways.
Inhibits these pathways by cleaving three peptide bonds in the alpha-
chain of C3b and two bonds in the alpha-chain of C4b thereby
inactivating these proteins (PubMed:7360115, PubMed:17320177).
Essential cofactors for these reactions include factor H and C4BP in
the fluid phase and membrane cofactor protein/CD46 and CR1 on cell
surfaces (PubMed:2141838, PubMed:9605165, PubMed:12055245). The
presence of these cofactors on healthy cells allows degradation of
deposited C3b by CFI in order to prevent undesired complement
activation, while in apoptotic cells or microbes, the absence of such
cofactors leads to C3b-mediated complement activation and subsequent
opsonization (PubMed:28671664). {ECO:0000269|PubMed:12055245,
ECO:0000269|PubMed:17320177, ECO:0000269|PubMed:2141838,
ECO:0000269|PubMed:28671664, ECO:0000269|PubMed:7360115,
ECO:0000269|PubMed:9605165}.
-!- CATALYTIC ACTIVITY:
Reaction=Inactivates complement subcomponents C3b, iC3b and C4b by
proteolytic cleavage.; EC=3.4.21.45;
-!- 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 (PubMed:21768352). Interacts with C3b (PubMed:9291131,
PubMed:28671664). Interacts with complement factor H (PubMed:9291131,
PubMed:28671664). {ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0000269|PubMed:9291131}.
-!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
clumping factor A/ClfA; this interaction enhances cleavage of C3b into
iC3b by CFI. {ECO:0000269|PubMed:18544012}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space. Secreted
{ECO:0000269|PubMed:6327681}.
-!- TISSUE SPECIFICITY: Expressed in the liver by hepatocytes
(PubMed:6327681). Also present in other cells such as monocytes,
fibroblasts or keratinocytes (PubMed:6444659, PubMed:17320177).
{ECO:0000269|PubMed:17320177, ECO:0000269|PubMed:6327681,
ECO:0000269|PubMed:6444659}.
-!- 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 variants 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 variants
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 variants 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=Extended N-terminus.; 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.
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; -.
SMR; P05156; -.
BioGRID; 109652; 9.
ComplexPortal; CPX-6165; Complement factor I complex.
IntAct; P05156; 11.
MINT; P05156; -.
STRING; 9606.ENSP00000378130; -.
DrugBank; DB09130; Copper.
DrugBank; DB01593; Zinc.
DrugBank; DB14487; Zinc acetate.
MEROPS; S01.199; -.
GlyConnect; 742; 21 N-Linked glycans (6 sites).
GlyGen; P05156; 6 sites, 33 N-linked glycans (6 sites).
iPTMnet; P05156; -.
PhosphoSitePlus; P05156; -.
BioMuta; CFI; -.
DMDM; 317373341; -.
SWISS-2DPAGE; P05156; -.
CPTAC; non-CPTAC-1113; -.
CPTAC; non-CPTAC-2659; -.
CPTAC; non-CPTAC-2660; -.
EPD; P05156; -.
jPOST; P05156; -.
MassIVE; P05156; -.
MaxQB; P05156; -.
PaxDb; P05156; -.
PeptideAtlas; P05156; -.
PRIDE; P05156; -.
ProteomicsDB; 51807; -.
Antibodypedia; 695; 669 antibodies from 33 providers.
DNASU; 3426; -.
Ensembl; ENST00000394634; ENSP00000378130; ENSG00000205403.
GeneID; 3426; -.
KEGG; hsa:3426; -.
MANE-Select; ENST00000394634.7; ENSP00000378130.2; NM_000204.5; NP_000195.3.
UCSC; uc003hzr.5; human.
CTD; 3426; -.
DisGeNET; 3426; -.
GeneCards; CFI; -.
GeneReviews; CFI; -.
HGNC; HGNC:5394; CFI.
HPA; ENSG00000205403; Tissue enriched (liver).
MalaCards; CFI; -.
MIM; 217030; gene.
MIM; 610984; phenotype.
MIM; 612923; phenotype.
MIM; 615439; phenotype.
neXtProt; NX_P05156; -.
OpenTargets; ENSG00000205403; -.
Orphanet; 544472; Atypical hemolytic uremic syndrome with complement gene abnormality.
Orphanet; 244275; De novo thrombotic microangiopathy after kidney transplantation.
Orphanet; 75376; Familial drusen.
Orphanet; 244242; HELLP syndrome.
Orphanet; 200418; Immunodeficiency with factor I anomaly.
Orphanet; 279; NON RARE IN EUROPE: Age-related macular degeneration.
PharmGKB; PA29641; -.
VEuPathDB; HostDB:ENSG00000205403; -.
eggNOG; KOG3627; Eukaryota.
GeneTree; ENSGT00930000151042; -.
InParanoid; P05156; -.
PhylomeDB; P05156; -.
TreeFam; TF330647; -.
BRENDA; 3.4.21.45; 2681.
PathwayCommons; P05156; -.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SignaLink; P05156; -.
SIGNOR; P05156; -.
BioGRID-ORCS; 3426; 5 hits in 1039 CRISPR screens.
ChiTaRS; CFI; human.
EvolutionaryTrace; P05156; -.
GeneWiki; Complement_factor_I; -.
GenomeRNAi; 3426; -.
Pharos; P05156; Tbio.
PRO; PR:P05156; -.
Proteomes; UP000005640; Chromosome 4.
RNAct; P05156; protein.
Bgee; ENSG00000205403; Expressed in liver and 192 other tissues.
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:1905370; C:serine-type endopeptidase complex; IPI:ComplexPortal.
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:ProtInc.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
GO; GO:0030451; P:regulation of complement activation, alternative pathway; IDA:ComplexPortal.
CDD; cd00112; LDLa; 2.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.10.10; -; 1.
Gene3D; 3.10.250.10; -; 1.
Gene3D; 4.10.400.10; -; 2.
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; IPR043504; Peptidase_S1_PA_chymotrypsin.
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;
Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
Hemolytic uremic syndrome; Host-virus interaction; Hydrolase; Immunity;
Innate immunity; Metal-binding; Protease; Reference proteome; Repeat;
Secreted; Serine protease; Signal.
SIGNAL 1..18
CHAIN 19..583
/note="Complement factor I"
/id="PRO_0000027568"
CHAIN 19..335
/note="Complement factor I heavy chain"
/id="PRO_0000027569"
CHAIN 340..583
/note="Complement factor I light chain"
/id="PRO_0000027570"
DOMAIN 55..108
/note="Kazal-like"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
DOMAIN 114..212
/note="SRCR"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
DOMAIN 213..257
/note="LDL-receptor class A 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 258..294
/note="LDL-receptor class A 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
DOMAIN 340..574
/note="Peptidase S1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
CA_BIND 239..253
/note="1"
/evidence="ECO:0000269|PubMed:21768352,
ECO:0007744|PDB:2XRC"
CA_BIND 276..290
/note="2"
/evidence="ECO:0000269|PubMed:21768352,
ECO:0007744|PDB:2XRC"
ACT_SITE 380
/note="Charge relay system"
/evidence="ECO:0000250|UniProtKB:P00750"
ACT_SITE 429
/note="Charge relay system"
/evidence="ECO:0000250|UniProtKB:P00750"
ACT_SITE 525
/note="Charge relay system"
/evidence="ECO:0000250|UniProtKB:P00750"
CARBOHYD 70
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC"
CARBOHYD 103
/note="N-linked (GlcNAc...) (complex) asparagine"
/evidence="ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:21768352,
ECO:0007744|PDB:2XRC"
CARBOHYD 177
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC"
CARBOHYD 464
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352,
ECO:0007744|PDB:2XRC"
CARBOHYD 494
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:21768352,
ECO:0007744|PDB:2XRC"
CARBOHYD 536
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC"
DISULFID 33..255
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 43..54
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 48..59
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 61..93
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 67..86
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 75..106
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 141..181
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 154..214
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 186..196
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 229..247
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 241..256
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 259..271
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 266..284
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 278..293
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 327..453
/note="Interchain (between heavy and light chains)"
/evidence="ECO:0000269|PubMed:21768352,
ECO:0007744|PDB:2XRC"
DISULFID 365..381
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 373..444
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 453
/note="Interchain (with C-327)"
/evidence="ECO:0000269|PubMed:28671664,
ECO:0007744|PDB:5O32"
DISULFID 467..531
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 495..510
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
DISULFID 521..550
/evidence="ECO:0000269|PubMed:21768352,
ECO:0000269|PubMed:28671664, ECO:0007744|PDB:2XRC,
ECO:0007744|PDB:5O32"
VARIANT 64
/note="P -> L (in AHUS3; dbSNP:rs773187287)"
/evidence="ECO:0000269|PubMed:20513133"
/id="VAR_063665"
VARIANT 119
/note="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)"
/evidence="ECO:0000269|PubMed:20513133,
ECO:0000269|PubMed:23685748"
/id="VAR_063666"
VARIANT 183
/note="H -> R (in AHUS3; dbSNP:rs75612300)"
/evidence="ECO:0000269|PubMed:20513133"
/id="VAR_063667"
VARIANT 188
/note="G -> A"
/evidence="ECO:0000269|PubMed:23685748"
/id="VAR_070843"
VARIANT 243
/note="G -> D (in CFI deficiency; dbSNP:rs121964916)"
/evidence="ECO:0000269|PubMed:17018561"
/id="VAR_034907"
VARIANT 287
/note="G -> R (in AHUS3; dbSNP:rs182078921)"
/evidence="ECO:0000269|PubMed:20513133"
/id="VAR_063668"
VARIANT 300
/note="T -> A (in dbSNP:rs11098044)"
/evidence="ECO:0000269|PubMed:2954545,
ECO:0000269|PubMed:2956252, ECO:0007744|PubMed:24275569"
/id="VAR_034908"
VARIANT 317
/note="R -> W (in AHUS3; dbSNP:rs121964917)"
/evidence="ECO:0000269|PubMed:16621965"
/id="VAR_063669"
VARIANT 340
/note="I -> T (in AHUS3; dbSNP:rs769419740)"
/evidence="ECO:0000269|PubMed:17106690"
/id="VAR_030343"
VARIANT 416
/note="I -> L (in AHUS3; dbSNP:rs61733901)"
/evidence="ECO:0000269|PubMed:20513133"
/id="VAR_063670"
VARIANT 418
/note="H -> L (in CFI deficiency; dbSNP:rs121964912)"
/evidence="ECO:0000269|PubMed:8613545"
/id="VAR_026757"
VARIANT 519
/note="D -> N (in AHUS3; dbSNP:rs121964918)"
/evidence="ECO:0000269|PubMed:16621965"
/id="VAR_063671"
VARIANT 522
/note="K -> T (in AHUS3)"
/evidence="ECO:0000269|PubMed:20513133"
/id="VAR_063672"
VARIANT 524
/note="D -> V (in AHUS3; dbSNP:rs121964914)"
/evidence="ECO:0000269|PubMed:15173250"
/id="VAR_030344"
CONFLICT 558
/note="V -> F (in Ref. 2; AAA52455)"
/evidence="ECO:0000305"
STRAND 31..33
/evidence="ECO:0007829|PDB:2XRC"
TURN 34..36
/evidence="ECO:0007829|PDB:2XRC"
HELIX 43..45
/evidence="ECO:0007829|PDB:2XRC"
STRAND 52..55
/evidence="ECO:0007829|PDB:2XRC"
STRAND 58..61
/evidence="ECO:0007829|PDB:2XRC"
HELIX 64..66
/evidence="ECO:0007829|PDB:2XRC"
STRAND 74..76
/evidence="ECO:0007829|PDB:2XRC"
TURN 77..79
/evidence="ECO:0007829|PDB:2XRC"
STRAND 80..84
/evidence="ECO:0007829|PDB:2XRC"
HELIX 85..94
/evidence="ECO:0007829|PDB:2XRC"
STRAND 100..105
/evidence="ECO:0007829|PDB:2XRC"
STRAND 113..118
/evidence="ECO:0007829|PDB:2XRC"
STRAND 124..130
/evidence="ECO:0007829|PDB:2XRC"
STRAND 138..140
/evidence="ECO:0007829|PDB:2XRC"
HELIX 147..156
/evidence="ECO:0007829|PDB:2XRC"
STRAND 173..175
/evidence="ECO:0007829|PDB:2XRC"
STRAND 182..185
/evidence="ECO:0007829|PDB:2XRC"
HELIX 193..195
/evidence="ECO:0007829|PDB:2XRC"
STRAND 196..199
/evidence="ECO:0007829|PDB:2XRC"
STRAND 211..214
/evidence="ECO:0007829|PDB:2XRC"
STRAND 242..244
/evidence="ECO:0007829|PDB:2XRC"
STRAND 247..258
/evidence="ECO:0007829|PDB:2XRC"
STRAND 260..262
/evidence="ECO:0007829|PDB:2XRC"
STRAND 264..266
/evidence="ECO:0007829|PDB:2XRC"
TURN 267..269
/evidence="ECO:0007829|PDB:2XRC"
STRAND 270..272
/evidence="ECO:0007829|PDB:2XRC"
HELIX 274..276
/evidence="ECO:0007829|PDB:2XRC"
STRAND 279..281
/evidence="ECO:0007829|PDB:2XRC"
STRAND 284..286
/evidence="ECO:0007829|PDB:2XRC"
STRAND 290..292
/evidence="ECO:0007829|PDB:2XRC"
HELIX 312..319
/evidence="ECO:0007829|PDB:2XRC"
STRAND 346..348
/evidence="ECO:0007829|PDB:2XRC"
STRAND 356..362
/evidence="ECO:0007829|PDB:2XRC"
STRAND 368..371
/evidence="ECO:0007829|PDB:2XRC"
STRAND 374..377
/evidence="ECO:0007829|PDB:2XRC"
HELIX 379..382
/evidence="ECO:0007829|PDB:2XRC"
STRAND 390..393
/evidence="ECO:0007829|PDB:2XRC"
STRAND 409..417
/evidence="ECO:0007829|PDB:2XRC"
TURN 423..425
/evidence="ECO:0007829|PDB:2XRC"
STRAND 431..435
/evidence="ECO:0007829|PDB:2XRC"
STRAND 439..442
/evidence="ECO:0007829|PDB:2XRC"
STRAND 466..470
/evidence="ECO:0007829|PDB:2XRC"
STRAND 486..491
/evidence="ECO:0007829|PDB:2XRC"
HELIX 496..499
/evidence="ECO:0007829|PDB:2XRC"
TURN 505..507
/evidence="ECO:0007829|PDB:2XRC"
STRAND 508..513
/evidence="ECO:0007829|PDB:2XRC"
STRAND 528..532
/evidence="ECO:0007829|PDB:2XRC"
STRAND 538..546
/evidence="ECO:0007829|PDB:2XRC"
STRAND 549..551
/evidence="ECO:0007829|PDB:2XRC"
STRAND 557..561
/evidence="ECO:0007829|PDB:2XRC"
HELIX 562..565
/evidence="ECO:0007829|PDB:2XRC"
HELIX 566..572
/evidence="ECO:0007829|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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Pathways :
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP977: Complement Activation, Classical Pathway
WP1095: Complement Activation, Classical Pathway
WP449: Complement and Coagulation Cascades
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP547: Complement and Coagulation Cascades
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP751: Complement Activation, Classical Pathway
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP2328: Allograft rejection
WP272: Blood Clotting Cascade
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1056: Complement and Coagulation Cascades
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP545: Complement Activation, Classical Pathway
WP1798: Complement cascade
WP1983: Splicing factor NOVA regulated synpatic proteins
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP81: Complement Activation, Classical Pathway
WP2148: Brain derived neurotrophic factor
WP859: Complement Activation, Classical Pathway
WP938: Complement and Coagulation Cascades
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor

Related Genes :
[CFI IF] Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain]
[Cfi If] Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain]
[Cfi If] Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain]
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc) (Neutrophil chemotactic factor-2) (ENCF-2); Complement C3 alpha chain; C3a anaphylatoxin (Neutrophil chemotactic factor-1) (ENCF-1); Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[CR1 C3BR] Complement receptor type 1 (C3b/C4b receptor) (CD antigen CD35)
[C3 CPAMD1] Complement C3 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1) [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C4B CO4 CPAMD3; C4B_2] Complement C4-B (Basic complement C4) (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 3) [Cleaved into: Complement C4 beta chain; Complement C4-B alpha chain; C4a anaphylatoxin; C4b-B; C4d-B; Complement C4 gamma chain]
[MASP1 CRARF CRARF1 PRSS5] Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
[Masp1 Crarf Masp3] Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
[C1S] Complement C1s subcomponent (EC 3.4.21.42) (C1 esterase) (Complement component 1 subcomponent s) [Cleaved into: Complement C1s subcomponent heavy chain; Complement C1s subcomponent light chain]
[C3] Complement C3 (HSE-MSF) [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[Masp1 Crarf Masp3] Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; Complement C3 alpha chain; C3a anaphylatoxin; C3-beta-c (C3bc); Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[c3] Complement C3 [Cleaved into: Complement C3 beta chain; Complement C3 alpha chain; C3a anaphylatoxin; Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2] (Fragment)
[C1R] Complement C1r subcomponent (EC 3.4.21.41) (Complement component 1 subcomponent r) [Cleaved into: Complement C1r subcomponent heavy chain; Complement C1r subcomponent light chain]
[C4A CO4 CPAMD2] Complement C4-A (Acidic complement C4) (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2) [Cleaved into: Complement C4 beta chain; Complement C4-A alpha chain; C4a anaphylatoxin; C4b-A; C4d-A; Complement C4 gamma chain]
[CFB BF BFD] Complement factor B (EC 3.4.21.47) (C3/C5 convertase) (Glycine-rich beta glycoprotein) (GBG) (PBF2) (Properdin factor B) [Cleaved into: Complement factor B Ba fragment; Complement factor B Bb fragment]
[C1s r-gsp] Complement C1s subcomponent (EC 3.4.21.42) (C1 esterase) (Complement component 1 subcomponent s) [Cleaved into: Complement C1s subcomponent heavy chain; Complement C1s subcomponent light chain]
[C2] Complement C2 (EC 3.4.21.43) (C3/C5 convertase) [Cleaved into: Complement C2b fragment; Complement C2a fragment]
[C1sa C1s] Complement C1s-A subcomponent (EC 3.4.21.42) (C1 esterase) (Complement component 1 subcomponent s-A) [Cleaved into: Complement C1s-A subcomponent heavy chain; Complement C1s-A subcomponent light chain]
[C1sb C1s Gm5077] Complement C1s-B subcomponent (EC 3.4.21.42) (C1 esterase) (Complement component 1 subcomponent s-B) [Cleaved into: Complement C1s-B subcomponent heavy chain; Complement C1s-B subcomponent light chain]
[F2] Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain]
[CFD DF PFD] Complement factor D (EC 3.4.21.46) (Adipsin) (C3 convertase activator) (Properdin factor D)
[C1ra C1r] Complement C1r-A subcomponent (EC 3.4.21.41) (Complement component 1 subcomponent r-A) [Cleaved into: Complement C1r-A subcomponent heavy chain; Complement C1r-A subcomponent light chain]
[F7] Coagulation factor VII (EC 3.4.21.21) (Proconvertin) (Serum prothrombin conversion accelerator) (SPCA) (Eptacog alfa) [Cleaved into: Factor VII light chain; Factor VII heavy chain]
[CFH HF HF1 HF2] Complement factor H (H factor 1)
[CLU APOJ CLI KUB1 AAG4] Clusterin (Aging-associated gene 4 protein) (Apolipoprotein J) (Apo-J) (Complement cytolysis inhibitor) (CLI) (Complement-associated protein SP-40,40) (Ku70-binding protein 1) (NA1/NA2) (Sulfated glycoprotein 2) (SGP-2) (Testosterone-repressed prostate message 2) (TRPM-2) [Cleaved into: Clusterin beta chain (ApoJalpha) (Complement cytolysis inhibitor a chain); Clusterin alpha chain (ApoJbeta) (Complement cytolysis inhibitor b chain)]
[C4BPA C4BP] C4b-binding protein alpha chain (C4bp) (Proline-rich protein) (PRP)

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