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UniProtKB/Swiss-Prot entry P05156


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CFAI_HUMAN
Primary accession number P05156
Secondary accession number O60442
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 103)
Name and origin of the protein
Protein name Complement factor I [Precursor]
Synonyms EC 3.4.21.45
C3B/C4B inactivator
Contains Complement factor I heavy chain
Complement factor I light chain
Gene name
Name: CFI
Synonyms: IF
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2954545 [NCBI, ExPASy, EBI, Israel, Japan]
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].
PubMed=2956252 [NCBI, ExPASy, EBI, Israel, Japan]
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 [GENOMIC DNA] OF 1-18.
TISSUE=Liver;
DOI=10.1016/S0378-1119(97)00632-X; PubMed=9479036 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
PROTEIN SEQUENCE OF 258-269.
DOI=10.1016/0014-5793(95)00916-W; PubMed=7672128 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1002/pmic.200300556; PubMed=14760718 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-103; ASN-177; ASN-464 AND ASN-536, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
VARIANT CFI DEFICIENCY LEU-418.
PubMed=8613545 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
INVOLVEMENT IN CFI DEFICIENCY.
DOI=10.1046/j.1365-2249.2003.02077.x; PubMed=12562389 [NCBI, ExPASy, EBI, Israel, Japan]
Baracho G.V., Nudelman V., Isaac L.;
"Molecular characterization of homozygous hereditary factor I deficiency.";
Clin. Exp. Immunol. 131:280-286(2003).
[9]
VARIANT VAL-524.
DOI=10.1136/jmg.2004.019083; PubMed=15173250 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
VARIANT CFI DEFICIENCY ASP-243.
DOI=10.1136/jmg.2006.045328; PubMed=17018561 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
VARIANT THR-340.
DOI=10.1007/s00467-006-0320-2; PubMed=17106690 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • 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 linked by disulfide bonds.
  • SUBCELLULAR LOCATION: Secreted, extracellular space.
  • TISSUE SPECIFICITY: Plasma.
  • DISEASE: Defects in CFI are the cause of component I deficiency (CFI deficiency) [MIM:217030]. CFI deficiency is an autosomal recessive condition associated with a propensity to pyogenic infections.
  • DISEASE: Defects in CFI may be associated with or predispose to hemolytic uraemic syndrome (HUS) [MIM:235400]. HUS, the most frequent cause of acute renal failure in childhood, is characterized by the association of acute renal failure, microangiopathic hemolytic anemia, and thrombocytopenia. The majority of HUS cases occur after an episode of infectious diarrhea, and are associated with E.coli O157:H7 infection. However, atypical cases of HUS occur in the absence of infectious diarrhea, although less commonly. Some are inherited in either an autosomal dominant or a recessive pattern and these patients often experience relapse and progress to hypertension and chronic renal disease. Sporadic forms can occur with many of the same signs and symptoms.
  • DISEASE: Defects in CFI are the cause of complement factor I deficiency (CFI deficiency) [MIM:610984]. CFI deficiency is an autosomal recessive condition associated with a propensity to pyogenic infections.
  • SIMILARITY: Belongs to the peptidase S1 family [view classification].
  • SIMILARITY: Contains 2 LDL-receptor class A domains.
  • SIMILARITY: Contains 1 peptidase S1 domain [view classification].
  • SIMILARITY: Contains 1 SRCR domain.
  • WEB RESOURCE: Name=CFIbase; Note=CFI mutation db; URL="http://bioinf.uta.fi/CFIbase/";.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=CFI";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y00318; CAA68416.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J02770; AAA52455.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF005095; AAC08733.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29154; A29154.
RefSeq NP_000195.2; -.
UniGene Hs.312485
3D structure databases
HSSP P00750; 1RTF. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P05156.
Protein family/group databases
MEROPS S01.199; -.
2D gel databases
SWISS-2DPAGE P05156; -.
Organism-specific databases
H-InvDB HIX0004438; -.
HGNC HGNC:5394; CFI.
GenAtlas CFI.
HPA CAB016777; -.
HPA001143; -.
MIM 217030; gene. [NCBI / EBI]
235400; phenotype. [NCBI / EBI]
610984; phenotype. [NCBI / EBI]
Orphanet 2134; Haemolytic uremic syndrome, atypical form.
GeneCards P05156.
Gene expression databases
ArrayExpress P05156; -.
CleanEx HS_CFI; -.
GermOnline ENSG00000205403; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0004252; Molecular function: serine-type endopeptidase activity (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR003884; FacI_MAC.
IPR002172; LDL_rcpt_classA_cys-rich.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
IPR011497; Prot_Inh_Kazal_2.
IPR001190; Srcr_rcpt.
IPR017448; Srcr_rcpt-rel.
Graphical view of domain structure.
Gene3D G3DSA:4.10.400.10; LDL_rcpt_classA_cys-rich; 1.
Pfam PF07648; Kazal_2; 1.
PF00057; Ldl_recept_a; 2.
PF00530; SRCR; 1.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PRINTS PR00722; CHYMOTRYPSIN.
PR00261; LDLRECEPTOR.
SMART SM00057; FIMAC; 1.
SM00192; LDLa; 2.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS01209; LDLRA_1; 1.
PS50068; LDLRA_2; 2.
PS00420; SRCR_1; FALSE_NEG.
PS50287; SRCR_2; 1.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P05156.
ProtoNet P05156.
Proteomic databases
PeptideAtlas P05156; -.
Genome annotation databases
Ensembl ENSG00000205403; Homo sapiens. [Contig view]
GeneID 3426; -.
KEGG hsa:3426; -.
Phylogenomic databases
HOGENOM P05156; -.
HOVERGEN P05156; -.
Other
NextBio 13512; -.
SOURCE CFI; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cleavage on pair of basic residues; Complement pathway; Direct protein sequencing; Disease mutation; Glycoprotein; Hydrolase; Immune response; Innate immunity; Protease; Repeat; Secreted; Serine protease; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18      
CHAIN   19   583  565     Complement factor I. PRO_0000027568
CHAIN   19   335  317     Complement factor I heavy chain. PRO_0000027569
CHAIN   340   583  244     Complement factor I light chain. PRO_0000027570
DOMAIN   114   212  99     SRCR. 
DOMAIN   213   257  45     LDL-receptor class A 1. 
DOMAIN   258   294  37     LDL-receptor class A 2. 
DOMAIN   340   574  235     Peptidase S1. 
ACT_SITE   380   380        Charge relay system (By similarity). 
ACT_SITE   429   429        Charge relay system (By similarity). 
ACT_SITE   525   525        Charge relay system (By similarity). 
CARBOHYD   70    70        N-linked (GlcNAc...). 
CARBOHYD   103   103        N-linked (GlcNAc...). 
CARBOHYD   177   177        N-linked (GlcNAc...). 
CARBOHYD   464   464        N-linked (GlcNAc...). 
CARBOHYD   494   494        N-linked (GlcNAc...) (Potential). 
CARBOHYD   536   536        N-linked (GlcNAc...). 
DISULFID   154   214        By similarity. 
DISULFID   186   196        By similarity. 
DISULFID   229   247        By similarity. 
DISULFID   241   256        By similarity. 
DISULFID   259   271        By similarity. 
DISULFID   266   284        By similarity. 
DISULFID   278   293        By similarity. 
DISULFID   365   381        By similarity. 
DISULFID   467   531        By similarity. 
DISULFID   495   510        By similarity. 
DISULFID   521   550        By similarity. 
VARIANT   243   243  1     G -> D (in CFI deficiency). VAR_034907 
VARIANT   300   300  1     A -> T (in dbSNP:rs11098044 [NCBI]). VAR_034908 
VARIANT   340   340  1     I -> T (predisposes to atypical HUS). VAR_030343 
VARIANT   418   418  1     H -> L (in CFI deficiency). VAR_026757 
VARIANT   524   524  1     D -> V (associated with atypical HUS). VAR_030344 
CONFLICT   558   558        V -> F (in Ref. 2; AAA52455). 
Sequence information
Length: 583 AA [This is the length of the unprocessed precursor] Molecular weight: 65720 Da [This is the MW of the unprocessed precursor] CRC64: 76BB11EAB7F063A8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKLLHVFLLF LCFHLRFCKV TYTSQEDLVE KKCLAKKYTH LSCDKVFCQP WQRCIEGTCV 

        70         80         90        100        110        120 
CKLPYQCPKN GTAVCATNRR SFPTYCQQKS LECLHPGTKF LNNGTCTAEG KFSVSLKHGN 

       130        140        150        160        170        180 
TDSEGIVEVK LVDQDKTMFI CKSSWSMREA NVACLDLGFQ QGADTQRRFK LSDLSINSTE 

       190        200        210        220        230        240 
CLHVHCRGLE TSLAECTFTK RRTMGYQDFA DVVCYTQKAD SPMDDFFQCV NGKYISQMKA 

       250        260        270        280        290        300 
CDGINDCGDQ SDELCCKACQ GKGFHCKSGV CIPSQYQCNG EVDCITGEDE VGCAGFASVA 

       310        320        330        340        350        360 
QEETEILTAD MDAERRRIKS LLPKLSCGVK NRMHIRRKRI VGGKRAQLGD LPWQVAIKDA 

       370        380        390        400        410        420 
SGITCGGIYI GGCWILTAAH CLRASKTHRY QIWTTVVDWI HPDLKRIVIE YVDRIIFHEN 

       430        440        450        460        470        480 
YNAGTYQNDI ALIEMKKDGN KKDCELPRSI PACVPWSPYL FQPNDTCIVS GWGREKDNER 

       490        500        510        520        530        540 
VFSLQWGEVK LISNCSKFYG NRFYEKEMEC AGTYDGSIDA CKGDSGGPLV CMDANNVTYV 

       550        560        570        580 
WGVVSWGENC GKPEFPGVYT KVANYFDWIS YHVGRPFISQ YNV 

P05156 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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