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P05156

- CFAI_HUMAN

UniProt

P05156 - CFAI_HUMAN

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Protein

Complement factor I

Gene

CFI

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Responsible for cleaving the alpha-chains of C4b and C3b in the presence of the cofactors C4-binding protein and factor H respectively.

Catalytic activityi

Inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei380 – 3801Charge relay systemBy similarity
Active sitei429 – 4291Charge relay systemBy similarity
Active sitei525 – 5251Charge relay systemBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi239 – 253151Add
BLAST
Calcium bindingi276 – 290152Add
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. scavenger receptor activity Source: InterPro
  3. serine-type endopeptidase activity Source: ProtInc

GO - Biological processi

  1. complement activation, classical pathway Source: UniProtKB-KW
  2. innate immune response Source: Reactome
  3. regulation of complement activation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Complement pathway, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.21.45. 2681.
ReactomeiREACT_118707. Regulation of Complement cascade.

Protein family/group databases

MEROPSiS01.199.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement factor I (EC:3.4.21.45)
Alternative name(s):
C3B/C4B inactivator
Cleaved into the following 2 chains:
Gene namesi
Name:CFI
Synonyms:IF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:5394. CFI.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProt
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

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.4 Publications
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641P → L in AHUS3. 1 Publication
VAR_063665
Natural varianti119 – 1191G → 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. 2 Publications
VAR_063666
Natural varianti183 – 1831H → R in AHUS3. 1 Publication
Corresponds to variant rs75612300 [ dbSNP | Ensembl ].
VAR_063667
Natural varianti287 – 2871G → R in AHUS3. 1 Publication
Corresponds to variant rs182078921 [ dbSNP | Ensembl ].
VAR_063668
Natural varianti317 – 3171R → W in AHUS3. 1 Publication
VAR_063669
Natural varianti340 – 3401I → T in AHUS3. 1 Publication
VAR_030343
Natural varianti416 – 4161I → L in AHUS3. 1 Publication
Corresponds to variant rs61733901 [ dbSNP | Ensembl ].
VAR_063670
Natural varianti519 – 5191D → N in AHUS3. 1 Publication
VAR_063671
Natural varianti522 – 5221K → T in AHUS3. 1 Publication
VAR_063672
Natural varianti524 – 5241D → V in AHUS3. 1 Publication
VAR_030344
Complement factor I deficiency (CFI deficiency) [MIM:610984]: Autosomal recessive condition associated with a propensity to pyogenic infections.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti243 – 2431G → D in CFI deficiency. 1 Publication
VAR_034907
Natural varianti418 – 4181H → L in CFI deficiency. 1 Publication
VAR_026757
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.1 Publication
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191G → 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. 2 Publications
VAR_063666

Keywords - Diseasei

Age-related macular degeneration, Disease mutation, Hemolytic uremic syndrome

Organism-specific databases

MIMi610984. phenotype.
612923. phenotype.
615439. phenotype.
Orphaneti279. Age-related macular degeneration.
93580. Atypical hemolytic-uremic syndrome with I factor anomaly.
244275. De novo thrombotic microangiopathy after kidney transplantation.
244242. HELLP syndrome.
200418. Immunodeficiency with factor I anomaly.
PharmGKBiPA29641.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 583565Complement factor IPRO_0000027568Add
BLAST
Chaini19 – 335317Complement factor I heavy chainPRO_0000027569Add
BLAST
Chaini340 – 583244Complement factor I light chainPRO_0000027570Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 2551 Publication
Disulfide bondi43 ↔ 541 Publication
Disulfide bondi48 ↔ 591 Publication
Disulfide bondi61 ↔ 931 Publication
Disulfide bondi67 ↔ 861 Publication
Glycosylationi70 – 701N-linked (GlcNAc...)1 Publication
Disulfide bondi75 ↔ 1061 Publication
Glycosylationi103 – 1031N-linked (GlcNAc...) (complex)4 Publications
Disulfide bondi141 ↔ 1811 Publication
Disulfide bondi154 ↔ 2141 Publication
Glycosylationi177 – 1771N-linked (GlcNAc...)1 Publication
Disulfide bondi186 ↔ 1961 Publication
Disulfide bondi229 ↔ 2471 Publication
Disulfide bondi259 ↔ 2711 Publication
Disulfide bondi266 ↔ 2841 Publication
Disulfide bondi278 ↔ 2931 Publication
Disulfide bondi327 ↔ 453Interchain (between heavy and light chains)1 PublicationPROSITE-ProRule annotation
Disulfide bondi365 ↔ 3811 Publication
Disulfide bondi373 ↔ 4441 Publication
Glycosylationi464 – 4641N-linked (GlcNAc...)2 Publications
Disulfide bondi467 ↔ 5311 Publication
Glycosylationi494 – 4941N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi495 ↔ 5101 Publication
Disulfide bondi521 ↔ 5501 Publication
Glycosylationi536 – 5361N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP05156.
PaxDbiP05156.
PeptideAtlasiP05156.
PRIDEiP05156.

2D gel databases

SWISS-2DPAGEP05156.

PTM databases

PhosphoSiteiP05156.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiP05156.
CleanExiHS_CFI.
ExpressionAtlasiP05156. baseline and differential.
GenevestigatoriP05156.

Organism-specific databases

HPAiCAB016777.
HPA001143.
HPA024061.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi109652. 3 interactions.
STRINGi9606.ENSP00000378130.

Structurei

Secondary structure

1
583
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 333
Turni34 – 363
Helixi43 – 453
Beta strandi52 – 554
Beta strandi58 – 614
Helixi64 – 663
Beta strandi74 – 763
Turni77 – 793
Beta strandi80 – 845
Helixi85 – 9410
Beta strandi100 – 1056
Beta strandi113 – 1186
Beta strandi124 – 1307
Beta strandi138 – 1403
Helixi147 – 15610
Beta strandi173 – 1753
Beta strandi182 – 1854
Helixi193 – 1953
Beta strandi196 – 1994
Beta strandi211 – 2144
Beta strandi242 – 2443
Beta strandi247 – 25812
Beta strandi260 – 2623
Beta strandi264 – 2663
Turni267 – 2693
Beta strandi270 – 2723
Helixi274 – 2763
Beta strandi279 – 2813
Beta strandi284 – 2863
Beta strandi290 – 2923
Helixi312 – 3198
Beta strandi356 – 3627
Beta strandi368 – 3714
Beta strandi374 – 3774
Helixi379 – 3824
Beta strandi390 – 3934
Beta strandi409 – 4179
Turni423 – 4253
Beta strandi431 – 4355
Beta strandi439 – 4424
Beta strandi466 – 4705
Beta strandi486 – 4916
Helixi496 – 4994
Turni505 – 5073
Beta strandi508 – 5136
Beta strandi528 – 5325
Beta strandi538 – 5469
Beta strandi557 – 5615
Helixi562 – 5654
Helixi566 – 5727

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XRCX-ray2.69A/B/C/D19-583[»]
ProteinModelPortaliP05156.
SMRiP05156. Positions 27-583.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05156.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 10854Kazal-likePROSITE-ProRule annotationAdd
BLAST
Domaini114 – 21299SRCRPROSITE-ProRule annotationAdd
BLAST
Domaini213 – 25745LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini258 – 29437LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini340 – 574235Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 Kazal-like domain.PROSITE-ProRule annotation
Contains 2 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 1 SRCR domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119008.
HOGENOMiHOG000060288.
HOVERGENiHBG005311.
InParanoidiP05156.
KOiK01333.
PhylomeDBiP05156.
TreeFamiTF330647.

Family and domain databases

Gene3Di3.10.250.10. 1 hit.
4.10.400.10. 2 hits.
InterProiIPR003884. FacI_MAC.
IPR002350. Kazal_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00057. Ldl_recept_a. 2 hits.
PF00530. SRCR. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00057. FIMAC. 1 hit.
SM00192. LDLa. 2 hits.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 2 hits.
PROSITEiPS51465. KAZAL_2. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 2 hits.
PS50287. SRCR_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05156-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLLHVFLLF LCFHLRFCKV TYTSQEDLVE KKCLAKKYTH LSCDKVFCQP
60 70 80 90 100
WQRCIEGTCV CKLPYQCPKN GTAVCATNRR SFPTYCQQKS LECLHPGTKF
110 120 130 140 150
LNNGTCTAEG KFSVSLKHGN TDSEGIVEVK LVDQDKTMFI CKSSWSMREA
160 170 180 190 200
NVACLDLGFQ QGADTQRRFK LSDLSINSTE CLHVHCRGLE TSLAECTFTK
210 220 230 240 250
RRTMGYQDFA DVVCYTQKAD SPMDDFFQCV NGKYISQMKA CDGINDCGDQ
260 270 280 290 300
SDELCCKACQ GKGFHCKSGV CIPSQYQCNG EVDCITGEDE VGCAGFASVT
310 320 330 340 350
QEETEILTAD MDAERRRIKS LLPKLSCGVK NRMHIRRKRI VGGKRAQLGD
360 370 380 390 400
LPWQVAIKDA SGITCGGIYI GGCWILTAAH CLRASKTHRY QIWTTVVDWI
410 420 430 440 450
HPDLKRIVIE YVDRIIFHEN YNAGTYQNDI ALIEMKKDGN KKDCELPRSI
460 470 480 490 500
PACVPWSPYL FQPNDTCIVS GWGREKDNER VFSLQWGEVK LISNCSKFYG
510 520 530 540 550
NRFYEKEMEC AGTYDGSIDA CKGDSGGPLV CMDANNVTYV WGVVSWGENC
560 570 580
GKPEFPGVYT KVANYFDWIS YHVGRPFISQ YNV
Length:583
Mass (Da):65,750
Last modified:January 11, 2011 - v2
Checksum:iF06070EFE6B572A1
GO

Sequence cautioni

The sequence CAA68416.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti558 – 5581V → F in AAA52455. (PubMed:2956252)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641P → L in AHUS3. 1 Publication
VAR_063665
Natural varianti119 – 1191G → 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. 2 Publications
VAR_063666
Natural varianti183 – 1831H → R in AHUS3. 1 Publication
Corresponds to variant rs75612300 [ dbSNP | Ensembl ].
VAR_063667
Natural varianti188 – 1881G → A.1 Publication
VAR_070843
Natural varianti243 – 2431G → D in CFI deficiency. 1 Publication
VAR_034907
Natural varianti287 – 2871G → R in AHUS3. 1 Publication
Corresponds to variant rs182078921 [ dbSNP | Ensembl ].
VAR_063668
Natural varianti300 – 3001T → A.2 Publications
Corresponds to variant rs11098044 [ dbSNP | Ensembl ].
VAR_034908
Natural varianti317 – 3171R → W in AHUS3. 1 Publication
VAR_063669
Natural varianti340 – 3401I → T in AHUS3. 1 Publication
VAR_030343
Natural varianti416 – 4161I → L in AHUS3. 1 Publication
Corresponds to variant rs61733901 [ dbSNP | Ensembl ].
VAR_063670
Natural varianti418 – 4181H → L in CFI deficiency. 1 Publication
VAR_026757
Natural varianti519 – 5191D → N in AHUS3. 1 Publication
VAR_063671
Natural varianti522 – 5221K → T in AHUS3. 1 Publication
VAR_063672
Natural varianti524 – 5241D → V in AHUS3. 1 Publication
VAR_030344

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00318 mRNA. Translation: CAA68416.1. Different initiation.
J02770 mRNA. Translation: AAA52455.1.
AC126283 Genomic DNA. No translation available.
AF005095 Genomic DNA. Translation: AAC08733.2.
CCDSiCCDS34049.1.
PIRiA29154.
RefSeqiNP_000195.2. NM_000204.3.
UniGeneiHs.312485.

Genome annotation databases

EnsembliENST00000394634; ENSP00000378130; ENSG00000205403.
GeneIDi3426.
KEGGihsa:3426.
UCSCiuc003hzq.3. human.

Polymorphism databases

DMDMi317373341.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

CFIbase

CFI mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00318 mRNA. Translation: CAA68416.1 . Different initiation.
J02770 mRNA. Translation: AAA52455.1 .
AC126283 Genomic DNA. No translation available.
AF005095 Genomic DNA. Translation: AAC08733.2 .
CCDSi CCDS34049.1.
PIRi A29154.
RefSeqi NP_000195.2. NM_000204.3.
UniGenei Hs.312485.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XRC X-ray 2.69 A/B/C/D 19-583 [» ]
ProteinModelPortali P05156.
SMRi P05156. Positions 27-583.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109652. 3 interactions.
STRINGi 9606.ENSP00000378130.

Protein family/group databases

MEROPSi S01.199.

PTM databases

PhosphoSitei P05156.

Polymorphism databases

DMDMi 317373341.

2D gel databases

SWISS-2DPAGE P05156.

Proteomic databases

MaxQBi P05156.
PaxDbi P05156.
PeptideAtlasi P05156.
PRIDEi P05156.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000394634 ; ENSP00000378130 ; ENSG00000205403 .
GeneIDi 3426.
KEGGi hsa:3426.
UCSCi uc003hzq.3. human.

Organism-specific databases

CTDi 3426.
GeneCardsi GC04M110661.
GeneReviewsi CFI.
HGNCi HGNC:5394. CFI.
HPAi CAB016777.
HPA001143.
HPA024061.
MIMi 217030. gene.
610984. phenotype.
612923. phenotype.
615439. phenotype.
neXtProti NX_P05156.
Orphaneti 279. Age-related macular degeneration.
93580. Atypical hemolytic-uremic syndrome with I factor anomaly.
244275. De novo thrombotic microangiopathy after kidney transplantation.
244242. HELLP syndrome.
200418. Immunodeficiency with factor I anomaly.
PharmGKBi PA29641.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000119008.
HOGENOMi HOG000060288.
HOVERGENi HBG005311.
InParanoidi P05156.
KOi K01333.
PhylomeDBi P05156.
TreeFami TF330647.

Enzyme and pathway databases

BRENDAi 3.4.21.45. 2681.
Reactomei REACT_118707. Regulation of Complement cascade.

Miscellaneous databases

EvolutionaryTracei P05156.
GeneWikii Complement_factor_I.
GenomeRNAii 3426.
NextBioi 13512.
PROi P05156.
SOURCEi Search...

Gene expression databases

Bgeei P05156.
CleanExi HS_CFI.
ExpressionAtlasi P05156. baseline and differential.
Genevestigatori P05156.

Family and domain databases

Gene3Di 3.10.250.10. 1 hit.
4.10.400.10. 2 hits.
InterProi IPR003884. FacI_MAC.
IPR002350. Kazal_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00057. Ldl_recept_a. 2 hits.
PF00530. SRCR. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00057. FIMAC. 1 hit.
SM00192. LDLa. 2 hits.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 1 hit.
SSF57424. SSF57424. 2 hits.
PROSITEi PS51465. KAZAL_2. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 2 hits.
PS50287. SRCR_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones."
    Catterall C.F., Lyons A., Sim R.M., Day A.J., Harris T.J.R.
    Biochem. J. 242:849-856(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-300.
    Tissue: Liver.
  2. "Human complement factor I: analysis of cDNA-derived primary structure and assignment of its gene to chromosome 4."
    Goldberger G., Bruns G.A.P., Rits M., Edge M.D., Kwiatkowski D.J.
    J. Biol. Chem. 262:10065-10071(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-300.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    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.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Cloning and characterization of the promoter for the human complement factor I (C3b/C4b inactivator) gene."
    Minta J.O., Fung M., Turner S., Eren R., Zemach L., Rits M., Goldberger G.
    Gene 208:17-24(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
    Tissue: Liver.
  5. "Beta-sheet secondary structure of an LDL receptor domain from complement factor I by consensus structure predictions and spectroscopy."
    Ullman C.G., Haris P.I., Smith K.F., Sim R.B., Emery V.C., Perkins S.J.
    FEBS Lett. 371:199-203(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 258-269.
  6. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
    Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
    Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464.
    Tissue: Plasma.
  7. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-103; ASN-177; ASN-464 AND ASN-536.
    Tissue: Plasma.
  8. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103.
    Tissue: Liver.
  9. Cited for: GLYCOSYLATION AT ASN-103.
  10. "Enrichment of glycopeptides for glycan structure and attachment site identification."
    Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
    Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-103, STRUCTURE OF CARBOHYDRATES.
    Tissue: Cerebrospinal fluid.
  11. "Structural basis for complement factor I control and its disease-associated sequence polymorphisms."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 108:12839-12844(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 19-583, CALCIUM-BINDING, SUBUNIT, DISULFIDE BONDS.
  12. Cited for: VARIANT CFI DEFICIENCY LEU-418.
  13. "Molecular characterization of homozygous hereditary factor I deficiency."
    Baracho G.V., Nudelman V., Isaac L.
    Clin. Exp. Immunol. 131:280-286(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CFI DEFICIENCY.
  14. "Complement factor I: a susceptibility gene for atypical haemolytic uraemic syndrome."
    Fremeaux-Bacchi V., Dragon-Durey M.-A., Blouin J., Vigneau C., Kuypers D., Boudailliez B., Loirat C., Rondeau E., Fridman W.H.
    J. Med. Genet. 41:E84-E84(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AHUS3 VAL-524.
  15. Cited for: VARIANTS AHUS3 TRP-317 AND ASN-519.
  16. "Primary glomerulonephritis with isolated C3 deposits: a new entity which shares common genetic risk factors with haemolytic uraemic syndrome."
    Servais A., Fremeaux-Bacchi V., Lequintrec M., Salomon R., Blouin J., Knebelmann B., Gruenfeld J.-P., Lesavre P., Noeel L.-H., Fakhouri F.
    J. Med. Genet. 44:193-199(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CFI DEFICIENCY ASP-243.
  17. "A missense mutation in factor I (IF) predisposes to atypical haemolytic uraemic syndrome."
    Geelen J., van den Dries K., Roos A., van de Kar N., de Kat Angelino C., Klasen I., Monnens L., van den Heuvel L.
    Pediatr. Nephrol. 22:371-375(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AHUS3 THR-340.
  18. "Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome."
    Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.
    Hum. Mutat. 31:E1445-E1460(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AHUS3 LEU-64; ARG-119; ARG-183; ARG-287; LEU-416 AND THR-522.
  19. Cited for: VARIANT ARMD13 ARG-119, VARIANT ALA-188, CHARACTERIZATION VARIANT ARMD13 ARG-119.

Entry informationi

Entry nameiCFAI_HUMAN
AccessioniPrimary (citable) accession number: P05156
Secondary accession number(s): O60442
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3