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P05156

- CFAI_HUMAN

UniProt

P05156 - CFAI_HUMAN

Protein

Complement factor I

Gene

CFI

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    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

    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: UniProt
    4. membrane Source: InterPro

    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

    ArrayExpressiP05156.
    BgeeiP05156.
    CleanExiHS_CFI.
    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. 2 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.
    HOGENOMiHOG000060288.
    HOVERGENiHBG005311.
    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

    MKLLHVFLLF LCFHLRFCKV TYTSQEDLVE KKCLAKKYTH LSCDKVFCQP    50
    WQRCIEGTCV CKLPYQCPKN GTAVCATNRR SFPTYCQQKS LECLHPGTKF 100
    LNNGTCTAEG KFSVSLKHGN TDSEGIVEVK LVDQDKTMFI CKSSWSMREA 150
    NVACLDLGFQ QGADTQRRFK LSDLSINSTE CLHVHCRGLE TSLAECTFTK 200
    RRTMGYQDFA DVVCYTQKAD SPMDDFFQCV NGKYISQMKA CDGINDCGDQ 250
    SDELCCKACQ GKGFHCKSGV CIPSQYQCNG EVDCITGEDE VGCAGFASVT 300
    QEETEILTAD MDAERRRIKS LLPKLSCGVK NRMHIRRKRI VGGKRAQLGD 350
    LPWQVAIKDA SGITCGGIYI GGCWILTAAH CLRASKTHRY QIWTTVVDWI 400
    HPDLKRIVIE YVDRIIFHEN YNAGTYQNDI ALIEMKKDGN KKDCELPRSI 450
    PACVPWSPYL FQPNDTCIVS GWGREKDNER VFSLQWGEVK LISNCSKFYG 500
    NRFYEKEMEC AGTYDGSIDA CKGDSGGPLV CMDANNVTYV WGVVSWGENC 550
    GKPEFPGVYT KVANYFDWIS YHVGRPFISQ YNV 583
    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. 2 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.
    HOGENOMi HOG000060288.
    HOVERGENi HBG005311.
    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

    ArrayExpressi P05156.
    Bgeei P05156.
    CleanExi HS_CFI.
    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

    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 1, 2014
    This is version 163 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