Q61129 (CFAI_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 125.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Complement factor I EC=3.4.21.45 Alternative name(s): C3B/C4B inactivator Cleaved into the following 2 chains: | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 603 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (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 structure | 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 By similarity. |
| Subcellular location | |
| Tissue specificity | Plasma. |
| Sequence similarities | Belongs to the peptidase S1 family. Contains 1 Kazal-like domain. Contains 2 LDL-receptor class A domains. Contains 1 peptidase S1 domain. Contains 1 SRCR domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | Potential | ||||||||
| Chain | 19 – 603 | 585 | Complement factor I | PRO_0000027571 | |||||||
| Chain | 19 – 356 | 338 | Complement factor I heavy chain | PRO_0000027572 | |||||||
| Chain | 361 – 603 | 243 | Complement factor I light chain | PRO_0000027573 | |||||||
Regions | |||||||||||
| Domain | 58 – 111 | 54 | Kazal-like | ||||||||
| Domain | 117 – 217 | 101 | SRCR | ||||||||
| Domain | 218 – 262 | 45 | LDL-receptor class A 1 | ||||||||
| Domain | 263 – 299 | 37 | LDL-receptor class A 2 | ||||||||
| Domain | 361 – 594 | 234 | Peptidase S1 | ||||||||
| Calcium binding | 244 – 258 | 15 | By similarity | ||||||||
| Calcium binding | 281 – 295 | 15 | By similarity | ||||||||
Sites | |||||||||||
| Active site | 401 | 1 | Charge relay system By similarity | ||||||||
| Active site | 449 | 1 | Charge relay system By similarity | ||||||||
| Active site | 545 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 106 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 116 | 1 | N-linked (GlcNAc...) Ref.4 | ||||||||
| Glycosylation | 174 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 182 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 267 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 514 | 1 | N-linked (GlcNAc...) Ref.5 | ||||||||
| Glycosylation | 556 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 36 ↔ 260 | By similarity | |||||||||
| Disulfide bond | 46 ↔ 57 | By similarity | |||||||||
| Disulfide bond | 51 ↔ 62 | By similarity | |||||||||
| Disulfide bond | 64 ↔ 96 | By similarity | |||||||||
| Disulfide bond | 70 ↔ 89 | By similarity | |||||||||
| Disulfide bond | 78 ↔ 109 | By similarity | |||||||||
| Disulfide bond | 144 ↔ 186 | By similarity | |||||||||
| Disulfide bond | 157 ↔ 219 | By similarity | |||||||||
| Disulfide bond | 191 ↔ 201 | By similarity | |||||||||
| Disulfide bond | 234 ↔ 252 | By similarity | |||||||||
| Disulfide bond | 264 ↔ 276 | By similarity | |||||||||
| Disulfide bond | 271 ↔ 289 | By similarity | |||||||||
| Disulfide bond | 283 ↔ 298 | By similarity | |||||||||
| Disulfide bond | 348 ↔ 473 | Interchain (between heavy and light chains) By similarity | |||||||||
| Disulfide bond | 386 ↔ 402 | By similarity | |||||||||
| Disulfide bond | 394 ↔ 464 | By similarity | |||||||||
| Disulfide bond | 487 ↔ 551 | By similarity | |||||||||
| Disulfide bond | 515 ↔ 530 | By similarity | |||||||||
| Disulfide bond | 541 ↔ 570 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 114 | 1 | K → N in AAB00438. Ref.1 | ||||||||
| Sequence conflict | 236 – 252 | 17 | NGKHI…GVNDC → MGSTFLRRKPATVSMTV in AAB00438. Ref.1 | ||||||||
| Sequence conflict | 554 | 1 | I → T in AAB00438. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "cDNA cloning, sequencing and chromosomal assignment of the gene for mouse complement factor I (C3b/C4b inactivator): identification of a species specific divergent segment in factor I." Minta J.O., Wong M.J., Kozak C.A., Kunnath-Muglia L.M., Goldberger G. Mol. Immunol. 33:101-112(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [3] | "Cloning and characterization of the non-catalytic heavy chain of mouse complement factor I gene: structure comparison with the human homologue." Yun Y.-S., Goldberger G., Minta J.O. Biochem. Mol. Biol. Int. 47:493-500(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 114-334. Strain: 129/Sv. Tissue: Kidney. |
| [4] | "Proteome-wide characterization of N-glycosylation events by diagonal chromatography." Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K. J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-116, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Plasma. |
| [5] | "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides." Bernhard O.K., Kapp E.A., Simpson R.J. J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-514, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Plasma. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U47810 mRNA. Translation: AAB00438.1. BC150751 mRNA. Translation: AAI50752.1. AH007741 Genomic DNA. Translation: AAD32965.1. |
| IPI | IPI00320675. |
| RefSeq | NP_031712.2. NM_007686.2. |
| UniGene | Mm.117180. |
3D structure databases | |
| ProteinModelPortal | Q61129. |
| SMR | Q61129. Positions 30-603. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10090.ENSMUSP00000077074. |
Protein family/group databases | |
| MEROPS | S01.199. |
PTM databases | |
| PhosphoSite | Q61129. |
Proteomic databases | |
| PaxDb | Q61129. |
| PRIDE | Q61129. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000077918; ENSMUSP00000077074; ENSMUSG00000058952. |
| GeneID | 12630. |
| KEGG | mmu:12630. |
Organism-specific databases | |
| CTD | 3426. |
| MGI | MGI:105937. Cfi. |
Phylogenomic databases | |
| eggNOG | COG5640. |
| GeneTree | ENSGT00700000104187. |
| HOGENOM | HOG000060288. |
| HOVERGEN | HBG005311. |
| InParanoid | B2RWX8. |
| KO | K01333. |
| OMA | WGREKDN. |
| OrthoDB | EOG4QFWD3. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.45. 3474. |
Gene expression databases | |
| Bgee | Q61129. |
| CleanEx | MM_CFI. |
| Genevestigator | Q61129. |
| GermOnline | ENSMUSG00000058952. Mus musculus. |
Family and domain databases | |
| Gene3D | 4.10.400.10. 2 hits. |
| InterPro | 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_rcpt. IPR017448. Srcr_rcpt-rel. IPR009003. Trypsin-like_Pept_dom. [Graphical view] |
| Pfam | PF07648. Kazal_2. 1 hit. PF00057. Ldl_recept_a. 2 hits. PF00530. SRCR. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR00722. CHYMOTRYPSIN. |
| SMART | SM00057. FIMAC. 1 hit. SM00280. KAZAL. 1 hit. SM00192. LDLa. 2 hits. SM00202. SR. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| SUPFAM | SSF57424. LDL_rcpt_classA_cys-rich. 2 hits. SSF50494. Pept_Ser_Cys. 1 hit. SSF56487. Srcr_receptor. 1 hit. |
| PROSITE | PS51465. KAZAL_2. 1 hit. PS01209. LDLRA_1. 1 hit. PS50068. LDLRA_2. 2 hits. PS00420. SRCR_1. False negative. PS50287. SRCR_2. 1 hit. PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 281812. |
| SOURCE | Search... |
Entry information
| Entry name | CFAI_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q61129 Secondary accession number(s): B2RWX8, Q9WU07 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
