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Q61129 (CFAI_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Complement factor I
EC=3.4.21.45
Alternative name(s):
C3B/C4B inactivator

Cleaved into the following 2 chains:

  1. Complement factor I heavy chain
  2. Complement factor I light chain
Gene names
Name:Cfi
Synonyms:If
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 linked by disulfide bonds.

Subcellular location

Secreted › extracellular space.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 603585Complement factor I
PRO_0000027571
Chain19 – 356338Complement factor I heavy chain
PRO_0000027572
Chain361 – 603243Complement factor I light chain
PRO_0000027573

Regions

Domain58 – 11154Kazal-like
Domain117 – 217101SRCR
Domain218 – 26245LDL-receptor class A 1
Domain263 – 29937LDL-receptor class A 2
Domain361 – 594234Peptidase S1

Sites

Active site4011Charge relay system By similarity
Active site4491Charge relay system By similarity
Active site5451Charge relay system By similarity

Amino acid modifications

Glycosylation1061N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Ref.4
Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation1821N-linked (GlcNAc...) Potential
Glycosylation2671N-linked (GlcNAc...) Potential
Glycosylation5141N-linked (GlcNAc...) Ref.5
Glycosylation5561N-linked (GlcNAc...) Potential
Disulfide bond157 ↔ 219 By similarity
Disulfide bond191 ↔ 201 By similarity
Disulfide bond234 ↔ 252 By similarity
Disulfide bond246 ↔ 261 By similarity
Disulfide bond264 ↔ 276 By similarity
Disulfide bond271 ↔ 289 By similarity
Disulfide bond283 ↔ 298 By similarity
Disulfide bond386 ↔ 402 By similarity
Disulfide bond487 ↔ 551 By similarity
Disulfide bond515 ↔ 530 By similarity
Disulfide bond541 ↔ 570 By similarity

Experimental info

Sequence conflict1141K → N in AAB00438. Ref.1
Sequence conflict236 – 25217NGKHI…GVNDC → MGSTFLRRKPATVSMTV in AAB00438. Ref.1
Sequence conflict5541I → T in AAB00438. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61129 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: A9B90E1EC78AEE37

FASTA60367,261
        10         20         30         40         50         60 
MKLAHLSLFL LALHLSSSRS PSASDLPQEE LVDQKCLLQK YTHRSCNKVF CQPWQRCIEG 

        70         80         90        100        110        120 
TCICKLPYQC PRAGTPVCAM NGRSYPTYCH QKSFECLHPE IKFSHNGTCA AEGKFNVSLI 

       130        140        150        160        170        180 
YGRTKTEGLV QVKLVDQDER MFICKNSWSM AEANVACVDL GFPLGVRDIQ GSFNISGNLH 

       190        200        210        220        230        240 
INDTECLHVH CRGVETSLAE CAFTKRRTEL SNGLAGVVCY KQDADFPTSL SFQCVNGKHI 

       250        260        270        280        290        300 
PQEKACNGVN DCGDQSDELC CKGCRGNASL CKSGVCIPDQ YKCNGEVDCI TGEDESRCEE 

       310        320        330        340        350        360 
DRQQNIPKGL ARSAQGEAEI ETEETEMLTP GMDNERKRIK SLLPKLSCGV KRNTHTRRKR 

       370        380        390        400        410        420 
VIGGKPANVG DYPWQVAIKD GQRITCGGIY IGGCWILTAA HCVRPSRAHS YQVWTALLDW 

       430        440        450        460        470        480 
LKPNSQLGIQ TVKRVIVHEK YNGATFQNDI ALIEMKMHTG KKECELPNSV PACVPWSPYL 

       490        500        510        520        530        540 
FQPNDRCIIS GWGRGKDNQK VYSLRWGEVD LIGNCSQFYP DRYYEKEMQC AGTRDGSIDA 

       550        560        570        580        590        600 
CKGDSGGPLV CEDINNVTYV WGIVSWGENC GKPEFPGVYT RVANYFDWIS YHVGRSLVSQ 


HNV

« Hide

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: 8604219] [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: 15489334] [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: 10204086] [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: 16944957] [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: 17330941] [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.
AF100565 expand/collapse EMBL AC list , AF100559, AF100560, AF100561, AF100562, AF100563, AF100564 Genomic DNA. Translation: AAD32965.1.
IPIIPI00320675.
RefSeqNP_031712.2. NM_007686.2.
UniGeneMm.117180.

3D structure databases

ProteinModelPortalQ61129.
SMRQ61129. Positions 30-603.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ61129.

Proteomic databases

PRIDEQ61129.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077918; ENSMUSP00000077074; ENSMUSG00000058952.
GeneID12630.
KEGGmmu:12630.

Organism-specific databases

CTD3426.
MGIMGI:105937. Cfi.

Phylogenomic databases

eggNOGroNOG05916.
GeneTreeENSGT00600000084256.
HOGENOMHBG447369.
HOVERGENHBG005311.
InParanoidQ61129.
OrthoDBEOG4QFWD3.

Enzyme and pathway databases

BRENDA3.4.21.45. 3474.

Gene expression databases

ArrayExpressQ61129.
BgeeQ61129.
CleanExMM_CFI.
GenevestigatorQ61129.
GermOnlineENSMUSG00000058952. Mus musculus.

Family and domain databases

InterProIPR003884. FacI_MAC.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR002350. Prot_inh_Kazal.
IPR011497. Prot_Inh_Kazal_2.
IPR001190. Srcr_rcpt.
IPR017448. Srcr_rcpt-rel.
[Graphical view]
Gene3DG3DSA:4.10.400.10. LDL_rcpt_classA_cys-rich. 2 hits.
KOK01333.
PfamPF07648. Kazal_2. 1 hit.
PF00057. Ldl_recept_a. 2 hits.
PF00530. SRCR. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00057. FIMAC. 1 hit.
SM00280. KAZAL. 1 hit.
SM00192. LDLa. 2 hits.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF57424. LDL_rcpt_classA_cys-rich. 2 hits.
SSF50494. Pept_Ser_Cys. 1 hit.
SSF56487. Srcr_receptor. 1 hit.
PROSITEPS51465. 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]
ProtoNetSearch...

Other

NextBio281812.
SOURCESearch...

Entry information

Entry nameCFAI_MOUSE
AccessionPrimary (citable) accession number: Q61129
Secondary accession number(s): B2RWX8, Q9WU07
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents