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Reviewed, UniProtKB/Swiss-Prot Q61129 (CFAI_MOUSE)

Last modified June 16, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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- Recommended name:
            Complement factor I heavy chain
    2- Recommended name:
            Complement factor I light chain
Gene names
Name: Cfi
Synonyms: If
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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

Secretedextracellular 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

Domain63 – 10947Kazal-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.3
Glycosylation1741N-linked (GlcNAc...) Potential
Glycosylation1821N-linked (GlcNAc...) Potential
Glycosylation2671N-linked (GlcNAc...) Potential
Glycosylation5141N-linked (GlcNAc...) Ref.4
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 conflict1141N → K in AAD32965. Ref.2
Sequence conflict236 – 25217NGKHI…GVNDC → MGSTFLRRKPATVSMTV in AAB00438. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61129-1 [UniParc].

Last modified May 4, 2001. Version 2.
Checksum: E2C1D43261C719E8

FASTA60367,234
        10         20         30         40         50         60 
MKLAHLSLFL LALHLSSSRS PSASDLPQEE LVDQKCLLQK YTHRSCNKVF CQPWQRCIEG 

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

       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 CEDTNNVTYV 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]"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.
[3]"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.
Tissue: Plasma.
[4]"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.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

U47810 mRNA. Translation: AAB00438.1.
AF100565 expand/collapse EMBL AC list , AF100559, AF100560, AF100561, AF100562, AF100563, AF100564 Genomic DNA. Translation: AAD32965.1.
IPIIPI00320675.
UniGeneMm.117180

3D structure databases

HSSPHSSP built from PDB template 1RTF based on UniProtKB P00750.
ModBaseSearch...

Proteomic databases

PRIDEQ61129.

Genome annotation databases

EnsemblENSMUSG00000058952. Mus musculus. [Contig view]

Organism-specific databases

MGIMGI:105937. Cfi.

Phylogenomic databases

HOGENOMQ61129.
HOVERGENQ61129.

Enzyme and pathway databases

BRENDA3.4.21.45. 244.

Gene expression databases

ArrayExpressQ61129.
BgeeQ61129.
CleanExMM_CFI.
GermOnlineENSMUSG00000058952. Mus musculus.

Family and domain databases

InterProIPR003884. FacI_MAC.
IPR002172. LDL_rcpt_classA_cys-rich.
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. 1 hit.
PfamPF07648. Kazal_2. 1 hit.
PF00057. Ldl_recept_a. 2 hits.
PF00530. SRCR. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
PR00261. LDLRECEPTOR.
SMARTSM00057. FIMAC. 1 hit.
SM00280. KAZAL. 1 hit.
SM00192. LDLa. 2 hits.
SM00202. SR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS01209. 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 Resources

SOURCESearch...

Entry information

Entry nameCFAI_MOUSE
AccessionPrimary (citable) accession number: Q61129
Secondary accession number(s): Q9WU07
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: May 4, 2001
Last modified: June 16, 2009
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents