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P04186 (CFAB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complement factor B

EC=3.4.21.47
Alternative name(s):
C3/C5 convertase
Gene names
Name:Cfb
Synonyms:Bf, H2-Bf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length761 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase.

Catalytic activity

Cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to yield C5a and C5b.

Subcellular location

Secreted.

Domain

The unliganded VWA domain has an inactive 'locked' conformation whereby the scissile Arg-256|Lys-257 bond is protected from proteolytic activation By similarity.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Contains 3 Sushi (CCP/SCR) domains.

Contains 1 VWFA domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 761739Complement factor B
PRO_0000027548
Chain23 – 256234Complement factor B Ba fragment
PRO_0000027549
Chain257 – 761505Complement factor B Bb fragment
PRO_0000027550

Regions

Domain32 – 9766Sushi 1
Domain98 – 15760Sushi 2
Domain160 – 21758Sushi 3
Domain267 – 466200VWFA
Domain474 – 754281Peptidase S1

Sites

Active site5231Charge relay system
Active site5731Charge relay system
Active site6961Charge relay system

Amino acid modifications

Glycosylation1191N-linked (GlcNAc...) Ref.6
Glycosylation1391N-linked (GlcNAc...) Potential
Glycosylation2821N-linked (GlcNAc...) Ref.5
Glycosylation3751N-linked (GlcNAc...) Potential
Disulfide bond34 ↔ 73 By similarity
Disulfide bond59 ↔ 95 By similarity
Disulfide bond100 ↔ 142 By similarity
Disulfide bond128 ↔ 155 By similarity
Disulfide bond162 ↔ 202 By similarity
Disulfide bond188 ↔ 215 By similarity
Disulfide bond508 ↔ 524 By similarity
Disulfide bond692 ↔ 722 By similarity

Experimental info

Sequence conflict7301L → P in AAA39549. Ref.4
Sequence conflict7451V → E in AAA39549. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P04186 [UniParc].

Last modified August 1, 1991. Version 2.
Checksum: 9E9015448A61020E

FASTA76185,004
        10         20         30         40         50         60 
MESPQLCLVL LVLGFSSGGV SATPVLEARP QVSCSLEGVE IKGGSFQLLQ GGQALEYLCP 

        70         80         90        100        110        120 
SGFYPYPVQT RTCRSTGSWS DLQTRDQKIV QKAECRAIRC PRPQDFENGE FWPRSPFYNL 

       130        140        150        160        170        180 
SDQISFQCYD GYVLRGSANR TCQENGRWDG QTAICDDGAG YCPNPGIPIG TRKVGSQYRL 

       190        200        210        220        230        240 
EDIVTYHCSR GLVLRGSQKR KCQEGGSWSG TEPSCQDSFM YDSPQEVAEA FLSSLTETIE 

       250        260        270        280        290        300 
GADAEDGHSP GEQQKRKIVL DPSGSMNIYL VLDGSDSIGS SNFTGAKRCL TNLIEKVASY 

       310        320        330        340        350        360 
GVRPRYGLLT YATVPKVLVR VSDERSSDAD WVTEKLNQIS YEDHKLKSGT NTKRALQAVY 

       370        380        390        400        410        420 
SMMSWAGDAP PEGWNRTRHV IIIMTDGLHN MGGNPVTVIQ DIRALLDIGR DPKNPREDYL 

       430        440        450        460        470        480 
DVYVFGVGPL VDSVNINALA SKKDNEHHVF KVKDMEDLEN VFYQMIDETK SLSLCGMVWE 

       490        500        510        520        530        540 
HKKGNDYHKQ PWQAKISVTR PLKGHETCMG AVVSEYFVLT AAHCFMVDDQ KHSIKVSVGG 

       550        560        570        580        590        600 
QRRDLEIEEV LFHPKYNING KKAEGIPEFY DYDVALVKLK NKLKYGQTLR PICLPCTEGT 

       610        620        630        640        650        660 
TRALRLPQTA TCKQHKEQLL PVKDVKALFV SEQGKSLTRK EVYIKNGDKK ASCERDATKA 

       670        680        690        700        710        720 
QGYEKVKDAS EVVTPRFLCT GGVDPYADPN TCKGDSGGPL IVHKRSRFIQ VGVISWGVVD 

       730        740        750        760 
VCRDQRRQQL VPSYARDFHI NLFQVLPWLK DKLKDEDLGF L 

« Hide

References

« Hide 'large scale' references
[1]"Murine complement C2 and factor B genomic and cDNA cloning reveals different mechanisms for multiple transcripts of C2 and B."
Ishikawa N., Nonaka M., Wetsel R.A., Colten H.R.
J. Biol. Chem. 265:19040-19046(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129.
[3]"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].
Strain: Czech II.
Tissue: Mammary gland.
[4]"Phylogenetic conservation of a class III major histocompatibility complex antigen, factor B. Isolation and nucleotide sequencing of mouse factor B cDNA clones."
Sackstein R., Colten H.R., Woods D.E.
J. Biol. Chem. 258:14693-14697(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 285-761.
[5]"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-282.
Strain: C57BL/6.
Tissue: Plasma.
[6]"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-119.
Strain: C57BL/6.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60646 expand/collapse EMBL AC list , M60629, M60630, M60631, M60632, M60633, M60634, M60635, M60636, M60637, M60638, M60639, M60640, M60641, M60642, M60643, M60644, M60645 Genomic DNA. Translation: AAA37379.1.
AF049850 Genomic DNA. Translation: AAC05283.1.
AF109906 Genomic DNA. Translation: AAC84160.1.
BC005451 mRNA. Translation: AAH05451.1.
K01496 mRNA. Translation: AAA39549.1.
K01497 mRNA. Translation: AAA39550.1.
K01498 mRNA. Translation: AAA39551.1.
M57890 mRNA. Translation: AAA63293.1.
PIRBBMS. A38875.
UniGeneMm.653.

3D structure databases

ProteinModelPortalP04186.
SMRP04186. Positions 33-761.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP04186. 1 interaction.
MINTMINT-1865229.
STRING10090.ENSMUSP00000117677.

Protein family/group databases

MEROPSS01.196.

PTM databases

PhosphoSiteP04186.

Proteomic databases

MaxQBP04186.
PaxDbP04186.
PRIDEP04186.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000128767; ENSMUSP00000119977; ENSMUSG00000090231.

Organism-specific databases

MGIMGI:105975. Cfb.

Phylogenomic databases

eggNOGNOG306397.
HOGENOMHOG000038034.
HOVERGENHBG002567.
InParanoidP04186.
OrthoDBEOG71CFK5.
PhylomeDBP04186.

Enzyme and pathway databases

BRENDA3.4.21.47. 3474.

Gene expression databases

BgeeP04186.
CleanExMM_CFB.
GenevestigatorP04186.

Family and domain databases

Gene3D3.40.50.410. 1 hit.
InterProIPR011360. Compl_C2_B.
IPR028341. Complement_B.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
IPR009003. Trypsin-like_Pept_dom.
IPR002035. VWF_A.
[Graphical view]
PfamPF00084. Sushi. 3 hits.
PF00089. Trypsin. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PIRSFPIRSF001154. Compl_C2_B. 1 hit.
PIRSF500181. Complement_B. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00032. CCP. 3 hits.
SM00020. Tryp_SPc. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF57535. SSF57535. 3 hits.
PROSITEPS50923. SUSHI. 3 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP04186.
SOURCESearch...

Entry information

Entry nameCFAB_MOUSE
AccessionPrimary (citable) accession number: P04186
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: August 1, 1991
Last modified: May 14, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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