Complement factor B precursor - Mus musculus (Mouse)

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P04186 (CFAB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 137. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Complement factor B
EC=3.4.21.47

Alternative name(s):
C3/C5 convertase

Gene names

Name:	Cfb
Synonyms:	Bf, H2-Bf

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	761 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	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.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain. Contains 3 Sushi (CCP/SCR) domains. Contains 1 VWFA domain.

Ontologies

Keywords
Biological process	Complement alternate pathway Immunity Innate immunity
Cellular component	Secreted
Domain	Repeat Signal Sushi
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Traceable author statement PubMed 9238044. Source: MGI complement activation, alternative pathway Inferred from mutant phenotype PubMed 9238044. Source: MGI proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

By similarity

Chain

23 – 761

739

Complement factor B

PRO_0000027548

Chain

23 – 256

234

Complement factor B Ba fragment

PRO_0000027549

Chain

257 – 761

505

Complement factor B Bb fragment

PRO_0000027550

Regions

Domain

32 – 97

Sushi 1

Domain

98 – 157

Sushi 2

Domain

160 – 217

Sushi 3

Domain

267 – 466

200

VWFA

Domain

474 – 754

281

Peptidase S1

Sites

Active site

523

Charge relay system

Active site

573

Charge relay system

Active site

696

Charge relay system

Amino acid modifications

Glycosylation

119

N-linked (GlcNAc...) Ref.6

Glycosylation

139

N-linked (GlcNAc...) Potential

Glycosylation

282

N-linked (GlcNAc...) Ref.5

Glycosylation

375

N-linked (GlcNAc...) Potential

Disulfide bond

34 ↔ 73

By similarity

Disulfide bond

59 ↔ 95

By similarity

Disulfide bond

100 ↔ 142

By similarity

Disulfide bond

128 ↔ 155

By similarity

Disulfide bond

162 ↔ 202

By similarity

Disulfide bond

188 ↔ 215

By similarity

Disulfide bond

508 ↔ 524

By similarity

Disulfide bond

692 ↔ 722

By similarity

Experimental info

Sequence conflict

730

L → P in AAA39549. Ref.4

Sequence conflict

745

V → E in AAA39549. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P04186 [UniParc].

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

FASTA

761

85,004

        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' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Plasma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M60646 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.
IPI	IPI00990279.
PIR	BBMS. A38875.
UniGene	Mm.653.
3D structure databases
ProteinModelPortal	P04186.
SMR	P04186. Positions 33-761.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000117677.
Protein family/group databases
MEROPS	S01.196.
PTM databases
PhosphoSite	P04186.
Proteomic databases
PaxDb	P04186.
PRIDE	P04186.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000128767; ENSMUSP00000119977; ENSMUSG00000090231.
Organism-specific databases
MGI	MGI:105975. Cfb.
Phylogenomic databases
eggNOG	NOG306397.
HOGENOM	HOG000038034.
HOVERGEN	HBG002567.
InParanoid	P04186.
Enzyme and pathway databases
BRENDA	3.4.21.47. 3474.
Gene expression databases
ArrayExpress	P04186.
Bgee	P04186.
CleanEx	MM_CFB.
Genevestigator	P04186.
GermOnline	ENSMUSG00000024371. Mus musculus.
Family and domain databases
InterPro	IPR011360. Compl_C2_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]
Pfam	PF00084. Sushi. 3 hits. PF00089. Trypsin. 1 hit. PF00092. VWA. 1 hit. [Graphical view]
PIRSF	PIRSF001154. Compl_C2_B. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00032. CCP. 3 hits. SM00020. Tryp_SPc. 1 hit. SM00327. VWA. 1 hit. [Graphical view]
SUPFAM	SSF57535. Complement_control_module. 3 hits. SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50923. SUSHI. 3 hits. PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. PS50234. VWFA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

CFAB_MOUSE

Accession

Primary (citable) accession number: P04186

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	August 1, 1991
Last modified:	April 3, 2013
This is version 137 of the entry and version 2 of the sequence. [Complete 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents