| Tag | Content |
|---|
| CPLM ID | CPLM-001807 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Complement factor B |
Protein Synonyms/Alias | C3/C5 convertase; Glycine-rich beta glycoprotein; GBG; PBF2; Properdin factor B; Complement factor B Ba fragment; Complement factor B Bb fragment |
Gene Name | CFB |
Gene Synonyms/Alias | BF; BFD |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 291 | SNFTGAKKCLVNLIE | glycation | [1, 2] |
|
Reference | [1] The principal site of glycation of human complement factor B. Niemann MA, Bhown AS, Miller EJ. Biochem J. 1991 Mar 1;274 ( Pt 2):473-80. [ PMID: 2006911] [2] Complete primary structure for the zymogen of human complement factor B. Mole JE, Anderson JK, Davison EA, Woods DE. J Biol Chem. 1984 Mar 25;259(6):3407-12. [ PMID: 6546754] |
Functional Description | 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. It has also been implicated in proliferation and differentiation of preactivated B- lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation of preactivated B-lymphocytes. |
Sequence Annotation | DOMAIN 35 100 Sushi 1.
DOMAIN 101 160 Sushi 2.
DOMAIN 163 220 Sushi 3.
DOMAIN 270 469 VWFA.
DOMAIN 477 757 Peptidase S1.
ACT_SITE 526 526 Charge relay system.
ACT_SITE 576 576 Charge relay system.
ACT_SITE 699 699 Charge relay system.
CARBOHYD 122 122 N-linked (GlcNAc...).
CARBOHYD 142 142 N-linked (GlcNAc...).
CARBOHYD 285 285 N-linked (GlcNAc...).
CARBOHYD 291 291 N-linked (Glc) (glycation).
CARBOHYD 378 378 N-linked (GlcNAc...).
DISULFID 37 76
DISULFID 62 98
DISULFID 103 145
DISULFID 131 158
DISULFID 165 205
DISULFID 191 218
DISULFID 478 596
DISULFID 511 527
DISULFID 599 615
DISULFID 656 682
DISULFID 695 725 |
Keyword | 3D-structure; Alternative splicing; Cleavage on pair of basic residues; Complement alternate pathway; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Glycation; Glycoprotein; Hemolytic uremic syndrome; Hydrolase; Immunity; Innate immunity; Polymorphism; Protease; Reference proteome; Repeat; Secreted; Serine protease; Signal; Sushi; Zymogen. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 764 AA |
Protein Sequence | MGSNLSPQLC LMPFILGLLS GGVTTTPWSL ARPQGSCSLE GVEIKGGSFR LLQEGQALEY 60
VCPSGFYPYP VQTRTCRSTG SWSTLKTQDQ KTVRKAECRA IHCPRPHDFE NGEYWPRSPY 120
YNVSDEISFH CYDGYTLRGS ANRTCQVNGR WSGQTAICDN GAGYCSNPGI PIGTRKVGSQ 180
YRLEDSVTYH CSRGLTLRGS QRRTCQEGGS WSGTEPSCQD SFMYDTPQEV AEAFLSSLTE 240
TIEGVDAEDG HGPGEQQKRK IVLDPSGSMN IYLVLDGSDS IGASNFTGAK KCLVNLIEKV 300
ASYGVKPRYG LVTYATYPKI WVKVSEADSS NADWVTKQLN EINYEDHKLK SGTNTKKALQ 360
AVYSMMSWPD DVPPEGWNRT RHVIILMTDG LHNMGGDPIT VIDEIRDLLY IGKDRKNPRE 420
DYLDVYVFGV GPLVNQVNIN ALASKKDNEQ HVFKVKDMEN LEDVFYQMID ESQSLSLCGM 480
VWEHRKGTDY HKQPWQAKIS VIRPSKGHES CMGAVVSEYF VLTAAHCFTV DDKEHSIKVS 540
VGGEKRDLEI EVVLFHPNYN INGKKEAGIP EFYDYDVALI KLKNKLKYGQ TIRPICLPCT 600
EGTTRALRLP PTTTCQQQKE ELLPAQDIKA LFVSEEEKKL TRKEVYIKNG DKKGSCERDA 660
QYAPGYDKVK DISEVVTPRF LCTGGVSPYA DPNTCRGDSG GPLIVHKRSR FIQVGVISWG 720
VVDVCKNQKR QKQVPAHARD FHINLFQVLP WLKEKLQDED LGFL 764 |
Gene Ontology | GO:0005576; C:extracellular region; TAS:Reactome. GO:0005886; C:plasma membrane; TAS:Reactome. GO:0001848; F:complement binding; TAS:UniProtKB. GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome. GO:0006957; P:complement activation, alternative pathway; NAS:UniProtKB. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. GO:0030449; P:regulation of complement activation; TAS:Reactome. |
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Pfam | |
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