CFB
entrez
629
canonical
uniprot
P00751
canonical
ensembl
ENSG00000239754
resolver
ensembl
ENSG00000241253
resolver
ensembl
ENSG00000241534
resolver
ensembl
ENSG00000242335
resolver
ensembl
ENSG00000243570
resolver
ensembl
ENSG00000243649
resolver
ensp
ENSP00000382862
resolver
ensp
ENSP00000411474
resolver
ensp
ENSP00000416561
resolver
enst
ENST00000399981
resolver
enst
ENST00000419920
resolver
genesymbol
CFB
resolver
genesymbol_syn
BF
resolver
genesymbol_syn
BFD
resolver
hgnc
HGNC:1037
resolver
uniprot
B0QZQ6
resolver
uniprot
O15006
resolver
uniprot
Q29944
resolver
uniprot
Q53F89
resolver
uniprot
Q5JP67
resolver
uniprot
Q5ST50
resolver
uniprot
Q96HX6
resolver
uniprot
Q9BTF5
resolver
uniprot
Q9BX92
resolver
uniprot_entry
CFAB_HUMAN
resolver
uniprot_sec
B0QZQ6
resolver
uniprot_sec
O15006
resolver
uniprot_sec
Q29944
resolver
uniprot_sec
Q53F89
resolver
uniprot_sec
Q5JP67
resolver
uniprot_sec
Q5ST50
resolver
uniprot_sec
Q96HX6
resolver
uniprot_sec
Q9BTF5
resolver
uniprot_sec
Q9BX92
resolver
amino_acid_sequence
MGSNLSPQLCLMPFILGLLSGGVTTTPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL
uniprot
proteins
disease_involvement
DISEASE: Macular degeneration, age-related, 14 (ARMD14) [MIM:615489]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:16518403}. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry. Haplotype analyses have identified a statistically significant common risk haplotype and two protective haplotypes. CFB variant His-9 and C2 variant Asp-318, as well as CFB variant Gln-32 and a variant in intron 10 of C2, confer a significantly reduced risk of AMD. {ECO:0000269|PubMed:16518403}.; DISEASE: Hemolytic uremic syndrome, atypical, 4 (AHUS4) [MIM:612924]: An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. {ECO:0000269|PubMed:17182750, ECO:0000269|PubMed:20513133}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype.; DISEASE: Complement factor B deficiency (CFBD) [MIM:615561]: An immunologic disorder characterized by increased susceptibility to bacterial infections, particularly Neisseria infections, due to a defect in the alternative complement pathway. {ECO:0000269|PubMed:24152280}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.47
uniprot
proteins
function
FUNCTION: Precursor of the catalytic component of the C3 and C5 convertase complexes of the alternative pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:3638964, PubMed:624565, PubMed:6554279, PubMed:6919543, PubMed:9748277). The alternative complement pathway acts as an amplification loop that enhances other complement pathways (classical, lectin and GZMK) by promoting formation of additional C3 and C5 convertases (PubMed:3638964, PubMed:624565, PubMed:6554279, PubMed:6919543, PubMed:9748277). CFB is cleaved and activated by CFD to generate Ba and Bb chains; Bb chain constituting the catalytic component of the C3 and C5 convertases (PubMed:6769474, PubMed:9748277). {ECO:0000269|PubMed:3638964, ECO:0000269|PubMed:624565, ECO:0000269|PubMed:6554279, ECO:0000269|PubMed:6769474, ECO:0000269|PubMed:6919543, ECO:0000269|PubMed:9748277}.; FUNCTION: [Complement factor B Bb]: Serine protease component of the complement C3 and C5 convertase complexes of the alternative complement pathway (PubMed:30643019, PubMed:3638964, PubMed:624565, PubMed:6554279, PubMed:6919543). Following cleavage and activation by factor D (CFD), forms the C3 convertase together with complement C3b (PubMed:3638964, PubMed:624565, PubMed:6554279, PubMed:6919543, PubMed:9748277). As part of the C3 convertase, cleaves and activates C3 into C3a anaphylatoxin and C3b opsonin, the next components of the complement pathways (PubMed:3638964, PubMed:624565, PubMed:6554279, PubMed:6919543, PubMed:9748277). When an additional complement C3b molecule binds to the C3 convertase, forms the C5 convertase, which cleaves and activates C5 into C5a anaphylatoxin and C5b component of the membrane attack complex (PubMed:30643019, PubMed:624565, PubMed:6554279). {ECO:0000269|PubMed:30643019, ECO:0000269|PubMed:3638964, ECO:0000269|PubMed:624565, ECO:0000269|PubMed:6554279, ECO:0000269|PubMed:6919543, ECO:0000269|PubMed:9748277}.; FUNCTION: [Complement factor B Ba]: Involved in proliferation and differentiation of preactivated B-lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. {ECO:0000269|PubMed:3486249}.
uniprot
proteins
mass_dalton
85533
uniprot
proteins
mutagenesis
MUTAGEN 348..350; /note="KLK->AAA: Decreases binding to the pro-C3-convertase complex. Does not affect Complement C3 beta chain binding."; /evidence="ECO:0000269|PubMed:31507604"; MUTAGEN 471; /note="E->A: Reduced formation of C3 convertase."; /evidence="ECO:0000269|PubMed:21205667"; MUTAGEN 644; /note="E->L: Decreased cleavage and activation by CFD."; /evidence="ECO:0000269|PubMed:21205667"; MUTAGEN 689; /note="Y->F: Decreased cleavage and activation by CFD."; /evidence="ECO:0000269|PubMed:21205667"; MUTAGEN 690; /note="A->W: Decreased cleavage and activation by CFD."; /evidence="ECO:0000269|PubMed:21205667"; MUTAGEN 733; /note="Q->R: Decreased cleavage and activation by CFD."; /evidence="ECO:0000269|PubMed:21205667"; MUTAGEN 734; /note="V->G: Decreased cleavage and activation by CFD."; /evidence="ECO:0000269|PubMed:21205667"; MUTAGEN 740; /note="D->N,E,A,S,Y: Abolished ability to cleave C3, without affecting cleavage by CFD and interaction with complement C3b."; /evidence="ECO:0000269|PubMed:9748277"; MUTAGEN 741; /note="F->W,A: Abolished ability to cleave C3, without affecting cleavage by CFD and interaction with complement C3b."; /evidence="ECO:0000269|PubMed:9748277
uniprot
proteins
post_translational_modification
PTM: Cleaved by CFD following activation of the alternative complement system, generating Ba and Bb chains (PubMed:21205667, PubMed:6769474, PubMed:874324, PubMed:9748277). Cleavage and activation takes place when CFB is already associated with complement C3b (PubMed:21205667). {ECO:0000269|PubMed:21205667, ECO:0000269|PubMed:6769474, ECO:0000269|PubMed:874324, ECO:0000269|PubMed:9748277}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10637221
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14656967
uniprot
proteins
pubmed
15016353
uniprot
proteins
pubmed
15068800
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16301317
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16518403
uniprot
proteins
pubmed
17182750
uniprot
proteins
pubmed
17310251
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19503103
uniprot
proteins
pubmed
19574954
uniprot
proteins
pubmed
2006911
uniprot
proteins
pubmed
20513133
uniprot
proteins
pubmed
21205667
uniprot
proteins
pubmed
2249879
uniprot
proteins
pubmed
24152280
uniprot
proteins
pubmed
28264884
uniprot
proteins
pubmed
30643019
uniprot
proteins
pubmed
31507604
uniprot
proteins
pubmed
3486249
uniprot
proteins
pubmed
3638964
uniprot
proteins
pubmed
3643061
uniprot
proteins
pubmed
624565
uniprot
proteins
pubmed
6308626
uniprot
proteins
pubmed
6323161
uniprot
proteins
pubmed
6342610
uniprot
proteins
pubmed
6546754
uniprot
proteins
pubmed
6554279
uniprot
proteins
pubmed
6769474
uniprot
proteins
pubmed
6919543
uniprot
proteins
pubmed
6957884
uniprot
proteins
pubmed
8181962
uniprot
proteins
pubmed
8225386
uniprot
proteins
pubmed
8247029
uniprot
proteins
pubmed
874324
uniprot
proteins
pubmed
9748277
uniprot
proteins
sequence_length
764
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6769474}.; SUBCELLULAR LOCATION: [Complement factor B Bb]: Cell surface {ECO:0000269|PubMed:30643019}. Note=Recruited to the surface of pathogens by complement C3b opsonin. {ECO:0000269|PubMed:30643019}.
uniprot
proteins