| IED ID | IndEnz0002005700 |
| Enzyme Type ID | protease005700 |
| Protein Name |
Complement factor B EC 3.4.21.47 C3/C5 convertase Glycine-rich beta glycoprotein GBG PBF2 Properdin factor B Cleaved into: Complement factor B Ba fragment; Complement factor B Bb fragment |
| Gene Name | CFB BF BFD |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MGSNLSPQLCLMPFILGLLSGGVTTTPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL |
| Enzyme Length | 764 |
| Uniprot Accession Number | P00751 |
| Absorption | |
| Active Site | ACT_SITE 526; /note=Charge relay system; ACT_SITE 576; /note=Charge relay system; ACT_SITE 699; /note=Charge relay system |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=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.; EC=3.4.21.47; |
| DNA Binding | |
| EC Number | 3.4.21.47 |
| Enzyme Function | 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. 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Beta strand (48); Chain (3); Disulfide bond (11); Domain (5); Glycosylation (5); Helix (29); Mutagenesis (1); Natural variant (17); Sequence conflict (6); Signal peptide (1); Turn (6) |
| Keywords | 3D-structure;Age-related macular degeneration;Alternative splicing;Cleavage on pair of basic residues;Complement alternate pathway;Direct protein sequencing;Disease variant;Disulfide bond;Glycation;Glycoprotein;Hemolytic uremic syndrome;Hydrolase;Immunity;Innate immunity;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Sushi;Zymogen |
| Interact With | P01024; Q92496-1; Q92496-3 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000269|PubMed:6546754 |
| Structure 3D | X-ray crystallography (21) |
| Cross Reference PDB | 1DLE; 1Q0P; 1RRK; 1RS0; 1RTK; 2OK5; 2WIN; 2XWB; 2XWJ; 3HRZ; 3HS0; 6QSW; 6QSX; 6RAV; 6RUR; 6RUV; 6T8U; 6T8V; 6T8W; 7JTN; 7JTQ; |
| Mapped Pubmed ID | 10531307; 1067618; 11694537; 11803045; 15016353; 15068800; 15174051; 15199963; 15648851; 16061287; 16301317; 17182573; 17359931; 17395591; 17576744; 17767156; 17916747; 17921140; 18039777; 18096230; 18325906; 18493315; 18502988; 18515590; 18806293; 18806297; 18928972; 18936151; 18987644; 19000152; 19005416; 19015224; 19117936; 19143814; 19167759; 19169232; 19187590; 19255449; 19259132; 19277984; 19279234; 19336475; 19344414; 19399715; 19423540; 19503103; 19556007; 19603351; 19661236; 19696172; 19825847; 19833879; 19834535; 19838195; 19851445; 19899988; 19913121; 20007824; 20108004; 20109314; 20157618; 20193965; 20205591; 20378180; 20385819; 20406964; 20438785; 20466734; 20523265; 20575108; 20587610; 20628086; 20801516; 20837143; 20848568; 20888482; 21163532; 21205667; 21282580; 21541267; 21555552; 21816153; 21988832; 22232432; 22234447; 22273503; 22542119; 22714898; 22869612; 22930722; 23112567; 23233260; 23300094; 23313922; 23356914; 23373431; 23624872; 23864767; 2420889; 24287422; 24453474; 24519512; 24557084; 24652797; 24739633; 24906628; 24965207; 25057901; 25532781; 25604034; 25758434; 26496610; 26510395; 26537423; 26660535; 26671509; 26908325; 27241480; 27436813; 27461873; 27759029; 279011; 28173125; 28210841; 29308663; 293688; 301546; 30179527; 3052276; 30713161; 30829612; 30926668; 30974970; 31514225; 31541546; 32073845; 32762675; 33334325; 33419768; 33740660; 33847939; 33847940; 34075561; 3421908; 34233521; 6238120; 6707020; 6906228; 809512; 82604; 8786315; 950465; 978134; |
| Motif | |
| Gene Encoded By | |
| Mass | 85,533 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.47; |