Detail Information for IndEnz0002014266
IED ID IndEnz0002014266
Enzyme Type ID protease014266
Protein Name Complement factor D
EC 3.4.21.46
28 kDa adipocyte protein
Adipsin
C3 convertase activator
Properdin factor D
Gene Name Cfd Adn Df
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MHSSVYFVALVILGAAVCAAQPRGRILGGQEAAAHARPYMASVQVNGTHVCGGTLLDEQWVLSAAHCMDGVTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPHPGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGVVTHAGRRPDVLHQLRVSIMNRTTCNLRTYHDGVVTINMMCAESNRRDTCRGDSGSPLVCGDAVEGVVTWGSRVCGNGKKPGVYTRVSSYRMWIENITNGNMTS
Enzyme Length 259
Uniprot Accession Number P03953
Absorption
Active Site ACT_SITE 66; /note=Charge relay system; ACT_SITE 115; /note=Charge relay system; ACT_SITE 209; /note=Charge relay system
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor.; EC=3.4.21.46;
DNA Binding
EC Number 3.4.21.46
Enzyme Function FUNCTION: Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (1); Beta strand (14); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (5); Helix (4); Propeptide (1); Signal peptide (1); Turn (1)
Keywords 3D-structure;Alternative splicing;Complement alternate pathway;Disulfide bond;Glycoprotein;Hydrolase;Immunity;Innate immunity;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification PTM: N-glycosylated. {ECO:0000269|PubMed:16944957, ECO:0000269|PubMed:17330941}.
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D X-ray crystallography (1)
Cross Reference PDB 5FCR;
Mapped Pubmed ID 10725249; 10769753; 10982846; 10984455; 11130978; 11724962; 12401879; 12547703; 12558660; 12949072; 1374388; 15585877; 15883171; 15972690; 16141072; 16651386; 16951374; 17179051; 17410102; 17962484; 18068164; 18160458; 18188184; 19112490; 20038603; 20581430; 20709903; 20870940; 21263075; 21351141; 21378161; 21688269; 21704012; 21943708; 23012479; 23650618; 24036114; 24995977; 2506639; 25467802; 27564415; 27707997; 27775713; 28049691; 28057640; 28539427; 29531168; 31167128; 32012117; 32079203; 32376801; 3299705; 3299706; 33067533; 33135458; 34155972; 6411703; 7530249; 7592907; 7782070; 8043949; 8075499; 8996238;
Motif
Gene Encoded By
Mass 28,057
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.21.46;