| IED ID | IndEnz0002001068 |
| Enzyme Type ID | protease001068 |
| Protein Name |
Cobra venom factor CVF CVFk Complement C3 homolog Cleaved into: Cobra venom factor alpha chain; Cobra venom factor gamma chain; Cobra venom factor beta chain |
| Gene Name | |
| Organism | Naja kaouthia (Monocled cobra) (Naja siamensis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Elapidae Elapinae Naja Naja kaouthia (Monocled cobra) (Naja siamensis) |
| Enzyme Sequence | MERMALYLVAALLIGFPGSSHGALYTLITPAVLRTDTEEQILVEAHGDSTPKQLDIFVHDFPRKQKTLFQTRVDMNPAGGMLVTPTIEIPAKEVSTDSRQNQYVVVQVTGPQVRLEKVVLLSYQSSFLFIQTDKGIYTPGSPVLYRVFSMDHNTSKMNKTVIVEFQTPEGILVSSNSVDLNFFWPYNLPDLVSLGTWRIVAKYEHSPENYTAYFDVRKYVLPSFEVRLQPSEKFFYIDGNENFHVSITARYLYGEEVEGVAFVLFGVKIDDAKKSIPDSLTRIPIIDGDGKATLKRDTFRSRFPNLNELVGHTLYASVTVMTESGSDMVVTEQSGIHIVASPYQIHFTKTPKYFKPGMPYELTVYVTNPDGSPAAHVPVVSEAFHSMGTTLSDGTAKLILNIPLNAQSLPITVRTNHGDLPRERQATKSMTAIAYQTQGGSGNYLHVAITSTEIKPGDNLPVNFNVKGNANSLKQIKYFTYLILNKGKIFKVGRQPRRDGQNLVTMNLHITPDLIPSFRFVAYYQVGNNEIVADSVWVDVKDTCMGTLVVKGDNLIQMPGAAMKIKLEGDPGARVGLVAVDKAVYVLNDKYKISQAKIWDTIEKSDFGCTAGSGQNNLGVFEDAGLALTTSTNLNTKQRSAAKCPQPANRRRRSSVLLLDSNASKAAEFQDQDLRKCCEDVMHENPMGYTCEKRAKYIQEGDACKAAFLECCRYIKGVRDENQRESELFLARDDNEDGFIADSDIISRSDFPKSWLWLTKDLTEEPNSQGISSKTMSFYLRDSITTWVVLAVSFTPTKGICVAEPYEIRVMKVFFIDLQMPYSVVKNEQVEIRAILHNYVNEDIYVRVELLYNPAFCSASTKGQRYRQQFPIKALSSRAVPFVIVPLEQGLHDVEIKASVQEALWSDGVRKKLKVVPEGVQKSIVTIVKLDPRAKGVGGTQLEVIKARKLDDRVPDTEIETKIIIQGDPVAQIIENSIDGSKLNHLIITPSGCGEQNMIRMAAPVIATYYLDTTEQWETLGINRRTEAVNQIVTGYAQQMVYKKADHSYAAFTNRASSSWLTAYVVKVFAMAAKMVAGISHEIICGGVRWLILNRQQPDGAFKENAPVLSGTMQGGIQGAEEEVYLTAFILVALLESKTICNDYVNSLDSSIKKATNYLLKKYEKLQRPYTTALTAYALAAADQLNDDRVLMAASTGRDHWEEYNAHTHNIEGTSYALLALLKMKKFDQTGPIVRWLTDQNFYGETYGQTQATVMAFQALAEYEIQMPTHKDLNLDITIELPDREVPIRYRINYENALLARTVETKLNQDITVTASGDGKATMTILTFYNAQLQEKANVCNKFHLNVSVENIHLNAMGAKGALMLKICTRYLGEVDSTMTIIDISMLTGFLPDAEDLTRLSKGVDRYISRYEVDNNMAQKVAVIIYLNKVSHSEDECLHFKILKHFEVGFIQPGSVKVYSYYNLDEKCTKFYHPDKGTGLLNKICIGNVCRCAGETCSSLNHQERIDVPLQIEKACETNVDYVYKTKLLRIEEQDGNDIYVMDVLEVIKQGTDENPRAKTHQYISQRKCQEALNLKVNDDYLIWGSRSDLLPTKDKISYIITKNTWIERWPHEDECQEEEFQKLCDDFAQFSYTLTEFGCPT |
| Enzyme Length | 1642 |
| Uniprot Accession Number | Q91132 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Complement-activating protein in cobra venom. It is a structural and functional analog of complement component C3b, the activated form of C3. It binds factor B (CFB), which is subsequently cleaved by factor D (CFD) to form the bimolecular complex CVF/Bb. CVF/Bb is a C3/C5 convertase that cleaves both complement components C3 and C5. Structurally, it resembles the C3b degradation product C3c, which is not able to form a C3/C5 convertase. Unlike C3b/Bb, CVF/Bb is a stable complex and completely resistant to the actions of complement regulatory factors H (CFH) and I (CFI). Therefore, CVF continuously activates complement resulting in the depletion of complement activity. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (90); Chain (4); Cross-link (1); Disulfide bond (12); Domain (2); Glycosylation (4); Helix (25); Metal binding (4); Propeptide (2); Region (4); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Cleavage on pair of basic residues;Complement system impairing toxin;Disulfide bond;Glycoprotein;Inflammatory response;Magnesium;Metal-binding;Secreted;Signal;Thioester bond;Toxin |
| Interact With | P01031 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: First processed by the removal of 4 Arg residues by furin-type protease, forming two chains, alpha and gamma/beta precursor, linked by a disulfide bond. Probably, the cobrin cleaves the C3a-like domain and then the C3d-like domain, generating the mature cobra venom factor (CVF). This mature CVF is composed of three chains: alpha, gamma and beta.; PTM: Contains 3 N-linked oligosaccharide chains, two in the alpha-chain and one in the beta-chain. Glycosylation is not required for the biological activity. However, it contributes to the immunogenicity of CVF. The carbohydrate content is 7.4. The major oligosaccharide is a symmetric fucosylated biantennary complex-type chain with an unusual alpha-galactosylated Le(x) structure at its non-reducing end. {ECO:0000269|PubMed:11320058, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:21217642}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000250 |
| Structure 3D | Electron microscopy (1); X-ray crystallography (5) |
| Cross Reference PDB | 3FRP; 3HRZ; 3HS0; 3PRX; 3PVM; 6I2X; |
| Mapped Pubmed ID | 31209353; |
| Motif | |
| Gene Encoded By | |
| Mass | 184,518 |
| Kinetics | |
| Metal Binding | METAL 516; /note=Magnesium; via carbonyl oxygen; METAL 539; /note=Magnesium; METAL 540; /note=Magnesium; via carbonyl oxygen; METAL 542; /note=Magnesium |
| Rhea ID | |
| Cross Reference Brenda |