| IED ID | IndEnz0002001069 |
| Enzyme Type ID | protease001069 |
| Protein Name |
Ophiophagus venom factor OVF CVF-like Complement C3 homolog Cleaved into: OVF alpha chain; OVF gamma chain; OVF beta chain |
| Gene Name | |
| Organism | Ophiophagus hannah (King cobra) (Naja hannah) |
| 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 Ophiophagus Ophiophagus hannah (King cobra) (Naja hannah) |
| Enzyme Sequence | MEGMALYLVAALLIGFPGSSHGALYTLITPGVLRTDTEEQILVEAHGDNTPKQLDIFVHDFPRKQKILFQKRVDMNPAGDMLVTPTIKIPAEEVSKDSRQNQYVVVQVTGPQVRLEKVVLLSYQSGFVFIQTDKGIYTPGSPVLYRVFSMDHNMRQMDKTVVVEFQTPEGIVVSSNRIDLNFTRPYNLPELGSLGTWKIVAKYEHSPENYTAYFDVRKYVLPSFEVHLQPSEKSFYIDGNENFHVSITARYLYGEEVEGVAFVLFGVKIDGAKKSIPDSLTRIPILDGDGEATLKRDTLRSRFPNLNELVGHTLYASVTVITESGSDMVATEQSGIHIVTSPYQIYFTKTPKYFKPGMPYELTVYVTNPDGSPAAKVPVVSEAIHSEGTTLSDGTAKLILNTPLDTQSLLITVRTNHGDLPRERQATKSMTATAYQTQGGSGNYLHVAITSTEIKPGDNLPVNFNVRGNANSLNQVKYFTYLVGRQPKGAGQNLVAMNLRITPDLIPSFRFVAYYQVGNNEIVADSVWVDVKDTCMGTLVVKGASLTDNQIHMPGAAMKIKLEGDPGAQVGLVAVDKAVYVLNDKYKISQAKIWDTIEKSDFGCTAGGGQNNLGVFEDAGLALTTSTNLNTKQRSDTKCPQPANRRRRSSVLLLDSKASKAAQFQDQDLRKCCEDSMHENPMGYTCEKRAKYIQEGDACKAAFLECCRYIKGILDENQWESGLFLPRNDNEDGFIQDSDIIPRTDFPKSWLWHTVQLTEQPNSNGISSKTMSIYLKESITTWEVLAVSFTPTKGICVAEPYEIKVMKDFFIDLRVPYSVVRKEQVEIRAVLYNYAGRDIYVRVELLYNPAFCSASTEEQRYRQQFTIKALSSRAVPFVIVPLQQGLHDIEVRASVQGWESVSDGVKKKLKVVPEGVQKCIVTIIKLDPRAKGVDGTQREVVKARKLDDKVPDTEIETKITIQADPVAQIIENSIDGSKLNHLIITPSGCGEQNMIRMTAPVIATYYLDTTEQWETLGRNHRNEAVKQIMTGYAQQMVYKKANHSYAAFTNRASSTWLTAYVVKVFAMATKMVAGISHEIICGGVRWLILNRQQPDGAFKENAPVLSGTMQGGIQGDESEVTVTAFTLVALLESKTICNDSVNSLDSSIKKATDYLLKKYEKLQRPYTTALTAYALAAADRLNDDRVLMAASTGKNRWEEYNAHTHNVEGTSYALLALLKMKKFDQTGPIVRWLTDQNFYGGTYGQTQATVMLFQALAEYKIQMPTHKDLNLDIIIKLPERELPLHYRLDATNAILARTAETKLNQDFTVSASGDGTATMTILTVYNAQLQEKANVCNKFHLDVSVENIHLNFKHAKGAKGALMLKICMRYLGEVDSTMTIIDISMLTGFLPDAEDLTRLSEGVDRYISRYEVDNNMAQKVAVIIYLDKVSHSEDECLQFKILKHFEVGFIQPGSVKVYSYYNLDEQCTKFYHPDKGTGLLNKICVGNICRCAAETCSLLSQQEKIDLPLRIQKACASNVDYVYKTKLLRIEEKDGYDIYVMDVLEVIKPGTDENPQANARQYISQRKCQEALNLNVNDDYLIWGLRSDLWPMKDKFSYLITKNTWIERWPHEDECQDEEFQNLCLDFAHLSNILTIFGCPT |
| Enzyme Length | 1641 |
| Uniprot Accession Number | I2C090 |
| 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 OVF/Bb. OVF/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, OVF/Bb is a stable complex and completely resistant to the actions of complement regulatory factors H (CFH) and I (CFI). Therefore, OVF continuously activates complement (By similarity). As a result, OVF exhibits complement-depleting activity. {ECO:0000250, ECO:0000269|PubMed:22561424}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (4); Cross-link (1); Disulfide bond (12); Domain (2); Glycosylation (2); Metal binding (4); Propeptide (2); Region (4); Signal peptide (1) |
| Keywords | Cleavage on pair of basic residues;Complement system impairing toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Magnesium;Metal-binding;Secreted;Signal;Thioester bond;Toxin |
| Interact With | |
| 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, a cobrin-like protease cleaves the C3a-like domain and then the C3d-like domain, generating the mature venom factor (OVF) (By similarity). {ECO:0000250}.; PTM: The beta chain is not glycosylated. {ECO:0000269|PubMed:22561424}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000269|PubMed:22561424 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 183,928 |
| Kinetics | |
| Metal Binding | METAL 507; /note=Magnesium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 530; /note=Magnesium; /evidence=ECO:0000250; METAL 531; /note=Magnesium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 533; /note=Magnesium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |