| IED ID | IndEnz0002001066 |
| Enzyme Type ID | protease001066 |
| Protein Name |
A.superbus venom factor 2 AVF-2 CVF-like Complement C3 homolog Cleaved into: AVF-2 alpha chain; AVF-2 gamma chain; AVF-2 beta chain |
| Gene Name | |
| Organism | Austrelaps superbus (Lowland copperhead snake) (Hoplocephalus superbus) |
| 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 Acanthophiinae Austrelaps Austrelaps superbus (Lowland copperhead snake) (Hoplocephalus superbus) |
| Enzyme Sequence | MEGMALYLVAALLIGFPGSSHGALYTLITPGVLRTDTEEQILVEAHGDSAPKQPVISIHDFPRRQKILFQIRVDMNPAGGMLVTPTIKIPAKELNKESRQNQYVVVKVSGLPLELEKVVLLSSQSGFVFIQTDKGIYTPGSLVRYRVFSMDYNMHRMDKTVIVEFQTPEGVVVSSNPINPSSVLIRHYNLSELVSFGTWKAVAKYEHSPEESYTAYFDVREYVLPSFEVRLQPSDKFLYIDGNKNFHVSITARYLYGKKVEGVAFVLFGVKIDDAKKSIPDSLTRIPIIDGDGEAILKRDILRSRFQNLNELVGHTLYASVTVMTESGSDMVVTEQSGIHIVTSPYQIYFTKPPKYFKPGMPYELTVYVTNPDGSPAANVPVVSEAIHSEGTTLSDGTAKLILNTPLNTQSLPITVRTNHRDLPRERQATKSMTATAYQTQGGSGNYLHVAITSTEIKAGDNLPVSFNVRGNANSLNQIKYFTYLILTKGKIFKVGRQPRGEGQNLVTMNLRITPDLIPAFRFVAYYQVGNNEIVADSVWVDVKDTCMGMLVVKGASSRDNRIQKPGAAMKIKLEGDPGARVGLVAVDKAVYVLNDKYKISQAKIWDTIEKSDFGCTAGGGQDNLGVFEDAGLALTTSTNLNTKQRSVATCPQPTNRRRRSSVLLLDSKASKAAQFQEQNLHKCCEDGMHENPMGYTCEKRAKYTQEGDACKAAFLECCRYIKGIRDENQRESELFLARSDFEDEFFEEDNIISRSDFPDSWLWLTEDLNEPPNSQGISSKTLSFYLKDSITTWEVLAVSIAPTKGICVAEPYEITVMKDFFIDLRVPYSVVKNEQVEIRAVLYNYADEDIYVRVELLYNPAFCSASAEGQRYRVQVPVRALSSWAVPFVIVPLEQGLHDVEVKASVRGELASDGVRKKLKVVPEGERKNIVTVIELDPSVKGVGGTQEQTVVANKLDDKVPETEIETKFSVLGDPVAQIIENSIDGSKLSHLIITPSGSGEQNMITMTPSVIATYYLDATGQWENLGVDRRTEAVKQIMKGYAQQMVYKKADHSYASFVNRASSSWLTAYVVKVFAMAAKMVKDINHEIICGGVKWLILNRQQSDGVFKENAPVILGGMMGGTQGAEPEVSLTAFILVALLESRSVCNEHINILDNSINKATDYLLKKYEKLQRPYTTALTAYALAAAERLNDDRVLMAASTGRDRWEEHARTHNIEGTSYALLALLKMKKFAEAGPVVKWLIDQKYYGGTYGQTQATVMVFQALAEYEIQIPTHKDLNLNISINLPEREVPLRYSINYGNALVARTAETKLNEDFTVSASGDGKATMTILTVYNAQLREDANVCNKFHLNVSVENAQLNSKQAKGAKDTLRLKICTRYLGEVDSTMTIIDVSMLTGFLPDTEDLTRLSKGVDRYISKFEIDNNMVQKGTVVIYLDKVSHSEVECLNFKIHKHFEVGFIQPGPVKVYSYYNLDEQCTKFYHPDKGTGLLNKICHGNICRCAEQSCSLLNQQKKIDLPLRIQKACAPNVDYVYKAKLLRIEEKDGNDIYVMDVLEVIKGGTDRNPQAKARQYVSQRKCQEALNLNLNNDYLIWGLSSDLWPMKNDISYLITKNTWIERWPNEDECQDEEFQNLCDDFAQLSNTLTIFGCPT |
| Enzyme Length | 1651 |
| Uniprot Accession Number | A0RZC6 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Complement-activating protein in snake 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 AVF/Bb. AVF/Bb is a C3 convertase that cleaves complement component C3, but not C5 (as do CVF/Bb) (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (4); Disulfide bond (12); Domain (2); Glycosylation (3); Metal binding (4); Propeptide (2); Region (4); Signal peptide (1) |
| Keywords | Cleavage on pair of basic residues;Complement system impairing toxin;Disulfide bond;Glycoprotein;Inflammatory response;Magnesium;Metal-binding;Secreted;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| 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. This mature AVF is composed of three chains: alpha, gamma and beta (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 184,576 |
| Kinetics | |
| Metal Binding | METAL 519; /note=Magnesium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 542; /note=Magnesium; /evidence=ECO:0000250; METAL 543; /note=Magnesium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 545; /note=Magnesium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |