Detail Information for IndEnz0002001065
IED ID IndEnz0002001065
Enzyme Type ID protease001065
Protein Name A.superbus venom factor 1
AVF-1
CVF-like
Complement C3 homolog

Cleaved into: AVF-1 alpha chain; AVF-1 gamma chain; AVF-1 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 MEGMALYLVAALLIGFPGSSHGALYTLITPGVLRTDTEEQILVEAHGDSVPKQAVISIHDFPRRQKTLFQTRVDMNPAGGMLVTPTIKIPAKELNKESRQNQYVVVKVSGLPLELEKVVLLSYQSGFVFIQTDKGIYTPGSPVRYRVFSMDYNMHRMDKTVIVEFQTPEGVVVSSNPVNPSSVLIRPYNLPELVSFGTWKAVAKYEHSPEESYTAYFDVREYVLPSFEVRLQPSDKFLYIDGNKNFHVSITARYLYGKKVEGVAFVLFGVKIDDAKKSIPDSLTRIPIIDGDGEAILKRDTLRSRFQNLNELVGHTLYASVTVMTESGSDMVVTEQSGIHIVTSPYQIYFTKTPKYFKPGMPYELTVYVTNPDGSPAANVPVVSEAIRSEGTTLSDGTAKLILNTPLNTQSLPITVRTNHRDLPSERQATKSMTATAYQTQGGSGNYLHVAITSAEIKAGDNLPVNFNVRGNANSLNQIKYFTYLILTKGKIFKVGRQPKGEGQNLVTMNLRITPDLIPAFRFVAYYQVGNNEIVADSVWVDVKDTCMGTLVVKGASSRDNRIQKPGAAMKIKLEGDPGARVGLVAVDKAVYVLNDKYKISQAKIWDTIEKSDFGCTAGGGQNNLGVFEDAGLALTTSTNLNTKQRSVATCPQPTNRRRRSSVLLLDSKANKAAQFQDQNLRKCCEDGMHENPMGYTCEKRAKYIQEGDACKAAFLECCRYIKGIRDENQRESELFLARSDFEDELFGEDNIISRSDFPESWLWLTEDLKEPPNSQGISSKTLSFYLRDSITTWEVLAVSIAPTKGICVAEPYEITVMKDFFIDLRVPYSVVKNEQVEIRAVLYNYADEDIYVRVELLYNPAFCSASTEGQRYRVQVPVKALSSWAVPFVIVPLEQGLHDVEVKASVRGELASDGVRKKLKVVPEGERKNIVTVIELDPSVKGVDGTQEQTVIANKLDDKVPETEIETKISVLGDPVAQIIENSIDGSKLNHLIITPSGCGEQNMITMTPSVIATYYLDATGQWENLGVDRRTEAVKQIMKGYAQQMVYKKADHSYAAFPNRASSSWLTAYVVKVFAMAAKIVKDIKHEIICGGVKWLILNRQQPDGVFKENAPVIHGEMLGGTKGAEPEVSLTAFILTALLESRSVCNEHINILDSSINKAIDYLLKKYEKLQRPYTTALTAYALAAAERLNDDRVLMAASTGRDRWEEHNARTHNIEGTSYALLALLKMKKFAEAGPVVKWLIDQKYYGGTYGQTQATVMVFQALAEYEIQIPTHKDLNLDISINLPEREVPLRYSINYGNALVARTAETKLNEDFTVSASGDGKATMTILTVYNAQLREDANVCNKFHLDVSVENAQLNSKQAKGAKDTLRLKICTRYLGEVDSTMTIIDVSMLTGFLADAEDLTRLSKGVDRYISKFEIDNNMVQKGTVVIYLDKVSHSEVECLHFKIHKHFEVGFIQPGSVKVYSYYNLDEQCTKFYHPDKGTGLLNKICHGNICRCAEESCSLLNQQKKIDLQLRIQKACAPNVDYVYKTKLLQIEEKDGNDIYVMDVLEVIKGGTDRNPQAKARQYVSQRKCQEALNLKLNNDYLIWGLSSDLWPRKNDISYLITKNTWIERWPNEDECQDEEFQNLCDDFAQLSNTLTIFGCPT
Enzyme Length 1652
Uniprot Accession Number Q0ZZJ6
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 does CVF/Bb). {ECO:0000269|PubMed:17412383}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (4); Cross-link (1); Disulfide bond (12); Domain (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;Inflammatory response;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. 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 184,726
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