| IED ID | IndEnz0002013119 |
| Enzyme Type ID | protease013119 |
| Protein Name |
Snake venom metalloprotease inhibitor 02D01 02E11 10F07 Svmpi-Eoc7 Cleaved into: Tripeptide pEKW 1; Tripeptide pEKW 2; Tripeptide pEKW 3; Tripeptide pEKW 4; Tripeptide pEKW 5; Tripeptide pEKW 6; Tripeptide pEKW 7; Tripeptide pEKW 8; Tripeptide pEKW 9; Tripeptide pEKW 10; Tripeptide pEKW 11; Poly-His-poly-Gly peptide 4 pHpG-4 ; Poly-His-poly-Gly peptide 3 pHpG-3 ; Poly-His-poly-Gly peptide 2 pHpG-2 ; Poly-His-poly-Gly peptide 1 pHpG-1 ; C-type natriuretic peptide CNP |
| Gene Name | |
| Organism | Echis ocellatus (Ocellated saw-scaled viper) |
| 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 Viperidae Viperinae (vipers) Echis Echis ocellatus (Ocellated saw-scaled viper) |
| Enzyme Sequence | MFVSRLAASGLLLLSLLALSLDGKPLPQRQPHHIQPMEQKWLAPDAPPLEQKWLAPDAPPLEQKWLAPAAPPLEQKWLAPDAPPMEQKWLAPDAPPMEQKWLAPDAPPMEQKWLAPDAPPMEQKWLAPDAAPLEQKWLAPDAPPMEQKWLAPDAPPMEQKWQPQIPSLMEQRQLSSGGTTALRQELSPRAEAASGPAVVGGGGGGGGGSKAALALPKPPKAKGAAAATSRLMRDLRPDGKQASQKWGRLVDHDHDHHHHHHPGSSVGGGGGGGGGGARRLKGLAKKGVAKGCFGLKLDRIGSMSGLGC |
| Enzyme Length | 308 |
| Uniprot Accession Number | A8YPR6 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: pEKW and poly-His-poly-Gly peptides may serve as metalloproteinase inhibitors during glandular storage. Their inhibition may be instantly disengaged, by dilution or physiochemical change, when venom is injected into tissue of the prey. {ECO:0000303|PubMed:18029259}.; FUNCTION: [C-type natriuretic peptide]: Exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Disulfide bond (1); Modified residue (11); Natural variant (10); Peptide (16); Propeptide (13); Region (2); Signal peptide (1) |
| Keywords | Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Hypotensive agent;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Pyrrolidone carboxylic acid;Repeat;Secreted;Signal;Toxin;Vasoactive;Vasodilator |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 39; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:18029259; MOD_RES 51; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:18029259; MOD_RES 63; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:18029259; MOD_RES 75; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:18029259; MOD_RES 87; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:18029259; MOD_RES 99; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:18029259; MOD_RES 111; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:18029259; MOD_RES 123; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:18029259; MOD_RES 135; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:18029259; MOD_RES 147; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:18029259; MOD_RES 159; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:18029259 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,722 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |