IED ID | IndEnz0002016453 |
Enzyme Type ID | protease016453 |
Protein Name |
Endothelin-converting enzyme 1 ECE-1 EC 3.4.24.71 |
Gene Name | Ece1 |
Organism | Rattus norvegicus (Rat) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
Enzyme Sequence | MGSLRPPQGLGLQWSSFFLGKKGPGLTVSLPLLASSLQVNFRSPRSGQRCWAARTSVEKRLVVLVTLLAAGLVACLAALGIQYRTRTPPVCLTEACVSVTSSILNSMDPTVDPCQDFFSYACGGWIKANPVPDGHSRWGTFSNLWEHNQAIIKHLLENSTASASEAEKKAQVYYRACMNETRIEELRAKPLMELIEKLGGWNITGPWAKDNFQDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEDSIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNAIFYPVEINESEPIVVYDKEYLRQVSTLINSTDKCLLNNYMMWNLVRKTSSFLDQRFQDADEKFMEVMYGTKKTCLPRWKFCVSDTENNLGFALGPMFVKATFAEDSKNIASEIILEIKKAFEESLSTLKWMDEDTRRSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSLRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPNALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKQQTECMVQQYNNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEQILPTLGLTSNQLFFLGFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSLSNSKEFSEHFRCPLGSPMNPRHKCEVW |
Enzyme Length | 762 |
Uniprot Accession Number | P42893 |
Absorption | |
Active Site | ACT_SITE 600; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; ACT_SITE 663; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233" |
Activity Regulation | ACTIVITY REGULATION: Inhibited by phosphoramidon. {ECO:0000250}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.; EC=3.4.24.71; |
DNA Binding | |
EC Number | 3.4.24.71 |
Enzyme Function | FUNCTION: Converts big endothelin-1 to endothelin-1. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Alternative sequence (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (10); Metal binding (3); Mutagenesis (4); Topological domain (2); Transmembrane (1) |
Keywords | Alternative splicing;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10491078, ECO:0000269|PubMed:8645169}; Single-pass type II membrane protein {ECO:0000269|PubMed:10491078, ECO:0000269|PubMed:8645169}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10073607; 10401760; 10894793; 11043448; 11078391; 11145282; 11813889; 12189509; 12193087; 12193123; 12972712; 14627492; 15733912; 16170464; 16410403; 18385664; 18586023; 18767389; 19371338; 19596829; 20099522; 21878523; 22881710; 23600389; 8575076; 9449382; 9595392; |
Motif | |
Gene Encoded By | |
Mass | 86,126 |
Kinetics | |
Metal Binding | METAL 599; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 603; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 659; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233" |
Rhea ID | |
Cross Reference Brenda | 3.4.24.71; |