Detail Information for IndEnz0002016452
IED ID IndEnz0002016452
Enzyme Type ID protease016452
Protein Name Endothelin-converting enzyme 1
ECE-1
EC 3.4.24.71
Gene Name Ece1
Organism Mus musculus (Mouse)
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 Mus Mus Mus musculus (Mouse)
Enzyme Sequence MRTVWSPLAAALAALGMSTYKRATLDEEDLVDSLSEGDVYPNGLQVNFRSSRSGQRCWAARTSVEKRLVVLVTLLAAGLVACLAALGIQYQTRTPPVCLTEACVSVTSSILNSMDPTVDPCQDFFSYACGGWIKANPVPDGHSRWGTFSNLWEHNQAVIKHLLENATASVSEAERKAQVYYRACMNETRIEELRAKPLMELIEKLGGWNITGPWAKDNFQDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEDAIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVVYDKEYLRQVSTLINNTDKCLLNNYMMWNLVRKTSSFLDQRFQDADEKFMEVMYGTKKTCIPRWKFCVSDTENNLGFALGPMFVKATFAEDSKNIASEIIMEIKKAFEESLSTLKWMDEETRRSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPNALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKQQTECMVQQYSNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEQTLPTLGLTSNQLFFLGFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSLSNSKEFSEHFRCPPGSPMNPHHKCEVW
Enzyme Length 769
Uniprot Accession Number Q4PZA2
Absorption
Active Site ACT_SITE 607; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; ACT_SITE 670; /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. {ECO:0000250}.
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); Modified residue (1); Topological domain (2); Transmembrane (1)
Keywords Alternative splicing;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Modified Residue MOD_RES 24; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P42892
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10626068; 10811845; 11290299; 11328956; 12464614; 12520002; 12950083; 14610273; 14976138; 15226823; 16110338; 16602821; 16698938; 16912050; 17131407; 17967808; 18385664; 18401410; 18665160; 18772340; 18799693; 18973680; 18997155; 19261723; 19531493; 20802183; 21193583; 21267068; 21677750; 21878523; 22972025; 23306833; 23699715; 24586749; 24812665; 24875861; 25181417; 26849124; 27370713; 27644077; 28109039; 28409408; 29524599; 30735130; 32768584; 8062389; 8548579; 9449665; 9649553;
Motif
Gene Encoded By
Mass 87,073
Kinetics
Metal Binding METAL 606; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 610; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 666; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
Rhea ID
Cross Reference Brenda 3.4.24.71;