IED ID | IndEnz0002016459 |
Enzyme Type ID | protease016459 |
Protein Name |
Endothelin-converting enzyme-like 1 EC 3.4.24.- Damage-induced neuronal endopeptidase Xce protein |
Gene Name | Ecel1 Dine Xce |
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 | MEAPYSMTAHYDEFQEVKYESRCGTGGARGTSLPPGFPRSSGRSASGARSGLPRWNRREVCLLSGLVFAAGLCAILAAMLALKYLGPGAAGTGGACPEGCPERKAFARAARFLSANLDASIDPCQDFYSFACGGWLRRHAIPDDKLTYGTIAAIGEQNEERLRRLLARPTGGPGGAAQRKVRAFFRSCLDMREIERLGPRPMLEVIEDCGGWDLGGAADRPGAARWDLNRLLYKAQGVYSAAALFSLTVSLDDRNSSRYVIRIDQDGLTLPERTLYLAQDEGSEKVLAAYKVFMERLLRLLGADAVEQKAQEILQLEQRLANISVSEYDDLRRDVSSVYNKVTLGQLQKITPHLQWKWLLDQIFQEDFSEEEEVVLLATDYMQQVSQLIRSTPRRILHNYLVWRVVVVLSEHLSPPFREALHELAKEMEGNDKPQELARVCLGQANRHFGMALGALFVHEHFSAASKAKVQQLVEDIKYILGQRLEELDWMDAQTKAAARAKLQYMMVMVGYPDFLLKPEAVDKEYEFEVHEKTYLKNILNSIRFSIQLSVKKIRQEVDKSTWLLPPQALNAYYLPNKNQMVFPAGILQPTLYDPDFPQSLNYGGIGTIIGHELTHGYDDWGGQYDRSGNLLHWWTEASYSRFLHKAECIVRLYDNFTVYNQRVNGKHTLGENIADMGGLKLAYYAYQKWVREHGPEHPLHRLKYTHNQLFFIAFAQNWCIKRRSQSIYLQVLTDKHAPEHYRVLGSVSQFEEFGRAFHCPKDSPMNPVHKCSVW |
Enzyme Length | 775 |
Uniprot Accession Number | Q9JHL3 |
Absorption | |
Active Site | ACT_SITE 613; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; ACT_SITE 676; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233" |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: May contribute to the degradation of peptide hormones and be involved in the inactivation of neuronal peptides. Cleaves the synthetic substrate Z-Gly-Gly-Leu-pNA and releases pNA. May protect against C2-ceramide-induced apoptosis. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (3); Metal binding (3); Region (1); Sequence conflict (1); Topological domain (2); Transmembrane (1) |
Keywords | Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
Interact With | |
Induction | INDUCTION: By mechanical damage to nerve cells. |
Subcellular Location | SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12417666; 16675137; 18192274; |
Motif | |
Gene Encoded By | |
Mass | 87,944 |
Kinetics | |
Metal Binding | METAL 612; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 616; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 672; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233" |
Rhea ID | |
Cross Reference Brenda |