Detail Information for IndEnz0002006413
IED ID IndEnz0002006413
Enzyme Type ID protease006413
Protein Name Aspartic protease 10
EC 3.4.23.-
Heme transporter hrg-7
Heme-responsive gene 7 protein
Gene Name hrg-7 asp-10 C15C8.3
Organism Caenorhabditis elegans
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans
Enzyme Sequence MKTFIALLALLTVVSAEVHQFNIGYRPNMRQRMNAKGKLAEYEKERNELLSKKSLQLASSSSPVIDYEDMAYMVQISLGSPAQNFVLFIDSGSSNLWVPDITCAGGKDATCGSYCKSTPYDACLTFCQEECCTKTVEGVKVLSTTDACQSKHRFNSSLSSSYVTNGQKFDMTYNTGEVKGFFGVDTFCFTNTSVCATGQVFGQATTIGEAFAKQPEDGIIGLGWPALAVNQQTPPLFNLMNQGKLDQPYFVVYLANIGPTSQINGGAFTVGGLDTTHCSSNVDWVPLSTQTFWQFKLGGVSSGSYSQAPNSGWQAAADTAASFIGAPKSVVTSLAKAVGATYVPLTGAFFMDCDAVVPDIVFTINGKTYNMPSTSFVVSAGPGPCMFAFYELTAGGFYPAWMLGPPFMRAYCHVHDMKSGRLGLAKVL
Enzyme Length 428
Uniprot Accession Number Q18020
Absorption
Active Site ACT_SITE 90; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 318; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.23.-
Enzyme Function FUNCTION: Aspartic protease which plays a role in heme homeostasis and mediates inter-organ signaling between the intestine and extra-intestinal tissues when cellular heme levels are low. {ECO:0000269|PubMed:28581477}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Propeptide (1); Signal peptide (1)
Keywords Alternative splicing;Aspartyl protease;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal;Zymogen
Interact With
Induction INDUCTION: By heme deficiency. {ECO:0000269|PubMed:28581477}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28581477}.
Modified Residue
Post Translational Modification PTM: Proteolytically cleaved. {ECO:0000305|PubMed:28581477}.
Signal Peptide SIGNAL 1..16; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 16672054; 21367940; 22560298; 23800452; 25487147; 29348603;
Motif
Gene Encoded By
Mass 45,993
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda