| IED ID | IndEnz0002018690 |
| Enzyme Type ID | protease018690 |
| Protein Name |
Dipeptidase 3 EC 3.4.13.19 |
| Gene Name | Dpep3 |
| 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 | MQPTGPEGPRALSLRPLGHRLSLLGVLLIIPSLWVTCNQTTPSLSSAPTSPGASSAMTTPGIPNDTTTSGVTSDPRLREQALALMRDFPLVDGHNDLPLLLRELFQNKLQDVNLHNFTRGQTSLDRLRDGLVGAQFWSAYIPCQTQDRDAVRVALEQIDLIRRMCSAYPELELVTSADGLNSTQKLACLIGLEGGHSLDTSLAVLRSFYELGVRYLTLTFTCSTPWAESATKFRHHFYTNISGLTSFGEKVVEEMNRIGMMIDLSHASDTLVKQTLEASRAPVIFSHSAARSVCDNLLNVPDDILQLLKKNGGIVMVTLSMGVLQCSLLANVSTVADHFDHIRTVIGSEFIGIGGSYDGSGRFPQGLEDVSTYPVLLEELLRRGWGEQELQGVLRGNLLRVFRQVEQVREKSLGQSPVEVVFPERQQSSTCHSHLLPQSQDAHLKVTKLPSSQVLQRASKAPPCPLLGLVAAVTSPAFTLWLCCSGHR |
| Enzyme Length | 488 |
| Uniprot Accession Number | Q5U2X4 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by L-penicillamine. {ECO:0000250|UniProtKB:Q9DA79}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid; Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000250|UniProtKB:Q9DA79, ECO:0000255|PROSITE-ProRule:PRU10073}; CATALYTIC ACTIVITY: Reaction=2 H2O + L-cystine-bis-glycine = 2 glycine + L-cystine; Xref=Rhea:RHEA:60520, ChEBI:CHEBI:15377, ChEBI:CHEBI:35491, ChEBI:CHEBI:57305, ChEBI:CHEBI:143812; Evidence={ECO:0000250|UniProtKB:Q9DA79}; |
| DNA Binding | |
| EC Number | 3.4.13.19 |
| Enzyme Function | FUNCTION: Dipeptidase that hydrolyzes cystinyl-bis-glycine. Does not hydrolyze leukotriene D4 (LTD4) into leukotriene E4 (LTE4). {ECO:0000250|UniProtKB:Q9DA79}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (3); Glycosylation (1); Lipidation (1); Metal binding (6); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Dipeptidase;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9DA79}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9DA79}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..35; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,370 |
| Kinetics | |
| Metal Binding | METAL 94; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 96; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 193; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 193; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 266; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 287; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073 |
| Rhea ID | RHEA:48940; RHEA:60520 |
| Cross Reference Brenda |