| IED ID | IndEnz0002001373 |
| Enzyme Type ID | protease001373 |
| Protein Name |
Tripeptidyl-peptidase 1 TPP-1 EC 3.4.14.9 Tripeptidyl aminopeptidase Tripeptidyl-peptidase I TPP-I |
| Gene Name | Tpp1 Cln2 |
| 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 | MGLQARFLGLLALVIAGKCTHSPEPDQRWMLPPGWVSLGRVDPEEELSLTFALKQQNLDRLSELVQAVSDPSSPRYGKYLTLEDVAELVQPSPLTLRTVQKWLLAAGARDCHSVTTQDFLTCWLSVRQAELLLPGAEFHRYVGGPAKTHIIRSPHPYQLPQALAPHVDLVAGLHRFPPLSSPRQRPEPQGVGPVGLHLGVTPSVLRQRYNLTARDVGSGTTNNSQACAQFLEQYFHNSDLTEFMRLFGSSFAHQASVARVVGKQGRGRAGIEASLDVEYLMSAGANISTWVYSSPGRHEAQEPFLQWLLLLSNESSLPHVHTVSYGDDEDSLSSVYIQRVNTEFMKAAARGLTLLFASGDTGAGCWSVSGRHKFRPSFPASSPYVTTVGGTSFKNPFLVTNEVVDYISGGGFSNVFPQPSYQEEAVAQFLKSSSHLPPSSYFNASGRAYPDVAALSDGYWVVSNMVPIPWVSGTSASTPVFGGILSLINEHRLLNGRPPLGFLNPRLYQQHGAGLFDVTHGCHESCLNEEVEGQGFCSGPGWDPVTGWGTPNFPALLKTLLNP |
| Enzyme Length | 563 |
| Uniprot Accession Number | Q9EQV6 |
| Absorption | |
| Active Site | ACT_SITE 272; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O14773; ACT_SITE 276; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O14773; ACT_SITE 475; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O14773 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.; EC=3.4.14.9; |
| DNA Binding | |
| EC Number | 3.4.14.9 |
| Enzyme Function | FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus. {ECO:0000269|PubMed:9659384}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4. Unstable above pH 7. {ECO:0000269|PubMed:9659384}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (5); Metal binding (5); Propeptide (1); Sequence conflict (3); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Metal-binding;Protease;Reference proteome;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:O14773}. Melanosome {ECO:0000250|UniProtKB:O14773}. |
| Modified Residue | |
| Post Translational Modification | PTM: Activated by autocatalytic proteolytical processing upon acidification. N-glycosylation is required for processing and activity (By similarity). {ECO:0000250|UniProtKB:O14773}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000250|UniProtKB:O14773 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10679303; 16396496; |
| Motif | |
| Gene Encoded By | |
| Mass | 61,332 |
| Kinetics | |
| Metal Binding | METAL 517; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O14773; METAL 518; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O14773; METAL 539; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O14773; METAL 541; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O14773; METAL 543; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O14773 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.9; |