| IED ID | IndEnz0002001370 |
| Enzyme Type ID | protease001370 |
| Protein Name |
Tripeptidyl-peptidase 1 TPP-1 EC 3.4.14.9 Lysosomal pepstatin-insensitive protease LPIC Tripeptidyl aminopeptidase Tripeptidyl-peptidase I TPP-I |
| Gene Name | Tpp1 Cln2 |
| 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 | MGLQARLLGLLALVIAGKCTYNPEPDQRWMLPPGWVSLGRVDPEEELSLTFALKQRNLERLSELVQAVSDPSSPQYGKYLTLEDVAELVQPSPLTLLTVQKWLSAAGARNCDSVTTQDFLTCWLSVRQAELLLPGAEFHRYVGGPTKTHVIRSPHPYQLPQALAPHVDFVGGLHRFPPSSPRQRPEPQQVGTVSLHLGVTPSVLRQRYNLTAKDVGSGTTNNSQACAQFLEQYFHNSDLTEFMRLFGGSFTHQASVAKVVGKQGRGRAGIEASLDVEYLMSAGANISTWVYSSPGRHEAQEPFLQWLLLLSNESSLPHVHTVSYGDDEDSLSSIYIQRVNTEFMKAAARGLTLLFASGDTGAGCWSVSGRHKFRPSFPASSPYVTTVGGTSFKNPFLITDEVVDYISGGGFSNVFPRPPYQEEAVAQFLKSSSHLPPSSYFNASGRAYPDVAALSDGYWVVSNMVPIPWVSGTSASTPVFGGILSLINEHRILNGRPPLGFLNPRLYQQHGTGLFDVTHGCHESCLNEEVEGQGFCSGPGWDPVTGWGTPNFPALLKTLLNP |
| Enzyme Length | 562 |
| Uniprot Accession Number | O89023 |
| Absorption | |
| Active Site | ACT_SITE 271; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O14773; ACT_SITE 275; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:O14773; ACT_SITE 474; /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; Evidence={ECO:0000269|PubMed:28464005}; |
| DNA Binding | |
| EC Number | 3.4.14.9 |
| Enzyme Function | FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I activity (PubMed:28464005). May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases (By similarity). Requires substrates with an unsubstituted N-terminus (By similarity). {ECO:0000250|UniProtKB:O14773, ECO:0000269|PubMed:28464005}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (3); Domain (1); Erroneous initiation (1); Glycosylation (5); Metal binding (5); Mutagenesis (1); Propeptide (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Calcium;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Metal-binding;Protease;Reference proteome;Serine protease;Signal;Zymogen |
| Interact With | Q91WC1 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19941651}. 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 | 10330339; 10527801; 11217851; 11423996; 12038963; 12466851; 14609438; 14651853; 15158442; 15483130; 16602821; 16615898; 17053789; 17948054; 18343701; 18570628; 18639872; 19429009; 19749771; 19995905; 20231318; 20493811; 21267068; 21996941; 22099311; 22101936; 22792360; 22989886; 23804102; 25056954; 25303899; 25917818; 26778124; 27101989; 28728022; 29408933; 30022158; 30928643; |
| Motif | |
| Gene Encoded By | |
| Mass | 61,342 |
| Kinetics | |
| Metal Binding | METAL 516; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O14773; METAL 517; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O14773; METAL 538; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O14773; METAL 540; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O14773; METAL 542; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O14773 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.9; |