| IED ID | IndEnz0002001366 |
| Enzyme Type ID | protease001366 |
| Protein Name |
Tripeptidyl-peptidase 1 TPP-1 EC 3.4.14.9 Tripeptidyl aminopeptidase Tripeptidyl-peptidase I TPP-I |
| Gene Name | tpp1 |
| Organism | Danio rerio (Zebrafish) (Brachydanio rerio) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Otomorpha Ostariophysi Otophysi Cypriniphysae Cypriniformes (carps and others) Cyprinoidei Danionidae Danioninae Danio Danio rerio (Zebrafish) (Brachydanio rerio) |
| Enzyme Sequence | MRVAVFVLSFIWLVNGELLEADQDAVVPGDWTFLGRVGPLEEVELTFALKQQNVSKMEELLKLVSDPDSHQYGKYLSLDEVAALSRPSPLTEKVVENWLRSHGVMDCHTIITRDFLQCVMTVEVAEALLPGSKFHRFSKNTKTLLRSTSQYSVHEDVHQHLDFVGGVHRFPQKRKIVSKGWEGARQAILGYHLGVTPAVIRNRYNLTAKDVGTAANNSQAVAQFLEQYYHPADLAEFMSLFGGGFTHMSTVERVVGTQGGGKAGIEASLDVEYIMSSGANISTWVFTNPGRHESQEPFLQWMLLLSNMSAVPWVHTISYGDDEDSLSEAYMNRINIEFMKAGLRGISMLFASGDSGAGCRHLTKERNTFRPSFPASSPYVTTVGGTSFQNPFKLSYEVTDYISGGGFSNVFPMPDYQVDAVRAYLKSVQSLPPQTYFNTTGRAYPDLAALSDNYWVVSNRVPIPWVSGTSASTPVVGGILSLINDQRFLKGLPALGFINPRLYKMQGKGLYDVTVGCHLSCLDDKVEGKGFCASPSWDPVTGWGTPNYPVFLASLMD |
| Enzyme Length | 557 |
| Uniprot Accession Number | F8W2M8 |
| Absorption | |
| Active Site | ACT_SITE 266; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01032; ACT_SITE 270; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01032; ACT_SITE 470; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01032 |
| 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:23587805}; |
| DNA Binding | |
| EC Number | 3.4.14.9 |
| Enzyme Function | FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I activity (PubMed:23587805). 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:23587805}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (6); Metal binding (3); Mutagenesis (2); Propeptide (1); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Calcium;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}. |
| Modified Residue | |
| Post Translational Modification | PTM: Activated by autocatalytic proteolytical processing. {ECO:0000250|UniProtKB:O14773}. |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 14609438; 28437249; 32028681; |
| Motif | |
| Gene Encoded By | |
| Mass | 61,539 |
| Kinetics | |
| Metal Binding | METAL 512; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O14773; METAL 513; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O14773; METAL 538; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O14773 |
| Rhea ID | |
| Cross Reference Brenda |