Detail Information for IndEnz0002001372
IED ID IndEnz0002001372
Enzyme Type ID protease001372
Protein Name Tripeptidyl-peptidase 1
TPP-1
EC 3.4.14.9
Tripeptidyl aminopeptidase
Tripeptidyl-peptidase I
TPP-I
Gene Name TPP1 CLN2
Organism Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Ponginae Pongo Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Enzyme Sequence MGLQACLLGLFALILSGKCSYSPEPDQRRTLPPGWVSLGRADPEEELSLTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCHSVITQDFLTCWLSIRQAELLLPGAEFHHYVGGPTETHVVRSPHPYQLPQALAPHVDFVGGLHRFPPTSSLRQHPEPQVTGTVGLHLGVTPSVIRKRYNLTSQDVGSGTSNNSQACAQFLEQYFHDSDLAQFMRLFGGNFAHQASVARVVGQQGRGRAGIEASLDVQYLMSAGANISTWVYSSPGRHEGQEPFLQWLMLLSNESALPHVHTVSYGDEEDSLSSAYIQRVNTELMKAAARGLTLLFASGDSGAGCWSVSGRHQFRPTFPASSPYVTTVGGTSFLEPFLTTNEIVDYISGGGFSNVFPRPSYQEEAVTKFLSSSPHLPPSSYFNASGRAYPDVAALSDGYWVVSNRVPIPWVSGTSASTPVFGGGILSLINEHRILSGRPPLGFLNPRLYQQHGAGLFDVTHGCHESCLDEEVEGQGFCSGPGWDPVTGWGTPNFPALPKTLLNP
Enzyme Length 564
Uniprot Accession Number Q5RFL1
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 (By similarity). {ECO:0000250|UniProtKB:Q9EQV6}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (3); Domain (1); Glycosylation (5); Metal binding (5); 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}. 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 -
Motif
Gene Encoded By
Mass 61,238
Kinetics
Metal Binding METAL 518; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O14773; METAL 519; /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; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O14773; METAL 544; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O14773
Rhea ID
Cross Reference Brenda