Detail Information for IndEnz0002001375
IED ID IndEnz0002001375
Enzyme Type ID protease001375
Protein Name Tripeptidyl-peptidase 2
TPP-2
EC 3.4.14.10
Tripeptidyl aminopeptidase
Tripeptidyl-peptidase II
TPP-II
Gene Name TPP2
Organism Bos taurus (Bovine)
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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence MATAATEEPFPFHGLLPKKETGAAAFLCRYPEYDGRGVLIAVLDTGVDPGAPGMQVTTDGKPKIIDIIDTTGSGDVNTATVVEPKDGEIVGLSGRVLKIPVTWTNPSGRYHIGIKNGYDFYPKALKERIQKERKEKIWDPVHRAALAEACRKQEEFDVANNCPSQANKLIKEELHSQVELLNSFEKKYSDPGPVYDCLVWFDGETWRACIDSSEDGDLSKSTVLRNYKEAQEYGSFGAAEMLNYSVNIYDDGNLLSIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVINHKCDLVNYSYGEATHWPNSGRICEVINEAVWKHNIIYVSSAGNNGPCLSTVGCPGGTTSSVIGVGAYVSPDMMVAEYSLREKLPANQYTWSSRGPSADGALGVSVSAPGGAIASVPNWTLRGTQLMNGTSMSSPNACGGIALVLSGLKANDVNYTVHSVRRALENTAVKADNIEVFAQGHGIIQVDKAYDYLVQNTSFANKLGFTVTVGTNRGIYLRDPVQVAAPSDHGVGIEPVFPENTENSEKISLQLHLALTSNSSWVQCPSHLELMNQCRHVNIRVDPRGLREGLHYTEVCGYDIASPNAGPLFRVPITAVIAAKVNESTHYDLALTDVHFKPGQIRRHFIEVPEGATWAEVTVCSCSSEVSAKFVLHAVQLVKQRAYRSHEFYKFCSLPEKGTLTEAFPVLGGKAIEFCIARWWASLSDVNIDYTVSFHGIVCTAPQLNIHSSEGINRFDVQSSLKYEDLAPCITLKSWVQTLRPLSAKTKPLGSRDVLPNNRQLYEMILTYNFHQPKSGEVTPSCPLLCELLYESEFDSQLWIIFDQNKRQMGSGDAYPHQYSLKLEKGDYTIRLQIRHEQISDLERLKDLPFIVSHRLSNTLSLDIHENHSLALLGKKKSSNLTLPPKYNQPFFVTSLPDDKIPKGAGPGCYLTGSLTLSKTELGKKADVIPVHYYLISPPTKTKNGSKDKEKDSEKEKDLKEEFTEALRDLKIQWMTKLDSSDIYNELKETYPNYLPLYVARLHQLDAEKERMKRLNEIVEAANAVISHIDQTALAVYIAMKTDPRPDAAIIKNDMDKQKSTLVDALCRKGCALADHLLQAQDQDGAVSSDSEGREEEGESTLDSLTETFWETTKWTDLFDNKVLTFAYKHALVNKMYGRGLKFATKLVEEKPTKENWKNCIQLMKLLGWTHCASFTENWLPIMYPPDYCVF
Enzyme Length 1249
Uniprot Accession Number A5PK39
Absorption
Active Site ACT_SITE 44; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 264; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 449; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of an N-terminal tripeptide from a polypeptide.; EC=3.4.14.10; Evidence={ECO:0000250|UniProtKB:P29144};
DNA Binding
EC Number 3.4.14.10
Enzyme Function FUNCTION: Cytosolic tripeptidyl-peptidase that releases N-terminal tripeptides from polypeptides and is a component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. It plays an important role in intracellular amino acid homeostasis (By similarity). Stimulates adipogenesis (By similarity). {ECO:0000250|UniProtKB:P29144, ECO:0000250|UniProtKB:Q64514}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Compositional bias (1); Domain (1); Initiator methionine (1); Modified residue (3); Region (2)
Keywords Acetylation;Aminopeptidase;Cytoplasm;Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Serine protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the nucleus in response to gamma-irradiation. {ECO:0000250}.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:P29144; MOD_RES 401; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q64514; MOD_RES 915; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P29144
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 138,361
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda