| IED ID | IndEnz0002001377 |
| Enzyme Type ID | protease001377 |
| Protein Name |
Tripeptidyl-peptidase 2 TPP-2 EC 3.4.14.10 Tripeptidyl aminopeptidase Tripeptidyl-peptidase II TPP-II dTPP II |
| Gene Name | TppII CG3991 |
| Organism | Drosophila melanogaster (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
| Enzyme Sequence | MFNRFRLVHKQLRLYKNFGLLGQKASVGLTLPIISLSRPYMAYMGTERSVVMITAPATKEFAESSERSNSSKKTTNKEQSDKSAESRMATSGIVESFPTGALVPKAETGVLNFLQKYPEYDGRDVTIAIFDSGVDPRATGLETLCDGKTVKVIERYDCSGCGDVDMKKKVTPDENGNIKGLSGNSLKLSPELMALNTDPEKAVRVGLKSFSDLLPSKVRNNIVAQAKLKHWDKPHKTATANASRKIVEFESQNPGEASKLPWDKKILKENLDFELEMLNSYEKVYGDIKTSYDCILFPTADGWLTIVDTTEQGDLDQALRIGEYSRTHETRNVDDFLSISVNVHDEGNVLEVVGMSSPHGTHVSSIASGNHSSRDVDGVAPNAKIVSMTIGDGRLGSMETGTALVRAMTKVMELCRDGRRIDVINMSYGEHANWSNSGRIGELMNEVVNKYGVVWVASAGNHGPALCTVGTPPDISQPSLIGVGAYVSPQMMEAEYAMREKLPGNVYTWTSRDPCIDGGQGVTVCAPGGAIASVPQFTMSKSQLMNGTSMAAPHVAGAVALLISGLKQQNIEYSPYSIKRAISVTATKLGYVDPFAQGHGLLNVEKAFEHLTEHRQSKDNMLRFSVRVGNNADKGIHLRQGVQRNSIDYNVYIEPIFYNDKEADPKDKFNFNVRLNLIASQPWVQCGAFLDLSYGTRSIAVRVDPTGLQPGVHSAVIRAYDTDCVQKGSLFEIPVTVVQPHVLESDQNTPVFEPASSKGDNSVEFQPNTIQRDFILVPERATWAELRMRITDPNRGEDIGKFFVHTNQLLPKQSCRKLETMKIVSVGSENESIMAFKVKSGRILELCIAKYWSNYGQSHLKYSLRFRGVEAHNPNAYVMHAGRGIHKLEIEALVAEDVQPQLQLKNAEVVLKPTEAKISPLSATRDVIPDGRQVYQNLLAFNLNVAKAADVSIYAPIFNDLLYEAEFESQMWMLFDANKALVATGDAHSHTSFTKLDKGEYTIRLQVRHEKRDLLEKISEANLVASFKLTSPLTLDFYENYNQCIVGGRKYVSSPLRLSTRVLYIAPITQERLTKANLPAQCAWLSGNLVFPQDEVGRRVAQHPFTYILNPAEKKSHTNGSSNGSSAAGSTATAAAVTTANGAKPKAPATPQAATSVTNPAAGDGISVQNDPPVDSSGSPASPKKGKANADDYAESFRDFQCSQIVKCELEMAEKIYNDVVAAHPKHLQANLLLIQNIESNQLKSQLPLTFVNAQKTSPPEAGESADKQKEDQKKVRSALERIVKLADKVIQETDSEALLSYYGLKNDTRADAAKIKTNMDKQKNTLIEALSKKGIAVAKLAVLDDCIKDSLAEINELYTEIIKFVDANDSKAIQFALWHAYAHGHYGRMYKYVVKLIEEKRTRDHFVELAAINGALGHEHIRTVINRMMITAFPSSFRLF |
| Enzyme Length | 1441 |
| Uniprot Accession Number | Q9V6K1 |
| Absorption | |
| Active Site | ACT_SITE 131; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:20676100"; ACT_SITE 359; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:20676100"; ACT_SITE 549; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:20676100" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride (PMSF) and butabindide, but not by peptidase inhibitor pepstatin, EDTA, nor bestatin. {ECO:0000269|PubMed:9668104}. |
| 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:0000269|PubMed:9668104}; |
| DNA Binding | |
| EC Number | 3.4.14.10 |
| Enzyme Function | FUNCTION: Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway (By similarity). Efficiently cleaves Ala-Ala-Ala-polypeptide and Pro-Pro-Ala-polypeptide, Val-Leu-Lys-polypeptide only at high concentration. Does not cleave Ala-Phe-Pro-polypeptide nor Pro-Leu-Gly-polypeptide. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-7.8. {ECO:0000269|PubMed:9668104}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Beta strand (67); Chain (1); Compositional bias (2); Domain (1); Helix (35); Modified residue (1); Region (3); Sequence conflict (2); Turn (15) |
| Keywords | 3D-structure;Alternative splicing;Aminopeptidase;Cytoplasm;Hydrolase;Phosphoprotein;Protease;Reference proteome;Serine protease |
| Interact With | Itself |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | MOD_RES 1182; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18327897 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3LXU; |
| Mapped Pubmed ID | 11606538; 11739392; 12593803; 14605208; 15592865; 15985179; 16799156; 18816840; 19718442; 20220848; 20371351; 21074052; 21946061; 22266401; 22771804; 23071443; 23944235; 25294943; 25312911; 25687947; 26290570; 26526100; 26870755; 27582081; 30426565; 31690598; 31722958; 33563832; 33827210; |
| Motif | |
| Gene Encoded By | |
| Mass | 158,737 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.10; |