| IED ID | IndEnz0002013276 |
| Enzyme Type ID | protease013276 |
| Protein Name |
Peroxisomal leader peptide-processing protease EC 3.4.21.- Trypsin domain-containing protein 1 Cleaved into: Peroxisomal leader peptide-processing protease, 10 kDa form; Peroxisomal leader peptide-processing protease, 49 kDa form |
| Gene Name | Tysnd1 |
| 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 | MGRQWGPSMRVAEQAGCVVSASRAGQPDAGSWSCSGVILSRNPGLVLCHGGIFTPFLRTGSAALTQTGTAFLPGDSCSDDLRLHVQWGPTAASPAGRADQELPGLCTPQCASLGLEPGAPSRARARPLQPPRPAQLLLLLSCPAFRSHFARLFGADAVDQWHFVSSAPDDAVSEEEEEDQLRALGWFALLRVQRGAAAEERRGPVVTVAPLGAVVKGAPLLACGSPFGAFCPDIFLNTLSRGVLSNAAGPLLLTDARCLPGTEGGGVFAARPAGALVALVAAPLCWKAREWVGLTLLCAAAPLLQVARWALARLHPGSASLSVLLPPPDVSTPRGLPLRDLGPPWAAAAVLVECGTVWGSGVVVAPRLVVTCRHVAPREAARVLVHSATPKNVAIWGQVVFATQETSPYDIAVVSLEEELNGVPTPVPAGHFHEGEPVSVVGFGVFGQACGPSVTSGILSAVVRVDGSPVMLQTTCAVHGGSSGGPLFSSGSGDLLGIVASNTRDNNTGATYPHLNFSIPITVLQPALKQYSQTGDLGGLRELDHTTEPVRVVWRLQRPLSEVPRSKL |
| Enzyme Length | 568 |
| Uniprot Accession Number | Q9DBA6 |
| Absorption | |
| Active Site | ACT_SITE 374; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 410; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 483; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by N-ethylmaleimide (NEM). Not affected by leupeptin or trans-epoxysuccinyl-l-leucylamido-(4-gianidino) butane (E64). {ECO:0000269|PubMed:17255948}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Peroxisomal protease that mediates both the removal of the leader peptide from proteins containing a PTS2 target sequence and processes several PTS1-containing proteins. Catalyzes the processing of PTS1-proteins involved in the peroxisomal beta-oxidation of fatty acids (By similarity). {ECO:0000250, ECO:0000269|PubMed:17255948}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (3); Region (1); Site (1) |
| Keywords | Direct protein sequencing;Hydrolase;Peroxisome;Protease;Reference proteome;Serine protease |
| Interact With | |
| Induction | INDUCTION: By the proliferator-activated receptor alpha agonist bezafibrate. {ECO:0000269|PubMed:17255948}. |
| Subcellular Location | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17255948}. |
| Modified Residue | |
| Post Translational Modification | PTM: Self-cleavage gives rise to an N-terminal 10-kDa fragment and C-terminal 49-kDa fragment upon import into the peroxisomes. The full-lengh TYSND1 is the active the proteolytic processing of PTS1- and PTS2-proteins and in self-cleavage, and intermolecular self-cleavage of TYSND1 down-regulates its protease activity. {ECO:0000269|PubMed:17255948}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 20059953; 22002062; 23459139; |
| Motif | |
| Gene Encoded By | |
| Mass | 59,066 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |