| IED ID | IndEnz0002001367 |
| Enzyme Type ID | protease001367 |
| Protein Name |
Tripeptidyl-peptidase 1 TPP-1 EC 3.4.14.9 Tripeptidyl aminopeptidase Tripeptidyl-peptidase I TPP-I |
| Gene Name | tpp1 DDB_G0269914 |
| Organism | Dictyostelium discoideum (Slime mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Amoebozoa Evosea Eumycetozoa Dictyostelia (dictyostelid cellular slime molds) Dictyosteliales Dictyosteliaceae Dictyostelium Dictyostelium discoideum (Slime mold) |
| Enzyme Sequence | MNIKFNLIIIILFILFISNVNCKKIKNKKHLTPQRLRRFVEHSKPISLNKKVWKITEIENIFSAQIELTFGIRQRNIVELEDFVWRVSDPNDSLYGSYKTFEEIKEWVKPLDESIDAVKNWLIENDINEFTVTKSGDFIRTIVSIDKAEELLSVRYNKMVHKLSKQSFFRSLDPYTIPRELYDHIDFIGGVNHLPLLSPRPKESSGSAGGGGGGKVNGIGYELESLRNNKQIKSFNDKKVAARNGDPYLSPDLIRKEMNVSQTSTNSTHLGNSQAIAQFLKEYFSPSDLKIFQYRFGLEPSQVDNIIGPNQNLNPGIETALDIQYIMAMAPDVPTWIVSTGGLHEGQEPFLDWLVDLSSNPKLPLVHSISYGDDESSIGLAYTDRVDTEFKKYAAMGRTIVFSSGDFGVGCNDDCDSFSPGWPASSRFVLAVGGVIKKKDGSIIGDEISGGGFSNYFSRPWYQVDECSSYIEWLNGSLSSFYNQSGRGFPDISSFSENVVILYKDKLMPIGGTSASAPIIAGLLSLINDQRLQKNQSPIGLFNPLLYKIARDHPNSFLDIDFGENNYKCCTNGFKSKSGWDPVTGLGLPNFDELVKYCLE |
| Enzyme Length | 600 |
| Uniprot Accession Number | Q55CT0 |
| Absorption | |
| Active Site | ACT_SITE 318; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 322; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 514; /note=Charge relay system; /evidence=ECO:0000250 |
| 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: Serine protease with tripeptidyl-peptidase I activity. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (5); Metal binding (4); Propeptide (1); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Calcium;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| 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}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11553701; 25540127; |
| Motif | |
| Gene Encoded By | |
| Mass | 67,296 |
| Kinetics | |
| Metal Binding | METAL 559; /note=Calcium; /evidence=ECO:0000250; METAL 560; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 579; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 581; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |