Detail Information for IndEnz0002001367
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