| IED ID | IndEnz0002007068 |
| Enzyme Type ID | protease007068 |
| Protein Name |
Protein tyrosine phosphatase PRL-1 EC 3.1.3.48 |
| Gene Name | PLR-1 Tc00.1047053503851.24 |
| Organism | Trypanosoma cruzi (strain CL Brener) |
| Taxonomic Lineage | cellular organisms Eukaryota Discoba Euglenozoa Kinetoplastea (kinetoplasts) Metakinetoplastina Trypanosomatida Trypanosomatidae Trypanosoma Schizotrypanum Trypanosoma cruzi Trypanosoma cruzi (strain CL Brener) |
| Enzyme Sequence | MGANGTLVECKRGESDAVVFRFLIFDAPSPSSVTAYVKLMQKYNVRHIVRACGQTYSAEAFEKQGMVVHGWSFDDGAPPTQTVIDNWLNLLEQEKNKSPPETIAVHCVAGLGRAPILVALALVEYGGMPPLDAVGYVRGRRKGAINQVQLNWLMRYKPRHQEGNEGSLSCAGCAVM |
| Enzyme Length | 176 |
| Uniprot Accession Number | Q4CUJ8 |
| Absorption | |
| Active Site | ACT_SITE 75; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q4QEZ7; ACT_SITE 107; /note=Phosphocysteine intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU00160 |
| Activity Regulation | ACTIVITY REGULATION: Activated in a reduced environment which promotes the reduction of the disulfide bond between the regulatory Cys-52 and the catalytic Cys-107 residues (By similarity). Inhibited by sodium orthovanadate (PubMed:16151248). {ECO:0000250|UniProtKB:Q4QEZ7, ECO:0000269|PubMed:16151248}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:16151248}; |
| DNA Binding | |
| EC Number | 3.1.3.48 |
| Enzyme Function | FUNCTION: Has protein tyrosine phosphatase activity. {ECO:0000269|PubMed:16151248}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8. {ECO:0000269|PubMed:16151248}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (1); Domain (1); Lipidation (1); Modified residue (1); Mutagenesis (2); Propeptide (1); Region (1); Sequence conflict (2) |
| Keywords | Disulfide bond;Hydrolase;Lipoprotein;Methylation;Prenylation;Protein phosphatase;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Flagellar pocket {ECO:0000269|PubMed:16151248}. Note=In epimastigotes, localizes close to flagellar pocket, cytostome and to reservosomes. Reservosomes are prelysosomal-like acidic organelles found at the cell posterior end which contain the protease cruzipain and ingested proteins and lipids. In amastigotes and trypomastigotes partially co-localizes with concavalin A, a marker of the endocytic pathway. {ECO:0000269|PubMed:16151248}. |
| Modified Residue | MOD_RES 173; /note=Cysteine methyl ester; /evidence=ECO:0000305 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 19,237 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:10684 |
| Cross Reference Brenda | 3.1.3.48; |