ID PRL1_TRYCC Reviewed; 176 AA.
AC Q4CUJ8; Q6JHV2;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Protein tyrosine phosphatase PRL-1 {ECO:0000305};
DE EC=3.1.3.48 {ECO:0000269|PubMed:16151248};
DE Flags: Precursor;
GN Name=PLR-1 {ECO:0000303|PubMed:16151248};
GN ORFNames=Tc00.1047053503851.24 {ECO:0000312|EMBL:EAN83950.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000312|Proteomes:UP000002296};
RN [1] {ECO:0000312|EMBL:AAS19277.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, ISOPRENYLATION AT CYS-173, AND MUTAGENESIS OF CYS-107
RP AND 173-CYS--MET-176.
RC STRAIN=CL Brener {ECO:0000312|EMBL:AAS19277.1};
RX PubMed=16151248; DOI=10.1128/ec.4.9.1550-1561.2005;
RA Cuevas I.C., Rohloff P., Sanchez D.O., Docampo R.;
RT "Characterization of farnesylated protein tyrosine phosphatase TcPRL-1 from
RT Trypanosoma cruzi.";
RL Eukaryot. Cell 4:1550-1561(2005).
RN [2] {ECO:0000312|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000312|Proteomes:UP000002296};
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
CC -!- FUNCTION: Has protein tyrosine phosphatase activity.
CC {ECO:0000269|PubMed:16151248}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:16151248};
CC -!- ACTIVITY REGULATION: Activated in a reduced environment which promotes
CC the reduction of the disulfide bond between the regulatory Cys-52 and
CC the catalytic Cys-107 residues (By similarity). Inhibited by sodium
CC orthovanadate (PubMed:16151248). {ECO:0000250|UniProtKB:Q4QEZ7,
CC ECO:0000269|PubMed:16151248}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-8. {ECO:0000269|PubMed:16151248};
CC -!- SUBCELLULAR LOCATION: Flagellar pocket {ECO:0000269|PubMed:16151248}.
CC Note=In epimastigotes, localizes close to flagellar pocket, cytostome
CC and to reservosomes. Reservosomes are prelysosomal-like acidic
CC organelles found at the cell posterior end which contain the protease
CC cruzipain and ingested proteins and lipids. In amastigotes and
CC trypomastigotes partially co-localizes with concavalin A, a marker of
CC the endocytic pathway. {ECO:0000269|PubMed:16151248}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the amastigote life cycle stage (at
CC protein level). Expressed at the epimastigote, amastigote and
CC trypomastigote life cycle stages. {ECO:0000269|PubMed:16151248}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AY461711; AAS19277.1; -; Genomic_DNA.
DR EMBL; AAHK01001847; EAN83950.1; -; Genomic_DNA.
DR RefSeq; XP_805801.1; XM_800708.1.
DR AlphaFoldDB; Q4CUJ8; -.
DR SMR; Q4CUJ8; -.
DR STRING; 353153.Q4CUJ8; -.
DR PaxDb; 353153-Q4CUJ8; -.
DR EnsemblProtists; EAN83950; EAN83950; Tc00.1047053503851.24.
DR GeneID; 3535648; -.
DR KEGG; tcr:503851.24; -.
DR eggNOG; KOG2836; Eukaryota.
DR InParanoid; Q4CUJ8; -.
DR OMA; VNIKFRE; -.
DR OrthoDB; 117411at2759; -.
DR BRENDA; 3.1.3.48; 6524.
DR Proteomes; UP000002296; Unassembled WGS sequence.
DR GO; GO:0020016; C:ciliary pocket; IDA:UniProtKB.
DR GO; GO:0031910; C:cytostome; IDA:UniProtKB.
DR GO; GO:0000323; C:lytic vacuole; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:UniProtKB.
DR CDD; cd14500; PTP-IVa; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR23339:SF123; PROTEIN TYROSINE PHOSPHATASE TYPE IVA A-RELATED; 1.
DR PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Hydrolase; Lipoprotein; Methylation; Prenylation;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..176
FT /note="Protein tyrosine phosphatase PRL-1"
FT /id="PRO_0000441638"
FT PROPEP 174..176
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000441639"
FT DOMAIN 13..165
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 75
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q4QEZ7"
FT ACT_SITE 107
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 109..113
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4QEZ7"
FT MOD_RES 173
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 173
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:16151248"
FT DISULFID 52..107
FT /evidence="ECO:0000250|UniProtKB:Q4QEZ7"
FT MUTAGEN 107
FT /note="C->S: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:16151248"
FT MUTAGEN 173..176
FT /note="Missing: Loss of farnesylation. Localizes to the
FT cytoplasm and loses localization to reservosomes."
FT /evidence="ECO:0000269|PubMed:16151248"
FT CONFLICT 21
FT /note="R -> H (in Ref. 2; EAN83950)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="F -> L (in Ref. 2; EAN83950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 19237 MW; AA97B236BE4AB64F CRC64;
MGANGTLVEC KRGESDAVVF RFLIFDAPSP SSVTAYVKLM QKYNVRHIVR ACGQTYSAEA
FEKQGMVVHG WSFDDGAPPT QTVIDNWLNL LEQEKNKSPP ETIAVHCVAG LGRAPILVAL
ALVEYGGMPP LDAVGYVRGR RKGAINQVQL NWLMRYKPRH QEGNEGSLSC AGCAVM
//
