ID   PTP3_CHLMO              Reviewed;         276 AA.
AC   Q39491;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Dual specificity protein phosphatase;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
GN   Name=VH-PTP13;
OS   Chlamydomonas moewusii (Chlamydomonas eugametos).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND MUTAGENESIS OF CYS-172.
RC   STRAIN=UTEX 10;
RX   PubMed=7599654; DOI=10.1046/j.1365-313x.1995.07060981.x;
RA   Haring M.A., Siderius M., Jonak C., Hirt H., Walton K.M., Musgrave A.;
RT   "Tyrosine phosphatase signalling in a lower plant: cell-cycle and oxidative
RT   stress-regulated expression of the Chlamydomonas eugametos VH-PTP13 gene.";
RL   Plant J. 7:981-988(1995).
CC   -!- FUNCTION: Could be involved in tyrosine phosphatase signalling
CC       pathways, having MAP-kinases as substrates.
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- DEVELOPMENTAL STAGE: Non-dividing gametes did not express the VH-PTP13
CC       gene whereas synchronously dividing vegetative cells only expressed VH-
CC       PTP13 in the early G1-phase of the cycle.
CC   -!- INDUCTION: By oxidative stress.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
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DR   EMBL; X77938; CAA54910.1; -; mRNA.
DR   PIR; T48906; T48906.
DR   AlphaFoldDB; Q39491; -.
DR   SMR; Q39491; -.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Protein phosphatase; Stress response.
FT   CHAIN           1..276
FT                   /note="Dual specificity protein phosphatase"
FT                   /id="PRO_0000094873"
FT   DOMAIN          86..228
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..276
FT                   /note="Catalytic"
FT   ACT_SITE        172
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   MUTAGEN         172
FT                   /note="C->S: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:7599654"
SQ   SEQUENCE   276 AA;  30310 MW;  034EF63951E03381 CRC64;
     MTSHAANPKE EQDQRLPFKS DISGPIAPSQ APAHTVQAHD SQPKPSDDSS DEHLSFYEAK
     ARIVRAFAAS RAPQPAAPAA KALEGDASVI VPGKLILSSC EVEESSELLT KLGVTHILQV
     GEELKPSHPG RFTYLSLPIL DMEGQDIVAL LPSCFQFLQQ AQASGGVCLV HCLAGISRSA
     SVVIAYLMWT QGMPYTEARA MVRRARSKVY PNTGFTLQLQ ELDRLRESGA IQWGDTPSLA
     SSLEQHRQPW NLIRYLEVKE KQAQEEGWTW GRTLVI