ID   DUS26_PONAB             Reviewed;         211 AA.
AC   Q5R6H6;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   RecName: Full=Dual specificity protein phosphatase 26;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
GN   Name=DUSP26;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inactivates MAPK1 and MAPK3 which leads to dephosphorylation
CC       of heat shock factor protein 4 and a reduction in its DNA-binding
CC       activity. {ECO:0000250}.
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   -!- SUBUNIT: Interacts with HSF4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Golgi apparatus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
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DR   EMBL; CR860513; CAH92640.1; -; mRNA.
DR   RefSeq; NP_001126545.1; NM_001133073.1.
DR   AlphaFoldDB; Q5R6H6; -.
DR   SMR; Q5R6H6; -.
DR   STRING; 9601.ENSPPYP00000020739; -.
DR   Ensembl; ENSPPYT00000021569.3; ENSPPYP00000020739.2; ENSPPYG00000018499.3.
DR   GeneID; 100173535; -.
DR   KEGG; pon:100173535; -.
DR   CTD; 78986; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   GeneTree; ENSGT00940000158107; -.
DR   HOGENOM; CLU_027074_11_3_1; -.
DR   InParanoid; Q5R6H6; -.
DR   OMA; MSIHFQA; -.
DR   OrthoDB; 1082488at2759; -.
DR   TreeFam; TF105128; -.
DR   Proteomes; UP000001595; Chromosome 8.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:Ensembl.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR   CDD; cd14578; DUSP26; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR020405; Atypical_DUSP_subfamA.
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   PANTHER; PTHR45682; AGAP008228-PA; 1.
DR   PANTHER; PTHR45682:SF8; DUAL SPECIFICITY PROTEIN PHOSPHATASE 26; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
DR   PRINTS; PR01909; ADSPHPHTASEA.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Golgi apparatus; Hydrolase; Nucleus; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..211
FT                   /note="Dual specificity protein phosphatase 26"
FT                   /id="PRO_0000292221"
FT   DOMAIN          60..207
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        152
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   211 AA;  23959 MW;  8F13442A42D3D8DD CRC64;
     MCPGNWLWAS MTFMARFSRS SSRSPVRTRG NLEEMPTVQH PFLNVFELER LLYTGKTACN
     HADEVWPGLY LGDQDMANNR RELRRLGITH VLNASHSRWR GTPEAYEGLG IRYLGVEAHD
     SPAFDMSIHF QTAADFIHRA LSQPGGKILV HCAVGVSRSA TLVLAYLMLY HHLTLVEAIK
     KVKDHRGIIP NRGFLRQLLA LDRRLRQGLE A
//