ID   DUS29_XENLA             Reviewed;         209 AA.
AC   Q4KL92;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Dual specificity phosphatase 29;
DE   AltName: Full=Dual specificity phosphatase DUPD1;
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:Q68J44};
DE            EC=3.1.3.48 {ECO:0000250|UniProtKB:Q68J44};
GN   Name=dusp29; Synonyms=dupd1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Dual specificity phosphatase able to dephosphorylate
CC       phosphotyrosine, phosphoserine and phosphothreonine residues, with a
CC       preference for phosphotyrosine as a substrate.
CC       {ECO:0000250|UniProtKB:Q68J44}.
CC   -!- FUNCTION: Dual specificity phosphatase able to dephosphorylate
CC       phosphotyrosine, phosphoserine and phosphothreonine residues within the
CC       same substrate, with a preference for phosphotyrosine as a substrate
CC       (By similarity). Involved in the modulation of AMPK and MAPK1/2
CC       signaling pathway (By similarity). {ECO:0000250|UniProtKB:Q68J44,
CC       ECO:0000250|UniProtKB:Q8BK84}.
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:0000250|UniProtKB:Q68J44};
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         Evidence={ECO:0000250|UniProtKB:Q68J44};
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         Evidence={ECO:0000250|UniProtKB:Q68J44};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68J44}. Nucleus
CC       {ECO:0000250|UniProtKB:Q8BK84}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH99351.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAI33236.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC099351; AAH99351.1; ALT_INIT; mRNA.
DR   EMBL; BC133235; AAI33236.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001153482.1; NM_001160010.1.
DR   AlphaFoldDB; Q4KL92; -.
DR   SMR; Q4KL92; -.
DR   GeneID; 733311; -.
DR   KEGG; xla:733311; -.
DR   CTD; 733311; -.
DR   Xenbase; XB-GENE-5944548; dusp29.S.
DR   OrthoDB; 1576308at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 733311; Expressed in muscle tissue and 6 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR020405; Atypical_DUSP_subfamA.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR45682; PTHR45682; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   PRINTS; PR01909; ADSPHPHTASEA.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT   CHAIN           1..209
FT                   /note="Dual specificity phosphatase 29"
FT                   /id="PRO_0000295891"
FT   DOMAIN          45..193
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        138
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   BINDING         137..144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68J44"
SQ   SEQUENCE   209 AA;  23750 MW;  6BB945FAF4E4A539 CRC64;
     MPADTPIRKK PNAYASVVDP DTGYCTPGAF ELERLFWHGA PKYTHVNEVW PNLYIGDEKT
     ALDRYSLEKN GFTHILNAAH GRWNVDTGPE YYSDMTVEYY GVEAEDLPSF NLSQFFYPAA
     QFIHKALSTP NSKLLVNCAM GRSRSASLVL AYLMIYKNMT VVESITQVLK HRCILPNRGF
     LKQLRELDIK LALEKRDTHG TANKAQKDD