DUS29_TAKRU
ID DUS29_TAKRU Reviewed; 210 AA.
AC P0C599;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 59.
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 Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12142439; DOI=10.1126/science.1072104;
RA Aparicio S., Chapman J., Stupka E., Putnam N., Chia J.M., Dehal P.,
RA Christoffels A., Rash S., Hoon S., Smit A., Gelpke M.D., Roach J., Oh T.,
RA Ho I.Y., Wong M., Detter C., Verhoef F., Predki P., Tay A., Lucas S.,
RA Richardson P., Smith S.F., Clark M.S., Edwards Y.J., Doggett N.,
RA Zharkikh A., Tavtigian S.V., Pruss D., Barnstead M., Evans C., Baden H.,
RA Powell J., Glusman G., Rowen L., Hood L., Tan Y.H., Elgar G., Hawkins T.,
RA Venkatesh B., Rokhsar D., Brenner S.;
RT "Whole-genome shotgun assembly and analysis of the genome of Fugu
RT rubripes.";
RL Science 297:1301-1310(2002).
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 pathways (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}.
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DR EMBL; CAAB01002848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C599; -.
DR SMR; P0C599; -.
DR STRING; 31033.ENSTRUP00000037650; -.
DR eggNOG; KOG1716; Eukaryota.
DR InParanoid; P0C599; -.
DR Proteomes; UP000005226; Unplaced.
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; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
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 SMART; SM00404; PTPc_motif; 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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..210
FT /note="Dual specificity phosphatase 29"
FT /id="PRO_0000295886"
FT DOMAIN 46..194
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 139
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 138..145
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68J44"
SQ SEQUENCE 210 AA; 23702 MW; 940C87A022441CF0 CRC64;
MSSVVKSKSK NPYAAVRVDP DSDYITPGTL DLEQLFWSGP GVQYTHVNQV WPGIYIGDEK
TALERPGLRD LGITHVLNAA EGKWNNVLTG ADYYSDTNIQ YYGIEADDKP TFNISQFFHP
AAQFIHEALS QPHNVLVHCV MGRSRSATLV LAYLMMEHSL SVVDAIEHVR QRRCILPNHG
FLKQLRALDI TLQEARLKQK TQTQGQEKPR
