DUS29_BOVIN
ID DUS29_BOVIN Reviewed; 219 AA.
AC P0C591;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11282978; DOI=10.1101/gr.170101;
RA Smith T.P.L., Grosse W.M., Freking B.A., Roberts A.J., Stone R.T.,
RA Casas E., Wray J.E., White J., Cho J., Fahrenkrug S.C., Bennett G.L.,
RA Heaton M.P., Laegreid W.W., Rohrer G.A., Chitko-McKown C.G., Pertea G.,
RA Holt I., Karamycheva S., Liang F., Quackenbush J., Keele J.W.;
RT "Sequence evaluation of four pooled-tissue normalized bovine cDNA libraries
RT and construction of a gene index for cattle.";
RL Genome Res. 11:626-630(2001).
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 intracellular signaling
CC cascades. May regulate glucose metabolism by activating, AMPK, an
CC energy sensor protein kinase. Affects MAP kinase signaling though
CC modulation of the ERK1/2 cascade in skeletal muscle promoting muscle
CC cell differentiation, development and atrophy (By similarity).
CC {ECO:0000250|UniProtKB:Q68J44, 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 -!- SUBUNIT: Homodimer (By similarity). Interacts with PRKAA2 (By
CC similarity). {ECO:0000250|UniProtKB:Q68J44,
CC ECO:0000250|UniProtKB:Q8BK84}.
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; BF074326; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CK773828; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_005226533.1; XM_005226476.3.
DR AlphaFoldDB; P0C591; -.
DR SMR; P0C591; -.
DR STRING; 9913.ENSBTAP00000003800; -.
DR PaxDb; P0C591; -.
DR Ensembl; ENSBTAT00000003800; ENSBTAP00000003800; ENSBTAG00000002924.
DR GeneID; 616082; -.
DR CTD; 338599; -.
DR VEuPathDB; HostDB:ENSBTAG00000002924; -.
DR VGNC; VGNC:28245; DUSP29.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000160190; -.
DR HOGENOM; CLU_027074_11_3_1; -.
DR InParanoid; P0C591; -.
DR OMA; NAAHGQR; -.
DR OrthoDB; 1576308at2759; -.
DR TreeFam; TF105128; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000002924; Expressed in biceps femoris and 31 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; ISS:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; 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; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0042692; P:muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
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; 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; 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; Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..219
FT /note="Dual specificity phosphatase 29"
FT /id="PRO_0000295875"
FT DOMAIN 53..201
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 146
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 145..152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68J44"
SQ SEQUENCE 219 AA; 24984 MW; F5ED15F29BD7E36A CRC64;
MTSGESKTGL KNVYPSAKKL LPKVEEGEAE DYCTPGAFEL ERLFWKGSPQ YTHVNEVWPK
LYIGDETTAL DRYGLQKAGF THVLNAAHGR WNVDTGPDYY RDMAIEYHGV EADDLPSFDL
SVFFYPAAAF IDAALRYDHN KILVHCVMGR SRSATLVLAY LMIHRNMTLV DAIQQVAKNR
CVLPNRGFLK QLRELDRQLV QQRRQAQQGE DAEKCEQEP
