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Database: UniProt
Entry: P0C591
LinkDB: P0C591
Original site: P0C591 
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   24-JAN-2024, entry version 89.
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; 9913-ENSBTAP00000003800; -.
DR   Ensembl; ENSBTAT00000003800.5; ENSBTAP00000003800.4; ENSBTAG00000002924.5.
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; 1082488at2759; -.
DR   TreeFam; TF105128; -.
DR   Proteomes; UP000009136; Chromosome 28.
DR   Bgee; ENSBTAG00000002924; Expressed in biceps femoris and 31 other cell types or 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   CDD; cd14575; DUPD1; 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:SF6; DUAL SPECIFICITY PHOSPHATASE 29; 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; 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
//
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