ID DUS29_PIG Reviewed; 222 AA. AC P0C596; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 02-SEP-2026, entry version 71. 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 Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Porcine genome sequencing project; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. 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. In skeletal muscle regulates systemic glucose homeostasis by CC activating, AMPK, an energy sensor protein kinase. Affects MAP kinase CC signaling though modulation of the MAPK1/2 cascade in skeletal muscle CC promoting muscle cell differentiation, development and atrophy (By CC similarity). {ECO:0000250|UniProtKB:Q68J44, CC ECO:0000250|UniProtKB:Q8BK84}. CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:20101, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:61978; EC=3.1.3.48; CC Evidence={ECO:0000250|UniProtKB:Q68J44}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O-phospho-L-seryl-[protein] + H2O = 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=O-phospho-L-threonyl-[protein] + H2O = 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CT737343; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; P0C596; -. DR SMR; P0C596; -. DR FunCoup; P0C596; 126. DR STRING; 9823.ENSSSCP00000031343; -. DR PaxDb; 9823-ENSSSCP00000031343; -. DR eggNOG; KOG1716; Eukaryota. DR InParanoid; P0C596; -. DR Proteomes; UP000008227; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0033549; F:MAP kinase phosphatase activity; ISS:UniProtKB. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISS:UniProtKB. 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 FunFam; 3.90.190.10:FF:000037; dual specificity protein phosphatase 26; 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 3: Inferred from homology; KW Cytoplasm; Hydrolase; Nucleus; Protein phosphatase; Reference proteome. FT CHAIN 1..222 FT /note="Dual specificity phosphatase 29" FT /id="PRO_0000295882" FT DOMAIN 54..202 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 201..222 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 209..222 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 147 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT BINDING 146..153 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q68J44" SQ SEQUENCE 222 AA; 25132 MW; 3BF05F9905E94649 CRC64; MTSGESKTSL KNAYPAAKKL LPKVEEEGEA EEYCTPGAFE LERLFWKGSP QYTHVNEVWP KLYIGDEATA LDRYGLQKAG FTHVLNAAHG RWNVDTGPDY YRDMAIEYHG VEADDLPTFD LSIFFYPAAA FIDAALRYEH SKILVHCAMG RSRSATLVLA YLMIHRNMTL VDAIRQVAKN RCVLPNRGFL KQLRELDKQL VQQRRGAQHR GEAGEKAGEK EP //