ID DUS29_ANOCA Reviewed; 217 AA. AC P0C598; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 22-FEB-2023, entry version 63. 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 Anolis carolinensis (Green anole) (American chameleon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Iguania; Dactyloidae; Anolis. OX NCBI_TaxID=28377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21881562; DOI=10.1038/nature10390; RA Alfoeldi J., Di Palma F., Grabherr M., Williams C., Kong L., Mauceli E., RA Russell P., Lowe C.B., Glor R.E., Jaffe J.D., Ray D.A., Boissinot S., RA Shedlock A.M., Botka C., Castoe T.A., Colbourne J.K., Fujita M.K., RA Moreno R.G., ten Hallers B.F., Haussler D., Heger A., Heiman D., RA Janes D.E., Johnson J., de Jong P.J., Koriabine M.Y., Lara M., Novick P.A., RA Organ C.L., Peach S.E., Poe S., Pollock D.D., de Queiroz K., Sanger T., RA Searle S., Smith J.D., Smith Z., Swofford R., Turner-Maier J., Wade J., RA Young S., Zadissa A., Edwards S.V., Glenn T.C., Schneider C.J., Losos J.B., RA Lander E.S., Breen M., Ponting C.P., Lindblad-Toh K.; RT "The genome of the green anole lizard and a comparative analysis with birds RT and mammals."; RL Nature 477:587-591(2011). 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}. 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; AAWZ01006385; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAWZ01006387; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; P0C598; -. DR SMR; P0C598; -. DR STRING; 28377.ENSACAP00000008506; -. DR eggNOG; KOG1716; Eukaryota. DR InParanoid; P0C598; -. DR Proteomes; UP000001646; 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; IBA:GO_Central. 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: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 3: Inferred from homology; KW Cytoplasm; Hydrolase; Nucleus; Protein phosphatase; Reference proteome. FT CHAIN 1..217 FT /note="Dual specificity phosphatase 29" FT /id="PRO_0000295884" 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 217 AA; 24410 MW; F5A23775C2FDC3AA CRC64; MSSTALKSGK ISAYAAVKVD PDGDYCTPGA FDLERLFWKG SPKYTHVNEV WPNLYIGDEK TALDRYSLEK AGFTHILNAA HGRWNVDTGP EYYSDMNIEY HGVEADDLPT FNLSPFFYSA AEFIHTALQN ETSKILVHCA MGRSRSAALV LAYLMIYKNM TVVDAIDQVL QHRCILPNRG FLKQLRELDI KLALERRDNM NGTNSSEKTG TSTETEI //