ID DUS18_RAT Reviewed; 204 AA. AC Q6AXW7; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 08-NOV-2023, entry version 120. DE RecName: Full=Dual specificity protein phosphatase 18; DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q8NEJ0}; DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q8NEJ0}; GN Name=Dusp18; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP SUBCELLULAR LOCATION. RX PubMed=18385140; DOI=10.1074/jbc.m709547200; RA Rardin M.J., Wiley S.E., Murphy A.N., Pagliarini D.J., Dixon J.E.; RT "Dual specificity phosphatases 18 and 21 target to opposing sides of the RT mitochondrial inner membrane."; RL J. Biol. Chem. 283:15440-15450(2008). CC -!- FUNCTION: Can dephosphorylate single and diphosphorylated synthetic CC MAPK peptides, with preference for the phosphotyrosine and CC diphosphorylated forms over phosphothreonine. In vitro, CC dephosphorylates p-nitrophenyl phosphate (pNPP). CC {ECO:0000250|UniProtKB:Q8NEJ0}. 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; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10044}; 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:Q8NEJ0}; 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:Q8NEJ0}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8VE01}. Nucleus CC {ECO:0000250|UniProtKB:Q8NEJ0}. Mitochondrion inner membrane CC {ECO:0000269|PubMed:18385140}; Peripheral membrane protein CC {ECO:0000269|PubMed:18385140}; Intermembrane side CC {ECO:0000269|PubMed:18385140}. Note=Translocates to cytoplasm in CC response to apoptotic stimuli such as staurosporine treatment. CC {ECO:0000250|UniProtKB:Q8VE01}. 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; BC079285; AAH79285.1; -; mRNA. DR RefSeq; NP_001013146.2; NM_001013128.2. DR AlphaFoldDB; Q6AXW7; -. DR SMR; Q6AXW7; -. DR STRING; 10116.ENSRNOP00000005516; -. DR PhosphoSitePlus; Q6AXW7; -. DR PaxDb; 10116-ENSRNOP00000005516; -. DR GeneID; 305477; -. DR KEGG; rno:305477; -. DR UCSC; RGD:1306929; rat. DR AGR; RGD:1306929; -. DR CTD; 150290; -. DR RGD; 1306929; Dusp18. DR eggNOG; KOG1718; Eukaryota. DR InParanoid; Q6AXW7; -. DR OrthoDB; 127323at2759; -. DR PhylomeDB; Q6AXW7; -. DR PRO; PR:Q6AXW7; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:RGD. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISS:UniProtKB. DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB. DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISS:UniProtKB. DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB. DR CDD; cd14573; DUSP18_21; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR020420; Atypical_DUSP_subfamB. 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; PTHR46495:SF2; DUAL SPECIFICITY PROTEIN PHOSPHATASE 18; 1. DR PANTHER; PTHR46495; DUAL SPECIFICITY PROTEIN PHOSPHATASE 21; 1. DR Pfam; PF00782; DSPc; 1. DR PRINTS; PR01908; ADSPHPHTASE. DR PRINTS; PR01910; ADSPHPHTASEB. 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; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Nucleus; Protein phosphatase; KW Reference proteome. FT CHAIN 1..204 FT /note="Dual specificity protein phosphatase 18" FT /id="PRO_0000094831" FT DOMAIN 19..160 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 95..141 FT /note="Sufficient for mitochondrial localization" FT /evidence="ECO:0000250" FT ACT_SITE 104 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" SQ SEQUENCE 204 AA; 22754 MW; 1A5BBC759522E442 CRC64; MTSPWSACPV QFPQPSISGL SQITKSLFIS NGAAANDKLL LSSNQITTVI NVSVEVANTF YEDIQYVQVP VVDAPIARLS DFFDPIADHI HSVEMKQGRT LLHCAAGVSR SAALCLAYLM KYHVMSLLDA HAWTKSRRPI IRPNSGFWEQ LIHYEFQLFG KNTMQMVNSP MGLIPDIYEK ETRMMIPLST PDGAFHKGKE KALL //