ID DUS18_BOVIN Reviewed; 188 AA. AC Q5BIP9; Q32KN1; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 12-APR-2005, sequence version 1. DT 08-NOV-2023, entry version 110. 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 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 [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Liver; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases. 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:0000250|UniProtKB:Q8VE01}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q8VE01}; Intermembrane side CC {ECO:0000250|UniProtKB:Q8VE01}. 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; BT021175; AAX31357.1; -; mRNA. DR EMBL; BC110013; AAI10014.1; -; mRNA. DR RefSeq; NP_001029431.1; NM_001034259.1. DR AlphaFoldDB; Q5BIP9; -. DR SMR; Q5BIP9; -. DR STRING; 9913.ENSBTAP00000023205; -. DR PaxDb; 9913-ENSBTAP00000023205; -. DR GeneID; 505912; -. DR KEGG; bta:505912; -. DR CTD; 150290; -. DR eggNOG; KOG1718; Eukaryota. DR HOGENOM; CLU_027074_3_4_1; -. DR InParanoid; Q5BIP9; -. DR OrthoDB; 127323at2759; -. DR TreeFam; TF316009; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. 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; IBA:GO_Central. 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..188 FT /note="Dual specificity protein phosphatase 18" FT /id="PRO_0000094827" 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" FT CONFLICT 31 FT /note="S -> R (in Ref. 2; AAI10014)" FT /evidence="ECO:0000305" SQ SEQUENCE 188 AA; 21028 MW; 3EADB96A25E1CE6B CRC64; MTASPCAFPV QFRQPSVSGL SQITSSLYIS SGVAANNRLM LSSNRISTVI NVSVEVVNAL YEDIHYVQVP VADTPTSRLC DFFDPIADHI HSVEMKQGRT LLHCAAGVSR SAALCLAYLM KYHAMSLLDA HTWTKSCRPI IRPNNGFWEQ LIHYEFQLFG RNTVHMVSSP VGMIPDIYEK EVRQMIPL //