DUS18_RAT
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 03-AUG-2022, entry version 116.
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}.
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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; Q6AXW7; -.
DR GeneID; 305477; -.
DR KEGG; rno:305477; -.
DR UCSC; RGD:1306929; rat.
DR CTD; 150290; -.
DR RGD; 1306929; Dusp18.
DR eggNOG; KOG1718; Eukaryota.
DR InParanoid; Q6AXW7; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q6AXW7; -.
DR PRO; PR:Q6AXW7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
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 Gene3D; 3.90.190.10; -; 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 Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01910; ADSPHPHTASEB.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 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
