DUS18_MOUSE
ID DUS18_MOUSE Reviewed; 188 AA.
AC Q8VE01;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Dual specificity protein phosphatase 18;
DE EC=3.1.3.16 {ECO:0000269|PubMed:18385140};
DE EC=3.1.3.48 {ECO:0000269|PubMed:18385140};
GN Name=Dusp18;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP CATALYTIC ACTIVITY, AND 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, ECO:0000269|PubMed:18385140};
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:0000269|PubMed:18385140};
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:0000269|PubMed:18385140};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18385140}. 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:0000269|PubMed:18385140}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AK015917; BAC25470.1; -; mRNA.
DR EMBL; AK081916; BAC38371.1; -; mRNA.
DR EMBL; AL731853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020036; AAH20036.1; -; mRNA.
DR CCDS; CCDS24369.1; -.
DR RefSeq; NP_776106.1; NM_173745.5.
DR RefSeq; XP_006514936.1; XM_006514873.2.
DR AlphaFoldDB; Q8VE01; -.
DR SMR; Q8VE01; -.
DR STRING; 10090.ENSMUSP00000057346; -.
DR iPTMnet; Q8VE01; -.
DR PhosphoSitePlus; Q8VE01; -.
DR PaxDb; Q8VE01; -.
DR PRIDE; Q8VE01; -.
DR Antibodypedia; 24819; 41 antibodies from 13 providers.
DR DNASU; 75219; -.
DR Ensembl; ENSMUST00000055931; ENSMUSP00000057346; ENSMUSG00000047205.
DR Ensembl; ENSMUST00000109996; ENSMUSP00000105624; ENSMUSG00000047205.
DR GeneID; 75219; -.
DR KEGG; mmu:75219; -.
DR UCSC; uc007htu.2; mouse.
DR CTD; 150290; -.
DR MGI; MGI:1922469; Dusp18.
DR VEuPathDB; HostDB:ENSMUSG00000047205; -.
DR eggNOG; KOG1718; Eukaryota.
DR GeneTree; ENSGT00940000161186; -.
DR HOGENOM; CLU_027074_3_2_1; -.
DR InParanoid; Q8VE01; -.
DR OMA; MGMIPDV; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q8VE01; -.
DR TreeFam; TF316009; -.
DR BioGRID-ORCS; 75219; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Dusp18; mouse.
DR PRO; PR:Q8VE01; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VE01; protein.
DR Bgee; ENSMUSG00000047205; Expressed in animal zygote and 185 other tissues.
DR Genevisible; Q8VE01; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISS:MGI.
DR GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; ISS:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:MGI.
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 GO; GO:0033365; P:protein localization to organelle; ISS:MGI.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:MGI.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISS:MGI.
DR GO; GO:0046677; P:response to antibiotic; ISS:MGI.
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 1: Evidence at protein 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_0000094829"
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 ACT_SITE 104
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 188 AA; 21119 MW; 86CB43E390DC7DE3 CRC64;
MTSPWSAFPV QIPQPSIRGL SQITKSLFIS NGVAANNKLL LSSNQITTVI NVSVEVANTF
YEDIQYVQVP VVDAPVARLS NFFDSVADRI HSVEMQKGRT LLHCAAGVSR SAALCLAYLM
KYHAMSLVDA HTWTKSCRPI IRPNSGFWEQ LIHYELQLFG KNTMQMMDSP MGRIPDIYEK
ETRLMIPL
