DUS15_MOUSE
ID DUS15_MOUSE Reviewed; 235 AA.
AC Q8R4V2; A2APC1; Q14AH2;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Dual specificity protein phosphatase 15 {ECO:0000250|UniProtKB:Q9H1R2};
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q9H1R2, ECO:0000255|PROSITE-ProRule:PRU10044};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q9H1R2, ECO:0000255|PROSITE-ProRule:PRU10044};
DE AltName: Full=Dual specificity protein phosphatase T-DSP10 {ECO:0000303|PubMed:11432789};
GN Name=Dusp15 {ECO:0000312|MGI:MGI:1934928};
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 [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=11432789; DOI=10.1093/oxfordjournals.jbchem.a002952;
RA Aoki N., Aoyama K., Nagata M., Matsuda T.;
RT "A growing family of dual specificity phosphatases with low molecular
RT masses.";
RL J. Biochem. 130:133-140(2001).
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] (ISOFORM 2).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-125 (ISOFORM 1).
RX PubMed=11812828; DOI=10.1093/nar/29.24.4983;
RA Mu X., Zhao S., Pershad R., Hsieh T.-F., Scarpa A., Wang S.W., White R.A.,
RA Beremand P.D., Thomas T.L., Gan L., Klein W.H.;
RT "Gene expression in the developing mouse retina by EST sequencing and
RT microarray analysis.";
RL Nucleic Acids Res. 29:4983-4993(2001).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15138252; DOI=10.1074/jbc.m403442200;
RA Alonso A., Narisawa S., Bogetz J., Tautz L., Hadzic R., Huynh H.,
RA Williams S., Gjoerloff-Wingren A., Bremer M.C.D., Holsinger L.J.,
RA Millan J.L., Mustelin T.;
RT "VHY, a novel myristoylated testis-restricted dual specificity protein
RT phosphatase related to VHX.";
RL J. Biol. Chem. 279:32586-32591(2004).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=22792334; DOI=10.1371/journal.pone.0040457;
RA Schmidt F., van den Eijnden M., Pescini Gobert R., Saborio G.P.,
RA Carboni S., Alliod C., Pouly S., Staugaitis S.M., Dutta R., Trapp B.,
RA Hooft van Huijsduijnen R.;
RT "Identification of VHY/Dusp15 as a regulator of oligodendrocyte
RT differentiation through a systematic genomics approach.";
RL PLoS ONE 7:E40457-E40457(2012).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=27532821; DOI=10.1002/glia.23044;
RA Muth K.N., Piefke S., Weider M., Sock E., Hermans-Borgmeyer I., Wegner M.,
RA Kuespert M.;
RT "The dual-specificity phosphatase Dusp15 is regulated by Sox10 and Myrf in
RT myelinating oligodendrocytes.";
RL Glia 64:2120-2132(2016).
CC -!- FUNCTION: May dephosphorylate MAPK13, ATF2, ERBB3, PDGFRB and SNX6 (By
CC similarity). {ECO:0000250|UniProtKB:Q9H1R2}.
CC -!- FUNCTION: [Isoform 1]: May play a role in the regulation of
CC oligodendrocyte differentiation (PubMed:22792334). May play a role in
CC the regulation of myelin formation (By similarity). Involved in the
CC regulation of Erk1/2 phosphorylation in Schwann cells; the signaling
CC may be linked to the regulation of myelination (By similarity).
CC {ECO:0000250|UniProtKB:B4F7B7, ECO:0000269|PubMed:22792334}.
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:Q9H1R2, 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 -!- 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H1R2};
CC Lipid-anchor; Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R4V2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R4V2-2; Sequence=VSP_007294, VSP_007295;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in testis; predominantly in
CC developing spermatocytes (at protein level) (PubMed:15138252). Isoform
CC 2 is highly expressed in testis (PubMed:11432789). Expressed in spinal
CC cord and specifically in oligodendroglial cells (PubMed:27532821).
CC Expressed in embryonic brain cortex; down-regulated in mice with
CC experimental autoimmune encephalomyelitis (EAE) (PubMed:22792334).
CC {ECO:0000269|PubMed:11432789, ECO:0000269|PubMed:22792334,
CC ECO:0000269|PubMed:27532821}.
CC -!- DEVELOPMENTAL STAGE: Expression increases during oligodendrocyte
CC differentiation. Detected in spinal cord in late fetal (18.5 dpc) and
CC early postnatal (P3 and P7) stages. Expression decreases in later
CC postnatal development (P14 and P30). {ECO:0000269|PubMed:22792334,
CC ECO:0000269|PubMed:27532821}.
CC -!- INDUCTION: Down-regulated by nerve injury.
CC {ECO:0000269|PubMed:22792334}.
CC -!- MISCELLANEOUS: [Isoform 2]: Inactive. Lacks the active site.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BU924460; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF357887; AAM00226.1; -; mRNA.
DR EMBL; AL833801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC116841; AAI16842.1; -; mRNA.
DR EMBL; BC116843; AAI16844.1; -; mRNA.
DR EMBL; BU924460; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS16902.1; -. [Q8R4V2-2]
DR CCDS; CCDS50754.1; -. [Q8R4V2-1]
DR RefSeq; NP_001152848.1; NM_001159376.1. [Q8R4V2-1]
DR RefSeq; NP_665687.1; NM_145744.2. [Q8R4V2-2]
DR AlphaFoldDB; Q8R4V2; -.
DR SMR; Q8R4V2; -.
DR STRING; 10090.ENSMUSP00000123090; -.
DR iPTMnet; Q8R4V2; -.
DR PhosphoSitePlus; Q8R4V2; -.
DR SwissPalm; Q8R4V2; -.
DR MaxQB; Q8R4V2; -.
DR PaxDb; Q8R4V2; -.
DR PeptideAtlas; Q8R4V2; -.
DR PRIDE; Q8R4V2; -.
DR ProteomicsDB; 275411; -. [Q8R4V2-1]
DR ProteomicsDB; 275412; -. [Q8R4V2-2]
DR Antibodypedia; 25257; 215 antibodies from 23 providers.
DR DNASU; 252864; -.
DR Ensembl; ENSMUST00000037715; ENSMUSP00000045815; ENSMUSG00000042662. [Q8R4V2-2]
DR Ensembl; ENSMUST00000123121; ENSMUSP00000123090; ENSMUSG00000042662. [Q8R4V2-1]
DR GeneID; 252864; -.
DR KEGG; mmu:252864; -.
DR UCSC; uc008ngu.2; mouse. [Q8R4V2-2]
DR UCSC; uc012cgl.1; mouse. [Q8R4V2-1]
DR CTD; 128853; -.
DR MGI; MGI:1934928; Dusp15.
DR VEuPathDB; HostDB:ENSMUSG00000042662; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000162011; -.
DR HOGENOM; CLU_027074_5_0_1; -.
DR InParanoid; Q8R4V2; -.
DR OMA; TSPFNDE; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q8R4V2; -.
DR TreeFam; TF105126; -.
DR BioGRID-ORCS; 252864; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q8R4V2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8R4V2; protein.
DR Bgee; ENSMUSG00000042662; Expressed in sciatic nerve and 93 other tissues.
DR ExpressionAtlas; Q8R4V2; baseline and differential.
DR Genevisible; Q8R4V2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISO:MGI.
DR GO; GO:0016311; P:dephosphorylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0048713; P:regulation of oligodendrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 3.90.190.10; -; 1.
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 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 Alternative splicing; Cell membrane; Hydrolase; Lipoprotein; Membrane;
KW Myristate; Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..235
FT /note="Dual specificity protein phosphatase 15"
FT /id="PRO_0000094825"
FT DOMAIN 4..144
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 183..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 88
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1R2"
FT VAR_SEQ 88..105
FT /note="CFAGISRSTTIVIAYVMT -> WPLKHECRARSLSLLQCS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:11432789,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007294"
FT VAR_SEQ 106..235
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11432789,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007295"
SQ SEQUENCE 235 AA; 26186 MW; 09A3EB05A0A7F891 CRC64;
MGNGMTKVLP GLYLGNFIDA KDPDQLGRNK ITHIISIHES PQPLLQDITY LRISVSDTPE
VPIKKHFKEC VHFIHSCRLN GGNCLVHCFA GISRSTTIVI AYVMTVTGLG WQEVLEAIKA
SRPIANPNPG FRQQLEEFGW ANSQKLRRQL EERFGEIPFR DEEDLRALLP LCRRCRQGSA
TSAASATTAS SAAEGTLQRL VPRSPRDSHQ PLPLLARVKQ TFFCLPRCLS RKGGK
