ID   DS13A_MOUSE             Reviewed;         188 AA.
AC   Q6B8I0;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Dual specificity protein phosphatase 13A {ECO:0000250|UniProtKB:Q6B8I1};
DE            Short=DUSP13A {ECO:0000250|UniProtKB:Q6B8I1};
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:Q6B8I1};
DE            EC=3.1.3.48 {ECO:0000250|UniProtKB:Q6B8I1};
DE   AltName: Full=Muscle-restricted DSP;
GN   Name=Dusp13a {ECO:0000250|UniProtKB:Q6B8I1};
GN   Synonyms=Dusp13 {ECO:0000312|MGI:MGI:1351599}, Mdsp;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Skeletal muscle;
RX   PubMed=15252030; DOI=10.1074/jbc.m405286200;
RA   Chen H.-H., Luche R., Wei B., Tonks N.K.;
RT   "Characterization of two distinct dual specificity phosphatases encoded in
RT   alternative open reading frames of a single gene located on human
RT   chromosome 10q22.2.";
RL   J. Biol. Chem. 279:41404-41413(2004).
CC   -!- FUNCTION: Probable protein tyrosine phosphatase. Has phosphatase
CC       activity with synthetic substrates. Has a phosphatase activity-
CC       independent regulatory role in MAP3K5/ASK1-mediated apoptosis,
CC       preventing MAP3K5/ASK1 inhibition by AKT1. Shows no phosphatase
CC       activity on MAPK1/ERK2, MAPK8/JNK, MAPK14/p38 and MAP3K5/ASK1.
CC       {ECO:0000250|UniProtKB:Q6B8I1}.
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:Q6B8I1, 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:Q6B8I1};
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:Q6B8I1};
CC   -!- SUBUNIT: Monomer. Interacts with MAP3K5/ASK1; may compete with AKT1
CC       preventing MAP3K5/ASK1 phosphorylation by AKT1.
CC       {ECO:0000250|UniProtKB:Q6B8I1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Skeletal muscle-specific.
CC       {ECO:0000269|PubMed:15252030}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at very low levels in myotubes and early
CC       postnatal muscle. Expression markedly increases at approximately the
CC       3rd week after birth and continues to increase gradually into
CC       adulthood. {ECO:0000269|PubMed:15252030}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
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DR   EMBL; AY674052; AAT79357.1; -; mRNA.
DR   CCDS; CCDS36821.1; -.
DR   RefSeq; NP_001007269.1; NM_001007268.1.
DR   RefSeq; XP_017171528.1; XM_017316039.1.
DR   AlphaFoldDB; Q6B8I0; -.
DR   SMR; Q6B8I0; -.
DR   BioGRID; 205196; 2.
DR   Antibodypedia; 15503; 303 antibodies from 27 providers.
DR   DNASU; 27389; -.
DR   Ensembl; ENSMUST00000075040.9; ENSMUSP00000074553.3; ENSMUSG00000021768.16.
DR   GeneID; 128932648; -.
DR   KEGG; mmu:128932648; -.
DR   UCSC; uc007slo.2; mouse.
DR   CTD; 128854680; -.
DR   MGI; MGI:1351599; Dusp13.
DR   VEuPathDB; HostDB:ENSMUSG00000021768; -.
DR   GeneTree; ENSGT00940000154628; -.
DR   HOGENOM; CLU_027074_11_3_1; -.
DR   OMA; AHGTMFC; -.
DR   OrthoDB; 1082488at2759; -.
DR   BioGRID-ORCS; 27389; 2 hits in 61 CRISPR screens.
DR   ChiTaRS; Dusp13; mouse.
DR   Proteomes; UP000000589; Chromosome 14.
DR   Bgee; ENSMUSG00000021768; Expressed in spermatid and 48 other cell types or tissues.
DR   ExpressionAtlas; Q6B8I0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0033549; F:MAP kinase phosphatase activity; IBA:GO_Central.
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; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:MGI.
DR   GO; GO:0016311; P:dephosphorylation; ISO:MGI.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR   CDD; cd14580; DUSP13A; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR020405; Atypical_DUSP_subfamA.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR45682; AGAP008228-PA; 1.
DR   PANTHER; PTHR45682:SF3; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
DR   PRINTS; PR01909; ADSPHPHTASEA.
DR   SMART; SM00195; DSPc; 1.
DR   SMART; SM00404; PTPc_motif; 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.
DR   Genevisible; Q6B8I0; MM.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome.
FT   CHAIN           1..188
FT                   /note="Dual specificity protein phosphatase 13A"
FT                   /id="PRO_0000381974"
FT   DOMAIN          37..184
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        129
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   188 AA;  20646 MW;  340FA4CBB09FDCDE CRC64;
     MADASIPKPG EEKEATPCPS ILQLEELLRA GRASCSRVDE VWPNLFIGDA ATANNRFELW
     KLGITHVLNA AHGGLYCQGG PDFYGSSVCY LGIPAHDLPD FNISPYFSSA ADFIHRALTV
     PGAKVLVHCV VGVSRSATLV LAYLMLHQQL SLQQAIITVR ERRWIFPNRG FLRQLCQLDQ
     QLRGAGQS
//