DS13A_MOUSE
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 03-AUG-2022, entry version 120.
DE RecName: Full=Dual specificity protein phosphatase 13 isoform A;
DE Short=DUSP13A;
DE EC=3.1.3.16;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q6B8I1};
DE AltName: Full=Muscle-restricted DSP;
GN Name=Dusp13; Synonyms=Dusp13a, 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] (ISOFORM 1), ALTERNATIVE PROMOTER USAGE, TISSUE
RP 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; 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 -!- 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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1;
CC IsoId=Q6B8I0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QYJ7-1; Sequence=External;
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; -. [Q6B8I0-1]
DR RefSeq; NP_001007269.1; NM_001007268.1. [Q6B8I0-1]
DR RefSeq; XP_017171528.1; XM_017316039.1. [Q6B8I0-1]
DR AlphaFoldDB; Q6B8I0; -.
DR SMR; Q6B8I0; -.
DR BioGRID; 205196; 1.
DR PhosphoSitePlus; Q6B8I0; -.
DR PRIDE; Q6B8I0; -.
DR ProteomicsDB; 279582; -. [Q6B8I0-1]
DR Antibodypedia; 15503; 269 antibodies from 27 providers.
DR DNASU; 27389; -.
DR Ensembl; ENSMUST00000075040; ENSMUSP00000074553; ENSMUSG00000021768. [Q6B8I0-1]
DR GeneID; 27389; -.
DR KEGG; mmu:27389; -.
DR UCSC; uc007slo.2; mouse. [Q6B8I0-1]
DR CTD; 51207; -.
DR MGI; MGI:1351599; Dusp13.
DR VEuPathDB; HostDB:ENSMUSG00000021768; -.
DR GeneTree; ENSGT00940000154628; -.
DR HOGENOM; CLU_027074_11_3_1; -.
DR OMA; AHGTMFC; -.
DR BioGRID-ORCS; 27389; 2 hits in 58 CRISPR screens.
DR ChiTaRS; Dusp13; mouse.
DR Proteomes; UP000000589; Chromosome 14.
DR Bgee; ENSMUSG00000021768; Expressed in spermatid and 47 other tissues.
DR ExpressionAtlas; Q6B8I0; baseline and differential.
DR Genevisible; Q6B8I0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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 GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 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; PTHR45682; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01909; ADSPHPHTASEA.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 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 Alternative promoter usage; Cytoplasm; Hydrolase; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..188
FT /note="Dual specificity protein phosphatase 13 isoform A"
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
