DUS29_MOUSE
ID DUS29_MOUSE Reviewed; 215 AA.
AC Q8BK84; B2RW26;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Dual specificity phosphatase 29 {ECO:0000303|PubMed:32639872};
DE AltName: Full=Dual specificity phosphatase DUPD1;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q68J44};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q68J44};
GN Name=Dusp29;
GN Synonyms=Dupd1, Dusp27 {ECO:0000303|PubMed:17498703,
GN ECO:0000303|PubMed:30201684};
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;
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;
RA Brathwaite M., Waeltz P., Nagaraja R.;
RT "Genomic sequence analysis in the mouse T-complex region.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=17498703; DOI=10.1016/j.febslet.2007.04.059;
RA Friedberg I., Nika K., Tautz L., Saito K., Cerignoli F., Friedberg I.,
RA Godzik A., Mustelin T.;
RT "Identification and characterization of DUSP27, a novel dual-specific
RT protein phosphatase.";
RL FEBS Lett. 581:2527-2533(2007).
RN [5]
RP INTERACTION WITH PRKAA2, SUBCELLULAR LOCATION, FUNCTION, INDUCTION, AND
RP MUTAGENESIS OF CYS-146.
RX PubMed=30201684; DOI=10.2337/db18-0370;
RA Geng T., Liu Y., Xu Y., Jiang Y., Zhang N., Wang Z., Carmichael G.G.,
RA Taylor H.S., Li D., Huang Y.;
RT "H19 lncRNA Promotes Skeletal Muscle Insulin Sensitivity in Part by
RT Targeting AMPK.";
RL Diabetes 67:2183-2198(2018).
RN [6]
RP INDUCTION, SUBCELLULAR LOCATION, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=32639872; DOI=10.1152/ajpcell.00200.2020;
RA Cooper L.M., West R.C., Hayes C.S., Waddell D.S.;
RT "Dual-Specificity Phosphatase 29 is Induced During Neurogenic Skeletal
RT Muscle Atrophy and Attenuates Glucocorticoid Receptor Activity in Muscle
RT Cell Culture.";
RL Am. J. Physiol. 319:C441-C454(2020).
CC -!- FUNCTION: Dual specificity phosphatase able to dephosphorylate
CC phosphotyrosine, phosphoserine and phosphothreonine residues within the
CC same substrate, with a preference for phosphotyrosine as a substrate
CC (By similarity). Involved in the modulation of intracellular signaling
CC cascades. In skeletal muscle regulates systemic glucose homeostasis by
CC activating, AMPK, an energy sensor protein kinase (PubMed:30201684).
CC Affects MAP kinase signaling though modulation of the MAPK1/2 cascade
CC in skeletal muscle promoting muscle cell differentiation, development
CC and atrophy (PubMed:32639872). {ECO:0000250|UniProtKB:Q68J44,
CC ECO:0000269|PubMed:30201684, ECO:0000269|PubMed:32639872}.
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:Q68J44};
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:Q68J44};
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:Q68J44};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with PRKAA2
CC (PubMed:30201684). {ECO:0000250|UniProtKB:Q68J44,
CC ECO:0000269|PubMed:30201684}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30201684,
CC ECO:0000269|PubMed:32639872}. Nucleus {ECO:0000269|PubMed:32639872}.
CC -!- TISSUE SPECIFICITY: Skeletal muscle, liver and adipose tissue.
CC {ECO:0000269|PubMed:17498703}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during muscle cell differentiation.
CC {ECO:0000269|PubMed:32639872}.
CC -!- INDUCTION: Deletion of the long non-coding RNA (lncRNA) H19 leads to a
CC decreased DUSP29 expression in muscle (at protein level). Down-
CC regulated in muscle of high-fat diets-induced glucose-intolerant mice
CC (PubMed:30201684). Induced during neurogenic skeletal muscle atrophy
CC (PubMed:32639872). {ECO:0000269|PubMed:30201684,
CC ECO:0000269|PubMed:32639872}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK075665; BAC35883.1; -; mRNA.
DR EMBL; AY294423; AAQ01518.1; -; Genomic_DNA.
DR EMBL; BC147517; AAI47518.1; -; mRNA.
DR EMBL; BC147531; AAI47532.1; -; mRNA.
DR CCDS; CCDS26863.1; -.
DR RefSeq; NP_001013848.1; NM_001013826.2.
DR RefSeq; XP_006519280.1; XM_006519217.3.
DR AlphaFoldDB; Q8BK84; -.
DR SMR; Q8BK84; -.
DR BioGRID; 242278; 1.
DR IntAct; Q8BK84; 1.
DR MINT; Q8BK84; -.
DR STRING; 10090.ENSMUSP00000073534; -.
DR PhosphoSitePlus; Q8BK84; -.
DR MaxQB; Q8BK84; -.
DR PaxDb; Q8BK84; -.
DR PRIDE; Q8BK84; -.
DR ProteomicsDB; 279819; -.
DR Antibodypedia; 29633; 107 antibodies from 12 providers.
DR DNASU; 435391; -.
DR Ensembl; ENSMUST00000073870; ENSMUSP00000073534; ENSMUSG00000063821.
DR GeneID; 435391; -.
DR KEGG; mmu:435391; -.
DR UCSC; uc007sll.1; mouse.
DR CTD; 338599; -.
DR MGI; MGI:3647127; Dupd1.
DR VEuPathDB; HostDB:ENSMUSG00000063821; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000160190; -.
DR HOGENOM; CLU_027074_11_3_1; -.
DR InParanoid; Q8BK84; -.
DR OMA; NAAHGQR; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q8BK84; -.
DR TreeFam; TF105128; -.
DR BioGRID-ORCS; 435391; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Dupd1; mouse.
DR PRO; PR:Q8BK84; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BK84; protein.
DR Bgee; ENSMUSG00000063821; Expressed in quadriceps femoris and 21 other tissues.
DR ExpressionAtlas; Q8BK84; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; IMP:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization 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; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
DR GO; GO:0042692; P:muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
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; 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 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; Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..215
FT /note="Dual specificity phosphatase 29"
FT /id="PRO_0000295879"
FT DOMAIN 53..201
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 146
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 145..152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68J44"
FT MUTAGEN 146
FT /note="C->S: Does not affect AMPK activity."
FT /evidence="ECO:0000269|PubMed:30201684"
SQ SEQUENCE 215 AA; 24192 MW; B30C3F0C3C169FD7 CRC64;
MASGDTKTSV KHAHLCAERL SVREEEGDAE DYCTPGAFEL ERLFWKGSPQ YTHVNEVWPR
LHIGDEATAL DRYGLQKAGF THVLNAAHGR WNVDTGPDYY RDMAIEYHGV EADDVPTFDL
SIFFYSAAAF IDSALRDDHS KILVHCAMGR SRSATLVLAY LMIHKNMTLV DAIQQVAKNR
CVLPNRGFLK QLRELDKQLV KQRRQAGPGD SDLGL
