DUS7_MOUSE
ID DUS7_MOUSE Reviewed; 422 AA.
AC Q91Z46; E9PVF4; E9QMS8; Q3USH2;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 4.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Dual specificity protein phosphatase 7 {ECO:0000312|MGI:MGI:2387100};
DE EC=3.1.3.16 {ECO:0000269|PubMed:27783954};
DE EC=3.1.3.48 {ECO:0000269|PubMed:27783954};
GN Name=Dusp7 {ECO:0000312|MGI:MGI:2387100};
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
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] OF 65-422.
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 FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MAPK1, AND MUTAGENESIS OF
RP 105-ARG-ARG-106 AND CYS-334.
RX PubMed=27783954; DOI=10.1016/j.celrep.2016.10.007;
RA Tischer T., Schuh M.;
RT "The phosphatase Dusp7 drives meiotic resumption and chromosome alignment
RT in mouse oocytes.";
RL Cell Rep. 17:1426-1437(2016).
CC -!- FUNCTION: Dual specificity protein phosphatase (PubMed:27783954). Shows
CC high activity towards MAPK1/ERK2 (By similarity). Also has lower
CC activity towards MAPK14 and MAPK8 (By similarity). In arrested oocytes,
CC plays a role in meiotic resumption (PubMed:27783954). Promotes nuclear
CC envelope breakdown and activation of the CDK1/Cyclin-B complex in
CC oocytes, probably by dephosphorylating and inactivating the
CC conventional protein kinase C (cPKC) isozyme PRKCB (PubMed:27783954).
CC May also inactivate PRKCA and/or PRKCG (PubMed:27783954). Also
CC important in oocytes for normal chromosome alignment on the metaphase
CC plate and progression to anaphase, where it might regulate activity of
CC the spindle-assembly checkpoint (SAC) complex (PubMed:27783954).
CC {ECO:0000250|UniProtKB:Q16829, ECO:0000269|PubMed:27783954}.
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:0000269|PubMed:27783954};
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:27783954};
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:27783954};
CC -!- ACTIVITY REGULATION: Strongly inhibited by sodium orthovanadate.
CC {ECO:0000250|UniProtKB:Q16829}.
CC -!- SUBUNIT: Interacts with MAPK1/ERK2; the interaction enhances DUSP7
CC phosphatase activity. {ECO:0000269|PubMed:27783954}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16829}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91Z46-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91Z46-2; Sequence=VSP_041462;
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE24360.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK140372; BAE24360.1; ALT_INIT; mRNA.
DR EMBL; AC140202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010207; AAH10207.1; -; mRNA.
DR CCDS; CCDS23475.2; -. [Q91Z46-1]
DR RefSeq; NP_703189.3; NM_153459.4. [Q91Z46-1]
DR AlphaFoldDB; Q91Z46; -.
DR SMR; Q91Z46; -.
DR STRING; 10090.ENSMUSP00000126984; -.
DR iPTMnet; Q91Z46; -.
DR PhosphoSitePlus; Q91Z46; -.
DR EPD; Q91Z46; -.
DR MaxQB; Q91Z46; -.
DR PaxDb; Q91Z46; -.
DR PRIDE; Q91Z46; -.
DR ProteomicsDB; 277613; -. [Q91Z46-1]
DR ProteomicsDB; 277614; -. [Q91Z46-2]
DR Antibodypedia; 31149; 180 antibodies from 25 providers.
DR DNASU; 235584; -.
DR Ensembl; ENSMUST00000172306; ENSMUSP00000126984; ENSMUSG00000053716. [Q91Z46-1]
DR GeneID; 235584; -.
DR KEGG; mmu:235584; -.
DR UCSC; uc009rjm.2; mouse. [Q91Z46-1]
DR CTD; 1849; -.
DR MGI; MGI:2387100; Dusp7.
DR VEuPathDB; HostDB:ENSMUSG00000053716; -.
DR eggNOG; KOG1717; Eukaryota.
DR GeneTree; ENSGT00940000157262; -.
DR InParanoid; Q91Z46; -.
DR OMA; TAEWQQD; -.
DR PhylomeDB; Q91Z46; -.
DR TreeFam; TF105122; -.
DR Reactome; R-MMU-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-MMU-202670; ERKs are inactivated.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR BioGRID-ORCS; 235584; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Dusp7; mouse.
DR PRO; PR:Q91Z46; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q91Z46; protein.
DR Bgee; ENSMUSG00000053716; Expressed in animal zygote and 260 other tissues.
DR ExpressionAtlas; Q91Z46; baseline and differential.
DR Genevisible; Q91Z46; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; ISO:MGI.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISO:MGI.
DR Gene3D; 3.40.250.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..422
FT /note="Dual specificity protein phosphatase 7"
FT /id="PRO_0000094808"
FT DOMAIN 71..190
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 247..390
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..106
FT /note="Interaction with MAPK1"
FT /evidence="ECO:0000269|PubMed:27783954"
FT REGION 219..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 334
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 334..340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16829"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041462"
FT MUTAGEN 105..106
FT /note="RR->M: Loss of MAPK1 binding. No effect on nuclear
FT envelope breakdown activity in oocytes."
FT /evidence="ECO:0000269|PubMed:27783954"
FT MUTAGEN 334
FT /note="C->S: No effect on MAPK1 binding. Impairs nuclear
FT envelope breakdown activity in oocytes."
FT /evidence="ECO:0000269|PubMed:27783954"
FT CONFLICT 241
FT /note="P -> S (in Ref. 1; BAE24360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 45220 MW; 1CD040E34B1D339A CRC64;
MKNQLRGPPV RAHMSTSGAA AAAAAGGTRA GSEPGAGSGS GAGIGAGATT GAGAMPCKSA
EWLQEELEAR GGASLLLLDC RPHELFESSH IETAINLAIP GLMLRRLRKG NLPIRSIIPN
HADKERFATR CKAATVLLYD EATAEWQPEP GAPASVLGLL LQKLRDDGCQ AYYLQGGFNK
FQTEYSEHCE TNVDSSSSPS GSPPTSVLGL GGLRISSDCS DGESDRELPS SATESDGSPV
PSSQPAFPVQ ILPYLYLGCA KDSTNLDVLG KYGIKYILNV TPNLPNAFEH GGEFTYKQIP
ISDHWSQNLS QFFPEAISFI DEARSKKCGV LVHCLAGISR SVTVTVAYLM QKMNLSLNDA
YDFVKRKKSN ISPNFNFMGQ LLDFERTLGL SSPCDNHAPS EQLYFSTPTN HNLFPINTLE
ST
