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   24-JAN-2024, entry version 166.
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; 10090-ENSMUSP00000126984; -.
DR   ProteomicsDB; 277613; -. [Q91Z46-1]
DR   ProteomicsDB; 277614; -. [Q91Z46-2]
DR   Pumba; Q91Z46; -.
DR   Antibodypedia; 31149; 190 antibodies from 26 providers.
DR   DNASU; 235584; -.
DR   Ensembl; ENSMUST00000172306.3; ENSMUSP00000126984.3; ENSMUSG00000053716.10. [Q91Z46-1]
DR   GeneID; 235584; -.
DR   KEGG; mmu:235584; -.
DR   UCSC; uc009rjm.2; mouse. [Q91Z46-1]
DR   AGR; MGI:2387100; -.
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   OrthoDB; 2901840at2759; -.
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 80 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 263 other cell types or tissues.
DR   ExpressionAtlas; Q91Z46; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0033550; F:MAP kinase tyrosine phosphatase activity; IBA:GO_Central.
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:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR   CDD; cd14643; DSP_DUSP7; 1.
DR   CDD; cd01446; DSP_MapKP; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 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   PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR10159:SF305; DUAL SPECIFICITY PROTEIN PHOSPHATASE 7; 1.
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; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
DR   Genevisible; Q91Z46; MM.
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
//