DUS7_RAT
ID DUS7_RAT Reviewed; 419 AA.
AC Q63340; F1M7V9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Dual specificity protein phosphatase 7 {ECO:0000312|RGD:735026};
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q16829};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q16829};
DE AltName: Full=Dual specificity protein phosphatase MKP-X {ECO:0000303|PubMed:8626780};
GN Name=Dusp7 {ECO:0000312|RGD:735026};
GN Synonyms=Mkpx {ECO:0000303|PubMed:8626780};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:EDL77319.1};
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 141-419.
RC STRAIN=Sprague-Dawley; TISSUE=Neuron;
RX PubMed=8626780; DOI=10.1074/jbc.271.8.4319;
RA Muda M., Boschert U., Dickinson R., Martinou J.-C., Martinou I., Camps M.,
RA Schlegel W., Arkinstall S.;
RT "MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a
RT new class of mitogen-activated protein kinase phosphatase.";
RL J. Biol. Chem. 271:4319-4326(1996).
RN [4]
RP INTERACTION WITH MAPK1.
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 (By similarity). 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. Promotes nuclear envelope breakdown
CC and activation of the CDK1/Cyclin-B complex in oocytes, probably by
CC dephosphorylating and inactivating the conventional protein kinase C
CC (cPKC) isozyme PRKCB. May also inactivate PRKCA and/or PRKCG. 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.
CC {ECO:0000250|UniProtKB:Q16829, ECO:0000250|UniProtKB:Q91Z46}.
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:Q16829};
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:Q16829};
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:Q16829};
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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AABR07071436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473954; EDL77319.1; -; Genomic_DNA.
DR EMBL; X94186; CAA63896.1; -; mRNA.
DR RefSeq; NP_001094017.1; NM_001100547.1.
DR AlphaFoldDB; Q63340; -.
DR SMR; Q63340; -.
DR STRING; 10116.ENSRNOP00000014770; -.
DR PaxDb; Q63340; -.
DR Ensembl; ENSRNOT00000014770; ENSRNOP00000014770; ENSRNOG00000010789.
DR GeneID; 300980; -.
DR KEGG; rno:300980; -.
DR UCSC; RGD:735026; rat.
DR CTD; 1849; -.
DR RGD; 735026; Dusp7.
DR eggNOG; KOG1717; Eukaryota.
DR GeneTree; ENSGT00940000157262; -.
DR HOGENOM; CLU_027074_0_0_1; -.
DR InParanoid; Q63340; -.
DR OMA; TAEWQQD; -.
DR OrthoDB; 911920at2759; -.
DR PhylomeDB; Q63340; -.
DR TreeFam; TF105122; -.
DR Reactome; R-RNO-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-RNO-202670; ERKs are inactivated.
DR Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:Q63340; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000010789; Expressed in heart and 18 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; ISO:RGD.
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:RGD.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISO:RGD.
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 Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..419
FT /note="Dual specificity protein phosphatase 7"
FT /id="PRO_0000094809"
FT DOMAIN 68..187
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 244..387
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 331..337
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16829"
SQ SEQUENCE 419 AA; 45067 MW; 58A02C18A49A3670 CRC64;
MKNQLRGPPV RAHMSTSGAA AAGGTRAGSE PGAGSGSSAG IGAGATTGAG AMPCKSAEWL
QEELEARGGA SLLLLDCRPH ELFESSHIET AINLAIPGLM LRRLRKGNLP IRSIIPNHAD
KERFATRCKA ATVLLYDEAT AEWQPEPGAP ASVLGLLLQK LRDDGCQAYY LQGGFNKFQT
EYSEHCETNV DSSSSPSGSP PTSVLGLGGL RISSDCSDGE SDRELPSSAT ESDGSPVPSS
QPAFPVQILP YLYLGCAKDS TNLDVLGKYG IKYILNVTPN LPNAFEHGGE FTYKQIPISD
HWSQNLSQFF PEAISFIDEA RSKKCGVLVH CLAGISRSVT VTVAYLMQKM NLSLNDAYDF
VKRKKSNISP NFNFMGQLLD FERTLGLSSP CDNHTPSEQL YFSTPTNHNL FPINTLEST
