DUSK4_DROME
ID DUSK4_DROME Reviewed; 387 AA.
AC Q9VWF4; Q95TD9;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Dual specificity protein phosphatase MPK-4 {ECO:0000303|PubMed:18456458};
DE EC=3.1.3.16 {ECO:0000269|PubMed:18456458};
DE EC=3.1.3.48 {ECO:0000269|PubMed:18456458};
GN Name=MKP-4 {ECO:0000303|PubMed:18456458};
GN ORFNames=CG14211 {ECO:0000312|FlyBase:FBgn0031044};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:ABX00756.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABX00756.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:ABX00756.1};
RA Stapleton M., Carlson J., Frise E., Kapadia B., Park S., Wan K., Yu C.,
RA Celniker S.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAL13359.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 314-387.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL13359.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL13359.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH BSK,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-126.
RX PubMed=18456458; DOI=10.1016/j.cellsig.2008.03.003;
RA Sun L., Yu M.C., Kong L., Zhuang Z.H., Hu J.H., Ge B.X.;
RT "Molecular identification and functional characterization of a Drosophila
RT dual-specificity phosphatase DMKP-4 which is involved in PGN-induced
RT activation of the JNK pathway.";
RL Cell. Signal. 20:1329-1337(2008).
CC -!- FUNCTION: Dual specificity phosphatase; can dephosphorylate both
CC phosphotyrosine and phosphoserine or phosphothreonine residues. May
CC suppress bsk/JNK activation during the immune response.
CC {ECO:0000269|PubMed:18456458}.
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:18456458};
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:18456458};
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:18456458};
CC -!- ACTIVITY REGULATION: Inhibited by the tyrosine phosphatase inhibitor
CC sodium vanadate. {ECO:0000269|PubMed:18456458}.
CC -!- SUBUNIT: Interacts (via tyrosine-protein phosphatase domain) with
CC bsk/JNK; the interaction dephosphorylates bsk.
CC {ECO:0000269|PubMed:18456458}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18456458}. Cytoplasm
CC {ECO:0000269|PubMed:18456458}. Note=Mainly found in the nucleus.
CC {ECO:0000269|PubMed:18456458}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13359.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF48988.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95557.1; -; Genomic_DNA.
DR EMBL; BT031134; ABX00756.1; -; mRNA.
DR EMBL; AY059453; AAL13359.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001259717.1; NM_001272788.1.
DR RefSeq; NP_608332.2; NM_134488.2.
DR AlphaFoldDB; Q9VWF4; -.
DR SMR; Q9VWF4; -.
DR IntAct; Q9VWF4; 2.
DR STRING; 7227.FBpp0074510; -.
DR PaxDb; Q9VWF4; -.
DR PRIDE; Q9VWF4; -.
DR DNASU; 32963; -.
DR EnsemblMetazoa; FBtr0074741; FBpp0074510; FBgn0031044.
DR EnsemblMetazoa; FBtr0332481; FBpp0304757; FBgn0031044.
DR GeneID; 32963; -.
DR KEGG; dme:Dmel_CG14211; -.
DR UCSC; CG14211-RB; d. melanogaster.
DR CTD; 32963; -.
DR FlyBase; FBgn0031044; MKP-4.
DR VEuPathDB; VectorBase:FBgn0031044; -.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_023312_1_0_1; -.
DR InParanoid; Q9VWF4; -.
DR OMA; RIMLNTQ; -.
DR OrthoDB; 1482182at2759; -.
DR PhylomeDB; Q9VWF4; -.
DR BioGRID-ORCS; 32963; 0 hits in 3 CRISPR screens.
DR ChiTaRS; MKP-4; fly.
DR GenomeRNAi; 32963; -.
DR PRO; PR:Q9VWF4; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0031044; Expressed in egg cell and 23 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IDA:FlyBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IDA:FlyBase.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IMP:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR016278; DUSP12.
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 Pfam; PF00782; DSPc; 1.
DR PIRSF; PIRSF000941; DUSP12; 1.
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..387
FT /note="Dual specificity protein phosphatase MPK-4"
FT /id="PRO_0000439451"
FT DOMAIN 35..182
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000305|PubMed:18456458"
FT MUTAGEN 126
FT /note="C->S: Abolishes phosphatase activity. Loss of
FT bsk/JNK binding. Reduced nuclear localization."
FT /evidence="ECO:0000269|PubMed:18456458"
SQ SEQUENCE 387 AA; 43742 MW; 107F3DFFB6E72896 CRC64;
MEQSQSQRQA WPSSSAGGGK AQDSGVLTRE DFDGGPVSID EVDTGLFLGN LTAATHMETL
RSFKITHILT LDSVPLPQHI LEASFLTTKY IQIADMPRED ILQHLEGCVD FISSALAQQG
NVLVHCYFGV SRSSSTVIAY MMKRHNLDFL PAYELVKAKR RFVQPNAGFV SQLKLFRRMG
CKIDPNCQRY KIHRLRLAGE QMRKAKILPQ SFHSVVRPDP DITRENPEPI VFRCRRCRRV
LASKSHVLEH KPRDRPPQEV VPKEKEEVAA AKLPAQSHDQ AENHHGARML EQLSERIRQS
SLGSPGHEST PNYCRSILFV EPIAWMHRIM LNTQGRLYCP KCEQKLGNFS WINACKCPCG
ETMTPAFYLI PSKVELSKAV QNVQTTV
