DUS1A_XENLA
ID DUS1A_XENLA Reviewed; 369 AA.
AC Q91790; Q90W59;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Dual specificity protein phosphatase 1-A {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000269|PubMed:11854404, ECO:0000269|PubMed:7593328};
DE EC=3.1.3.48 {ECO:0000269|PubMed:11854404, ECO:0000269|PubMed:7593328};
DE AltName: Full=XCL100 {ECO:0000303|PubMed:7593328};
DE AltName: Full=XCL100-alfa {ECO:0000303|PubMed:11854404};
GN Name=dusp1-a {ECO:0000312|Xenbase:XB-GENE-975062};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Embryonic kidney {ECO:0000269|PubMed:7593328};
RX PubMed=7593328; DOI=10.1242/jcs.108.8.2885;
RA Lewis T., Groom L.A., Sneddon A.A., Smythe C., Keyse S.M.;
RT "XCL100, an inducible nuclear MAP kinase phosphatase from Xenopus laevis:
RT its role in MAP kinase inactivation in differentiated cells and its
RT expression during early development.";
RL J. Cell Sci. 108:2885-2896(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION
RP AT THR-168, PHOSPHORYLATION AT SERINE RESIDUES, AND MUTAGENESIS OF THR-168
RP AND CYS-260.
RC TISSUE=Ovary {ECO:0000312|EMBL:CAC44126.1};
RX PubMed=11854404; DOI=10.1091/mbc.01-11-0553;
RA Sohaskey M.L., Ferrell J.E. Jr.;
RT "Activation of p42 mitogen-activated protein kinase (MAPK), but not c-Jun
RT NH(2)-terminal kinase, induces phosphorylation and stabilization of MAPK
RT phosphatase XCL100 in Xenopus oocytes.";
RL Mol. Biol. Cell 13:454-468(2002).
CC -!- FUNCTION: Dual specificity phosphatase that dephosphorylates MAP kinase
CC MAPK1/ERK2 on both 'Thr-188' and 'Tyr-190', regulating its activity
CC during the meiotic cell cycle. {ECO:0000269|PubMed:11854404,
CC ECO:0000269|PubMed:7593328}.
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:11854404, ECO:0000269|PubMed:7593328};
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:11854404, ECO:0000269|PubMed:7593328};
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:11854404,
CC ECO:0000269|PubMed:7593328};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7593328}.
CC -!- TISSUE SPECIFICITY: Expressed in XIK-2 kidney cells.
CC {ECO:0000269|PubMed:7593328}.
CC -!- DEVELOPMENTAL STAGE: Present in both immature and mature oocytes (at
CC protein level). Expressed at a constant level during oocyte growth as
CC well as during oocyte maturation. Levels decline somewhat during
CC cleavage (stages 3-6). Levels rise dramatically during the mid-blastula
CC transition. This higher level of expression is then maintained through
CC gastrulation and all subsequent developmental stages.
CC {ECO:0000269|PubMed:7593328}.
CC -!- INDUCTION: By serum stimulation, heat shock and oxidative stress.
CC {ECO:0000269|PubMed:7593328}.
CC -!- PTM: Phosphorylated by MAPK1/ERK2 at Thr-168 and at one or more serine
CC residues in a progesterone-dependent manner. Phosphorylation reduces
CC its rate of degradation but does not seem to affect phosphatase
CC activity. {ECO:0000269|PubMed:11854404}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000255}.
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DR EMBL; X83742; CAA58710.1; -; mRNA.
DR EMBL; AJ320158; CAC44126.1; -; mRNA.
DR RefSeq; NP_001080570.1; NM_001087101.1.
DR AlphaFoldDB; Q91790; -.
DR SMR; Q91790; -.
DR iPTMnet; Q91790; -.
DR GeneID; 380262; -.
DR KEGG; xla:380262; -.
DR CTD; 380262; -.
DR Xenbase; XB-GENE-975062; dusp1.L.
DR OMA; PSCSPCN; -.
DR OrthoDB; 1576308at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 380262; Expressed in kidney and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IMP:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IMP:UniProtKB.
DR Gene3D; 3.40.250.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020420; Atypical_DUSP_subfamB.
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; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR PRINTS; PR01910; ADSPHPHTASEB.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 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 Hydrolase; Meiosis; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Stress response.
FT CHAIN 1..369
FT /note="Dual specificity protein phosphatase 1-A"
FT /id="PRO_0000421473"
FT DOMAIN 21..138
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 175..316
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 260
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 168
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:11854404"
FT MUTAGEN 168
FT /note="T->E: Abolishes threonine phosphorylation; when
FT associated with S-260. No effect on phosphatase activity
FT and MAPK1 binding; when associated with S-260."
FT /evidence="ECO:0000269|PubMed:11854404"
FT MUTAGEN 168
FT /note="T->V: Abolishes threonine phosphorylation; when
FT associated with S-260. No effect on phosphatase activity
FT and MAPK1 binding; when associated with S-260."
FT /evidence="ECO:0000269|PubMed:11854404"
FT MUTAGEN 260
FT /note="C->S: Loss of phosphatase activity. Increases
FT stability. Enables stable complex formation with active
FT MAPK1. Abolishes threonine phosphorylation; when associated
FT with E-168 or V-168. No effect on phosphatase activity and
FT MAPK1 binding; when associated with E-168 or V-168."
FT /evidence="ECO:0000269|PubMed:11854404"
SQ SEQUENCE 369 AA; 40264 MW; 14336CA5EC35AAF7 CRC64;
MVNMETCAMD CCVLKALLAE RAHKCLILDC RSFFSFSSCS IVGSSNVRLS TIVKRRAKGS
MGLEHIVPNE EQRCRLVAGM YEAVVLLDER TSELDMLRKD STMMLAVNAL CRDSRGSSIY
FLKGGYETFS AQCPEFCTKN SPPVGLSLPL CANNVPGSAD SNCTPCGTPL YDQGGPVEIL
PFLYLGSAYH ASRKDMLDTL GITALINVSA NCPNHFEGHF QYKSIPVEDS HKADISSWFN
EAIDFIDSVK NSGGRVFVHC QAGISRSATI CLAYLMRTNR VKLDEAFEFV KQRRSIISPN
FSFMGQLLQF ESQVLAPSCS AEAGSPTISV LDRGTSTTTV FNFPVSIPVH SGANSLSYLQ
NPITTSPSC
