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Dual specificity protein phosphatase 1-A (EC 3 1 3 16) (EC 3 1 3 48) (XCL100) (XCL100-alfa)

 DUS1A_XENLA             Reviewed;         369 AA.
Q91790; Q90W59;
06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
16-JAN-2019, entry version 111.
RecName: Full=Dual specificity protein phosphatase 1-A {ECO:0000305};
EC=3.1.3.16 {ECO:0000269|PubMed:11854404, ECO:0000269|PubMed:7593328};
EC=3.1.3.48 {ECO:0000269|PubMed:11854404, ECO:0000269|PubMed:7593328};
AltName: Full=XCL100 {ECO:0000303|PubMed:7593328};
AltName: Full=XCL100-alfa {ECO:0000303|PubMed:11854404};
Name=dusp1-a {ECO:0000312|Xenbase:XB-GENE-975062};
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
TISSUE=Embryonic kidney {ECO:0000269|PubMed:7593328};
PubMed=7593328;
Lewis T., Groom L.A., Sneddon A.A., Smythe C., Keyse S.M.;
"XCL100, an inducible nuclear MAP kinase phosphatase from Xenopus
laevis: its role in MAP kinase inactivation in differentiated cells
and its expression during early development.";
J. Cell Sci. 108:2885-2896(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
PHOSPHORYLATION AT THR-168, PHOSPHORYLATION AT SERINE RESIDUES, AND
MUTAGENESIS OF THR-168 AND CYS-260.
TISSUE=Ovary {ECO:0000312|EMBL:CAC44126.1};
PubMed=11854404; DOI=10.1091/mbc.01-11-0553;
Sohaskey M.L., Ferrell J.E. Jr.;
"Activation of p42 mitogen-activated protein kinase (MAPK), but not c-
Jun NH(2)-terminal kinase, induces phosphorylation and stabilization
of MAPK phosphatase XCL100 in Xenopus oocytes.";
Mol. Biol. Cell 13:454-468(2002).
-!- FUNCTION: Dual specificity phosphatase that dephosphorylates MAP
kinase MAPK1/ERK2 on both 'Thr-188' and 'Tyr-190', regulating its
activity during the meiotic cell cycle.
{ECO:0000269|PubMed:11854404, ECO:0000269|PubMed:7593328}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999,
ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16;
Evidence={ECO:0000269|PubMed:11854404,
ECO:0000269|PubMed:7593328};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
EC=3.1.3.16; Evidence={ECO:0000269|PubMed:11854404,
ECO:0000269|PubMed:7593328};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein]
+ phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10044,
ECO:0000269|PubMed:11854404, ECO:0000269|PubMed:7593328};
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7593328}.
-!- TISSUE SPECIFICITY: Expressed in XIK-2 kidney cells.
{ECO:0000269|PubMed:7593328}.
-!- DEVELOPMENTAL STAGE: Present in both immature and mature oocytes
(at protein level). Expressed at a constant level during oocyte
growth as well as during oocyte maturation. Levels decline
somewhat during cleavage (stages 3-6). Levels rise dramatically
during the mid-blastula transition. This higher level of
expression is then maintained through gastrulation and all
subsequent developmental stages. {ECO:0000269|PubMed:7593328}.
-!- INDUCTION: By serum stimulation, heat shock and oxidative stress.
{ECO:0000269|PubMed:7593328}.
-!- PTM: Phosphorylated by MAPK1/ERK2 at Thr-168 and at one or more
serine residues in a progesterone-dependent manner.
Phosphorylation reduces its rate of degradation but does not seem
to affect phosphatase activity. {ECO:0000269|PubMed:11854404}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class dual specificity subfamily. {ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; X83742; CAA58710.1; -; mRNA.
EMBL; AJ320158; CAC44126.1; -; mRNA.
RefSeq; NP_001080570.1; NM_001087101.1.
UniGene; Xl.1243; -.
ProteinModelPortal; Q91790; -.
SMR; Q91790; -.
iPTMnet; Q91790; -.
GeneID; 380262; -.
KEGG; xla:380262; -.
CTD; 380262; -.
Xenbase; XB-GENE-975062; dusp1.
HOVERGEN; HBG007347; -.
KO; K21278; -.
OrthoDB; 1576308at2759; -.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IMP:UniProtKB.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
GO; GO:0000188; P:inactivation of MAPK activity; IMP:UniProtKB.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0071850; P:mitotic cell cycle arrest; IMP:UniProtKB.
GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:UniProtKB.
GO; GO:0051447; P:negative regulation of meiotic cell cycle; IMP:UniProtKB.
GO; GO:0070262; P:peptidyl-serine dephosphorylation; ISS:UniProtKB.
GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IMP:UniProtKB.
CDD; cd00127; DSPc; 1.
Gene3D; 3.40.250.10; -; 1.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR020417; Atypical_DUSP.
InterPro; IPR020420; Atypical_DUSP_famB.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR024950; DUSP.
InterPro; IPR008343; MKP.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR001763; Rhodanese-like_dom.
InterPro; IPR036873; Rhodanese-like_dom_sf.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
PANTHER; PTHR10159; PTHR10159; 1.
Pfam; PF00782; DSPc; 1.
PIRSF; PIRSF000939; MAPK_Ptase; 1.
PRINTS; PR01908; ADSPHPHTASE.
PRINTS; PR01910; ADSPHPHTASEB.
PRINTS; PR01764; MAPKPHPHTASE.
SMART; SM00195; DSPc; 1.
SMART; SM00404; PTPc_motif; 1.
SMART; SM00450; RHOD; 1.
SUPFAM; SSF52799; SSF52799; 1.
SUPFAM; SSF52821; SSF52821; 1.
PROSITE; PS50206; RHODANESE_3; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
1: Evidence at protein level;
Hydrolase; Meiosis; Nucleus; Phosphoprotein; Protein phosphatase;
Stress response.
CHAIN 1 369 Dual specificity protein phosphatase 1-A.
/FTId=PRO_0000421473.
DOMAIN 21 138 Rhodanese. {ECO:0000255|PROSITE-
ProRule:PRU00173}.
DOMAIN 175 369 Tyrosine-protein phosphatase.
{ECO:0000255, ECO:0000305}.
ACT_SITE 260 260 Phosphocysteine intermediate.
{ECO:0000250|UniProtKB:P28563,
ECO:0000255|PROSITE-ProRule:PRU10044}.
MOD_RES 168 168 Phosphothreonine; by MAPK1.
{ECO:0000269|PubMed:11854404}.
MUTAGEN 168 168 T->E: Abolishes threonine
phosphorylation; when associated with S-
260. No effect on phosphatase activity
and MAPK1 binding; when associated with
S-260. {ECO:0000269|PubMed:11854404}.
MUTAGEN 168 168 T->V: Abolishes threonine
phosphorylation; when associated with S-
260. No effect on phosphatase activity
and MAPK1 binding; when associated with
S-260. {ECO:0000269|PubMed:11854404}.
MUTAGEN 260 260 C->S: Loss of phosphatase activity.
Increases stability. Enables stable
complex formation with active MAPK1.
Abolishes threonine phosphorylation; when
associated with E-168 or V-168. No effect
on phosphatase activity and MAPK1
binding; when associated with E-168 or V-
168. {ECO:0000269|PubMed:11854404}.
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


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