DUS1B_XENLA
ID DUS1B_XENLA Reviewed; 369 AA.
AC Q90W58;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Dual specificity protein phosphatase 1-B {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q91790};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q91790};
DE AltName: Full=XCL100-beta {ECO:0000303|PubMed:11854404};
GN Name=dusp1-b {ECO:0000250|UniProtKB:Q91790};
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] {ECO:0000312|EMBL:CAC44127.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary {ECO:0000312|EMBL:CAC44127.1};
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:0000250|UniProtKB:Q91790}.
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:Q91790};
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:Q91790};
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:Q91790, ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91790}.
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 (By similarity). {ECO:0000250|UniProtKB:Q91790}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000255}.
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DR EMBL; AJ320159; CAC44127.1; -; mRNA.
DR RefSeq; NP_001082153.1; NM_001088684.1.
DR AlphaFoldDB; Q90W58; -.
DR SMR; Q90W58; -.
DR DNASU; 398254; -.
DR GeneID; 398254; -.
DR CTD; 398254; -.
DR Xenbase; XB-GENE-17344125; dusp1.S.
DR OMA; NIHCPPI; -.
DR OrthoDB; 1576308at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 398254; Expressed in lung and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; ISS: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; ISS:UniProtKB.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
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; 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; 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 2: Evidence at transcript level;
KW Hydrolase; Meiosis; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..369
FT /note="Dual specificity protein phosphatase 1-B"
FT /id="PRO_0000421474"
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:0000250|UniProtKB:Q91790"
SQ SEQUENCE 369 AA; 40363 MW; 5E280CA6EF633CC6 CRC64;
MVNMEICAMD CCVFKGLLAE RAHKCLILDC RSFFAFSSSS IIGSSNVRLS TIVKRRAKGS
MGLEHIIPNE EQRGRLVAGM YEAVVLLDER TSELDMLRKD STMMLAVNAL SRDPRGSRIY
FLKGGYETFS SQCPEFCNKN SPPVALSLPL SPNNVPGSAD SNCTPCGTPL YDQGGPVEIL
PFLYLGSAYH ASRKDMLEAL GITALINVSA NCPNHFEGHF QYKSIPVEDS HKADISSWFN
EAIDFIDSIK TCGGRVFVHC QAGISRSATI CLAYLMRTNR VKLDEAFEFV KQRRSIISPN
FSFMGQLLQF ESQVLAPSCS AEAGSPTISV LDRGTSTTTV FNFPVSIPVH SGANSLSYLQ
NPITTSPSC
