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   27-MAR-2024, entry version 109.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ320159; CAC44127.1; -; mRNA.
DR   RefSeq; NP_001082153.1; NM_001088684.1.
DR   AlphaFoldDB; Q90W58; -.
DR   SMR; Q90W58; -.
DR   DNASU; 398254; -.
DR   AGR; Xenbase:XB-GENE-17344125; -.
DR   Xenbase; XB-GENE-17344125; dusp1.S.
DR   OMA; MCTKPSS; -.
DR   OrthoDB; 2901840at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 398254; Expressed in lung and 19 other cell types or 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   CDD; cd14638; DSP_DUSP1; 1.
DR   CDD; cd01446; DSP_MapKP; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 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   PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR10159:SF309; DUAL SPECIFICITY PROTEIN PHOSPHATASE 1; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
DR   PRINTS; PR01764; MAPKPHPHTASE.
DR   SMART; SM00195; DSPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 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
//