ID   DUS22_XENLA             Reviewed;         209 AA.
AC   Q6GQJ8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Dual specificity protein phosphatase 22;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
GN   Name=dusp22;
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 [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Activates the Jnk signaling pathway. Dephosphorylates and
CC       deactivates p38 and stress-activated protein kinase/c-Jun N-terminal
CC       kinase (SAPK/JNK) (By similarity). {ECO:0000250}.
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   -!- 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   -!- 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
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DR   EMBL; BC072744; AAH72744.1; -; mRNA.
DR   RefSeq; NP_001085436.1; NM_001091967.1.
DR   AlphaFoldDB; Q6GQJ8; -.
DR   SMR; Q6GQJ8; -.
DR   DNASU; 443862; -.
DR   GeneID; 443862; -.
DR   KEGG; xla:443862; -.
DR   AGR; Xenbase:XB-GENE-6077590; -.
DR   CTD; 443862; -.
DR   Xenbase; XB-GENE-6077590; dusp22.S.
DR   OrthoDB; 3037246at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 443862; Expressed in heart and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14581; DUSP22; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR45948:SF3; DUAL SPECIFICITY PROTEIN PHOSPHATASE 22; 1.
DR   PANTHER; PTHR45948; DUAL SPECIFICITY PROTEIN PHOSPHATASE DDB_G0269404-RELATED; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT   CHAIN           1..209
FT                   /note="Dual specificity protein phosphatase 22"
FT                   /id="PRO_0000244754"
FT   DOMAIN          4..144
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          169..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        88
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   209 AA;  23485 MW;  E89FB752048C902E CRC64;
     MGNGMNKILT GLFLGNFKDA RDVEQLHKNN ITHILSIHDS ARPMLEGMKY LCIPASDSPS
     QNLIQHFKDS IAFIHECRLK GEGCLVHCLA GVSRSVTLVV AYVMTVTDFG WEDSLSAVRG
     ARTCANPNMG FQKQLEDFGK CEVHHFRTWL KDTYGESTFH DKDEAKQLLD KHKQQEAAES
     QNATSSGRQW NSHLTSLSSR SYSNYTTET
//