ID   DUS6_BOVIN              Reviewed;         381 AA.
AC   Q2KJ36;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Dual specificity protein phosphatase 6;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
GN   Name=DUSP6;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inactivates MAP kinases. Has a specificity for the ERK
CC       family. Plays an important role in alleviating chronic postoperative
CC       pain. Necessary for the normal dephosphorylation of the long-lasting
CC       phosphorylated forms of spinal MAPK1/3 and MAP kinase p38 induced by
CC       peripheral surgery, which drives the resolution of acute postoperative
CC       allodynia. Also important for dephosphorylation of MAPK1/3 in local
CC       wound tissue, which further contributes to resolution of acute pain.
CC       {ECO:0000250|UniProtKB:Q16828, ECO:0000250|UniProtKB:Q9DBB1}.
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   -!- SUBUNIT: Interacts with MAPK1/ERK2. {ECO:0000250|UniProtKB:Q16828}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16828}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
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DR   EMBL; BT025424; ABF57380.1; -; mRNA.
DR   EMBL; BC105538; AAI05539.1; -; mRNA.
DR   RefSeq; NP_001039660.1; NM_001046195.1.
DR   RefSeq; XP_010803074.1; XM_010804772.2.
DR   RefSeq; XP_015326381.1; XM_015470895.1.
DR   AlphaFoldDB; Q2KJ36; -.
DR   BMRB; Q2KJ36; -.
DR   SMR; Q2KJ36; -.
DR   STRING; 9913.ENSBTAP00000006022; -.
DR   PaxDb; 9913-ENSBTAP00000006022; -.
DR   Ensembl; ENSBTAT00000006022.5; ENSBTAP00000006022.4; ENSBTAG00000004587.5.
DR   GeneID; 515310; -.
DR   KEGG; bta:515310; -.
DR   CTD; 1848; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004587; -.
DR   VGNC; VGNC:28262; DUSP6.
DR   eggNOG; KOG1717; Eukaryota.
DR   GeneTree; ENSGT00940000158342; -.
DR   HOGENOM; CLU_027074_0_0_1; -.
DR   InParanoid; Q2KJ36; -.
DR   OMA; NDQRCIG; -.
DR   OrthoDB; 2901840at2759; -.
DR   TreeFam; TF105122; -.
DR   Reactome; R-BTA-112409; RAF-independent MAPK1/3 activation.
DR   Reactome; R-BTA-202670; ERKs are inactivated.
DR   Reactome; R-BTA-5675221; Negative regulation of MAPK pathway.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000004587; Expressed in monocyte and 108 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0033550; F:MAP kinase tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0060420; P:regulation of heart growth; IBA:GO_Central.
DR   GO; GO:0051409; P:response to nitrosative stress; IEA:Ensembl.
DR   CDD; cd01446; DSP_MapKP; 1.
DR   CDD; cd14566; DSP_MKP_classII; 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; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR10159:SF45; DUAL SPECIFICITY PROTEIN PHOSPHATASE 6; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR   PRINTS; PR01764; MAPKPHPHTASE.
DR   SMART; SM00195; DSPc; 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; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome.
FT   CHAIN           1..381
FT                   /note="Dual specificity protein phosphatase 6"
FT                   /id="PRO_0000281919"
FT   DOMAIN          30..148
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          206..349
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          176..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        293
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   381 AA;  42307 MW;  15BD1500AAA88DA8 CRC64;
     MIDTLRPVPF ASEMAISKTV AWLNEQLELG NERLLLMDCR PQELYESSHI ESAINVAIPG
     IMLRRLQKGS LPVRALFTRG EDRDRFTRRC GTDTVVLYDE SSSDWNENTG GESVLGLLLK
     KLKDEGCRAF YLEGGFSKFQ AEFALHCETN LDGSCSSSSP PLPVLGLGGL RISSDSSSDI
     ESDLDRDPNS ATDSDGSPLS NSQPSFPVEI LPFLYLGCAK DSTNLDVLEE FGIKYILNVT
     PNLPNLFENA GEFKYKQIPI SDHWSQNLSQ FFPEAISFID EARGKNCGVL VHCLAGISRS
     VTVTVAYLMQ KLNLSMNDAY DIVKMKKSNI SPNFNFMGQL LDFERTLGLS SPCDNRVPTQ
     QLYFTTPSNQ NVYQVDSLQS T
//