DUS14_BOVIN
ID DUS14_BOVIN Reviewed; 198 AA.
AC Q17QM8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Dual specificity protein phosphatase 14;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
GN Name=DUSP14;
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].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the inactivation of MAP kinases. Dephosphorylates
CC ERK, JNK and p38 MAP-kinases (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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
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 CD28. {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; BC118267; AAI18268.1; -; mRNA.
DR RefSeq; NP_001068776.1; NM_001075308.1.
DR RefSeq; XP_005220051.1; XM_005219994.3.
DR RefSeq; XP_010814059.1; XM_010815757.2.
DR AlphaFoldDB; Q17QM8; -.
DR SMR; Q17QM8; -.
DR STRING; 9913.ENSBTAP00000013570; -.
DR PaxDb; Q17QM8; -.
DR PRIDE; Q17QM8; -.
DR Ensembl; ENSBTAT00000013570; ENSBTAP00000013570; ENSBTAG00000010279.
DR GeneID; 507294; -.
DR KEGG; bta:507294; -.
DR CTD; 11072; -.
DR VEuPathDB; HostDB:ENSBTAG00000010279; -.
DR VGNC; VGNC:28252; DUSP14.
DR eggNOG; KOG1718; Eukaryota.
DR GeneTree; ENSGT00940000160675; -.
DR HOGENOM; CLU_027074_3_2_1; -.
DR InParanoid; Q17QM8; -.
DR OMA; IPDVYDR; -.
DR OrthoDB; 1576308at2759; -.
DR TreeFam; TF316009; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000010279; Expressed in surface of tongue and 103 other tissues.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
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:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020420; Atypical_DUSP_subfamB.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01910; ADSPHPHTASEB.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 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; Protein phosphatase; Reference proteome.
FT CHAIN 1..198
FT /note="Dual specificity protein phosphatase 14"
FT /id="PRO_0000283054"
FT DOMAIN 26..167
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 111
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 198 AA; 22237 MW; 1FAAADC68CF8FDBE CRC64;
MSSRGHSTLP RTLMAPRMIS EGDLGGIAQI TSSLFLGRGS VASNRHLLQA RGITCIVNAT
IEIPNFNWPQ FEYVKVPLAD MPHAPIGLYF DTVADKIHSV SRKHGATLVH CAAGVSRSAT
LCIAYLMKFH NVCLLEAYNW VKARRPVIRP NVGFWRQLID YERQLFGKST VKMVQTPYGI
VPDVYEKESR HLLPYWGI