DUS18_BOVIN
ID DUS18_BOVIN Reviewed; 188 AA.
AC Q5BIP9; Q32KN1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Dual specificity protein phosphatase 18;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q8NEJ0};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q8NEJ0};
GN Name=DUSP18;
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=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Can dephosphorylate single and diphosphorylated synthetic
CC MAPK peptides, with preference for the phosphotyrosine and
CC diphosphorylated forms over phosphothreonine. In vitro,
CC dephosphorylates p-nitrophenyl phosphate (pNPP).
CC {ECO:0000250|UniProtKB:Q8NEJ0}.
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 Evidence={ECO:0000250|UniProtKB:Q8NEJ0};
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:Q8NEJ0};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8VE01}. Nucleus
CC {ECO:0000250|UniProtKB:Q8NEJ0}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q8VE01}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8VE01}; Intermembrane side
CC {ECO:0000250|UniProtKB:Q8VE01}. Note=Translocates to cytoplasm in
CC response to apoptotic stimuli such as staurosporine treatment.
CC {ECO:0000250|UniProtKB:Q8VE01}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; BT021175; AAX31357.1; -; mRNA.
DR EMBL; BC110013; AAI10014.1; -; mRNA.
DR RefSeq; NP_001029431.1; NM_001034259.1.
DR AlphaFoldDB; Q5BIP9; -.
DR SMR; Q5BIP9; -.
DR STRING; 9913.ENSBTAP00000023205; -.
DR PaxDb; Q5BIP9; -.
DR PRIDE; Q5BIP9; -.
DR GeneID; 505912; -.
DR KEGG; bta:505912; -.
DR CTD; 150290; -.
DR eggNOG; KOG1718; Eukaryota.
DR HOGENOM; CLU_027074_3_4_1; -.
DR InParanoid; Q5BIP9; -.
DR OrthoDB; 1576308at2759; -.
DR TreeFam; TF316009; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
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 Cytoplasm; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleus; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..188
FT /note="Dual specificity protein phosphatase 18"
FT /id="PRO_0000094827"
FT DOMAIN 19..160
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 95..141
FT /note="Sufficient for mitochondrial localization"
FT /evidence="ECO:0000250"
FT ACT_SITE 104
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT CONFLICT 31
FT /note="S -> R (in Ref. 2; AAI10014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 21028 MW; 3EADB96A25E1CE6B CRC64;
MTASPCAFPV QFRQPSVSGL SQITSSLYIS SGVAANNRLM LSSNRISTVI NVSVEVVNAL
YEDIHYVQVP VADTPTSRLC DFFDPIADHI HSVEMKQGRT LLHCAAGVSR SAALCLAYLM
KYHAMSLLDA HTWTKSCRPI IRPNNGFWEQ LIHYEFQLFG RNTVHMVSSP VGMIPDIYEK
EVRQMIPL
