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DUS18_RAT
ID   DUS18_RAT               Reviewed;         204 AA.
AC   Q6AXW7;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18385140; DOI=10.1074/jbc.m709547200;
RA   Rardin M.J., Wiley S.E., Murphy A.N., Pagliarini D.J., Dixon J.E.;
RT   "Dual specificity phosphatases 18 and 21 target to opposing sides of the
RT   mitochondrial inner membrane.";
RL   J. Biol. Chem. 283:15440-15450(2008).
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:0000269|PubMed:18385140}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:18385140}; Intermembrane side
CC       {ECO:0000269|PubMed:18385140}. 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; BC079285; AAH79285.1; -; mRNA.
DR   RefSeq; NP_001013146.2; NM_001013128.2.
DR   AlphaFoldDB; Q6AXW7; -.
DR   SMR; Q6AXW7; -.
DR   STRING; 10116.ENSRNOP00000005516; -.
DR   PhosphoSitePlus; Q6AXW7; -.
DR   PaxDb; Q6AXW7; -.
DR   GeneID; 305477; -.
DR   KEGG; rno:305477; -.
DR   UCSC; RGD:1306929; rat.
DR   CTD; 150290; -.
DR   RGD; 1306929; Dusp18.
DR   eggNOG; KOG1718; Eukaryota.
DR   InParanoid; Q6AXW7; -.
DR   OrthoDB; 1576308at2759; -.
DR   PhylomeDB; Q6AXW7; -.
DR   PRO; PR:Q6AXW7; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:RGD.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
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; ISO:RGD.
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..204
FT                   /note="Dual specificity protein phosphatase 18"
FT                   /id="PRO_0000094831"
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"
SQ   SEQUENCE   204 AA;  22754 MW;  1A5BBC759522E442 CRC64;
     MTSPWSACPV QFPQPSISGL SQITKSLFIS NGAAANDKLL LSSNQITTVI NVSVEVANTF
     YEDIQYVQVP VVDAPIARLS DFFDPIADHI HSVEMKQGRT LLHCAAGVSR SAALCLAYLM
     KYHVMSLLDA HAWTKSRRPI IRPNSGFWEQ LIHYEFQLFG KNTMQMVNSP MGLIPDIYEK
     ETRMMIPLST PDGAFHKGKE KALL
 
 
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