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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
 
 
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