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GSTO1_RAT
ID   GSTO1_RAT               Reviewed;         241 AA.
AC   Q9Z339;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Glutathione S-transferase omega-1;
DE            Short=GSTO-1;
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:P78417};
DE   AltName: Full=Glutathione S-transferase omega 1-1;
DE            Short=GSTO 1-1;
DE   AltName: Full=Glutathione-dependent dehydroascorbate reductase;
DE            EC=1.8.5.1 {ECO:0000250|UniProtKB:P78417};
DE   AltName: Full=Monomethylarsonic acid reductase;
DE            Short=MMA(V) reductase;
DE            EC=1.20.4.2 {ECO:0000250|UniProtKB:P78417};
DE   AltName: Full=S-(Phenacyl)glutathione reductase;
DE            Short=SPG-R;
GN   Name=Gsto1;
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 [MRNA].
RC   TISSUE=Liver;
RX   PubMed=9786866; DOI=10.1074/jbc.273.44.28708;
RA   Ishikawa T., Casini A.F., Nishikimi M.;
RT   "Molecular cloning and functional expression of rat liver glutathione-
RT   dependent dehydroascorbate reductase.";
RL   J. Biol. Chem. 273:28708-28712(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 38-43 AND 123-132, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Diao W., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
CC   -!- FUNCTION: Exhibits glutathione-dependent thiol transferase and
CC       dehydroascorbate reductase activities. Has S-(phenacyl)glutathione
CC       reductase activity. Has also glutathione S-transferase activity.
CC       Participates in the biotransformation of inorganic arsenic and reduces
CC       monomethylarsonic acid (MMA) and dimethylarsonic acid.
CC       {ECO:0000250|UniProtKB:P78417}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000250|UniProtKB:P78417};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide +
CC         L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC         Evidence={ECO:0000250|UniProtKB:P78417};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H(+) + methylarsonate = glutathione disulfide
CC         + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17826, ChEBI:CHEBI:33409,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.20.4.2;
CC         Evidence={ECO:0000250|UniProtKB:P78417};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P78417}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA34217.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB008807; BAA34217.1; ALT_FRAME; mRNA.
DR   AlphaFoldDB; Q9Z339; -.
DR   SMR; Q9Z339; -.
DR   IntAct; Q9Z339; 2.
DR   STRING; 10116.ENSRNOP00000016851; -.
DR   iPTMnet; Q9Z339; -.
DR   PhosphoSitePlus; Q9Z339; -.
DR   SwissPalm; Q9Z339; -.
DR   World-2DPAGE; 0004:Q9Z339; -.
DR   jPOST; Q9Z339; -.
DR   PaxDb; Q9Z339; -.
DR   PRIDE; Q9Z339; -.
DR   UCSC; RGD:70952; rat.
DR   RGD; 70952; Gsto1.
DR   eggNOG; KOG0406; Eukaryota.
DR   InParanoid; Q9Z339; -.
DR   PhylomeDB; Q9Z339; -.
DR   Reactome; R-RNO-156581; Methylation.
DR   Reactome; R-RNO-156590; Glutathione conjugation.
DR   Reactome; R-RNO-196836; Vitamin C (ascorbate) metabolism.
DR   PRO; PR:Q9Z339; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0005604; C:basement membrane; IDA:RGD.
DR   GO; GO:0044297; C:cell body; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0043209; C:myelin sheath; IDA:RGD.
DR   GO; GO:0031965; C:nuclear membrane; IDA:RGD.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IDA:RGD.
DR   GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR   GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR   GO; GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:RGD.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISO:RGD.
DR   GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; ISO:RGD.
DR   GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:RGD.
DR   GO; GO:0042178; P:xenobiotic catabolic process; ISS:UniProtKB.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR005442; GST_omega.
DR   InterPro; IPR045073; Omega/Tau-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   PRINTS; PR01625; GSTRNSFRASEO.
DR   SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   CHAIN           2..241
FT                   /note="Glutathione S-transferase omega-1"
FT                   /id="PRO_0000185887"
FT   DOMAIN          22..101
FT                   /note="GST N-terminal"
FT   DOMAIN          106..228
FT                   /note="GST C-terminal"
FT   ACT_SITE        32
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   BINDING         59
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   BINDING         72
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   BINDING         85..86
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   MOD_RES         57
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   MOD_RES         143
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   MOD_RES         148
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   MOD_RES         152
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
SQ   SEQUENCE   241 AA;  27669 MW;  31EAC5A7CAF22BC6 CRC64;
     MSGASARSLG KGSAPPGPVP EGQIRVYSMR FCPFAQRTLM VLKAKGIRHE IININLKNKP
     EWFFEKNPFG LVPVLENTQG HLITESVITC EYLDEAYPEK KLFPDDPYEK ACQKMTFELF
     SKVPSLVTSF IRAKRKEDHP GIKEELKKEF SKLEEAMANK RTAFFGGNSL SMIDYLIWPW
     FQRLEALELN ECIDHTPKLK LWMATMQEDP VASSHFIDAK TYRDYLSLYL QDSPEACDYG
     L
 
 
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