GSTM5_RAT
ID GSTM5_RAT Reviewed; 225 AA.
AC Q9Z1B2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Glutathione S-transferase Mu 5;
DE EC=2.5.1.18;
DE AltName: Full=GST class-mu 5;
GN Name=Gstm5;
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], PROTEIN SEQUENCE OF 6-27; 36-50; 57-71; 74-87;
RP 89-120; 157-177; 179-186; 198-215 AND 219-224, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND KINETIC PARAMETERS.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=9545290; DOI=10.1074/jbc.273.16.9593;
RA Rowe J.D., Patskovsky Y.V., Patskovska L.N., Novikova E., Listowsky I.;
RT "Rationale for reclassification of a distinctive subdivision of mammalian
RT class Mu glutathione S-transferases that are primarily expressed in
RT testis.";
RL J. Biol. Chem. 273:9593-9601(1998).
RN [2]
RP PROTEIN SEQUENCE OF 157-172, INITIATOR METHIONINE, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for glutathione {ECO:0000269|PubMed:9545290};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9545290}.
CC -!- TISSUE SPECIFICITY: Expressed in testis and brain. Very low expression
CC in liver, kidney, heart and lung. {ECO:0000269|PubMed:9545290}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; U86635; AAD00603.1; -; mRNA.
DR RefSeq; NP_742035.1; NM_172038.1.
DR RefSeq; XP_017446822.1; XM_017591333.1.
DR RefSeq; XP_017452258.1; XM_017596769.1.
DR AlphaFoldDB; Q9Z1B2; -.
DR SMR; Q9Z1B2; -.
DR BioGRID; 249037; 1.
DR STRING; 10116.ENSRNOP00000064813; -.
DR iPTMnet; Q9Z1B2; -.
DR PhosphoSitePlus; Q9Z1B2; -.
DR SwissPalm; Q9Z1B2; -.
DR World-2DPAGE; 0004:Q9Z1B2; -.
DR jPOST; Q9Z1B2; -.
DR PaxDb; Q9Z1B2; -.
DR PRIDE; Q9Z1B2; -.
DR Ensembl; ENSRNOT00000072342; ENSRNOP00000065389; ENSRNOG00000049743.
DR GeneID; 64352; -.
DR KEGG; rno:64352; -.
DR UCSC; RGD:61964; rat.
DR CTD; 2949; -.
DR RGD; 61964; Gstm5.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000157663; -.
DR HOGENOM; CLU_039475_2_0_1; -.
DR InParanoid; Q9Z1B2; -.
DR OMA; DIMENQV; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; Q9Z1B2; -.
DR TreeFam; TF353040; -.
DR Reactome; R-RNO-156590; Glutathione conjugation.
DR SABIO-RK; Q9Z1B2; -.
DR PRO; PR:Q9Z1B2; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000049743; Expressed in testis and 19 other tissues.
DR Genevisible; Q9Z1B2; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0035686; C:sperm fibrous sheath; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0043295; F:glutathione binding; ISO:RGD.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0070458; P:cellular detoxification of nitrogen compound; ISO:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR GO; GO:0018916; P:nitrobenzene metabolic process; ISO:RGD.
DR GO; GO:0043627; P:response to estrogen; ISO:RGD.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO:RGD.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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 Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..225
FT /note="Glutathione S-transferase Mu 5"
FT /id="PRO_0000271421"
FT DOMAIN 5..92
FT /note="GST N-terminal"
FT DOMAIN 94..212
FT /note="GST C-terminal"
FT BINDING 11..12
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 50..54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 63..64
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 76..77
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 225 AA; 26629 MW; 45A2DC2DDCE5ACA4 CRC64;
MSCSKSMVLG YWDIRGLAHA IRMLLEFTDT SYEEKQYTCG EAPDYDRSQW LDVKFKLDLD
FPNLPYLMDG KNKITQSNAI LRYIARKHNM CGDTEEEKIR VDIMENQIMD FRMQLVRLCY
NSNHESLKPQ YLEQLPAQLK QFSLFLGKFT WFAGEKLTFV DFLTYDVLDQ NRMFEPKCLD
EFPNLKAFMC RFEALEKIAA FLQSDRCFKM PINNKMAKWG NKSIC
