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Database: UniProt/SWISS-PROT
Entry: GSTM5_RAT
LinkDB: GSTM5_RAT
Original site: 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   29-OCT-2014, entry version 99.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 6-27; 36-50; 57-71;
RP   74-87; 89-120; 157-177; 179-186; 198-215 AND 219-224, TISSUE
RP   SPECIFICITY, 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.,
RA   Listowsky I.;
RT   "Rationale for reclassification of a distinctive subdivision of
RT   mammalian class Mu glutathione S-transferases that are primarily
RT   expressed in testis.";
RL   J. Biol. Chem. 273:9593-9601(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 157-172, INITIATOR METHIONINE, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (NOV-2006) to UniProtKB.
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC   -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
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
CC       expression in liver, kidney, heart and lung.
CC       {ECO:0000269|PubMed:9545290}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Mu family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 GST C-terminal domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 GST N-terminal domain. {ECO:0000305}.
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DR   EMBL; U86635; AAD00603.1; -; mRNA.
DR   RefSeq; NP_742035.1; NM_172038.1.
DR   RefSeq; XP_003749426.1; XM_003749378.3.
DR   UniGene; Rn.9158; -.
DR   ProteinModelPortal; Q9Z1B2; -.
DR   SMR; Q9Z1B2; 2-225.
DR   STRING; 10116.ENSRNOP00000025589; -.
DR   World-2DPAGE; 0004:Q9Z1B2; -.
DR   PaxDb; Q9Z1B2; -.
DR   PRIDE; Q9Z1B2; -.
DR   Ensembl; ENSRNOT00000072342; ENSRNOP00000065389; ENSRNOG00000049743.
DR   Ensembl; ENSRNOT00000073649; ENSRNOP00000064813; ENSRNOG00000047034.
DR   GeneID; 100912430; -.
DR   GeneID; 64352; -.
DR   KEGG; rno:100912430; -.
DR   KEGG; rno:64352; -.
DR   UCSC; RGD:61964; rat.
DR   CTD; 2949; -.
DR   RGD; 61964; Gstm5.
DR   eggNOG; NOG300089; -.
DR   GeneTree; ENSGT00550000074559; -.
DR   HOGENOM; HOG000115735; -.
DR   HOVERGEN; HBG106842; -.
DR   InParanoid; Q9Z1B2; -.
DR   KO; K00799; -.
DR   OMA; CYNSDHE; -.
DR   OrthoDB; EOG7KH9M3; -.
DR   PhylomeDB; Q9Z1B2; -.
DR   TreeFam; TF353040; -.
DR   NextBio; 613032; -.
DR   PRO; PR:Q9Z1B2; -.
DR   Genevestigator; Q9Z1B2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
DR   GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR003081; GST_mu.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01267; GSTRNSFRASEM.
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   Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Reference proteome; Transferase.
FT   CHAIN         1    225       Glutathione S-transferase Mu 5.
FT                                /FTId=PRO_0000271421.
FT   DOMAIN        5     92       GST N-terminal.
FT   DOMAIN       94    212       GST C-terminal.
FT   REGION       11     12       Glutathione binding. {ECO:0000250}.
FT   REGION       50     54       Glutathione binding. {ECO:0000250}.
FT   REGION       63     64       Glutathione binding. {ECO:0000250}.
FT   REGION       76     77       Glutathione binding. {ECO:0000250}.
FT   BINDING     120    120       Substrate. {ECO:0000250}.
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
//
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