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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   14-MAY-2014, entry version 97.
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;
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in testis and brain. Very low
CC       expression in liver, kidney, heart and lung.
CC   -!- PTM: The N-terminus is blocked (Probable).
CC   -!- SIMILARITY: Belongs to the GST superfamily. Mu family.
CC   -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC   -!- SIMILARITY: Contains 1 GST N-terminal domain.
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DR   EMBL; U86635; AAD00603.1; -; mRNA.
DR   RefSeq; NP_742035.1; NM_172038.1.
DR   RefSeq; XP_003749426.1; XM_003749378.2.
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-SubCell.
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 (By similarity).
FT   REGION       50     54       Glutathione binding (By similarity).
FT   REGION       63     64       Glutathione binding (By similarity).
FT   REGION       76     77       Glutathione binding (By similarity).
FT   BINDING     120    120       Substrate (By similarity).
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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