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-APR-2013, entry version 89.
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 MASS
RP 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 IPI; IPI00208636; -.
DR RefSeq; NP_742035.1; NM_172038.1.
DR RefSeq; XP_003749426.1; XM_003749378.1.
DR UniGene; Rn.9158; -.
DR HSSP; P21266; 3GTU.
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; MSCESSM; -.
DR OrthoDB; EOG47D9H2; -.
DR NextBio; 613032; -.
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; IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
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; GST_C_like; 1.
DR SUPFAM; SSF52833; Thiordxn-like_fd; 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 INIT_MET 1 1 Removed.
FT CHAIN 2 225 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
//
