ID Q4R5L3_MACFA Unreviewed; 218 AA.
AC Q4R5L3;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 103.
DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU003494};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU003494};
GN Name=GSTM5 {ECO:0000313|EMBL:ABO21634.1,
GN ECO:0000313|Ensembl:ENSMFAP00000030336.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|EMBL:BAE01612.1};
RN [1] {ECO:0000313|EMBL:BAE01612.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15944441; DOI=10.1093/molbev/msi187;
RA Osada N., Hirata M., Tanuma R., Kusuda J., Hida M., Suzuki Y., Sugano S.,
RA Gojobori T., Shen C.K., Wu C.I., Hashimoto K.;
RT "Substitution rate and structural divergence of 5'UTR evolution:
RT comparative analysis between human and cynomolgus monkey cDNAs.";
RL Mol. Biol. Evol. 22:1976-1982(2005).
RN [2] {ECO:0000313|EMBL:BAE01612.1}
RP NUCLEOTIDE SEQUENCE.
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:BAE73099.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain temporal lobe {ECO:0000313|EMBL:BAE73099.1};
RA Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA Hashimoto K.;
RT "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA
RT oligo-chips.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ABO21634.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19088266; DOI=10.1124/dmd.108.023747;
RA Uno Y., Ohuchi T., Uehara S., Kito G., Kamataki T., Nagata R.;
RT "Sex-related differences in the expression of mfGSTA2, a novel GST
RT identified in cynomolgus monkey (Macaca fascicularis).";
RL Drug Metab. Dispos. 37:453-456(2009).
RN [5] {ECO:0000313|Ensembl:ENSMFAP00000030336.1, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|Ensembl:ENSMFAP00000030336.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|RuleBase:RU003494};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family.
CC {ECO:0000256|ARBA:ARBA00005861, ECO:0000256|RuleBase:RU003494}.
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DR EMBL; EF104257; ABO21634.1; -; mRNA.
DR EMBL; AB169530; BAE01612.1; -; mRNA.
DR EMBL; AB220566; BAE73099.1; -; mRNA.
DR RefSeq; NP_001272186.1; NM_001285257.1.
DR STRING; 9541.ENSMFAP00000030336; -.
DR Ensembl; ENSMFAT00000004541.2; ENSMFAP00000030336.1; ENSMFAG00000038873.2.
DR VEuPathDB; HostDB:ENSMFAG00000042340; -.
DR GeneTree; ENSGT00940000155416; -.
DR OrthoDB; 5488107at2759; -.
DR Proteomes; UP000233100; Chromosome 1.
DR Bgee; ENSMFAG00000038873; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:UniProt.
DR CDD; cd03209; GST_C_Mu; 1.
DR CDD; cd03075; GST_N_Mu; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
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; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF249; GLUTATHIONE S-TRANSFERASE MU 5; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
DR SFLD; SFLDG01205; AMPS.1; 1.
DR SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Transferase {ECO:0000256|RuleBase:RU003494, ECO:0000313|EMBL:BAE01612.1}.
FT DOMAIN 1..88
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 90..207
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 218 AA; 25767 MW; B5A148D85E771BF6 CRC64;
MPMILGYWDI RGLAHAIRLL LEYTDSNYEE KKYRMGHAPD YDRSQWLNEK FKLGLDFPNL
PYLIDGTHKI TQSNAILRYI ARKHNLCGET EEEKILVDIL ENQLMDSRME MVRLCFDPNF
EKLKPKYLEE LPEKLKLYSQ FLGKRPWFTG DKITFVDFLA YDVLDMRRIV EPGCLDAFPN
LKDFISRFEG LKKISAYMKS SRFHRGLLFG TTATWNST
//