ID   GSTM5_HUMAN             Reviewed;         218 AA.
AC   P46439; A8K0V8; Q6PD78;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Glutathione S-transferase Mu 5;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-mu 5;
DE   AltName: Full=GSTM5-5;
GN   Name=GSTM5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=8473333; DOI=10.1016/s0021-9258(18)52957-4;
RA   Takahashi Y., Campbell E.A., Hirata Y., Takayama T., Listowsky I.;
RT   "A basis for differentiating among the multiple human Mu-glutathione S-
RT   transferases and molecular cloning of brain GSTM5.";
RL   J. Biol. Chem. 268:8893-8898(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-67.
RC   TISSUE=Amygdala;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-67.
RC   TISSUE=PNS;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
RX   PubMed=10587441; DOI=10.1021/bi991714t;
RA   Patskovsky Y.V., Patskovska L.N., Listowsky I.;
RT   "An asparagine-phenylalanine substitution accounts for catalytic
RT   differences between hGSTM3-3 and other human class mu glutathione S-
RT   transferases.";
RL   Biochemistry 38:16187-16194(1999).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC       {ECO:0000269|PubMed:10587441}.
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:0000269|PubMed:10587441};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10587441}.
CC   -!- INTERACTION:
CC       P46439; Q9Y2J4: AMOTL2; NbExp=4; IntAct=EBI-4312072, EBI-746752;
CC       P46439; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-4312072, EBI-10187270;
CC       P46439; Q92917: GPKOW; NbExp=3; IntAct=EBI-4312072, EBI-746309;
CC       P46439; P28161: GSTM2; NbExp=6; IntAct=EBI-4312072, EBI-9023362;
CC       P46439; P21266: GSTM3; NbExp=12; IntAct=EBI-4312072, EBI-350350;
CC       P46439; Q6FGJ9: GSTM3; NbExp=3; IntAct=EBI-4312072, EBI-10209603;
CC       P46439; Q03013: GSTM4; NbExp=3; IntAct=EBI-4312072, EBI-713363;
CC       P46439; P46439: GSTM5; NbExp=8; IntAct=EBI-4312072, EBI-4312072;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR   EMBL; L02321; AAA20040.1; -; mRNA.
DR   EMBL; AK289673; BAF82362.1; -; mRNA.
DR   EMBL; BC058881; AAH58881.1; -; mRNA.
DR   CCDS; CCDS811.1; -.
DR   PIR; A46048; A46048.
DR   RefSeq; NP_000842.2; NM_000851.3.
DR   RefSeq; XP_005270841.1; XM_005270784.4.
DR   AlphaFoldDB; P46439; -.
DR   SMR; P46439; -.
DR   BioGRID; 109204; 16.
DR   IntAct; P46439; 10.
DR   STRING; 9606.ENSP00000256593; -.
DR   ChEMBL; CHEMBL2819; -.
DR   DrugBank; DB00321; Amitriptyline.
DR   DrugBank; DB00291; Chlorambucil.
DR   DrugBank; DB03619; Deoxycholic acid.
DR   DrugBank; DB00143; Glutathione.
DR   DrugBank; DB03310; Glutathione disulfide.
DR   iPTMnet; P46439; -.
DR   PhosphoSitePlus; P46439; -.
DR   BioMuta; GSTM5; -.
DR   DMDM; 67476963; -.
DR   jPOST; P46439; -.
DR   MassIVE; P46439; -.
DR   PaxDb; 9606-ENSP00000256593; -.
DR   PeptideAtlas; P46439; -.
DR   ProteomicsDB; 55739; -.
DR   Antibodypedia; 20076; 215 antibodies from 30 providers.
DR   DNASU; 2949; -.
DR   Ensembl; ENST00000256593.8; ENSP00000256593.3; ENSG00000134201.12.
DR   GeneID; 2949; -.
DR   KEGG; hsa:2949; -.
DR   MANE-Select; ENST00000256593.8; ENSP00000256593.3; NM_000851.4; NP_000842.2.
DR   AGR; HGNC:4637; -.
DR   CTD; 2949; -.
DR   DisGeNET; 2949; -.
DR   GeneCards; GSTM5; -.
DR   HGNC; HGNC:4637; GSTM5.
DR   HPA; ENSG00000134201; Tissue enriched (breast).
DR   MIM; 138385; gene.
DR   neXtProt; NX_P46439; -.
DR   OpenTargets; ENSG00000134201; -.
DR   PharmGKB; PA29027; -.
DR   VEuPathDB; HostDB:ENSG00000134201; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000155416; -.
DR   HOGENOM; CLU_039475_2_0_1; -.
DR   InParanoid; P46439; -.
DR   OMA; KANCATI; -.
DR   OrthoDB; 5488107at2759; -.
DR   PhylomeDB; P46439; -.
DR   TreeFam; TF353040; -.
DR   BRENDA; 2.5.1.18; 2681.
DR   PathwayCommons; P46439; -.
DR   Reactome; R-HSA-156590; Glutathione conjugation.
DR   SABIO-RK; P46439; -.
DR   SignaLink; P46439; -.
DR   BioGRID-ORCS; 2949; 6 hits in 1143 CRISPR screens.
DR   GenomeRNAi; 2949; -.
DR   Pharos; P46439; Tbio.
DR   PRO; PR:P46439; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P46439; Protein.
DR   Bgee; ENSG00000134201; Expressed in left ovary and 136 other cell types or tissues.
DR   ExpressionAtlas; P46439; baseline and differential.
DR   Genevisible; P46439; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
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; 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   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; SFLDS00019; Glutathione_Transferase_(cytos; 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   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..218
FT                   /note="Glutathione S-transferase Mu 5"
FT                   /id="PRO_0000185825"
FT   DOMAIN          2..88
FT                   /note="GST N-terminal"
FT   DOMAIN          90..207
FT                   /note="GST C-terminal"
FT   BINDING         7..8
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         46..50
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         59..60
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         72..73
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   VARIANT         67
FT                   /note="A -> T (in dbSNP:rs17854972)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_065098"
FT   VARIANT         179
FT                   /note="L -> P (in dbSNP:rs2227963)"
FT                   /id="VAR_049491"
FT   CONFLICT        35
FT                   /note="L -> M (in Ref. 1; AAA20040)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   218 AA;  25675 MW;  62B03FCD960FB4AB CRC64;
     MPMTLGYWDI RGLAHAIRLL LEYTDSSYVE KKYTLGDAPD YDRSQWLNEK FKLGLDFPNL
     PYLIDGAHKI TQSNAILRYI ARKHNLCGET EEEKIRVDIL ENQVMDNHME LVRLCYDPDF
     EKLKPKYLEE LPEKLKLYSE FLGKRPWFAG DKITFVDFLA YDVLDMKRIF EPKCLDAFLN
     LKDFISRFEG LKKISAYMKS SQFLRGLLFG KSATWNSK
//

ID   Q5T8R2_HUMAN            Unreviewed;       218 AA.
AC   Q5T8R2;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 159.
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:EAW56408.1};
GN   ORFNames=hCG_40245 {ECO:0000313|EMBL:EAW56408.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG37677.1};
RN   [1] {ECO:0000313|EMBL:EAW56408.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA   Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA   Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA   Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA   McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA   Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA   Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA   Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA   Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA   Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA   Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA   Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA   Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA   Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA   Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA   Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA   Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA   Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA   Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA   Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA   Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA   Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA   McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA   Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA   Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA   Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA   Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA   Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA   Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA   Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA   Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA   Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA   Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA   Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA   Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA   Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA   Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:EAW56408.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:BAG37677.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:BAG37677.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y.,
RA   Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R.,
RA   Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N.,
RA   Isogai T.;
RT   "NEDO functional analysis of protein and research application project.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ADO22159.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Hoernsten L., Su C., Osbourn A.E., Hellman U., Wernstedt C., Oliw E.H.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
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; GQ891297; ADO22159.1; -; mRNA.
DR   EMBL; AK315260; BAG37677.1; -; mRNA.
DR   EMBL; CH471122; EAW56408.1; -; Genomic_DNA.
DR   RefSeq; NP_000842.2; NM_000851.3.
DR   RefSeq; XP_005270841.1; XM_005270784.4.
DR   AlphaFoldDB; Q5T8R2; -.
DR   SMR; Q5T8R2; -.
DR   Antibodypedia; 20076; 215 antibodies from 30 providers.
DR   DNASU; 2949; -.
DR   GeneID; 2949; -.
DR   KEGG; hsa:2949; -.
DR   UCSC; uc001dyn.4; human.
DR   CTD; 2949; -.
DR   PharmGKB; PA29027; -.
DR   VEuPathDB; HostDB:ENSG00000134201; -.
DR   HOGENOM; CLU_039475_2_0_1; -.
DR   OMA; KANCATI; -.
DR   OrthoDB; 5488107at2759; -.
DR   BioGRID-ORCS; 2949; 6 hits in 1143 CRISPR screens.
DR   GenomeRNAi; 2949; -.
DR   ExpressionAtlas; Q5T8R2; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IEA:UniProt.
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; 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   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; SFLDS00019; Glutathione_Transferase_(cytos; 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   Transferase {ECO:0000256|RuleBase:RU003494, ECO:0000313|EMBL:BAG37677.1}.
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;  25675 MW;  62B03FCD960FB4AB CRC64;
     MPMTLGYWDI RGLAHAIRLL LEYTDSSYVE KKYTLGDAPD YDRSQWLNEK FKLGLDFPNL
     PYLIDGAHKI TQSNAILRYI ARKHNLCGET EEEKIRVDIL ENQVMDNHME LVRLCYDPDF
     EKLKPKYLEE LPEKLKLYSE FLGKRPWFAG DKITFVDFLA YDVLDMKRIF EPKCLDAFLN
     LKDFISRFEG LKKISAYMKS SQFLRGLLFG KSATWNSK
//