ID MGST3_HUMAN Reviewed; 152 AA.
AC O14880; B2R592; Q6ICN4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 194.
DE RecName: Full=Glutathione S-transferase 3, mitochondrial {ECO:0000305|PubMed:9278457};
DE Short=GST-3;
DE EC=2.5.1.- {ECO:0000269|PubMed:36370807};
DE AltName: Full=Glutathione peroxidase MGST3 {ECO:0000305|PubMed:9278457};
DE EC=1.11.1.- {ECO:0000269|PubMed:9278457};
DE AltName: Full=LTC4 synthase MGST3 {ECO:0000305|PubMed:9278457};
DE EC=4.4.1.20 {ECO:0000269|PubMed:9278457};
GN Name=MGST3 {ECO:0000312|HGNC:HGNC:7064};
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], CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, PATHWAY, AND CAUTION.
RX PubMed=9278457; DOI=10.1074/jbc.272.36.22934;
RA Jakobsson P.-J., Mancini J.A., Riendeau D., Ford-Hutchinson A.W.;
RT "Identification and characterization of a novel microsomal enzyme with
RT glutathione-dependent transferase and peroxidase activities.";
RL J. Biol. Chem. 272:22934-22939(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Lung;
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP MUTAGENESIS OF CYS-150 AND CYS-151, AND PALMITOYLATION AT CYS-150 AND
RP CYS-151.
RX PubMed=21044946; DOI=10.1194/jlr.d011106;
RA Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,
RA Stamler J.S., Casey P.J.;
RT "Site-specific analysis of protein S-acylation by resin-assisted capture.";
RL J. Lipid Res. 52:393-398(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND CAUTION.
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND CAUTION.
RX PubMed=27184847; DOI=10.1016/j.celrep.2016.04.064;
RA Lee S.Y., Kang M.G., Park J.S., Lee G., Ting A.Y., Rhee H.W.;
RT "APEX Fingerprinting Reveals the Subcellular Localization of Proteins of
RT Interest.";
RL Cell Rep. 15:1837-1847(2016).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=36370807; DOI=10.1016/j.jlr.2022.100310;
RA Steinmetz-Spaeh J., Liu J., Singh R., Ekoff M., Boddul S., Tang X.,
RA Bergqvist F., Idborg H., Heitel P., Roennberg E., Merk D., Wermeling F.,
RA Haeggstroem J.Z., Nilsson G., Steinhilber D., Larsson K., Korotkova M.,
RA Jakobsson P.J.;
RT "Biosynthesis of prostaglandin 15dPGJ2 -glutathione and 15dPGJ2-cysteine
RT conjugates in macrophages and mast cells via MGST3.";
RL J. Lipid Res. 63:100310-100310(2022).
CC -!- FUNCTION: Displays both glutathione S-transferase and glutathione
CC peroxidase activities toward oxyeicosanoids, as part of cellular
CC detoxification as well as synthesis of bioactive metabolites
CC (PubMed:9278457, PubMed:36370807). Catalyzes conjugate addition of
CC reduced glutathione to the alpha, beta-unsaturated C=C carbonyl group
CC of eisosanoids such as leukotriene A4 and 15-deoxy-Delta12,14-
CC prostaglandin J2 to form GSH adducts relevant to the inflammatory
CC response (PubMed:9278457, PubMed:36370807). Catalyzes glutathione-
CC dependent reduction of eicosanoid peroxides to yield the corresponding
CC eicosanoid hydroxides (PubMed:9278457). {ECO:0000269|PubMed:36370807,
CC ECO:0000269|PubMed:9278457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=leukotriene C4 = glutathione + leukotriene A4;
CC Xref=Rhea:RHEA:17617, ChEBI:CHEBI:57463, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:57973; EC=4.4.1.20;
CC Evidence={ECO:0000269|PubMed:9278457};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17619;
CC Evidence={ECO:0000305|PubMed:9278457};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15-deoxy-Delta(12,14)-prostaglandin J2 + glutathione = 15-
CC deoxy-Delta(12,14)-prostaglandin J2-S-(R)-glutathione;
CC Xref=Rhea:RHEA:75963, ChEBI:CHEBI:57925, ChEBI:CHEBI:85236,
CC ChEBI:CHEBI:194498; Evidence={ECO:0000269|PubMed:36370807};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75964;
CC Evidence={ECO:0000305|PubMed:36370807};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2
CC glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate +
CC glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC ChEBI:CHEBI:90632; Evidence={ECO:0000269|PubMed:9278457};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48621;
CC Evidence={ECO:0000305|PubMed:9278457};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate
CC {ECO:0000269|PubMed:9278457};
CC KM=9.2 uM for 15-deoxy-Delta12,14-prostaglandin J2
CC {ECO:0000269|PubMed:36370807};
CC -!- PATHWAY: Lipid metabolism; leukotriene C4 biosynthesis.
CC {ECO:0000305|PubMed:9278457}.
CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC {ECO:0000305|PubMed:9278457}.
CC -!- INTERACTION:
CC O14880; Q9NRZ5: AGPAT4; NbExp=3; IntAct=EBI-724754, EBI-1754287;
CC O14880; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-724754, EBI-11522760;
CC O14880; P05090: APOD; NbExp=3; IntAct=EBI-724754, EBI-715495;
CC O14880; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-724754, EBI-4290634;
CC O14880; P29972: AQP1; NbExp=3; IntAct=EBI-724754, EBI-745213;
CC O14880; Q96PS8: AQP10; NbExp=3; IntAct=EBI-724754, EBI-12820279;
CC O14880; Q92482: AQP3; NbExp=3; IntAct=EBI-724754, EBI-2808854;
CC O14880; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-724754, EBI-714543;
CC O14880; Q8N6S5: ARL6IP6; NbExp=3; IntAct=EBI-724754, EBI-2808844;
CC O14880; O15155: BET1; NbExp=3; IntAct=EBI-724754, EBI-749204;
CC O14880; O95393: BMP10; NbExp=3; IntAct=EBI-724754, EBI-3922513;
CC O14880; Q96F05: C11orf24; NbExp=3; IntAct=EBI-724754, EBI-2836238;
CC O14880; Q06432: CACNG1; NbExp=3; IntAct=EBI-724754, EBI-9686780;
CC O14880; P24863: CCNC; NbExp=3; IntAct=EBI-724754, EBI-395261;
CC O14880; O14735: CDIPT; NbExp=3; IntAct=EBI-724754, EBI-358858;
CC O14880; P58418: CLRN1; NbExp=3; IntAct=EBI-724754, EBI-17274839;
CC O14880; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-724754, EBI-11522780;
CC O14880; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-724754, EBI-6942903;
CC O14880; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-724754, EBI-2680384;
CC O14880; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-724754, EBI-711490;
CC O14880; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-724754, EBI-12142299;
CC O14880; Q9BWH2: FUNDC2; NbExp=3; IntAct=EBI-724754, EBI-714482;
CC O14880; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-724754, EBI-713304;
CC O14880; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-724754, EBI-11991950;
CC O14880; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-724754, EBI-6166686;
CC O14880; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-724754, EBI-13345167;
CC O14880; Q8TED1: GPX8; NbExp=3; IntAct=EBI-724754, EBI-11721746;
CC O14880; Q14416: GRM2; NbExp=3; IntAct=EBI-724754, EBI-10232876;
CC O14880; P30519: HMOX2; NbExp=3; IntAct=EBI-724754, EBI-712096;
CC O14880; P11215: ITGAM; NbExp=3; IntAct=EBI-724754, EBI-2568251;
CC O14880; Q68G75: LEMD1; NbExp=3; IntAct=EBI-724754, EBI-12268900;
CC O14880; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-724754, EBI-12033434;
CC O14880; Q7Z4F1: LRP10; NbExp=3; IntAct=EBI-724754, EBI-2830349;
CC O14880; O14880: MGST3; NbExp=3; IntAct=EBI-724754, EBI-724754;
CC O14880; P30301: MIP; NbExp=3; IntAct=EBI-724754, EBI-8449636;
CC O14880; Q6IN84: MRM1; NbExp=3; IntAct=EBI-724754, EBI-5454865;
CC O14880; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-724754, EBI-3923617;
CC O14880; Q99519: NEU1; NbExp=3; IntAct=EBI-724754, EBI-721517;
CC O14880; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-724754, EBI-10317425;
CC O14880; Q16617: NKG7; NbExp=3; IntAct=EBI-724754, EBI-3919611;
CC O14880; Q8N912: NRAC; NbExp=3; IntAct=EBI-724754, EBI-12051377;
CC O14880; Q8IXM6: NRM; NbExp=3; IntAct=EBI-724754, EBI-10262547;
CC O14880; P42857: NSG1; NbExp=3; IntAct=EBI-724754, EBI-6380741;
CC O14880; O75459: PAGE1; NbExp=3; IntAct=EBI-724754, EBI-2559100;
CC O14880; P26678: PLN; NbExp=3; IntAct=EBI-724754, EBI-692836;
CC O14880; P60201-2: PLP1; NbExp=3; IntAct=EBI-724754, EBI-12188331;
CC O14880; Q04941: PLP2; NbExp=3; IntAct=EBI-724754, EBI-608347;
CC O14880; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-724754, EBI-10485931;
CC O14880; Q59EV6: PPGB; NbExp=3; IntAct=EBI-724754, EBI-14210385;
CC O14880; O00767: SCD; NbExp=3; IntAct=EBI-724754, EBI-2684237;
CC O14880; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-724754, EBI-17247926;
CC O14880; O75396: SEC22B; NbExp=3; IntAct=EBI-724754, EBI-1058865;
CC O14880; P43003: SLC1A3; NbExp=3; IntAct=EBI-724754, EBI-359038;
CC O14880; P22732: SLC2A5; NbExp=3; IntAct=EBI-724754, EBI-2825135;
CC O14880; P78382: SLC35A1; NbExp=3; IntAct=EBI-724754, EBI-12870360;
CC O14880; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-724754, EBI-2823239;
CC O14880; P30825: SLC7A1; NbExp=3; IntAct=EBI-724754, EBI-4289564;
CC O14880; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-724754, EBI-8640191;
CC O14880; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-724754, EBI-10244848;
CC O14880; Q6UX34: SNORC; NbExp=3; IntAct=EBI-724754, EBI-11957067;
CC O14880; Q13277: STX3; NbExp=3; IntAct=EBI-724754, EBI-1394295;
CC O14880; O15400: STX7; NbExp=3; IntAct=EBI-724754, EBI-3221827;
CC O14880; Q9UNK0: STX8; NbExp=3; IntAct=EBI-724754, EBI-727240;
CC O14880; Q8N2H4: SYS1; NbExp=3; IntAct=EBI-724754, EBI-13075176;
CC O14880; Q00059: TFAM; NbExp=4; IntAct=EBI-724754, EBI-1049924;
CC O14880; P02786: TFRC; NbExp=3; IntAct=EBI-724754, EBI-355727;
CC O14880; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-724754, EBI-12845616;
CC O14880; Q9BVC6: TMEM109; NbExp=3; IntAct=EBI-724754, EBI-1057733;
CC O14880; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-724754, EBI-10171534;
CC O14880; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-724754, EBI-2844246;
CC O14880; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-724754, EBI-12195227;
CC O14880; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-724754, EBI-2852148;
CC O14880; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-724754, EBI-2548832;
CC O14880; Q9Y320: TMX2; NbExp=3; IntAct=EBI-724754, EBI-6447886;
CC O14880; O95859: TSPAN12; NbExp=3; IntAct=EBI-724754, EBI-2466403;
CC O14880; O60636: TSPAN2; NbExp=3; IntAct=EBI-724754, EBI-3914288;
CC O14880; Q86UF1: TSPAN33; NbExp=3; IntAct=EBI-724754, EBI-12045841;
CC O14880; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-724754, EBI-10243654;
CC O14880; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-724754, EBI-2819725;
CC O14880; Q53HI1: UNC50; NbExp=3; IntAct=EBI-724754, EBI-7601760;
CC O14880; Q15836: VAMP3; NbExp=3; IntAct=EBI-724754, EBI-722343;
CC O14880; O75379: VAMP4; NbExp=3; IntAct=EBI-724754, EBI-744953;
CC O14880; O95070: YIF1A; NbExp=3; IntAct=EBI-724754, EBI-2799703;
CC O14880; O95159: ZFPL1; NbExp=3; IntAct=EBI-724754, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:27184847}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in heart, skeletal muscle,
CC and adrenal cortex. Also found in brain, placenta, liver, kidney,
CC pancreas, thyroid, testis and ovary. Almost absent in lung, thymus and
CC peripheral blood leukocytes. Expressed in mast cells.
CC {ECO:0000269|PubMed:36370807, ECO:0000269|PubMed:9278457}.
CC -!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
CC -!- CAUTION: Initially it was postulated to be an endoplasmic reticulum
CC membrane protein, but later it was proved by combined proteomic
CC analysis, APEX fingerprinting and confocal and electron microscopy to
CC be localized to the mitochondrion instead.
CC {ECO:0000269|PubMed:25944712, ECO:0000269|PubMed:27184847,
CC ECO:0000269|PubMed:9278457}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mgst3/";
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DR EMBL; AF026977; AAB82609.1; -; mRNA.
DR EMBL; CR450359; CAG29355.1; -; mRNA.
DR EMBL; AY388493; AAQ81301.1; -; Genomic_DNA.
DR EMBL; AK312103; BAG35039.1; -; mRNA.
DR EMBL; AL451074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90752.1; -; Genomic_DNA.
DR EMBL; BC000505; AAH00505.1; -; mRNA.
DR EMBL; BC003034; AAH03034.1; -; mRNA.
DR EMBL; BC005964; AAH05964.1; -; mRNA.
DR CCDS; CCDS1249.1; -.
DR RefSeq; NP_004519.1; NM_004528.3.
DR RefSeq; XP_005245231.2; XM_005245174.3.
DR AlphaFoldDB; O14880; -.
DR SMR; O14880; -.
DR BioGRID; 110415; 286.
DR IntAct; O14880; 399.
DR MINT; O14880; -.
DR STRING; 9606.ENSP00000356864; -.
DR ChEMBL; CHEMBL1743186; -.
DR DrugBank; DB00143; Glutathione.
DR SwissLipids; SLP:000001463; -.
DR CarbonylDB; O14880; -.
DR GlyGen; O14880; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14880; -.
DR PhosphoSitePlus; O14880; -.
DR SwissPalm; O14880; -.
DR BioMuta; MGST3; -.
DR EPD; O14880; -.
DR jPOST; O14880; -.
DR MassIVE; O14880; -.
DR MaxQB; O14880; -.
DR PaxDb; 9606-ENSP00000356864; -.
DR PeptideAtlas; O14880; -.
DR ProteomicsDB; 48280; -.
DR Pumba; O14880; -.
DR TopDownProteomics; O14880; -.
DR Antibodypedia; 34331; 150 antibodies from 21 providers.
DR DNASU; 4259; -.
DR Ensembl; ENST00000367884.6; ENSP00000356859.1; ENSG00000143198.13.
DR Ensembl; ENST00000367889.8; ENSP00000356864.3; ENSG00000143198.13.
DR GeneID; 4259; -.
DR KEGG; hsa:4259; -.
DR MANE-Select; ENST00000367889.8; ENSP00000356864.3; NM_004528.4; NP_004519.1.
DR UCSC; uc001gdf.4; human.
DR AGR; HGNC:7064; -.
DR CTD; 4259; -.
DR DisGeNET; 4259; -.
DR GeneCards; MGST3; -.
DR HGNC; HGNC:7064; MGST3.
DR HPA; ENSG00000143198; Low tissue specificity.
DR MIM; 604564; gene.
DR neXtProt; NX_O14880; -.
DR OpenTargets; ENSG00000143198; -.
DR PharmGKB; PA30793; -.
DR VEuPathDB; HostDB:ENSG00000143198; -.
DR eggNOG; ENOG502S4E5; Eukaryota.
DR GeneTree; ENSGT00390000008608; -.
DR HOGENOM; CLU_110291_1_0_1; -.
DR InParanoid; O14880; -.
DR OrthoDB; 5487436at2759; -.
DR PhylomeDB; O14880; -.
DR TreeFam; TF105328; -.
DR PathwayCommons; O14880; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
DR SignaLink; O14880; -.
DR UniPathway; UPA00383; -.
DR UniPathway; UPA00879; -.
DR BioGRID-ORCS; 4259; 12 hits in 1168 CRISPR screens.
DR ChiTaRS; MGST3; human.
DR GeneWiki; MGST3; -.
DR GenomeRNAi; 4259; -.
DR Pharos; O14880; Tbio.
DR PRO; PR:O14880; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O14880; Protein.
DR Bgee; ENSG00000143198; Expressed in corpus epididymis and 206 other cell types or tissues.
DR ExpressionAtlas; O14880; baseline and differential.
DR Genevisible; O14880; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:BHF-UCL.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004464; F:leukotriene-C4 synthase activity; IDA:BHF-UCL.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019370; P:leukotriene biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0006629; P:lipid metabolic process; IDA:BHF-UCL.
DR GO; GO:0006692; P:prostanoid metabolic process; IDA:UniProtKB.
DR Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1.
DR InterPro; IPR023352; MAPEG-like_dom_sf.
DR InterPro; IPR001129; Membr-assoc_MAPEG.
DR PANTHER; PTHR10250; MICROSOMAL GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR10250:SF27; MICROSOMAL GLUTATHIONE S-TRANSFERASE 3; 1.
DR Pfam; PF01124; MAPEG; 1.
DR SUPFAM; SSF161084; MAPEG domain-like; 1.
PE 1: Evidence at protein level;
KW Lipid metabolism; Lipoprotein; Lyase; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Oxidoreductase; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..152
FT /note="Glutathione S-transferase 3, mitochondrial"
FT /id="PRO_0000217741"
FT TOPO_DOM 1..8
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:27184847"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..119
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27184847"
FT LIPID 150
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21044946"
FT LIPID 151
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21044946"
FT VARIANT 15
FT /note="G -> C (in dbSNP:rs1802087)"
FT /id="VAR_012061"
FT VARIANT 48
FT /note="P -> S (in dbSNP:rs1802088)"
FT /id="VAR_012062"
FT MUTAGEN 150
FT /note="C->S: Abolishes S-acylation; when associated with S-
FT 151."
FT /evidence="ECO:0000269|PubMed:21044946"
FT MUTAGEN 151
FT /note="C->S: Abolishes S-acylation; when associated with S-
FT 150."
FT /evidence="ECO:0000269|PubMed:21044946"
SQ SEQUENCE 152 AA; 16516 MW; B721527247415E78 CRC64;
MAVLSKEYGF VLLTGAASFI MVAHLAINVS KARKKYKVEY PIMYSTDPEN GHIFNCIQRA
HQNTLEVYPP FLFFLAVGGV YHPRIASGLG LAWIVGRVLY AYGYYTGEPS KRSRGALGSI
ALLGLVGTTV CSAFQHLGWV KSGLGSGPKC CH
//
