MGST3_HUMAN
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 03-AUG-2022, entry version 185.
DE RecName: Full=Microsomal glutathione S-transferase 3 {ECO:0000305};
DE Short=Microsomal GST-3;
DE AltName: Full=Glutathione peroxidase MGST3 {ECO:0000305|PubMed:9278457};
DE EC=1.11.1.-;
DE AltName: Full=LTC4 synthase MGST3 {ECO:0000305|PubMed:9278457};
DE EC=4.4.1.20 {ECO:0000269|PubMed:9278457};
DE AltName: Full=Microsomal glutathione S-transferase III {ECO:0000303|PubMed:9278457};
DE Short=Microsomal GST-III {ECO:0000303|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 SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
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].
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).
CC -!- FUNCTION: Catalyzes oxydation of hydroxy-fatty acids (PubMed:9278457).
CC Also catalyzes the conjugation of a reduced glutathione to leukotriene
CC A4 in vitro (PubMed:9278457). May participate in the lipid metabolism
CC (PubMed:9278457). {ECO:0000269|PubMed:9278457,
CC ECO:0000303|PubMed:9278457}.
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 -!- 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 -!- ACTIVITY REGULATION: Inhibited by MK-886 and leukotriene C4.
CC {ECO:0000250|UniProtKB:D4ADS4}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate
CC {ECO:0000269|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: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}. Microsome membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Microsome
CC membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Membrane
CC {ECO:0000269|PubMed:9278457}.
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. {ECO:0000269|PubMed:9278457}.
CC -!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
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; 276.
DR IntAct; O14880; 396.
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; O14880; -.
DR PeptideAtlas; O14880; -.
DR PRIDE; O14880; -.
DR ProteomicsDB; 48280; -.
DR TopDownProteomics; O14880; -.
DR Antibodypedia; 34331; 127 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 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; 1609516at2759; -.
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 BioGRID-ORCS; 4259; 10 hits in 1086 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 204 other 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:BHF-UCL.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0019370; P:leukotriene biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0006629; P:lipid metabolic process; IDA:BHF-UCL.
DR Gene3D; 1.20.120.550; -; 1.
DR InterPro; IPR023352; MAPEG-like_dom_sf.
DR InterPro; IPR001129; Membr-assoc_MAPEG.
DR Pfam; PF01124; MAPEG; 1.
DR SUPFAM; SSF161084; SSF161084; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid metabolism; Lipoprotein; Lyase; Membrane;
KW Microsome; Oxidoreductase; Palmitate; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..152
FT /note="Microsomal glutathione S-transferase 3"
FT /id="PRO_0000217741"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
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
