MGST3_MOUSE
ID MGST3_MOUSE Reviewed; 153 AA.
AC Q9CPU4; Q3UXC5; Q9D834;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Microsomal glutathione S-transferase 3 {ECO:0000305};
DE Short=Microsomal GST-3;
DE AltName: Full=Glutathione peroxidase MGST3 {ECO:0000250|UniProtKB:O14880};
DE EC=1.11.1.-;
DE AltName: Full=Microsomal glutathione S-transferase III {ECO:0000250|UniProtKB:O14880};
DE Short=Microsomal GST-III {ECO:0000250|UniProtKB:O14880};
GN Name=Mgst3 {ECO:0000312|MGI:MGI:1913697};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, Embryo, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PROTEIN SEQUENCE OF 85-97, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes oxydation of hydroxy-fatty acids. May participate
CC to the lipid metabolism. {ECO:0000250|UniProtKB:O14880}.
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:0000250|UniProtKB:O14880};
CC -!- ACTIVITY REGULATION: Inhibited by MK-886 and leukotriene C4.
CC {ECO:0000250|UniProtKB:D4ADS4}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O14880}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O14880}. Microsome membrane
CC {ECO:0000250|UniProtKB:O14880}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O14880}. Microsome membrane
CC {ECO:0000250|UniProtKB:O14880}; Lipid-anchor
CC {ECO:0000250|UniProtKB:O14880}. Membrane
CC {ECO:0000250|UniProtKB:O14880}.
CC -!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
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DR EMBL; AK003246; BAB22665.1; -; mRNA.
DR EMBL; AK003309; BAB22706.1; -; mRNA.
DR EMBL; AK003476; BAB22808.1; -; mRNA.
DR EMBL; AK003492; BAB22819.1; -; mRNA.
DR EMBL; AK008533; BAB25726.1; -; mRNA.
DR EMBL; AK135742; BAE22638.1; -; mRNA.
DR EMBL; BC029669; AAH29669.1; -; mRNA.
DR CCDS; CCDS15457.1; -.
DR RefSeq; NP_079845.1; NM_025569.1.
DR AlphaFoldDB; Q9CPU4; -.
DR SMR; Q9CPU4; -.
DR BioGRID; 211481; 4.
DR IntAct; Q9CPU4; 4.
DR STRING; 10090.ENSMUSP00000028005; -.
DR iPTMnet; Q9CPU4; -.
DR PhosphoSitePlus; Q9CPU4; -.
DR SwissPalm; Q9CPU4; -.
DR EPD; Q9CPU4; -.
DR jPOST; Q9CPU4; -.
DR MaxQB; Q9CPU4; -.
DR PaxDb; Q9CPU4; -.
DR PeptideAtlas; Q9CPU4; -.
DR PRIDE; Q9CPU4; -.
DR ProteomicsDB; 290226; -.
DR Antibodypedia; 34331; 127 antibodies from 21 providers.
DR DNASU; 66447; -.
DR Ensembl; ENSMUST00000028005; ENSMUSP00000028005; ENSMUSG00000026688.
DR GeneID; 66447; -.
DR KEGG; mmu:66447; -.
DR UCSC; uc007dky.1; mouse.
DR CTD; 4259; -.
DR MGI; MGI:1913697; Mgst3.
DR VEuPathDB; HostDB:ENSMUSG00000026688; -.
DR eggNOG; ENOG502S4E5; Eukaryota.
DR GeneTree; ENSGT00390000008608; -.
DR HOGENOM; CLU_110291_1_0_1; -.
DR InParanoid; Q9CPU4; -.
DR OMA; YTGEPKN; -.
DR OrthoDB; 1609516at2759; -.
DR PhylomeDB; Q9CPU4; -.
DR TreeFam; TF105328; -.
DR Reactome; R-MMU-156590; Glutathione conjugation.
DR Reactome; R-MMU-5423646; Aflatoxin activation and detoxification.
DR BioGRID-ORCS; 66447; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Mgst3; mouse.
DR PRO; PR:Q9CPU4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CPU4; protein.
DR Bgee; ENSMUSG00000026688; Expressed in fetal liver hematopoietic progenitor cell and 269 other tissues.
DR Genevisible; Q9CPU4; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISO:MGI.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004464; F:leukotriene-C4 synthase activity; ISO:MGI.
DR GO; GO:0019370; P:leukotriene biosynthetic process; ISO:MGI.
DR GO; GO:0006629; P:lipid metabolic process; ISO:MGI.
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 Direct protein sequencing; Endoplasmic reticulum; Lipid metabolism;
KW Lipoprotein; Membrane; Microsome; Oxidoreductase; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..153
FT /note="Microsomal glutathione S-transferase 3"
FT /id="PRO_0000217742"
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 151
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O14880"
FT CONFLICT 142
FT /note="P -> R (in Ref. 1; BAB25726)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 153 AA; 16958 MW; F54175ACB9C4C845 CRC64;
MAVLSKEYGF VLLTGAASFV MVLHLAINVG KARKKYKVEY PVMYSTDPEN GHMFNCIQRA
HQNTLEVYPP FLFFLTVGGV YHPRIASGLG LAWIIGRVLY AYGYYTGDPS KRYRGAVGSL
ALFALMGTTV CSAFQHLGWI RPGLGYGSRS CHH
