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Microsomal glutathione S-transferase 2 (Microsomal GST-2) (EC 2.5.1.18) (Microsomal GST-II)

 MGST2_HUMAN             Reviewed;         147 AA.
Q99735; D6RBB5; Q7Z5B8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
25-OCT-2017, entry version 153.
RecName: Full=Microsomal glutathione S-transferase 2;
Short=Microsomal GST-2;
EC=2.5.1.18;
AltName: Full=Microsomal GST-II;
Name=MGST2; Synonyms=GST2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8703034; DOI=10.1074/jbc.271.36.22203;
Jakobsson P.-J., Mancini J.A., Ford-Hutchinson A.W.;
"Identification and characterization of a novel human microsomal
glutathione S-transferase with leukotriene C4 synthase activity and
significant sequence identity to 5-lipoxygenase-activating protein and
leukotriene C4 synthase.";
J. Biol. Chem. 271:22203-22210(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-101.
NIEHS SNPs program;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung, and Neuroblastoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Can catalyze the production of LTC4 from LTA4 and
reduced glutathione. Can catalyze the conjugation of 1-chloro-2,4-
dinitrobenzene with reduced glutathione.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- SUBUNIT: Homotrimer.
-!- INTERACTION:
O43889-2:CREB3; NbExp=3; IntAct=EBI-11324706, EBI-625022;
Q96BA8:CREB3L1; NbExp=4; IntAct=EBI-11324706, EBI-6942903;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Microsome membrane {ECO:0000305}; Multi-pass membrane protein
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99735-1; Sequence=Displayed;
Name=2;
IsoId=Q99735-2; Sequence=VSP_044538;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Liver, spleen, skeletal muscle, heart,
adrenals, pancreas, prostate, testis, fetal liver, and fetal
spleen. Very low expression in lung, brain, placenta and bone
marrow.
-!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mgst2/";
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EMBL; U77604; AAC51768.1; -; mRNA.
EMBL; CR407640; CAG28568.1; -; mRNA.
EMBL; AY341028; AAP88934.1; ALT_SEQ; Genomic_DNA.
EMBL; AC108053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC112236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC025416; AAH25416.1; -; mRNA.
EMBL; BG519599; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS3749.1; -. [Q99735-1]
CCDS; CCDS56339.1; -. [Q99735-2]
RefSeq; NP_001191295.1; NM_001204366.1. [Q99735-1]
RefSeq; NP_001191297.1; NM_001204368.1. [Q99735-2]
RefSeq; NP_002404.1; NM_002413.4. [Q99735-1]
RefSeq; XP_016863700.1; XM_017008211.1. [Q99735-1]
RefSeq; XP_016863701.1; XM_017008212.1. [Q99735-1]
RefSeq; XP_016863702.1; XM_017008213.1. [Q99735-1]
UniGene; Hs.81874; -.
ProteinModelPortal; Q99735; -.
SMR; Q99735; -.
BioGrid; 110414; 5.
IntAct; Q99735; 7.
STRING; 9606.ENSP00000265498; -.
ChEMBL; CHEMBL1743185; -.
DrugBank; DB01008; Busulfan.
DrugBank; DB00143; Glutathione.
SwissLipids; SLP:000001464; -.
iPTMnet; Q99735; -.
PhosphoSitePlus; Q99735; -.
BioMuta; MGST2; -.
DMDM; 2842764; -.
EPD; Q99735; -.
MaxQB; Q99735; -.
PaxDb; Q99735; -.
PeptideAtlas; Q99735; -.
PRIDE; Q99735; -.
TopDownProteomics; Q99735-1; -. [Q99735-1]
DNASU; 4258; -.
Ensembl; ENST00000265498; ENSP00000265498; ENSG00000085871. [Q99735-1]
Ensembl; ENST00000503816; ENSP00000423008; ENSG00000085871. [Q99735-1]
Ensembl; ENST00000506797; ENSP00000424278; ENSG00000085871. [Q99735-2]
Ensembl; ENST00000616265; ENSP00000482639; ENSG00000085871. [Q99735-1]
GeneID; 4258; -.
KEGG; hsa:4258; -.
UCSC; uc003ihy.4; human. [Q99735-1]
CTD; 4258; -.
DisGeNET; 4258; -.
EuPathDB; HostDB:ENSG00000085871.8; -.
GeneCards; MGST2; -.
HGNC; HGNC:7063; MGST2.
HPA; HPA010707; -.
MIM; 601733; gene.
neXtProt; NX_Q99735; -.
OpenTargets; ENSG00000085871; -.
PharmGKB; PA30792; -.
eggNOG; ENOG410IX5K; Eukaryota.
eggNOG; ENOG41121Z4; LUCA.
GeneTree; ENSGT00430000030964; -.
HOGENOM; HOG000186087; -.
HOVERGEN; HBG105513; -.
InParanoid; Q99735; -.
KO; K00799; -.
OMA; IFRAQQN; -.
OrthoDB; EOG091G12NW; -.
PhylomeDB; Q99735; -.
TreeFam; TF105328; -.
Reactome; R-HSA-156590; Glutathione conjugation.
Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
ChiTaRS; MGST2; human.
GeneWiki; MGST2; -.
GenomeRNAi; 4258; -.
PRO; PR:Q99735; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000085871; -.
CleanEx; HS_MGST2; -.
Genevisible; Q99735; HS.
GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
GO; GO:0004602; F:glutathione peroxidase activity; IDA:BHF-UCL.
GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
GO; GO:0004464; F:leukotriene-C4 synthase activity; IDA:UniProtKB.
GO; GO:0006750; P:glutathione biosynthetic process; IDA:UniProtKB.
GO; GO:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome.
GO; GO:0019370; P:leukotriene biosynthetic process; IDA:UniProtKB.
GO; GO:0006629; P:lipid metabolic process; IDA:BHF-UCL.
GO; GO:0046466; P:membrane lipid catabolic process; IDA:BHF-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; NAS:BHF-UCL.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
Gene3D; 1.20.120.550; -; 1.
InterPro; IPR001446; 5_LipOase_AP.
InterPro; IPR018295; FLAP/GST2/LTC4S_CS.
InterPro; IPR023352; MAPEG-like_dom.
InterPro; IPR001129; Membr-assoc_MAPEG.
Pfam; PF01124; MAPEG; 1.
PRINTS; PR00488; 5LPOXGNASEAP.
SUPFAM; SSF161084; SSF161084; 1.
PROSITE; PS01297; FLAP_GST2_LTC4S; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Endoplasmic reticulum;
Leukotriene biosynthesis; Membrane; Microsome; Polymorphism;
Reference proteome; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 147 Microsomal glutathione S-transferase 2.
/FTId=PRO_0000217740.
TRANSMEM 6 26 Helical. {ECO:0000255}.
TRANSMEM 59 79 Helical. {ECO:0000255}.
TRANSMEM 111 131 Helical. {ECO:0000255}.
VAR_SEQ 53 147 QQNCVEFYPIFIITLWMAGWYFNQVFATCLGLVYIYGRHLY
FWGYSEAAKKRITGFRLSLGILALLTLLGALGIANSFLDEY
LDLNIAKKLRRQF -> HFCYLSGSGVHIWPSPILLGIFRS
C (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044538.
VARIANT 101 101 A -> V (in dbSNP:rs8192111).
{ECO:0000269|Ref.3}.
/FTId=VAR_019997.
SEQUENCE 147 AA; 16621 MW; D0E89B46885D16EF CRC64;
MAGNSILLAA VSILSACQQS YFALQVGKAR LKYKVTPPAV TGSPEFERVF RAQQNCVEFY
PIFIITLWMA GWYFNQVFAT CLGLVYIYGR HLYFWGYSEA AKKRITGFRL SLGILALLTL
LGALGIANSF LDEYLDLNIA KKLRRQF


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