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Protein

Microsomal glutathione S-transferase 1

Gene

MGST1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.By similarity

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

Enzyme regulationi

Can be activated by reagents that attack Cys-50 sulfhydryl, such as N-ethylmaleimide. Activation also occurs via nitration of Tyr-93 by peroxynitrite (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei38GlutathioneBy similarity1
Sitei50Activates the enzyme when modifiedBy similarity1
Binding sitei73GlutathioneBy similarity1
Binding sitei74GlutathioneBy similarity1
Binding sitei76GlutathioneBy similarity1
Binding sitei81GlutathioneBy similarity1
Binding sitei121GlutathioneBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase

Names & Taxonomyi

Protein namesi
Recommended name:
Microsomal glutathione S-transferase 1 (EC:2.5.1.18)
Short name:
Microsomal GST-1
Alternative name(s):
Microsomal GST-I
Gene namesi
Name:MGST1
Synonyms:GST12
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini3 – 9LumenalBy similarity7
Transmembranei10 – 33HelicalBy similarityAdd BLAST24
Topological domaini34 – 62CytoplasmicBy similarityAdd BLAST29
Transmembranei63 – 96HelicalBy similarityAdd BLAST34
Topological domaini97 – 99LumenalBy similarity3
Transmembranei100 – 123HelicalBy similarityAdd BLAST24
Topological domaini124 – 128CytoplasmicBy similarity5
Transmembranei129 – 148HelicalBy similarityAdd BLAST20
Topological domaini149 – 155LumenalBy similarity7

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002177381 – 155Microsomal glutathione S-transferase 1Add BLAST155

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei42N6-acetyllysineBy similarity1
Modified residuei55N6-acetyllysineBy similarity1
Modified residuei60N6-acetyllysineBy similarity1

Post-translational modificationi

Peroxynitrite induces nitration at Tyr-93 which activates the enzyme.By similarity

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

PeptideAtlasiP79382.
PRIDEiP79382.

Interactioni

Subunit structurei

Homotrimer; The trimer binds only one molecule of glutathione.By similarity

Structurei

3D structure databases

ProteinModelPortaliP79382.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MAPEG family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000011980.
HOVERGENiHBG052470.
InParanoidiP79382.
KOiK00799.

Family and domain databases

Gene3Di1.20.120.550. 1 hit.
InterProiView protein in InterPro
IPR023352. MAPEG-like_dom_sf.
IPR001129. Membr-assoc_MAPEG.
PfamiView protein in Pfam
PF01124. MAPEG. 1 hit.
SUPFAMiSSF161084. SSF161084. 1 hit.

Sequencei

Sequence statusi: Complete.

P79382-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLTELMKN EVFMAFASYA TIVLSKMMFM STATAFYRLT RKVFANPEDC
60 70 80 90 100
SSFGKGENAK KYLRTDERVE RVRRAHLNDL ENIVPFLGIG LLYSLSGPDL
110 120 130 140 150
STAILHFRLF VGARIYHTIA YLTPLPQPNR GLAFFLGYGV TLSMAYRLLK

SRLYL
Length:155
Mass (Da):17,650
Last modified:January 23, 2007 - v3
Checksum:iC48A76872F493A32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000884 mRNA. Translation: BAA19201.1.
RefSeqiNP_999465.1. NM_214300.1.
UniGeneiSsc.51886.

Genome annotation databases

EnsembliENSSSCT00000048776; ENSSSCP00000038329; ENSSSCG00000032580.
GeneIDi397567.
KEGGissc:397567.

Similar proteinsi

Entry informationi

Entry nameiMGST1_PIG
AccessioniPrimary (citable) accession number: P79382
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 84 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families