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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381GlutathioneBy similarity
Sitei50 – 501Activates the enzyme when modifiedBy similarity
Binding sitei73 – 731GlutathioneBy similarity
Binding sitei74 – 741GlutathioneBy similarity
Binding sitei76 – 761GlutathioneBy similarity
Binding sitei81 – 811GlutathioneBy similarity
Binding sitei121 – 1211GlutathioneBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein homotrimerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

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
ProteomesiUP000008227: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini3 – 97LumenalBy similarity
Transmembranei10 – 3324HelicalBy similarityAdd
BLAST
Topological domaini34 – 6229CytoplasmicBy similarityAdd
BLAST
Transmembranei63 – 9634HelicalBy similarityAdd
BLAST
Topological domaini97 – 993LumenalBy similarity
Transmembranei100 – 12324HelicalBy similarityAdd
BLAST
Topological domaini124 – 1285CytoplasmicBy similarity
Transmembranei129 – 14820HelicalBy similarityAdd
BLAST
Topological domaini149 – 1557LumenalBy similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB
  4. mitochondrial outer membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 155154Microsomal glutathione S-transferase 1PRO_0000217738Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421N6-acetyllysineBy similarity
Modified residuei55 – 551N6-acetyllysineBy similarity
Modified residuei60 – 601N6-acetyllysineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Nitration

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP79382.
SMRiP79382. Positions 10-148.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MAPEG family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG052470.
InParanoidiP79382.
KOiK00799.

Family and domain databases

Gene3Di1.20.120.550. 1 hit.
InterProiIPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]
PfamiPF01124. MAPEG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

GeneIDi397567.
KEGGissc:397567.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliP79382.
SMRiP79382. Positions 10-148.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397567.
KEGGissc:397567.

Organism-specific databases

CTDi4257.

Phylogenomic databases

HOVERGENiHBG052470.
InParanoidiP79382.
KOiK00799.

Family and domain databases

Gene3Di1.20.120.550. 1 hit.
InterProiIPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]
PfamiPF01124. MAPEG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Kawakami K., Kimura M., Suzuki H., Hamasima N.
    Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiMGST1_PIG
AccessioniPrimary (citable) accession number: P79382
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 74 of the entry and version 3 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.