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Protein

Glutathione S-transferase A2

Gene

GSTA2

Organism
Bos taurus (Bovine)
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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91GlutathioneBy similarity
Binding sitei45 – 451GlutathioneBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB

GO - Biological processi

  1. glutathione metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase A2 (EC:2.5.1.18)
Alternative name(s):
GST class-alpha member 2
Glutathione S-transferase alpha-2
Gene namesi
Name:GSTA2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 23

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 223222Glutathione S-transferase A2PRO_0000185781Add
BLAST

Proteomic databases

PaxDbiO18879.
PRIDEiO18879.

Expressioni

Tissue specificityi

Expressed in corpus luteum, adrenal gland, testis, liver, lung, thyroid and kidney.

Gene expression databases

ExpressionAtlasiO18879. baseline and differential.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000043661.

Structurei

3D structure databases

ProteinModelPortaliO18879.
SMRiO18879. Positions 2-221.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8381GST N-terminalAdd
BLAST
Domaini85 – 208124GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 552Glutathione bindingBy similarity
Regioni67 – 682Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Alpha family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiNOG266414.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiO18879.
KOiK00799.
OMAiNIRGRME.
OrthoDBiEOG79CZ0K.
TreeFamiTF105321.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O18879-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGKPKLHYF NGRGRMECIR WLLAAAGVEF EEKFIEQPED LDKLRNDGSL
60 70 80 90 100
MFQQVPMVEI DGMKLVQTRA ILNYIATKYN LYGKDMKERA LIDMYSEGVE
110 120 130 140 150
DLGEMIMHLP LCPPDQKDAK IAQIKERTTN RYFPAFEKVL KNHGQDYLVG
160 170 180 190 200
NKLSKADIHL VELLYYVEEL DPSLLANFPL LKGLKARVSS LPAVKKFLQP
210 220
GSQRKPPMDE KNLEEAKRIF RIK
Length:223
Mass (Da):25,717
Last modified:January 22, 2007 - v4
Checksum:iD61050D129901EB7
GO

Sequence cautioni

The sequence AAB83995.1 differs from that shown. Reason: Frameshift at positions 64 and 80. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027386 mRNA. Translation: AAB83995.1. Frameshift.
BC114835 mRNA. Translation: AAI14836.1.
RefSeqiNP_803481.1. NM_177515.2.
UniGeneiBt.62641.

Genome annotation databases

EnsembliENSBTAT00000046354; ENSBTAP00000043661; ENSBTAG00000006546.
GeneIDi281805.
KEGGibta:281805.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027386 mRNA. Translation: AAB83995.1. Frameshift.
BC114835 mRNA. Translation: AAI14836.1.
RefSeqiNP_803481.1. NM_177515.2.
UniGeneiBt.62641.

3D structure databases

ProteinModelPortaliO18879.
SMRiO18879. Positions 2-221.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000043661.

Proteomic databases

PaxDbiO18879.
PRIDEiO18879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000046354; ENSBTAP00000043661; ENSBTAG00000006546.
GeneIDi281805.
KEGGibta:281805.

Organism-specific databases

CTDi2939.

Phylogenomic databases

eggNOGiNOG266414.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiO18879.
KOiK00799.
OMAiNIRGRME.
OrthoDBiEOG79CZ0K.
TreeFamiTF105321.

Miscellaneous databases

NextBioi20805718.

Gene expression databases

ExpressionAtlasiO18879. baseline and differential.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "High expression of bovine alpha glutathione S-transferase (GSTA1, GSTA2) subunits is mainly associated with steroidogenically active cells and regulated by gonadotropins in bovine ovarian follicles."
    Rabahi F., Brule S., Sirois J., Beckers J.-F.M.P., Silversides D.W., Lussier J.G.
    Endocrinology 140:3507-3517(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Holstein.
    Tissue: Corpus luteum.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Thymus.

Entry informationi

Entry nameiGSTA2_BOVIN
AccessioniPrimary (citable) accession number: O18879
Secondary accession number(s): Q1RML3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 15, 2002
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 106 of the entry and version 4 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.