Glutathione S-transferase A1 - Mus musculus (Mouse)

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P13745 (GSTA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glutathione S-transferase A1
EC=2.5.1.18

Alternative name(s):
GST class-alpha member 1
Glutathione S-transferase Ya
Glutathione S-transferase Ya1

Gene names

Name:	Gsta1
Synonyms:	Gsta, Gstya

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	223 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer. Ref.4
Induction	Induced in the liver by beta-naphthoflavone (BNF) and 2₃-t-butyl-4-hydroxyanisole (BHA). Ref.3
Sequence similarities	Belongs to the GST superfamily. Alpha family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glutathione metabolic process Inferred from sequence or structural similarity. Source: UniProtKB response to stilbenoid Inferred from expression pattern PubMed 17086191. Source: UniProtKB
Molecular_function	glutathione transferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 223

222

Glutathione S-transferase A1

PRO_0000185788

Regions

Domain

3 – 83

GST N-terminal

Domain

85 – 208

124

GST C-terminal

Region

67 – 68

Glutathione binding

Sites

Binding site

Glutathione

Binding site

Glutathione

Binding site

Glutathione; via amide nitrogen and carbonyl oxygen

Secondary structure

223

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P13745 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A348A07133FBEC1D
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FASTA

223

25,608

        10         20         30         40         50         60 
MAGKPVLHYF NARGRMECIR WLLAAAGVEF EEKFIQSPED LEKLKKDGNL MFDQVPMVEI 

        70         80         90        100        110        120 
DGMKLAQTRA ILNYIATKYD LYGKDMKERA LIDMYSEGIL DLTEMIGQLV LCPPDQREAK 

       130        140        150        160        170        180 
TALAKDRTKN RYLPAFEKVL KSHGQDYLVG NRLTRVDIHL LEVLLYVEEF DASLLTPFPL 

       190        200        210        220 
LKAFKSRISS LPNVKKFLQP GSQRKPPMDA KQIQEARKAF KIQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse glutathione S-transferase Ya subunit: gene structure and sequence." Daniel V., Sharon R., Tichauer Y., Sarid S. DNA 6:317-324(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Regulation of mouse glutathione S-transferases by chemoprotectors. Molecular evidence for the existence of three distinct alpha-class glutathione S-transferase subunits, Ya1, Ya2, and Ya3, in mouse liver." McLellan L.I., Kerr L.A., Cronshaw A.D., Hayes J.D. Biochem. J. 276:461-469(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 16-36; 51-59; 63-165 AND 208-223, INDUCTION. Tissue: Liver.
[4]	"Residue R216 and catalytic efficiency of a murine class alpha glutathione S-transferase toward benzo[a]pyrene 7(R),8(S)-diol 9(S), 10(R)-epoxide." Gu Y., Singh S.V., Ji X. Biochemistry 39:12552-12557(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE AND SUBSTRATE, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M19256

M19255 Genomic DNA. Translation: AAA37750.1. Sequence problems.
BC132572 mRNA. Translation: AAI32573.1.
BC132576 mRNA. Translation: AAI32577.1.

IPI

IPI00554953.

PIR

A27848.

RefSeq

NP_032207.3. NM_008181.3.

UniGene

Mm.467426.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F3A	X-ray	1.90	A/B	2-222	[»]
1F3B	X-ray	2.00	A/B	2-222	[»]

ProteinModelPortal

P13745.

SMR

P13745. Positions 2-222.

ModBase

Search...

PTM databases

PhosphoSite

P13745.

Proteomic databases

PaxDb

P13745.

PRIDE

P13745.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000098537; ENSMUSP00000096139; ENSMUSG00000074183.

GeneID

14857.

KEGG

mmu:14857.

Organism-specific databases

CTD

2938.

MGI

MGI:1095417. Gsta1.

Phylogenomic databases

eggNOG

NOG266414.

GeneTree

ENSGT00670000097856.

HOGENOM

HOG000115734.

HOVERGEN

HBG053749.

InParanoid

A2RTN4.

K00799.

OMA

HRNERAV.

OrthoDB

EOG4XD3S0.

Gene expression databases

Bgee

P13745.

CleanEx

MM_GSTA1.

Genevestigator

P13745.

GermOnline

ENSMUSG00000074183. Mus musculus.

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

PANTHER

PTHR11571:SF4. PTHR11571:SF4. 1 hit.

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PRINTS

PR01266. GSTRNSFRASEA.

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00143. Glutathione.

EvolutionaryTrace

P13745.

NextBio

287087.

SOURCE

Search...

Entry information

Entry name

GSTA1_MOUSE

Accession

Primary (citable) accession number: P13745
Secondary accession number(s): A2RTN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents