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Glutathione S-transferase A1 (EC 2.5.1.18) (GST HA subunit 1) (GST class-alpha member 1) (GST-epsilon) (GSTA1-1) (GTH1) [Cleaved into: Glutathione S-transferase A1, N-terminally processed]

 GSTA1_HUMAN             Reviewed;         222 AA.
P08263; Q14750; Q5GHF8; Q5SZC1;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 196.
RecName: Full=Glutathione S-transferase A1;
EC=2.5.1.18;
AltName: Full=GST HA subunit 1;
AltName: Full=GST class-alpha member 1;
AltName: Full=GST-epsilon;
AltName: Full=GSTA1-1;
AltName: Full=GTH1;
Contains:
RecName: Full=Glutathione S-transferase A1, N-terminally processed;
Name=GSTA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3800996; DOI=10.1016/S0006-291X(86)80358-8;
Tu C.-P.D., Qian B.;
"Human liver glutathione S-transferases: complete primary sequence of
an Ha subunit cDNA.";
Biochem. Biophys. Res. Commun. 141:229-237(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3036131; DOI=10.1016/0006-291X(87)91345-3;
Rhoads D.M., Zarlengo R.P., Tu C.-P.D.;
"The basic glutathione S-transferases from human livers are products
of separate genes.";
Biochem. Biophys. Res. Commun. 145:474-481(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=3678589; DOI=10.1042/bst0150734;
Tu C.-P.D., Qian B.;
"Nucleotide sequence of the human liver glutathione S-transferase
subunit 1 cDNA.";
Biochem. Soc. Trans. 15:734-736(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3031680; DOI=10.1073/pnas.84.8.2377;
Board P.G., Webb G.C.;
"Isolation of a cDNA clone and localization of human glutathione S-
transferase 2 genes to chromosome band 6p12.";
Proc. Natl. Acad. Sci. U.S.A. 84:2377-2381(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1731620; DOI=10.1016/0003-9861(92)90035-U;
Rozen F., Nguyen T., Pickett C.B.;
"Isolation and characterization of a human glutathione S-transferase
Ha1 subunit gene.";
Arch. Biochem. Biophys. 292:589-593(1992).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1330133; DOI=10.1016/1046-5928(92)90060-A;
Stenberg G., Bjornestedt R., Mannervik B.;
"Heterologous expression of recombinant human glutathione transferase
A1-1 from a hepatoma cell line.";
Protein Expr. Purif. 3:80-84(1992).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Chen P., Zhang C., Xie D., Wu Y., Han L., Chen L.;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[11]
NUCLEOTIDE SEQUENCE OF 1-9.
PubMed=3138230;
Chow N.W., Whang-Peng J., Kao-Shan C.S., Tam M.F., Lai H.-C.J.,
Tu C.-P.D.;
"Human glutathione S-transferases. The Ha multigene family encodes
products of different but overlapping substrate specificities.";
J. Biol. Chem. 263:12797-12800(1988).
[12]
PROTEIN SEQUENCE OF 2-170; 188-195 AND 209-222.
PubMed=8431482; DOI=10.1016/0167-4838(93)90234-I;
Ahmad H., Singhal S.S., Saxena M., Awasthi Y.C.;
"Characterization of two novel subunits of the alpha-class glutathione
S-transferases of human liver.";
Biochim. Biophys. Acta 1161:333-336(1993).
[13]
PROTEIN SEQUENCE OF 16-36; 63-155 AND 208-212.
PubMed=2604726; DOI=10.1042/bj2640437;
Hayes J.D., Kerr L.A., Cronshaw A.D.;
"Evidence that glutathione S-transferases B1B1 and B2B2 are the
products of separate genes and that their expression in human liver is
subject to inter-individual variation. Molecular relationships between
the B1 and B2 subunits and other alpha class glutathione S-
transferases.";
Biochem. J. 264:437-445(1989).
[14]
PROTEIN SEQUENCE OF 200-222.
PubMed=2018473; DOI=10.1042/bj2750171;
Board P.G., Mannervik B.;
"The contribution of the C-terminal sequence to the catalytic activity
of GST2, a human alpha-class glutathione transferase.";
Biochem. J. 275:171-174(1991).
[15]
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).
[16]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH
S-BENZYL-GLUTATHIONE, AND SUBUNIT.
PubMed=8331657; DOI=10.1006/jmbi.1993.1376;
Sinning I., Kleywegt G.J., Cowan S.W., Reinemer P., Dirr H.W.,
Huber R., Gilliland G.L., Armstrong R.N., Ji X., Board P.G., Olin B.,
Mannervik B., Jones T.A.;
"Structure determination and refinement of human alpha class
glutathione transferase A1-1, and a comparison with the Mu and Pi
class enzymes.";
J. Mol. Biol. 232:192-212(1993).
[17]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH ETHACRYNIC
ACID AND GLUTATHIONE, AND SUBUNIT.
PubMed=8591048; DOI=10.1016/S0969-2126(01)00206-4;
Cameron A.D., Sinning I., L'Hermite G., Olin B., Board P.G.,
Mannervik B., Jones T.A.;
"Structural analysis of human alpha-class glutathione transferase A1-1
in the apo-form and in complexes with ethacrynic acid and its
glutathione conjugate.";
Structure 3:717-727(1995).
[18]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEXES WITH S-HEXYL
GLUTATHIONE, AND SUBUNIT.
PubMed=12211029; DOI=10.1002/prot.10162;
Le Trong I., Stenkamp R.E., Ibarra C., Atkins W.M., Adman E.T.;
"1.3-A resolution structure of human glutathione S-transferase with S-
hexyl glutathione bound reveals possible extended ligandin binding
site.";
Proteins 48:618-627(2002).
[19]
X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEX WITH
S-BENZYLGLUTATHIONE, AND MUTAGENESIS OF ALA-216.
PubMed=15333749; DOI=10.1073/pnas.0403045101;
Hederos S., Broo K.S., Jakobsson E., Kleywegt G.J., Mannervik B.,
Baltzer L.;
"Incorporation of a single His residue by rational design enables
thiol-ester hydrolysis by human glutathione transferase A1-1.";
Proc. Natl. Acad. Sci. U.S.A. 101:13163-13167(2004).
[20]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF MUTANT ALA-219 IN COMPLEX
WITH S-HEXYLGLUTATHIONE.
PubMed=15893769; DOI=10.1016/j.jmb.2005.04.025;
Kuhnert D.C., Sayed Y., Mosebi S., Sayed M., Sewell T., Dirr H.W.;
"Tertiary interactions stabilise the C-terminal region of human
glutathione transferase A1-1: a crystallographic and calorimetric
study.";
J. Mol. Biol. 349:825-838(2005).
[21]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
AND SUBUNIT.
PubMed=16421451; DOI=10.1107/S0907444905039296;
Grahn E., Novotny M., Jakobsson E., Gustafsson A., Grehn L., Olin B.,
Madsen D., Wahlberg M., Mannervik B., Kleywegt G.J.;
"New crystal structures of human glutathione transferase A1-1 shed
light on glutathione binding and the conformation of the C-terminal
helix.";
Acta Crystallogr. D 62:197-207(2006).
[22]
X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 1-210 IN COMPLEX WITH
GLUTATHIONE.
PubMed=19618965; DOI=10.1021/bi900895b;
Balogh L.M., Le Trong I., Kripps K.A., Tars K., Stenkamp R.E.,
Mannervik B., Atkins W.M.;
"Structural analysis of a glutathione transferase A1-1 mutant tailored
for high catalytic efficiency with toxic alkenals.";
Biochemistry 48:7698-7704(2009).
[23]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANTS ALA-71 AND VAL-71 IN
COMPLEX WITH S-HEXYLGLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, AND
MUTAGENESIS OF ILE-71.
PubMed=20606271; DOI=10.1107/S1744309110019135;
Achilonu I., Gildenhuys S., Fisher L., Burke J., Fanucchi S.,
Sewell B.T., Fernandes M., Dirr H.W.;
"The role of a topologically conserved isoleucine in glutathione
transferase structure, stability and function.";
Acta Crystallogr. F 66:776-780(2010).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles.
{ECO:0000269|PubMed:20606271}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000269|PubMed:20606271}.
-!- SUBUNIT: Homodimer or heterodimer of GSTA1 and GSTA2.
{ECO:0000269|PubMed:12211029, ECO:0000269|PubMed:15333749,
ECO:0000269|PubMed:15893769, ECO:0000269|PubMed:16421451,
ECO:0000269|PubMed:19618965, ECO:0000269|PubMed:20606271,
ECO:0000269|PubMed:8331657, ECO:0000269|PubMed:8591048}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Liver.
-!- DOMAIN: The C-terminal domain may form a component of the
hydrophobic substrate-binding site, but in contrast appears not to
be directly involved in GSH binding and is not absolutely
essential for catalytic activity.
-!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
{ECO:0000305}.
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EMBL; M15872; AAA70226.1; -; mRNA.
EMBL; M21758; AAA52615.1; -; mRNA.
EMBL; M25627; AAA36174.1; -; mRNA.
EMBL; M14777; AAA52618.1; -; mRNA.
EMBL; S76235; AAB20973.1; -; Genomic_DNA.
EMBL; S76221; AAB20973.1; JOINED; Genomic_DNA.
EMBL; S76223; AAB20973.1; JOINED; Genomic_DNA.
EMBL; S76225; AAB20973.1; JOINED; Genomic_DNA.
EMBL; S76228; AAB20973.1; JOINED; Genomic_DNA.
EMBL; S76232; AAB20973.1; JOINED; Genomic_DNA.
EMBL; S49975; AAB24012.1; -; mRNA.
EMBL; AY532928; AAT06769.1; -; mRNA.
EMBL; CR407656; CAG28584.1; -; mRNA.
EMBL; AL590363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX04385.1; -; Genomic_DNA.
EMBL; BC053578; AAH53578.1; -; mRNA.
EMBL; BC110891; AAI10892.1; -; mRNA.
CCDS; CCDS4945.1; -.
PIR; A25909; A56666.
PIR; S29657; S29657.
RefSeq; NP_665683.1; NM_145740.4.
UniGene; Hs.446309; -.
PDB; 1GSD; X-ray; 2.50 A; A/B/C/D=2-222.
PDB; 1GSE; X-ray; 2.00 A; A/B=2-222.
PDB; 1GSF; X-ray; 2.70 A; A/B/C/D=2-222.
PDB; 1GUH; X-ray; 2.60 A; A/B/C/D=2-222.
PDB; 1K3L; X-ray; 1.50 A; A/B=2-222.
PDB; 1K3O; X-ray; 1.80 A; A/B=2-222.
PDB; 1K3Y; X-ray; 1.30 A; A/B=2-222.
PDB; 1LBK; X-ray; 1.86 A; A/B=208-213.
PDB; 1PKW; X-ray; 2.00 A; A/B=1-222.
PDB; 1PKZ; X-ray; 2.10 A; A/B=1-222.
PDB; 1PL1; X-ray; 1.75 A; A/B=1-222.
PDB; 1PL2; X-ray; 1.80 A; A/B=1-222.
PDB; 1USB; X-ray; 2.07 A; A/B=2-222.
PDB; 1XWG; X-ray; 1.85 A; A/B=2-222.
PDB; 1YDK; X-ray; 1.95 A; A/B=1-222.
PDB; 2R3X; X-ray; 1.80 A; A/B=1-222.
PDB; 2R6K; X-ray; 2.51 A; A/B=1-222.
PDB; 3I69; X-ray; 2.38 A; A/B/C/D/E/F/G/H=1-222.
PDB; 3I6A; X-ray; 1.98 A; A/B/C/D/E/F/G/H=1-222.
PDB; 3IK9; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-222.
PDB; 3KTL; X-ray; 1.75 A; A/B=2-222.
PDB; 3L0H; X-ray; 2.13 A; A/B=1-222.
PDB; 3Q74; X-ray; 1.79 A; A/B=2-222.
PDB; 3U6V; X-ray; 2.20 A; A/B=1-222.
PDB; 3ZFB; X-ray; 1.86 A; A/B=1-222.
PDB; 3ZFL; X-ray; 1.88 A; A/B=1-222.
PDB; 4HJ2; X-ray; 2.10 A; A/B=4-220.
PDB; 5JCU; X-ray; 1.93 A; A/B/C/D=2-222.
PDB; 5LCZ; X-ray; 2.33 A; A/B=1-100, A/B=201-222.
PDB; 5LD0; X-ray; 1.60 A; A=1-85, A=214-222.
PDBsum; 1GSD; -.
PDBsum; 1GSE; -.
PDBsum; 1GSF; -.
PDBsum; 1GUH; -.
PDBsum; 1K3L; -.
PDBsum; 1K3O; -.
PDBsum; 1K3Y; -.
PDBsum; 1LBK; -.
PDBsum; 1PKW; -.
PDBsum; 1PKZ; -.
PDBsum; 1PL1; -.
PDBsum; 1PL2; -.
PDBsum; 1USB; -.
PDBsum; 1XWG; -.
PDBsum; 1YDK; -.
PDBsum; 2R3X; -.
PDBsum; 2R6K; -.
PDBsum; 3I69; -.
PDBsum; 3I6A; -.
PDBsum; 3IK9; -.
PDBsum; 3KTL; -.
PDBsum; 3L0H; -.
PDBsum; 3Q74; -.
PDBsum; 3U6V; -.
PDBsum; 3ZFB; -.
PDBsum; 3ZFL; -.
PDBsum; 4HJ2; -.
PDBsum; 5JCU; -.
PDBsum; 5LCZ; -.
PDBsum; 5LD0; -.
ProteinModelPortal; P08263; -.
SMR; P08263; -.
BioGrid; 109193; 15.
IntAct; P08263; 6.
MINT; MINT-5000131; -.
STRING; 9606.ENSP00000335620; -.
BindingDB; P08263; -.
ChEMBL; CHEMBL3409; -.
DrugBank; DB02486; 2-Hydroxyethyl Disulfide.
DrugBank; DB00993; Azathioprine.
DrugBank; DB01008; Busulfan.
DrugBank; DB00143; Glutathione.
DrugBank; DB03003; Glutathione Sulfonic Acid.
DrugBank; DB02943; N-(4-Aminobutanoyl)-S-(4-Methoxybenzyl)-L-Cysteinylglycine.
DrugBank; DB03602; S-Benzyl-Glutathione.
DrugBank; DB04132; S-Hexylglutathione.
DrugBank; DB01915; S-Hydroxycysteine.
SwissLipids; SLP:000001476; -.
iPTMnet; P08263; -.
PhosphoSitePlus; P08263; -.
BioMuta; GSTA1; -.
DMDM; 121730; -.
REPRODUCTION-2DPAGE; IPI00657682; -.
MaxQB; P08263; -.
PaxDb; P08263; -.
PeptideAtlas; P08263; -.
PRIDE; P08263; -.
DNASU; 2938; -.
Ensembl; ENST00000334575; ENSP00000335620; ENSG00000243955.
GeneID; 2938; -.
KEGG; hsa:2938; -.
UCSC; uc003paz.4; human.
CTD; 2938; -.
DisGeNET; 2938; -.
EuPathDB; HostDB:ENSG00000243955.5; -.
GeneCards; GSTA1; -.
HGNC; HGNC:4626; GSTA1.
HPA; HPA004342; -.
HPA; HPA048934; -.
HPA; HPA053817; -.
MIM; 138359; gene.
neXtProt; NX_P08263; -.
OpenTargets; ENSG00000243955; -.
PharmGKB; PA29016; -.
eggNOG; KOG1695; Eukaryota.
eggNOG; ENOG4111VAU; LUCA.
GeneTree; ENSGT00670000097856; -.
HOGENOM; HOG000115734; -.
HOVERGEN; HBG053749; -.
InParanoid; P08263; -.
KO; K00799; -.
OMA; NEMIIVL; -.
OrthoDB; EOG091G0O3D; -.
PhylomeDB; P08263; -.
TreeFam; TF105321; -.
BioCyc; MetaCyc:G66-32542-MONOMER; -.
BRENDA; 2.5.1.18; 2681.
Reactome; R-HSA-156590; Glutathione conjugation.
SABIO-RK; P08263; -.
SIGNOR; P08263; -.
ChiTaRS; GSTA1; human.
EvolutionaryTrace; P08263; -.
GeneWiki; Glutathione_S-transferase_A1; -.
GenomeRNAi; 2938; -.
PRO; PR:P08263; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000243955; -.
CleanEx; HS_GSTA1; -.
ExpressionAtlas; P08263; baseline and differential.
Genevisible; P08263; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0004602; F:glutathione peroxidase activity; IDA:BHF-UCL.
GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
GO; GO:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome.
GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
GO; GO:0043651; P:linoleic acid metabolic process; IDA:BHF-UCL.
GO; GO:0008152; P:metabolic process; IC:UniProtKB.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR003080; GST_alpha.
InterPro; IPR004046; GST_C.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00043; GST_C; 1.
Pfam; PF02798; GST_N; 1.
PRINTS; PR01266; GSTRNSFRASEA.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Polymorphism; Reference proteome;
Transferase.
CHAIN 1 222 Glutathione S-transferase A1.
/FTId=PRO_0000423203.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:P30115,
ECO:0000269|PubMed:8431482}.
CHAIN 2 222 Glutathione S-transferase A1, N-
terminally processed.
/FTId=PRO_0000185783.
DOMAIN 3 83 GST N-terminal.
DOMAIN 85 207 GST C-terminal.
REGION 54 55 Glutathione binding.
{ECO:0000269|PubMed:16421451,
ECO:0000269|PubMed:19618965}.
REGION 67 68 Glutathione binding.
{ECO:0000269|PubMed:16421451,
ECO:0000269|PubMed:19618965}.
BINDING 9 9 Glutathione.
{ECO:0000269|PubMed:16421451,
ECO:0000269|PubMed:19618965}.
BINDING 45 45 Glutathione.
{ECO:0000269|PubMed:16421451,
ECO:0000269|PubMed:19618965}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P80894}.
MOD_RES 2 2 N-acetylalanine; in Glutathione S-
transferase A1, N-terminally processed.
{ECO:0000250|UniProtKB:P30115}.
MOD_RES 4 4 N6-succinyllysine.
{ECO:0000250|UniProtKB:P30115}.
VARIANT 19 19 T -> I (in dbSNP:rs1051578).
/FTId=VAR_033978.
VARIANT 113 113 P -> Q (in dbSNP:rs1051745).
/FTId=VAR_049482.
VARIANT 117 117 K -> Q (in dbSNP:rs1051757).
/FTId=VAR_049483.
MUTAGEN 71 71 I->A,V: No significant effect on enzyme
activity. Reduces protein stability.
{ECO:0000269|PubMed:20606271}.
MUTAGEN 216 216 A->H: Confers ability to hydrolyze S-
glutathionyl benzoate to glutathione and
benzoic acid.
{ECO:0000269|PubMed:15333749}.
CONFLICT 18 18 S -> C (in Ref. 3; AAA36174).
{ECO:0000305}.
CONFLICT 51 51 M -> T (in Ref. 7; AAT06769).
{ECO:0000305}.
CONFLICT 56 58 PMV -> AML (in Ref. 3; AAA36174).
{ECO:0000305}.
CONFLICT 212 212 S -> L (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 216 216 A -> S (in Ref. 12; AA sequence).
{ECO:0000305}.
STRAND 6 13 {ECO:0000244|PDB:1K3Y}.
TURN 14 16 {ECO:0000244|PDB:1K3Y}.
HELIX 17 26 {ECO:0000244|PDB:1K3Y}.
STRAND 31 35 {ECO:0000244|PDB:1K3Y}.
HELIX 38 46 {ECO:0000244|PDB:1K3Y}.
STRAND 57 60 {ECO:0000244|PDB:1K3Y}.
STRAND 63 67 {ECO:0000244|PDB:1K3Y}.
HELIX 68 78 {ECO:0000244|PDB:1K3Y}.
HELIX 86 108 {ECO:0000244|PDB:1K3Y}.
HELIX 109 111 {ECO:0000244|PDB:1K3Y}.
HELIX 114 130 {ECO:0000244|PDB:1K3Y}.
HELIX 132 143 {ECO:0000244|PDB:1K3Y}.
STRAND 146 149 {ECO:0000244|PDB:1K3Y}.
HELIX 155 170 {ECO:0000244|PDB:1K3Y}.
TURN 172 177 {ECO:0000244|PDB:1K3Y}.
HELIX 179 190 {ECO:0000244|PDB:1K3Y}.
HELIX 192 198 {ECO:0000244|PDB:1K3Y}.
HELIX 210 220 {ECO:0000244|PDB:1K3Y}.
SEQUENCE 222 AA; 25631 MW; C8B6786DCD761350 CRC64;
MAEKPKLHYF NARGRMESTR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL MFQQVPMVEI
DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYIEGIA DLGEMILLLP VCPPEEKDAK
LALIKEKIKN RYFPAFEKVL KSHGQDYLVG NKLSRADIHL VELLYYVEEL DSSLISSFPL
LKALKTRISN LPTVKKFLQP GSPRKPPMDE KSLEEARKIF RF


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