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Database: UniProt
Entry: P08263
LinkDB: P08263
Original site: P08263 
ID   GSTA1_HUMAN             Reviewed;         222 AA.
AC   P08263; Q14750; Q5GHF8; Q5SZC1;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-OCT-2019, entry version 208.
DE   RecName: Full=Glutathione S-transferase A1 {ECO:0000305|PubMed:20606271, ECO:0000305|PubMed:9084911};
DE            EC=2.5.1.18 {ECO:0000269|PubMed:20606271};
DE   AltName: Full=13-hydroperoxyoctadecadienoate peroxidase {ECO:0000305|PubMed:16624487};
DE            EC=1.11.1.- {ECO:0000269|PubMed:16624487};
DE   AltName: Full=Androst-5-ene-3,17-dione isomerase {ECO:0000305|PubMed:11152686};
DE            EC=5.3.3.- {ECO:0000269|PubMed:11152686};
DE   AltName: Full=GST HA subunit 1;
DE   AltName: Full=GST class-alpha member 1;
DE   AltName: Full=GST-epsilon;
DE   AltName: Full=GSTA1-1;
DE   AltName: Full=GTH1;
DE   Contains:
DE     RecName: Full=Glutathione S-transferase A1, N-terminally processed;
GN   Name=GSTA1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3800996; DOI=10.1016/s0006-291x(86)80358-8;
RA   Tu C.-P.D., Qian B.;
RT   "Human liver glutathione S-transferases: complete primary sequence of
RT   an Ha subunit cDNA.";
RL   Biochem. Biophys. Res. Commun. 141:229-237(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3036131; DOI=10.1016/0006-291x(87)91345-3;
RA   Rhoads D.M., Zarlengo R.P., Tu C.-P.D.;
RT   "The basic glutathione S-transferases from human livers are products
RT   of separate genes.";
RL   Biochem. Biophys. Res. Commun. 145:474-481(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=3678589; DOI=10.1042/bst0150734;
RA   Tu C.-P.D., Qian B.;
RT   "Nucleotide sequence of the human liver glutathione S-transferase
RT   subunit 1 cDNA.";
RL   Biochem. Soc. Trans. 15:734-736(1987).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3031680; DOI=10.1073/pnas.84.8.2377;
RA   Board P.G., Webb G.C.;
RT   "Isolation of a cDNA clone and localization of human glutathione S-
RT   transferase 2 genes to chromosome band 6p12.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:2377-2381(1987).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1731620; DOI=10.1016/0003-9861(92)90035-u;
RA   Rozen F., Nguyen T., Pickett C.B.;
RT   "Isolation and characterization of a human glutathione S-transferase
RT   Ha1 subunit gene.";
RL   Arch. Biochem. Biophys. 292:589-593(1992).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1330133; DOI=10.1016/1046-5928(92)90060-a;
RA   Stenberg G., Bjornestedt R., Mannervik B.;
RT   "Heterologous expression of recombinant human glutathione transferase
RT   A1-1 from a hepatoma cell line.";
RL   Protein Expr. Purif. 3:80-84(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Chen P., Zhang C., Xie D., Wu Y., Han L., Chen L.;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   NUCLEOTIDE SEQUENCE OF 1-9.
RX   PubMed=3138230;
RA   Chow N.W., Whang-Peng J., Kao-Shan C.S., Tam M.F., Lai H.-C.J.,
RA   Tu C.-P.D.;
RT   "Human glutathione S-transferases. The Ha multigene family encodes
RT   products of different but overlapping substrate specificities.";
RL   J. Biol. Chem. 263:12797-12800(1988).
RN   [12]
RP   PROTEIN SEQUENCE OF 2-170; 188-195 AND 209-222.
RX   PubMed=8431482; DOI=10.1016/0167-4838(93)90234-i;
RA   Ahmad H., Singhal S.S., Saxena M., Awasthi Y.C.;
RT   "Characterization of two novel subunits of the alpha-class glutathione
RT   S-transferases of human liver.";
RL   Biochim. Biophys. Acta 1161:333-336(1993).
RN   [13]
RP   PROTEIN SEQUENCE OF 16-36; 63-155 AND 208-212.
RX   PubMed=2604726; DOI=10.1042/bj2640437;
RA   Hayes J.D., Kerr L.A., Cronshaw A.D.;
RT   "Evidence that glutathione S-transferases B1B1 and B2B2 are the
RT   products of separate genes and that their expression in human liver is
RT   subject to inter-individual variation. Molecular relationships between
RT   the B1 and B2 subunits and other alpha class glutathione S-
RT   transferases.";
RL   Biochem. J. 264:437-445(1989).
RN   [14]
RP   PROTEIN SEQUENCE OF 200-222.
RX   PubMed=2018473; DOI=10.1042/bj2750171;
RA   Board P.G., Mannervik B.;
RT   "The contribution of the C-terminal sequence to the catalytic activity
RT   of GST2, a human alpha-class glutathione transferase.";
RL   Biochem. J. 275:171-174(1991).
RN   [15]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9084911; DOI=10.1021/tx9601770;
RA   Bogaards J.J., Venekamp J.C., van Bladeren P.J.;
RT   "Stereoselective conjugation of prostaglandin A2 and prostaglandin J2
RT   with glutathione, catalyzed by the human glutathione S-transferases
RT   A1-1, A2-2, M1a-1a, and P1-1.";
RL   Chem. Res. Toxicol. 10:310-317(1997).
RN   [16]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, AND MUTAGENESIS OF TYR-9.
RX   PubMed=11152686; DOI=10.1074/jbc.m009146200;
RA   Pettersson P.L., Mannervik B.;
RT   "The role of glutathione in the isomerization of delta 5-androstene-
RT   3,17-dione catalyzed by human glutathione transferase A1-1.";
RL   J. Biol. Chem. 276:11698-11704(2001).
RN   [17]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16624487; DOI=10.1016/j.bbagen.2006.02.020;
RA   Seeley S.K., Poposki J.A., Maksimchuk J., Tebbe J., Gaudreau J.,
RA   Mannervik B., Bull A.W.;
RT   "Metabolism of oxidized linoleic acid by glutathione transferases:
RT   peroxidase activity toward 13-hydroperoxyoctadecadienoic acid.";
RL   Biochim. Biophys. Acta 1760:1064-1070(2006).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH
RP   S-BENZYL-GLUTATHIONE, AND SUBUNIT.
RX   PubMed=8331657; DOI=10.1006/jmbi.1993.1376;
RA   Sinning I., Kleywegt G.J., Cowan S.W., Reinemer P., Dirr H.W.,
RA   Huber R., Gilliland G.L., Armstrong R.N., Ji X., Board P.G., Olin B.,
RA   Mannervik B., Jones T.A.;
RT   "Structure determination and refinement of human alpha class
RT   glutathione transferase A1-1, and a comparison with the Mu and Pi
RT   class enzymes.";
RL   J. Mol. Biol. 232:192-212(1993).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH ETHACRYNIC
RP   ACID AND GLUTATHIONE, AND SUBUNIT.
RX   PubMed=8591048; DOI=10.1016/s0969-2126(01)00206-4;
RA   Cameron A.D., Sinning I., L'Hermite G., Olin B., Board P.G.,
RA   Mannervik B., Jones T.A.;
RT   "Structural analysis of human alpha-class glutathione transferase A1-1
RT   in the apo-form and in complexes with ethacrynic acid and its
RT   glutathione conjugate.";
RL   Structure 3:717-727(1995).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEXES WITH S-HEXYL
RP   GLUTATHIONE, AND SUBUNIT.
RX   PubMed=12211029; DOI=10.1002/prot.10162;
RA   Le Trong I., Stenkamp R.E., Ibarra C., Atkins W.M., Adman E.T.;
RT   "1.3-A resolution structure of human glutathione S-transferase with S-
RT   hexyl glutathione bound reveals possible extended ligandin binding
RT   site.";
RL   Proteins 48:618-627(2002).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEX WITH
RP   S-BENZYLGLUTATHIONE, AND MUTAGENESIS OF ALA-216.
RX   PubMed=15333749; DOI=10.1073/pnas.0403045101;
RA   Hederos S., Broo K.S., Jakobsson E., Kleywegt G.J., Mannervik B.,
RA   Baltzer L.;
RT   "Incorporation of a single His residue by rational design enables
RT   thiol-ester hydrolysis by human glutathione transferase A1-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13163-13167(2004).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF MUTANT ALA-219 IN COMPLEX
RP   WITH S-HEXYLGLUTATHIONE.
RX   PubMed=15893769; DOI=10.1016/j.jmb.2005.04.025;
RA   Kuhnert D.C., Sayed Y., Mosebi S., Sayed M., Sewell T., Dirr H.W.;
RT   "Tertiary interactions stabilise the C-terminal region of human
RT   glutathione transferase A1-1: a crystallographic and calorimetric
RT   study.";
RL   J. Mol. Biol. 349:825-838(2005).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP   AND SUBUNIT.
RX   PubMed=16421451; DOI=10.1107/s0907444905039296;
RA   Grahn E., Novotny M., Jakobsson E., Gustafsson A., Grehn L., Olin B.,
RA   Madsen D., Wahlberg M., Mannervik B., Kleywegt G.J.;
RT   "New crystal structures of human glutathione transferase A1-1 shed
RT   light on glutathione binding and the conformation of the C-terminal
RT   helix.";
RL   Acta Crystallogr. D 62:197-207(2006).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 1-210 IN COMPLEX WITH
RP   GLUTATHIONE.
RX   PubMed=19618965; DOI=10.1021/bi900895b;
RA   Balogh L.M., Le Trong I., Kripps K.A., Tars K., Stenkamp R.E.,
RA   Mannervik B., Atkins W.M.;
RT   "Structural analysis of a glutathione transferase A1-1 mutant tailored
RT   for high catalytic efficiency with toxic alkenals.";
RL   Biochemistry 48:7698-7704(2009).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANTS ALA-71 AND VAL-71 IN
RP   COMPLEX WITH S-HEXYLGLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, AND
RP   MUTAGENESIS OF ILE-71.
RX   PubMed=20606271; DOI=10.1107/s1744309110019135;
RA   Achilonu I., Gildenhuys S., Fisher L., Burke J., Fanucchi S.,
RA   Sewell B.T., Fernandes M., Dirr H.W.;
RT   "The role of a topologically conserved isoleucine in glutathione
RT   transferase structure, stability and function.";
RL   Acta Crystallogr. F 66:776-780(2010).
CC   -!- FUNCTION: Glutathione S-transferase that catalyzes the
CC       nucleophilic attack of the sulfur atom of glutathione on the
CC       electrophilic groups of a wide range of exogenous and endogenous
CC       compounds (Probable). Involved in the formation of glutathione
CC       conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2
CC       (PGJ2) (PubMed:9084911). It also catalyzes the isomerization of
CC       D5-androstene-3,17-dione (AD) into D4-androstene-3,17-dione and
CC       may therefore play an important role in hormone biosynthesis
CC       (PubMed:11152686). Through its glutathione-dependent peroxidase
CC       activity toward the fatty acid hydroperoxide (13S)-hydroperoxy-
CC       (9Z,11E)-octadecadienoate/13-HPODE it is also involved in the
CC       metabolism of oxidized linoleic acid (PubMed:16624487).
CC       {ECO:0000269|PubMed:11152686, ECO:0000269|PubMed:16624487,
CC       ECO:0000269|PubMed:9084911, ECO:0000305|PubMed:20606271}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000269|PubMed:20606271};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC         Evidence={ECO:0000305|PubMed:20606271};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(R)-
CC         glutathione; Xref=Rhea:RHEA:50796, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:133370, ChEBI:CHEBI:133768;
CC         Evidence={ECO:0000269|PubMed:9084911};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50797;
CC         Evidence={ECO:0000305|PubMed:9084911};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-
CC         glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:133396, ChEBI:CHEBI:133771;
CC         Evidence={ECO:0000269|PubMed:9084911};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805;
CC         Evidence={ECO:0000305|PubMed:9084911};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2
CC         glutathione = (13S)-hydroxy-(9Z,11E)-octadecadienoate +
CC         glutathione disulfide + H2O; Xref=Rhea:RHEA:48888,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57466, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:58297, ChEBI:CHEBI:90850;
CC         Evidence={ECO:0000269|PubMed:16624487};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889;
CC         Evidence={ECO:0000305|PubMed:16624487};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione;
CC         Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865;
CC         Evidence={ECO:0000269|PubMed:11152686};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937;
CC         Evidence={ECO:0000305|PubMed:11152686};
CC   -!- ACTIVITY REGULATION: The isomerase activity is inhibited by S-
CC       methylglutathione (GSMe). {ECO:0000269|PubMed:11152686}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=160 uM for prostaglandin A2 (at pH 7.0 and 37 degrees
CC         Celsius) {ECO:0000269|PubMed:9084911};
CC         KM=160 uM for glutathione (at pH 8.0)
CC         {ECO:0000269|PubMed:11152686};
CC         KM=58 uM for androst-5-ene-3,17-dione (at pH 8.0)
CC         {ECO:0000269|PubMed:11152686};
CC         Vmax=121 nmol/min/mg enzyme for the formation of the
CC         glutathione-S-conjugate of prostaglandin A2 (at pH 7.0 and 37
CC         degrees Celsius) {ECO:0000269|PubMed:9084911};
CC         Vmax=40 umol/min/mg enzyme for the isomerization of androst-5-
CC         ene-3,17-dione (at pH 8.0) {ECO:0000269|PubMed:11152686};
CC         Note=kcat is 29.3 sec(-1) for the isomerization of androst-5-
CC         ene-3,17-dione. {ECO:0000269|PubMed:11152686};
CC       pH dependence:
CC         Optimum pH is 8.0 for the isomerization of androst-5-ene-3,17-
CC         dione. {ECO:0000269|PubMed:11152686};
CC   -!- SUBUNIT: Homodimer or heterodimer of GSTA1 and GSTA2.
CC       {ECO:0000269|PubMed:12211029, ECO:0000269|PubMed:15333749,
CC       ECO:0000269|PubMed:15893769, ECO:0000269|PubMed:16421451,
CC       ECO:0000269|PubMed:19618965, ECO:0000269|PubMed:20606271,
CC       ECO:0000269|PubMed:8331657, ECO:0000269|PubMed:8591048}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Liver.
CC   -!- DOMAIN: The C-terminal domain may form a component of the
CC       hydrophobic substrate-binding site, but in contrast appears not to
CC       be directly involved in GSH binding and is not absolutely
CC       essential for catalytic activity.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000305}.
DR   EMBL; M15872; AAA70226.1; -; mRNA.
DR   EMBL; M21758; AAA52615.1; -; mRNA.
DR   EMBL; M25627; AAA36174.1; -; mRNA.
DR   EMBL; M14777; AAA52618.1; -; mRNA.
DR   EMBL; S76235; AAB20973.1; -; Genomic_DNA.
DR   EMBL; S76221; AAB20973.1; JOINED; Genomic_DNA.
DR   EMBL; S76223; AAB20973.1; JOINED; Genomic_DNA.
DR   EMBL; S76225; AAB20973.1; JOINED; Genomic_DNA.
DR   EMBL; S76228; AAB20973.1; JOINED; Genomic_DNA.
DR   EMBL; S76232; AAB20973.1; JOINED; Genomic_DNA.
DR   EMBL; S49975; AAB24012.1; -; mRNA.
DR   EMBL; AY532928; AAT06769.1; -; mRNA.
DR   EMBL; CR407656; CAG28584.1; -; mRNA.
DR   EMBL; AL590363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX04385.1; -; Genomic_DNA.
DR   EMBL; BC053578; AAH53578.1; -; mRNA.
DR   EMBL; BC110891; AAI10892.1; -; mRNA.
DR   CCDS; CCDS4945.1; -.
DR   PIR; A25909; A56666.
DR   PIR; S29657; S29657.
DR   RefSeq; NP_665683.1; NM_145740.4.
DR   PDB; 1GSD; X-ray; 2.50 A; A/B/C/D=2-222.
DR   PDB; 1GSE; X-ray; 2.00 A; A/B=2-222.
DR   PDB; 1GSF; X-ray; 2.70 A; A/B/C/D=2-222.
DR   PDB; 1GUH; X-ray; 2.60 A; A/B/C/D=2-222.
DR   PDB; 1K3L; X-ray; 1.50 A; A/B=2-222.
DR   PDB; 1K3O; X-ray; 1.80 A; A/B=2-222.
DR   PDB; 1K3Y; X-ray; 1.30 A; A/B=2-222.
DR   PDB; 1LBK; X-ray; 1.86 A; A/B=208-213.
DR   PDB; 1PKW; X-ray; 2.00 A; A/B=1-222.
DR   PDB; 1PKZ; X-ray; 2.10 A; A/B=1-222.
DR   PDB; 1PL1; X-ray; 1.75 A; A/B=1-222.
DR   PDB; 1PL2; X-ray; 1.80 A; A/B=1-222.
DR   PDB; 1USB; X-ray; 2.07 A; A/B=2-222.
DR   PDB; 1XWG; X-ray; 1.85 A; A/B=2-222.
DR   PDB; 1YDK; X-ray; 1.95 A; A/B=1-222.
DR   PDB; 2R3X; X-ray; 1.80 A; A/B=1-222.
DR   PDB; 2R6K; X-ray; 2.51 A; A/B=1-222.
DR   PDB; 3I69; X-ray; 2.38 A; A/B/C/D/E/F/G/H=1-222.
DR   PDB; 3I6A; X-ray; 1.98 A; A/B/C/D/E/F/G/H=1-222.
DR   PDB; 3IK9; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-222.
DR   PDB; 3KTL; X-ray; 1.75 A; A/B=2-222.
DR   PDB; 3L0H; X-ray; 2.13 A; A/B=1-222.
DR   PDB; 3Q74; X-ray; 1.79 A; A/B=2-222.
DR   PDB; 3U6V; X-ray; 2.20 A; A/B=1-222.
DR   PDB; 3ZFB; X-ray; 1.86 A; A/B=1-222.
DR   PDB; 3ZFL; X-ray; 1.88 A; A/B=1-222.
DR   PDB; 4HJ2; X-ray; 2.10 A; A/B=4-220.
DR   PDB; 5JCU; X-ray; 1.93 A; A/B/C/D=2-222.
DR   PDB; 5LCZ; X-ray; 2.33 A; A/B=1-100, A/B=201-222.
DR   PDB; 5LD0; X-ray; 1.60 A; A=1-85, A=214-222.
DR   PDB; 6ATO; X-ray; 1.55 A; A/B=2-222.
DR   PDB; 6ATP; X-ray; 1.70 A; A/B=2-222.
DR   PDB; 6ATQ; X-ray; 2.00 A; A/B=2-222.
DR   PDB; 6ATR; X-ray; 1.29 A; A/B=2-222.
DR   PDBsum; 1GSD; -.
DR   PDBsum; 1GSE; -.
DR   PDBsum; 1GSF; -.
DR   PDBsum; 1GUH; -.
DR   PDBsum; 1K3L; -.
DR   PDBsum; 1K3O; -.
DR   PDBsum; 1K3Y; -.
DR   PDBsum; 1LBK; -.
DR   PDBsum; 1PKW; -.
DR   PDBsum; 1PKZ; -.
DR   PDBsum; 1PL1; -.
DR   PDBsum; 1PL2; -.
DR   PDBsum; 1USB; -.
DR   PDBsum; 1XWG; -.
DR   PDBsum; 1YDK; -.
DR   PDBsum; 2R3X; -.
DR   PDBsum; 2R6K; -.
DR   PDBsum; 3I69; -.
DR   PDBsum; 3I6A; -.
DR   PDBsum; 3IK9; -.
DR   PDBsum; 3KTL; -.
DR   PDBsum; 3L0H; -.
DR   PDBsum; 3Q74; -.
DR   PDBsum; 3U6V; -.
DR   PDBsum; 3ZFB; -.
DR   PDBsum; 3ZFL; -.
DR   PDBsum; 4HJ2; -.
DR   PDBsum; 5JCU; -.
DR   PDBsum; 5LCZ; -.
DR   PDBsum; 5LD0; -.
DR   PDBsum; 6ATO; -.
DR   PDBsum; 6ATP; -.
DR   PDBsum; 6ATQ; -.
DR   PDBsum; 6ATR; -.
DR   SMR; P08263; -.
DR   BioGrid; 109193; 15.
DR   IntAct; P08263; 12.
DR   STRING; 9606.ENSP00000335620; -.
DR   BindingDB; P08263; -.
DR   ChEMBL; CHEMBL3409; -.
DR   DrugBank; DB02486; 2-Hydroxyethyl Disulfide.
DR   DrugBank; DB00993; Azathioprine.
DR   DrugBank; DB01008; Busulfan.
DR   DrugBank; DB11672; Curcumin.
DR   DrugBank; DB14635; Curcumin sulfate.
DR   DrugBank; DB00143; Glutathione.
DR   DrugBank; DB03003; Glutathione Sulfonic Acid.
DR   DrugBank; DB13014; Hypericin.
DR   DrugBank; DB02943; N-(4-Aminobutanoyl)-S-(4-Methoxybenzyl)-L-Cysteinylglycine.
DR   DrugBank; DB03602; S-Benzyl-Glutathione.
DR   DrugBank; DB04132; S-Hexylglutathione.
DR   DrugBank; DB01915; S-Hydroxycysteine.
DR   DrugCentral; P08263; -.
DR   SwissLipids; SLP:000001476; -.
DR   iPTMnet; P08263; -.
DR   PhosphoSitePlus; P08263; -.
DR   BioMuta; GSTA1; -.
DR   DMDM; 121730; -.
DR   REPRODUCTION-2DPAGE; IPI00657682; -.
DR   jPOST; P08263; -.
DR   MassIVE; P08263; -.
DR   MaxQB; P08263; -.
DR   PaxDb; P08263; -.
DR   PeptideAtlas; P08263; -.
DR   PRIDE; P08263; -.
DR   ProteomicsDB; 12637; -.
DR   ProteomicsDB; 52103; -.
DR   DNASU; 2938; -.
DR   Ensembl; ENST00000334575; ENSP00000335620; ENSG00000243955.
DR   GeneID; 2938; -.
DR   KEGG; hsa:2938; -.
DR   UCSC; uc003paz.4; human.
DR   CTD; 2938; -.
DR   DisGeNET; 2938; -.
DR   GeneCards; GSTA1; -.
DR   HGNC; HGNC:4626; GSTA1.
DR   HPA; HPA004342; -.
DR   HPA; HPA048934; -.
DR   HPA; HPA053817; -.
DR   MIM; 138359; gene.
DR   neXtProt; NX_P08263; -.
DR   OpenTargets; ENSG00000243955; -.
DR   PharmGKB; PA29016; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   eggNOG; ENOG4111VAU; LUCA.
DR   GeneTree; ENSGT00940000164034; -.
DR   HOGENOM; HOG000115734; -.
DR   InParanoid; P08263; -.
DR   KO; K00799; -.
DR   OMA; ILMFPFL; -.
DR   OrthoDB; 1162336at2759; -.
DR   PhylomeDB; P08263; -.
DR   TreeFam; TF105321; -.
DR   BioCyc; MetaCyc:G66-32542-MONOMER; -.
DR   BRENDA; 2.5.1.18; 2681.
DR   Reactome; R-HSA-156590; Glutathione conjugation.
DR   SABIO-RK; P08263; -.
DR   SIGNOR; P08263; -.
DR   ChiTaRS; GSTA1; human.
DR   EvolutionaryTrace; P08263; -.
DR   GeneWiki; Glutathione_S-transferase_A1; -.
DR   GenomeRNAi; 2938; -.
DR   Pharos; P08263; -.
DR   PRO; PR:P08263; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000243955; Expressed in 143 organ(s), highest expression level in nephron tubule.
DR   ExpressionAtlas; P08263; baseline and differential.
DR   Genevisible; P08263; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IDA:BHF-UCL.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR   GO; GO:0004769; F:steroid delta-isomerase activity; IDA:UniProtKB.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR   GO; GO:1901687; P:glutathione derivative biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
DR   GO; GO:0043651; P:linoleic acid metabolic process; IDA:BHF-UCL.
DR   GO; GO:0006693; P:prostaglandin metabolic process; IDA:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR003080; GST_alpha.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Isomerase; Oxidoreductase; Peroxidase;
KW   Polymorphism; Reference proteome; Transferase.
FT   CHAIN         1    222       Glutathione S-transferase A1.
FT                                /FTId=PRO_0000423203.
FT   INIT_MET      1      1       Removed; alternate.
FT                                {ECO:0000250|UniProtKB:P30115,
FT                                ECO:0000269|PubMed:8431482}.
FT   CHAIN         2    222       Glutathione S-transferase A1, N-
FT                                terminally processed.
FT                                /FTId=PRO_0000185783.
FT   DOMAIN        3     83       GST N-terminal.
FT   DOMAIN       85    207       GST C-terminal.
FT   REGION       54     55       Glutathione binding.
FT                                {ECO:0000269|PubMed:16421451,
FT                                ECO:0000269|PubMed:19618965}.
FT   REGION       67     68       Glutathione binding.
FT                                {ECO:0000269|PubMed:16421451,
FT                                ECO:0000269|PubMed:19618965}.
FT   BINDING       9      9       Glutathione.
FT                                {ECO:0000269|PubMed:16421451,
FT                                ECO:0000269|PubMed:19618965}.
FT   BINDING      45     45       Glutathione.
FT                                {ECO:0000269|PubMed:16421451,
FT                                ECO:0000269|PubMed:19618965}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:P80894}.
FT   MOD_RES       2      2       N-acetylalanine; in Glutathione S-
FT                                transferase A1, N-terminally processed.
FT                                {ECO:0000250|UniProtKB:P30115}.
FT   MOD_RES       4      4       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P30115}.
FT   VARIANT      19     19       T -> I (in dbSNP:rs1051578).
FT                                /FTId=VAR_033978.
FT   VARIANT     113    113       P -> Q (in dbSNP:rs1051745).
FT                                /FTId=VAR_049482.
FT   VARIANT     117    117       K -> Q (in dbSNP:rs1051757).
FT                                /FTId=VAR_049483.
FT   MUTAGEN       9      9       Y->F: Decreased isomerase activity.
FT                                {ECO:0000269|PubMed:11152686}.
FT   MUTAGEN      71     71       I->A,V: No significant effect on enzyme
FT                                activity. Reduces protein stability.
FT                                {ECO:0000269|PubMed:20606271}.
FT   MUTAGEN     216    216       A->H: Confers ability to hydrolyze S-
FT                                glutathionyl benzoate to glutathione and
FT                                benzoic acid.
FT                                {ECO:0000269|PubMed:15333749}.
FT   CONFLICT     18     18       S -> C (in Ref. 3; AAA36174).
FT                                {ECO:0000305}.
FT   CONFLICT     51     51       M -> T (in Ref. 7; AAT06769).
FT                                {ECO:0000305}.
FT   CONFLICT     56     58       PMV -> AML (in Ref. 3; AAA36174).
FT                                {ECO:0000305}.
FT   CONFLICT    212    212       S -> L (in Ref. 13; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    216    216       A -> S (in Ref. 12; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND        6     13       {ECO:0000244|PDB:6ATR}.
FT   TURN         14     16       {ECO:0000244|PDB:6ATR}.
FT   HELIX        17     25       {ECO:0000244|PDB:6ATR}.
FT   STRAND       31     35       {ECO:0000244|PDB:6ATR}.
FT   HELIX        38     46       {ECO:0000244|PDB:6ATR}.
FT   STRAND       57     60       {ECO:0000244|PDB:6ATR}.
FT   STRAND       63     67       {ECO:0000244|PDB:6ATR}.
FT   HELIX        68     78       {ECO:0000244|PDB:6ATR}.
FT   HELIX        86    108       {ECO:0000244|PDB:6ATR}.
FT   HELIX       109    111       {ECO:0000244|PDB:6ATR}.
FT   HELIX       114    130       {ECO:0000244|PDB:6ATR}.
FT   HELIX       132    143       {ECO:0000244|PDB:6ATR}.
FT   STRAND      146    149       {ECO:0000244|PDB:6ATR}.
FT   HELIX       155    170       {ECO:0000244|PDB:6ATR}.
FT   TURN        172    177       {ECO:0000244|PDB:6ATR}.
FT   HELIX       179    190       {ECO:0000244|PDB:6ATR}.
FT   HELIX       192    198       {ECO:0000244|PDB:6ATR}.
FT   HELIX       210    220       {ECO:0000244|PDB:6ATR}.
SQ   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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