GSTA4_HUMAN
ID GSTA4_HUMAN Reviewed; 222 AA.
AC O15217; B2RD15; Q5T7Q8; Q6P4G1; Q9BX18; Q9H414;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Glutathione S-transferase A4;
DE EC=2.5.1.18;
DE AltName: Full=GST class-alpha member 4;
DE AltName: Full=Glutathione S-transferase A4-4;
GN Name=GSTA4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9461507; DOI=10.1042/bj3300175;
RA Hubatsch I., Ridderstrom M., Mannervik B.;
RT "Human glutathione transferase A4-4: an alpha class enzyme with high
RT catalytic efficiency in the conjugation of 4-hydroxynonenal and other
RT genotoxic products of lipid peroxidation.";
RL Biochem. J. 330:175-179(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9480897; DOI=10.1042/bj3300827;
RA Board P.G.;
RT "Identification of cDNAs encoding two human alpha class glutathione
RT transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-
RT 4.";
RL Biochem. J. 330:827-831(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9587421; DOI=10.1006/abbi.1998.0608;
RA Liu S., Stoesz S.P., Pickett C.B.;
RT "Identification of a novel human glutathione S-transferase using
RT bioinformatics.";
RL Arch. Biochem. Biophys. 352:306-313(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart, Pancreas, and Skeletal muscle;
RA Piper J.T., Awasthi Y.C.;
RT "The 4-HNE metabolizing GST isozyme hGSTA4-4 is expressed in human heart,
RT pancreas, and skeletal muscle.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9820822; DOI=10.1042/bj3360437;
RA Desmots F., Rauch C., Henry C., Guillouzo A., Morel F.;
RT "Genomic organization, 5'-flanking region and chromosomal localization of
RT the human glutathione transferase A4 gene.";
RL Biochem. J. 336:437-442(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-100 AND ALA-163.
RG NIEHS SNPs program;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Esophageal carcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Uterus;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH 2-IODOBENZYL
RP GLUTATHIONE, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF TYR-212, AND
RP SUBUNIT.
RX PubMed=10329152; DOI=10.1006/jmbi.1999.2697;
RA Bruns C.M., Hubatsch I., Ridderstroem M., Mannervik B., Tainer J.A.;
RT "Human glutathione transferase A4-4 crystal structures and mutagenesis
RT reveal the basis of high catalytic efficiency with toxic lipid peroxidation
RT products.";
RL J. Mol. Biol. 288:427-439(1999).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF TYR-9.
RX PubMed=20085333; DOI=10.1021/bi902038u;
RA Balogh L.M., Le Trong I., Kripps K.A., Shireman L.M., Stenkamp R.E.,
RA Zhang W., Mannervik B., Atkins W.M.;
RT "Substrate specificity combined with stereopromiscuity in glutathione
RT transferase A4-4-dependent metabolism of 4-hydroxynonenal.";
RL Biochemistry 49:1541-1548(2010).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. This isozyme has a
CC high catalytic efficiency with 4-hydroxyalkenals such as 4-
CC hydroxynonenal (4-HNE). {ECO:0000269|PubMed:10329152,
CC ECO:0000269|PubMed:20085333}.
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:10329152, ECO:0000269|PubMed:20085333};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10329152,
CC ECO:0000269|PubMed:20085333}.
CC -!- INTERACTION:
CC O15217; Q96LR7: C2orf50; NbExp=6; IntAct=EBI-752440, EBI-10290932;
CC O15217; O95995: GAS8; NbExp=3; IntAct=EBI-752440, EBI-1052570;
CC O15217; P09210: GSTA2; NbExp=11; IntAct=EBI-752440, EBI-10196201;
CC O15217; O15217: GSTA4; NbExp=5; IntAct=EBI-752440, EBI-752440;
CC O15217; O15116: LSM1; NbExp=3; IntAct=EBI-752440, EBI-347619;
CC O15217; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-752440, EBI-741158;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15217-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15217-2; Sequence=VSP_056473;
CC -!- TISSUE SPECIFICITY: Expressed at a high level in brain, placenta, and
CC skeletal muscle and much lower in lung and liver.
CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/gsta4/";
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DR EMBL; Y13047; CAA73482.1; -; mRNA.
DR EMBL; AF020918; AAD04711.1; -; mRNA.
DR EMBL; AF025887; AAC39695.1; -; mRNA.
DR EMBL; AF125271; AAD27704.1; -; mRNA.
DR EMBL; AF125272; AAD27705.1; -; mRNA.
DR EMBL; AF125273; AAD27706.1; -; mRNA.
DR EMBL; AF050059; AAC72706.1; -; Genomic_DNA.
DR EMBL; AF050054; AAC72706.1; JOINED; Genomic_DNA.
DR EMBL; AF050055; AAC72706.1; JOINED; Genomic_DNA.
DR EMBL; AF050056; AAC72706.1; JOINED; Genomic_DNA.
DR EMBL; AF050057; AAC72706.1; JOINED; Genomic_DNA.
DR EMBL; AF050058; AAC72706.1; JOINED; Genomic_DNA.
DR EMBL; AY878121; AAW56075.1; -; Genomic_DNA.
DR EMBL; AK315369; BAG37762.1; -; mRNA.
DR EMBL; CR749474; CAH18304.1; -; mRNA.
DR EMBL; AL121969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04393.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04394.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04395.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04396.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04397.1; -; Genomic_DNA.
DR EMBL; BC015523; AAH15523.1; -; mRNA.
DR EMBL; BC063439; AAH63439.1; -; mRNA.
DR CCDS; CCDS4948.1; -. [O15217-1]
DR RefSeq; NP_001503.1; NM_001512.3. [O15217-1]
DR RefSeq; XP_005249092.1; XM_005249035.3. [O15217-1]
DR PDB; 1GUL; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-222.
DR PDB; 1GUM; X-ray; 3.00 A; A/B/C/D/E/F/G/H=1-222.
DR PDB; 3IK7; X-ray; 1.97 A; A/B/C/D=1-222.
DR PDBsum; 1GUL; -.
DR PDBsum; 1GUM; -.
DR PDBsum; 3IK7; -.
DR AlphaFoldDB; O15217; -.
DR SMR; O15217; -.
DR BioGRID; 109196; 24.
DR IntAct; O15217; 10.
DR MINT; O15217; -.
DR STRING; 9606.ENSP00000360002; -.
DR ChEMBL; CHEMBL4933; -.
DR DrugBank; DB00143; Glutathione.
DR iPTMnet; O15217; -.
DR PhosphoSitePlus; O15217; -.
DR BioMuta; GSTA4; -.
DR EPD; O15217; -.
DR MassIVE; O15217; -.
DR MaxQB; O15217; -.
DR PaxDb; O15217; -.
DR PeptideAtlas; O15217; -.
DR PRIDE; O15217; -.
DR ProteomicsDB; 48514; -. [O15217-1]
DR ProteomicsDB; 66976; -.
DR Antibodypedia; 17233; 319 antibodies from 30 providers.
DR DNASU; 2941; -.
DR Ensembl; ENST00000370959.1; ENSP00000359998.1; ENSG00000170899.11. [O15217-1]
DR Ensembl; ENST00000370960.5; ENSP00000359999.1; ENSG00000170899.11. [O15217-2]
DR Ensembl; ENST00000370963.9; ENSP00000360002.4; ENSG00000170899.11. [O15217-1]
DR GeneID; 2941; -.
DR KEGG; hsa:2941; -.
DR MANE-Select; ENST00000370963.9; ENSP00000360002.4; NM_001512.4; NP_001503.1.
DR UCSC; uc003pbf.4; human. [O15217-1]
DR CTD; 2941; -.
DR DisGeNET; 2941; -.
DR GeneCards; GSTA4; -.
DR HGNC; HGNC:4629; GSTA4.
DR HPA; ENSG00000170899; Tissue enhanced (adrenal).
DR MIM; 605450; gene.
DR neXtProt; NX_O15217; -.
DR OpenTargets; ENSG00000170899; -.
DR PharmGKB; PA29019; -.
DR VEuPathDB; HostDB:ENSG00000170899; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000162778; -.
DR HOGENOM; CLU_039475_4_0_1; -.
DR InParanoid; O15217; -.
DR OMA; TVYNVFM; -.
DR PhylomeDB; O15217; -.
DR TreeFam; TF105321; -.
DR BRENDA; 2.5.1.18; 2681.
DR PathwayCommons; O15217; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR SignaLink; O15217; -.
DR SIGNOR; O15217; -.
DR BioGRID-ORCS; 2941; 14 hits in 1076 CRISPR screens.
DR ChiTaRS; GSTA4; human.
DR EvolutionaryTrace; O15217; -.
DR GeneWiki; GSTA4; -.
DR GenomeRNAi; 2941; -.
DR Pharos; O15217; Tbio.
DR PRO; PR:O15217; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O15217; protein.
DR Bgee; ENSG00000170899; Expressed in adrenal tissue and 216 other tissues.
DR ExpressionAtlas; O15217; baseline and differential.
DR Genevisible; O15217; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
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; PF14497; GST_C_3; 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; Alternative splicing; Cytoplasm;
KW Reference proteome; Transferase.
FT CHAIN 1..222
FT /note="Glutathione S-transferase A4"
FT /id="PRO_0000185786"
FT DOMAIN 3..83
FT /note="GST N-terminal"
FT DOMAIN 85..208
FT /note="GST C-terminal"
FT BINDING 9
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P13745"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P30711"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P13745"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P14942"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_056473"
FT VARIANT 100
FT /note="L -> P (in dbSNP:rs45551133)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_022210"
FT VARIANT 163
FT /note="T -> A (in dbSNP:rs4147617)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_022211"
FT MUTAGEN 9
FT /note="Y->F: Reduces catalytic activity 70-fold."
FT /evidence="ECO:0000269|PubMed:20085333"
FT MUTAGEN 212
FT /note="Y->A,F,S: Strongly reduced activity towards 4-
FT hydroxynon-2-enal and 1-chloro-2,4-dinitrobenzene."
FT /evidence="ECO:0000269|PubMed:10329152"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:3IK7"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:3IK7"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:3IK7"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:3IK7"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:3IK7"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:3IK7"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:3IK7"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:3IK7"
FT HELIX 86..108
FT /evidence="ECO:0007829|PDB:3IK7"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3IK7"
FT HELIX 114..131
FT /evidence="ECO:0007829|PDB:3IK7"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:3IK7"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:3IK7"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:3IK7"
FT TURN 172..177
FT /evidence="ECO:0007829|PDB:3IK7"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:3IK7"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:3IK7"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1GUM"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:3IK7"
SQ SEQUENCE 222 AA; 25704 MW; 1BD98B41E413BB4E CRC64;
MAARPKLHYP NGRGRMESVR WVLAAAGVEF DEEFLETKEQ LYKLQDGNHL LFQQVPMVEI
DGMKLVQTRS ILHYIADKHN LFGKNLKERT LIDMYVEGTL DLLELLIMHP FLKPDDQQKE
VVNMAQKAII RYFPVFEKIL RGHGQSFLVG NQLSLADVIL LQTILALEEK IPNILSAFPF
LQEYTVKLSN IPTIKRFLEP GSKKKPPPDE IYVRTVYNIF RP
