GSTA5_HUMAN
ID GSTA5_HUMAN Reviewed; 222 AA.
AC Q7RTV2; Q5SZC2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Glutathione S-transferase A5;
DE EC=2.5.1.18;
DE AltName: Full=GST class-alpha member 5;
DE AltName: Full=Glutathione S-transferase A5-5;
GN Name=GSTA5;
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 [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 [2]
RP IDENTIFICATION.
RX PubMed=12042665; DOI=10.1097/00008571-200206000-00003;
RA Morel F., Rauch C., Coles B., Ferrec E.L., Guillouzo A.;
RT "The human glutathione transferase alpha locus: genomic organization of the
RT gene cluster and functional characterization of the genetic polymorphism in
RT the hGSTA1 promoter.";
RL Pharmacogenetics 12:277-286(2002).
RN [3]
RP CATALYTIC ACTIVITY.
RX PubMed=19664689; DOI=10.1016/j.bbagen.2009.07.025;
RA Singh S.P., Zimniak L., Zimniak P.;
RT "The human hGSTA5 gene encodes an enzymatically active protein.";
RL Biochim. Biophys. Acta 1800:16-22(2010).
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:19664689};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q7RTV2; P09210: GSTA2; NbExp=4; IntAct=EBI-13328621, EBI-10196201;
CC Q7RTV2; Q8N6V9: TEX9; NbExp=3; IntAct=EBI-13328621, EBI-746341;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expression not detected.
CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {ECO:0000305}.
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DR EMBL; AL590363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK000212; DAA00071.1; -; Genomic_DNA.
DR CCDS; CCDS4946.1; -.
DR RefSeq; NP_714543.1; NM_153699.1.
DR AlphaFoldDB; Q7RTV2; -.
DR SMR; Q7RTV2; -.
DR BioGRID; 128713; 8.
DR IntAct; Q7RTV2; 2.
DR STRING; 9606.ENSP00000360028; -.
DR DrugBank; DB00143; Glutathione.
DR iPTMnet; Q7RTV2; -.
DR PhosphoSitePlus; Q7RTV2; -.
DR BioMuta; GSTA5; -.
DR DMDM; 50400409; -.
DR jPOST; Q7RTV2; -.
DR MassIVE; Q7RTV2; -.
DR MaxQB; Q7RTV2; -.
DR PaxDb; Q7RTV2; -.
DR PeptideAtlas; Q7RTV2; -.
DR PRIDE; Q7RTV2; -.
DR ProteomicsDB; 68912; -.
DR Antibodypedia; 30946; 74 antibodies from 19 providers.
DR DNASU; 221357; -.
DR Ensembl; ENST00000370989.6; ENSP00000360028.1; ENSG00000182793.12.
DR GeneID; 221357; -.
DR KEGG; hsa:221357; -.
DR UCSC; uc003pba.2; human.
DR CTD; 221357; -.
DR DisGeNET; 221357; -.
DR GeneCards; GSTA5; -.
DR HGNC; HGNC:19662; GSTA5.
DR HPA; ENSG00000182793; Not detected.
DR MIM; 607605; gene.
DR neXtProt; NX_Q7RTV2; -.
DR OpenTargets; ENSG00000182793; -.
DR PharmGKB; PA134962856; -.
DR VEuPathDB; HostDB:ENSG00000182793; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000163367; -.
DR HOGENOM; CLU_039475_4_0_1; -.
DR InParanoid; Q7RTV2; -.
DR OMA; HLVEMIY; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; Q7RTV2; -.
DR TreeFam; TF105321; -.
DR BRENDA; 2.5.1.18; 2681.
DR PathwayCommons; Q7RTV2; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR SignaLink; Q7RTV2; -.
DR BioGRID-ORCS; 221357; 53 hits in 1036 CRISPR screens.
DR GenomeRNAi; 221357; -.
DR Pharos; Q7RTV2; Tbio.
DR PRO; PR:Q7RTV2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q7RTV2; protein.
DR Bgee; ENSG00000182793; Expressed in olfactory segment of nasal mucosa and 11 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISS: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; 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 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 Acetylation; Cytoplasm; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P30115"
FT CHAIN 2..222
FT /note="Glutathione S-transferase A5"
FT /id="PRO_0000185787"
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 45
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08263"
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P30115"
FT MOD_RES 4
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30115"
FT VARIANT 55
FT /note="V -> I (in dbSNP:rs2397118)"
FT /id="VAR_024483"
SQ SEQUENCE 222 AA; 25722 MW; 6DFCECF202F2D898 CRC64;
MAEKPKLHYS NARGSMESIR WLLAAAGVEL EEKFLESAED LDKLRNDGSL LFQQVPMVEI
DGMKLVQTRA ILNYIASKYN LYGKDMKERA LIDMYTEGIV DLTEMILLLL ICQPEERDAK
TALVKEKIKN RYFPAFEKVL KSHRQDYLVG NKLSWADIHL VELFYYVEEL DSSLISSFPL
LKALKTRISN LPTVKKFLQP GSQRKPPMDE KSLEEARKIF RF
