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   27-MAR-2024, entry version 161.
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; 3.
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; 9606-ENSP00000360028; -.
DR   PeptideAtlas; Q7RTV2; -.
DR   ProteomicsDB; 68912; -.
DR   Antibodypedia; 30946; 95 antibodies from 19 providers.
DR   DNASU; 221357; -.
DR   Ensembl; ENST00000370989.6; ENSP00000360028.1; ENSG00000182793.12.
DR   GeneID; 221357; -.
DR   KEGG; hsa:221357; -.
DR   MANE-Select; ENST00000370989.7; ENSP00000360028.1; NM_153699.3; NP_714543.1.
DR   UCSC; uc003pba.2; human.
DR   AGR; HGNC:19662; -.
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; WIDRWAN; -.
DR   OrthoDB; 3412208at2759; -.
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 1116 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 male germ line stem cell (sensu Vertebrata) in testis and 13 other cell types or 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   CDD; cd03208; GST_C_Alpha; 1.
DR   CDD; cd03077; GST_N_Alpha; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF245; GLUTATHIONE S-TRANSFERASE A5; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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
//