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Protein

Glutathione S-transferase A3

Gene

GSTA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)-pregnene-3,20-dione, precursors to testosterone and progesterone, respectively.2 Publications

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

Kineticsi

  1. KM=23 µM for delta(5)-androstene-3,17-dione1 Publication
  1. Vmax=99 µmol/min/mg enzyme for delta(5)-androstene-3,17-dione isomerization1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91Glutathione2 Publications
Binding sitei45 – 451Glutathione2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.5.1.18. 2681.
5.3.3.1. 2681.
ReactomeiREACT_6926. Glutathione conjugation.
SABIO-RKQ16772.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase A3 (EC:2.5.1.18)
Alternative name(s):
GST class-alpha member 3
Glutathione S-transferase A3-3
Gene namesi
Name:GSTA3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:4628. GSTA3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29018.

Chemistry

DrugBankiDB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiGSTA3.
DMDMi21264437.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 222221Glutathione S-transferase A3PRO_0000185785Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei4 – 41N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ16772.
PaxDbiQ16772.
PRIDEiQ16772.

PTM databases

PhosphoSiteiQ16772.

Expressioni

Gene expression databases

BgeeiQ16772.
CleanExiHS_GSTA3.
ExpressionAtlasiQ16772. baseline and differential.
GenevestigatoriQ16772.

Organism-specific databases

HPAiHPA004342.
HPA048934.
HPA053817.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi109195. 4 interactions.
STRINGi9606.ENSP00000211122.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94Combined sources
Turni14 – 163Combined sources
Helixi17 – 259Combined sources
Beta strandi31 – 344Combined sources
Helixi38 – 469Combined sources
Beta strandi57 – 604Combined sources
Beta strandi63 – 675Combined sources
Helixi68 – 7811Combined sources
Helixi86 – 10823Combined sources
Helixi109 – 1113Combined sources
Helixi114 – 13017Combined sources
Helixi132 – 14312Combined sources
Beta strandi146 – 1494Combined sources
Helixi155 – 17016Combined sources
Turni172 – 1776Combined sources
Helixi179 – 19012Combined sources
Helixi192 – 1976Combined sources
Helixi210 – 22011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TDIX-ray2.40A/B1-222[»]
2VCVX-ray1.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-222[»]
ProteinModelPortaliQ16772.
SMRiQ16772. Positions 4-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16772.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 8381GST N-terminalAdd
BLAST
Domaini85 – 207123GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 552Glutathione binding
Regioni67 – 682Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Alpha family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiNOG266414.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiQ16772.
KOiK00799.
OMAiCPPAEKD.
PhylomeDBiQ16772.
TreeFamiTF105321.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q16772-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGKPKLHYF NGRGRMEPIR WLLAAAGVEF EEKFIGSAED LGKLRNDGSL
60 70 80 90 100
MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYTEGMA
110 120 130 140 150
DLNEMILLLP LCRPEEKDAK IALIKEKTKS RYFPAFEKVL QSHGQDYLVG
160 170 180 190 200
NKLSRADISL VELLYYVEEL DSSLISNFPL LKALKTRISN LPTVKKFLQP
210 220
GSPRKPPADA KALEEARKIF RF
Length:222
Mass (Da):25,302
Last modified:May 27, 2002 - v3
Checksum:i904AA17519B5343C
GO

Sequence cautioni

The sequence AAA74634.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAD04712.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631M → I in AAH20619 (PubMed:15489334).Curated
Sequence conflicti113 – 1142RP → PA in AAA74634 (PubMed:8307579).Curated
Sequence conflicti128 – 1281T → I in AAA74634 (PubMed:8307579).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361G → E.1 Publication
Corresponds to variant rs45504096 [ dbSNP | Ensembl ].
VAR_062276
Natural varianti71 – 711I → L.2 Publications
Corresponds to variant rs1052661 [ dbSNP | Ensembl ].
VAR_049484
Natural varianti73 – 731N → D.1 Publication
Corresponds to variant rs41273858 [ dbSNP | Ensembl ].
VAR_049485
Natural varianti113 – 1131R → Q.1 Publication
Corresponds to variant rs45602042 [ dbSNP | Ensembl ].
VAR_062277
Natural varianti208 – 2081A → T.1 Publication
Corresponds to variant rs45620832 [ dbSNP | Ensembl ].
VAR_062278

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13275
, L13270, L13271, L13272, L13273, L13274 Genomic DNA. Translation: AAA74634.1. Different initiation.
AF508266 mRNA. Translation: AAM33360.1.
DQ993361 Genomic DNA. Translation: ABI75350.1.
AL121969 Genomic DNA. Translation: CAC10389.1.
CH471081 Genomic DNA. Translation: EAX04391.1.
BC020619 mRNA. Translation: AAH20619.1.
AF020919 mRNA. Translation: AAD04712.1. Different initiation.
CCDSiCCDS4947.1.
PIRiA49365.
RefSeqiNP_000838.3. NM_000847.4.
UniGeneiHs.102484.

Genome annotation databases

EnsembliENST00000211122; ENSP00000211122; ENSG00000174156.
GeneIDi2940.
KEGGihsa:2940.
UCSCiuc003pbb.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13275
, L13270, L13271, L13272, L13273, L13274 Genomic DNA. Translation: AAA74634.1. Different initiation.
AF508266 mRNA. Translation: AAM33360.1.
DQ993361 Genomic DNA. Translation: ABI75350.1.
AL121969 Genomic DNA. Translation: CAC10389.1.
CH471081 Genomic DNA. Translation: EAX04391.1.
BC020619 mRNA. Translation: AAH20619.1.
AF020919 mRNA. Translation: AAD04712.1. Different initiation.
CCDSiCCDS4947.1.
PIRiA49365.
RefSeqiNP_000838.3. NM_000847.4.
UniGeneiHs.102484.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TDIX-ray2.40A/B1-222[»]
2VCVX-ray1.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P1-222[»]
ProteinModelPortaliQ16772.
SMRiQ16772. Positions 4-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109195. 4 interactions.
STRINGi9606.ENSP00000211122.

Chemistry

ChEMBLiCHEMBL4866.
DrugBankiDB00143. Glutathione.

PTM databases

PhosphoSiteiQ16772.

Polymorphism and mutation databases

BioMutaiGSTA3.
DMDMi21264437.

Proteomic databases

MaxQBiQ16772.
PaxDbiQ16772.
PRIDEiQ16772.

Protocols and materials databases

DNASUi2940.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000211122; ENSP00000211122; ENSG00000174156.
GeneIDi2940.
KEGGihsa:2940.
UCSCiuc003pbb.3. human.

Organism-specific databases

CTDi2940.
GeneCardsiGC06M052761.
HGNCiHGNC:4628. GSTA3.
HPAiHPA004342.
HPA048934.
HPA053817.
MIMi605449. gene.
neXtProtiNX_Q16772.
PharmGKBiPA29018.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG266414.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiQ16772.
KOiK00799.
OMAiCPPAEKD.
PhylomeDBiQ16772.
TreeFamiTF105321.

Enzyme and pathway databases

BRENDAi2.5.1.18. 2681.
5.3.3.1. 2681.
ReactomeiREACT_6926. Glutathione conjugation.
SABIO-RKQ16772.

Miscellaneous databases

EvolutionaryTraceiQ16772.
GeneWikiiGSTA3.
GenomeRNAii2940.
NextBioi11651.
PROiQ16772.
SOURCEiSearch...

Gene expression databases

BgeeiQ16772.
CleanExiHS_GSTA3.
ExpressionAtlasiQ16772. baseline and differential.
GenevestigatoriQ16772.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01266. GSTRNSFRASEA.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes."
    Suzuki T., Johnston P.N., Board P.G.
    Genomics 18:680-686(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones."
    Johansson A.-S., Mannervik B.
    J. Biol. Chem. 276:33061-33065(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
  3. NIEHS SNPs program
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-36; LEU-71; ASP-73; GLN-113 AND THR-208.
  4. "The DNA sequence and analysis of human chromosome 6."
    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.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  7. "Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4."
    Board P.G.
    Biochem. J. 330:827-831(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-222, VARIANT LEU-71.
  8. "Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity."
    Gu Y., Guo J., Pal A., Pan S.S., Zimniak P., Singh S.V., Ji X.
    Biochemistry 43:15673-15679(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION.
  9. "Structural basis for featuring of steroid isomerase activity in alpha class glutathione transferases."
    Tars K., Olin B., Mannervik B.
    J. Mol. Biol. 397:332-340(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND DELTA5-ANDROSTENE-3-17-DIONE, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiGSTA3_HUMAN
AccessioniPrimary (citable) accession number: Q16772
Secondary accession number(s): O43468
, Q068V6, Q8WWA8, Q9H415
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 27, 2002
Last modified: May 27, 2015
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.