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Q16772 (GSTA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase A3

EC=2.5.1.18
Alternative name(s):
GST class-alpha member 3
Glutathione S-transferase A3-3
Gene names
Name:GSTA3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9

Catalytic activity

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

Subunit structure

Homodimer. Ref.9

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the GST superfamily. Alpha family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

Kinetic parameters:

KM=23 µM for delta(5)-androstene-3,17-dione Ref.8

Vmax=99 µmol/min/mg enzyme for delta(5)-androstene-3,17-dione isomerization

Sequence caution

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

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 222221Glutathione S-transferase A3
PRO_0000185785

Regions

Domain3 – 8381GST N-terminal
Domain85 – 207123GST C-terminal
Region54 – 552Glutathione binding
Region67 – 682Glutathione binding

Sites

Binding site91Glutathione
Binding site451Glutathione

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue41N6-succinyllysine By similarity

Natural variations

Natural variant361G → E. Ref.3
Corresponds to variant rs45504096 [ dbSNP | Ensembl ].
VAR_062276
Natural variant711I → L. Ref.3 Ref.7
Corresponds to variant rs1052661 [ dbSNP | Ensembl ].
VAR_049484
Natural variant731N → D. Ref.3
Corresponds to variant rs41273858 [ dbSNP | Ensembl ].
VAR_049485
Natural variant1131R → Q. Ref.3
Corresponds to variant rs45602042 [ dbSNP | Ensembl ].
VAR_062277
Natural variant2081A → T. Ref.3
Corresponds to variant rs45620832 [ dbSNP | Ensembl ].
VAR_062278

Experimental info

Sequence conflict631M → I in AAH20619. Ref.6
Sequence conflict113 – 1142RP → PA in AAA74634. Ref.1
Sequence conflict1281T → I in AAA74634. Ref.1

Secondary structure

.................................. 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16772 [UniParc].

Last modified May 27, 2002. Version 3.
Checksum: 904AA17519B5343C

FASTA22225,302
        10         20         30         40         50         60 
MAGKPKLHYF NGRGRMEPIR WLLAAAGVEF EEKFIGSAED LGKLRNDGSL MFQQVPMVEI 

        70         80         90        100        110        120 
DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYTEGMA DLNEMILLLP LCRPEEKDAK 

       130        140        150        160        170        180 
IALIKEKTKS RYFPAFEKVL QSHGQDYLVG NKLSRADISL VELLYYVEEL DSSLISNFPL 

       190        200        210        220 
LKALKTRISN LPTVKKFLQP GSPRKPPADA KALEEARKIF RF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13275 expand/collapse EMBL AC list , 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.
PIRA49365.
RefSeqNP_000838.3. NM_000847.4.
UniGeneHs.102484.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ16772.
SMRQ16772. Positions 4-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109195. 2 interactions.
STRING9606.ENSP00000211122.

Chemistry

ChEMBLCHEMBL4866.
DrugBankDB00143. Glutathione.

PTM databases

PhosphoSiteQ16772.

Polymorphism databases

DMDM21264437.

Proteomic databases

PaxDbQ16772.
PRIDEQ16772.

Protocols and materials databases

DNASU2940.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000211122; ENSP00000211122; ENSG00000174156.
GeneID2940.
KEGGhsa:2940.
UCSCuc003pbb.3. human.

Organism-specific databases

CTD2940.
GeneCardsGC06M052761.
HGNCHGNC:4628. GSTA3.
HPAHPA004342.
MIM605449. gene.
neXtProtNX_Q16772.
PharmGKBPA29018.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266414.
HOGENOMHOG000115734.
HOVERGENHBG053749.
InParanoidQ16772.
KOK00799.
OMAESARIDM.
PhylomeDBQ16772.
TreeFamTF105321.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKQ16772.

Gene expression databases

ArrayExpressQ16772.
BgeeQ16772.
CleanExHS_GSTA3.
GenevestigatorQ16772.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR11571:SF4. PTHR11571:SF4. 1 hit.
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01266. GSTRNSFRASEA.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ16772.
GeneWikiGSTA3.
GenomeRNAi2940.
NextBio11651.
PROQ16772.
SOURCESearch...

Entry information

Entry nameGSTA3_HUMAN
AccessionPrimary (citable) accession number: Q16772
Secondary accession number(s): O43468 expand/collapse secondary AC list , Q068V6, Q8WWA8, Q9H415
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 27, 2002
Last modified: April 16, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM