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Q16772

- GSTA3_HUMAN

UniProt

Q16772 - GSTA3_HUMAN

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Protein
Glutathione S-transferase A3
Gene
GSTA3
Organism
Homo sapiens (Human)
Status
Reviewed - 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

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

Sites

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

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB

GO - Biological processi

  1. glutathione derivative biosynthetic process Source: Reactome
  2. glutathione metabolic process Source: UniProtKB
  3. small molecule metabolic process Source: Reactome
  4. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

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: Chromosome 6

Organism-specific databases

HGNCiHGNC:4628. GSTA3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29018.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 222221Glutathione S-transferase A3
PRO_0000185785Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei4 – 41N6-succinyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ16772.
PaxDbiQ16772.
PRIDEiQ16772.

PTM databases

PhosphoSiteiQ16772.

Expressioni

Gene expression databases

ArrayExpressiQ16772.
BgeeiQ16772.
CleanExiHS_GSTA3.
GenevestigatoriQ16772.

Organism-specific databases

HPAiHPA004342.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi109195. 2 interactions.
STRINGi9606.ENSP00000211122.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ16772.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the GST superfamily. Alpha family.

Phylogenomic databases

eggNOGiNOG266414.
HOGENOMiHOG000115734.
HOVERGENiHBG053749.
InParanoidiQ16772.
KOiK00799.
OMAiESARIDM.
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

MAGKPKLHYF NGRGRMEPIR WLLAAAGVEF EEKFIGSAED LGKLRNDGSL    50
MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYTEGMA 100
DLNEMILLLP LCRPEEKDAK IALIKEKTKS RYFPAFEKVL QSHGQDYLVG 150
NKLSRADISL VELLYYVEEL DSSLISNFPL LKALKTRISN LPTVKKFLQP 200
GSPRKPPADA KALEEARKIF RF 222
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.
The sequence AAD04712.1 differs from that shown. Reason: Erroneous initiation.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631M → I in AAH20619. 1 Publication
Sequence conflicti113 – 1142RP → PA in AAA74634. 1 Publication
Sequence conflicti128 – 1281T → I in AAA74634. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi21264437.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS4947.1.
PIRi A49365.
RefSeqi NP_000838.3. NM_000847.4.
UniGenei Hs.102484.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TDI X-ray 2.40 A/B 1-222 [» ]
2VCV X-ray 1.80 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 1-222 [» ]
ProteinModelPortali Q16772.
SMRi Q16772. Positions 4-222.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109195. 2 interactions.
STRINGi 9606.ENSP00000211122.

Chemistry

ChEMBLi CHEMBL4866.
DrugBanki DB00143. Glutathione.

PTM databases

PhosphoSitei Q16772.

Polymorphism databases

DMDMi 21264437.

Proteomic databases

MaxQBi Q16772.
PaxDbi Q16772.
PRIDEi Q16772.

Protocols and materials databases

DNASUi 2940.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000211122 ; ENSP00000211122 ; ENSG00000174156 .
GeneIDi 2940.
KEGGi hsa:2940.
UCSCi uc003pbb.3. human.

Organism-specific databases

CTDi 2940.
GeneCardsi GC06M052761.
HGNCi HGNC:4628. GSTA3.
HPAi HPA004342.
MIMi 605449. gene.
neXtProti NX_Q16772.
PharmGKBi PA29018.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG266414.
HOGENOMi HOG000115734.
HOVERGENi HBG053749.
InParanoidi Q16772.
KOi K00799.
OMAi ESARIDM.
PhylomeDBi Q16772.
TreeFami TF105321.

Enzyme and pathway databases

Reactomei REACT_6926. Glutathione conjugation.
SABIO-RK Q16772.

Miscellaneous databases

EvolutionaryTracei Q16772.
GeneWikii GSTA3.
GenomeRNAii 2940.
NextBioi 11651.
PROi Q16772.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16772.
Bgeei Q16772.
CleanExi HS_GSTA3.
Genevestigatori Q16772.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01266. GSTRNSFRASEA.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 136 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

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