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Reviewed, UniProtKB/Swiss-Prot Q16772 (GSTA3_HUMAN)

Last modified July 7, 2009. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the GST superfamily. Alpha family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglutathione transferase activity Ref.5

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 222222Glutathione S-transferase A3
PRO_0000185785

Regions

Domain3 – 8381GST N-terminal
Domain85 – 207123GST C-terminal

Natural variations

Natural variant711I → L: dbSNP rs1052661. Ref.5
VAR_049484
Natural variant731N → D: dbSNP rs41273858.
VAR_049485

Experimental info

Sequence conflict631M → I in AAH20619. Ref.4
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
Q16772-1 [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: 8307579] [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: 11418619] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[3]"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: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[5]"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: 9480897] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-222, VARIANT LEU-71.
+Additional computationally mapped references.

Cross-references

Sequence databases

L13275 expand/collapse EMBL AC list , L13270, L13271, L13272, L13273, L13274 Genomic DNA. Translation: AAA74634.1. Different initiation.
AF508266 mRNA. Translation: AAM33360.1.
AL121969 Genomic DNA. Translation: CAC10389.1.
BC020619 mRNA. Translation: AAH20619.1.
AF020919 mRNA. Translation: AAD04712.1. Different initiation.
IPIIPI00003929.
PIRA49365.
RefSeqNP_000838.3.
UniGeneHs.102484

3D structure databases

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[»]
ModBaseSearch...

Proteomic databases

PRIDEQ16772.

Genome annotation databases

EnsemblENSG00000174156. Homo sapiens. [Contig view]
GeneID2940.
KEGGhsa:2940.
UCSCuc003pbb.1. human.

Organism-specific databases

GeneCardsGC06M052869.
H-InvDBHIX0005957.
HGNCHGNC:4628. GSTA3.
HPAHPA004342.
MIM605449. gene.
PharmGKBPA29018.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ16772.
HOVERGENQ16772.
OMAQ16772. QSHGQDY.

Enzyme and pathway databases

BRENDA2.5.1.18. 247.
ReactomeREACT_13433. Biological oxidations.

Gene expression databases

ArrayExpressQ16772.
BgeeQ16772.
CleanExHS_GSTA3.
GermOnlineENSG00000174156. Homo sapiens.

Family and domain databases

InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHERPTHR11571:SF4. GST_alpha. 1 hit.
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01266. GSTRNSFRASEA.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00143. Glutathione.
NextBio11651.
SOURCESearch...

Entry information

Entry nameGSTA3_HUMAN
AccessionPrimary (citable) accession number: Q16772
Secondary accession number(s): O43468, Q8WWA8, Q9H415
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 27, 2002
Last modified: July 7, 2009
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 6

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents