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Q16772

- GSTA3_HUMAN

UniProt

Q16772 - GSTA3_HUMAN

Protein

Glutathione S-transferase A3

Gene

GSTA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 3 (27 May 2002)
      Previous versions | rss
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    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 isomerization1 Publication

    Sites

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

    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

    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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29018.

    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

    ArrayExpressiQ16772.
    BgeeiQ16772.
    CleanExiHS_GSTA3.
    GenevestigatoriQ16772.

    Organism-specific databases

    HPAiHPA004342.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi109195. 2 interactions.
    STRINGi9606.ENSP00000211122.

    Structurei

    Secondary structure

    1
    222
    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.
    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.
    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.

    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:
    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

    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: October 1, 2014
    This is version 137 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