LOCUS       NM_000847                908 bp    mRNA    linear   PRI 01-JUN-2024
DEFINITION  Homo sapiens glutathione S-transferase alpha 3 (GSTA3), transcript
            variant 1, mRNA.
ACCESSION   NM_000847
VERSION     NM_000847.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 908)
  AUTHORS   Li,W., Qiu,C., Wang,S., Wu,L. and Zhao,T.
  TITLE     Inhibitory effect of glutathione S-transferase A3 in the
            progression of cutaneous squamous cell carcinoma
  JOURNAL   J Cosmet Dermatol 20 (7), 2287-2295 (2021)
   PUBMED   33089654
  REMARK    GeneRIF: Inhibitory effect of glutathione S-transferase A3 in the
            progression of cutaneous squamous cell carcinoma.
REFERENCE   2  (bases 1 to 908)
  AUTHORS   Duan,S., Gong,B., Wang,P., Huang,H., Luo,L. and Liu,F.
  TITLE     Novel prognostic biomarkers of gastric cancer based on gene
            expression microarray: COL12A1, GSTA3, FGA and FGG
  JOURNAL   Mol Med Rep 18 (4), 3727-3736 (2018)
   PUBMED   30106150
  REMARK    GeneRIF: Certain core genes, including COL12A1, glutathione
            Stransferase alpha3 (GSTA3), fibrinogen alpha chain (FGA) and
            fibrinogen gamma chain (FGG), were the first reported to be
            associated with Gastric Cancer. Survival analysis suggested that
            these four genes, COL12A1 (P=0.002), GSTA3 (P=3.4x106), FGA
            (P=0.00075) and FGG (P=1.4x105), were significant poor prognostic
            factors of gastric cancer.
REFERENCE   3  (bases 1 to 908)
  AUTHORS   Wang,Y. and Tatakis,D.N.
  TITLE     Human gingiva transcriptome during wound healing
  JOURNAL   J Clin Periodontol 44 (4), 394-402 (2017)
   PUBMED   28005267
  REMARK    GeneRIF: GSTA3 expression is significantly downregulated in human
            masticatory mucosa during wound healing
REFERENCE   4  (bases 1 to 908)
  AUTHORS   Daka,J.L., Achilonu,I. and Dirr,H.W.
  TITLE     The isomerization of Delta5-androstene-3,17-dione by the human
            glutathione transferase A3-3 proceeds via a conjugated
            heteroannular diene intermediate
  JOURNAL   J Biol Chem 289 (46), 32243-32252 (2014)
   PUBMED   25248748
  REMARK    GeneRIF: analysis of how isomerization of the steroid
            Delta(5)-androstene-3,17-dione by the glutathione transferase A3-3
REFERENCE   5  (bases 1 to 908)
  AUTHORS   Dourado,D.F., Fernandes,P.A., Mannervik,B. and Ramos,M.J.
  TITLE     Isomerization of Delta5-androstene-3,17-dione into
            Delta4-androstene-3,17-dione catalyzed by human glutathione
            transferase A3-3: a computational study identifies a dual role for
            glutathione
  JOURNAL   J Phys Chem A 118 (31), 5790-5800 (2014)
   PUBMED   24739064
  REMARK    GeneRIF: Density functional theory calculations used to propose a
            refined mechanism for the isomerization of
            delta(5)-androstene-3,17-dione catalyzed by GST A3-3
REFERENCE   6  (bases 1 to 908)
  AUTHORS   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., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            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., 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.,
            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.,
            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., 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., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   7  (bases 1 to 908)
  AUTHORS   Johansson,A.S. and Mannervik,B.
  TITLE     Active-site residues governing high steroid isomerase activity in
            human glutathione transferase A3-3
  JOURNAL   J Biol Chem 277 (19), 16648-16654 (2002)
   PUBMED   11872752
REFERENCE   8  (bases 1 to 908)
  AUTHORS   Johansson,A.S. and Mannervik,B.
  TITLE     Human glutathione transferase A3-3, a highly efficient catalyst of
            double-bond isomerization in the biosynthetic pathway of steroid
            hormones
  JOURNAL   J Biol Chem 276 (35), 33061-33065 (2001)
   PUBMED   11418619
REFERENCE   9  (bases 1 to 908)
  AUTHORS   Board,P.G.
  TITLE     Identification of cDNAs encoding two human alpha class glutathione
            transferases (GSTA3 and GSTA4) and the heterologous expression of
            GSTA4-4
  JOURNAL   Biochem J 330 (Pt 2) (Pt 2), 827-831 (1998)
   PUBMED   9480897
REFERENCE   10 (bases 1 to 908)
  AUTHORS   Suzuki,T., Johnston,P.N. and Board,P.G.
  TITLE     Structure and organization of the human alpha class glutathione
            S-transferase genes and related pseudogenes
  JOURNAL   Genomics 18 (3), 680-686 (1993)
   PUBMED   8307579
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DT932587.1, BC020619.1,
            AL121969.12 and AI199811.1.
            
            On Nov 23, 2018 this sequence version replaced NM_000847.4.
            
            Summary: Cytosolic and membrane-bound forms of glutathione
            S-transferase are encoded by two distinct supergene families. These
            enzymes are involved in cellular defense against toxic,
            carcinogenic, and pharmacologically active electrophilic compounds.
            At present, eight distinct classes of the soluble cytoplasmic
            mammalian glutathione S-transferases have been identified: alpha,
            kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a
            glutathione S-tranferase belonging to the alpha class genes that
            are located in a cluster mapped to chromosome 6. Genes of the alpha
            class are highly related and encode enzymes with glutathione
            peroxidase activity. However, during evolution, this alpha class
            gene diverged accumulating mutations in the active site that
            resulted in differences in substrate specificity and catalytic
            activity. The enzyme encoded by this gene catalyzes the double bond
            isomerization of precursors for progesterone and testosterone
            during the biosynthesis of steroid hormones. An additional
            transcript variant has been identified, but its full length
            sequence has not been determined. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX365400.2, SRR5189667.387893.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267761 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000211122.4/ ENSP00000211122.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-13                DT932587.1         152-164
            14-267              BC020619.1         1-254
            268-268             AL121969.12        20481-20481         c
            269-901             BC020619.1         256-888
            902-908             AI199811.1         11-17               c
FEATURES             Location/Qualifiers
     source          1..908
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.2"
     gene            1..908
                     /gene="GSTA3"
                     /gene_synonym="GSTA3-3; GTA3"
                     /note="glutathione S-transferase alpha 3"
                     /db_xref="GeneID:2940"
                     /db_xref="HGNC:HGNC:4628"
                     /db_xref="MIM:605449"
     exon            1..58
                     /gene="GSTA3"
                     /gene_synonym="GSTA3-3; GTA3"
                     /inference="alignment:Splign:2.1.0"
     exon            59..166
                     /gene="GSTA3"
                     /gene_synonym="GSTA3-3; GTA3"
                     /inference="alignment:Splign:2.1.0"
     CDS             80..748
                     /gene="GSTA3"
                     /gene_synonym="GSTA3-3; GTA3"
                     /EC_number="2.5.1.18"
                     /note="isoform 1 is encoded by transcript variant 1;
                     glutathione S-alkyltransferase A3; glutathione
                     S-aryltransferase A3; S-(hydroxyalkyl)glutathione lyase
                     A3; glutathione S-aralkyltransferase A3; glutathione
                     S-transferase A3-3; GST class-alpha member 3"
                     /codon_start=1
                     /product="glutathione S-transferase A3 isoform 1"
                     /protein_id="NP_000838.3"
                     /db_xref="CCDS:CCDS4947.1"
                     /db_xref="GeneID:2940"
                     /db_xref="HGNC:HGNC:4628"
                     /db_xref="MIM:605449"
                     /translation="MAGKPKLHYFNGRGRMEPIRWLLAAAGVEFEEKFIGSAEDLGKL
                     RNDGSLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYTEGMADL
                     NEMILLLPLCRPEEKDAKIALIKEKTKSRYFPAFEKVLQSHGQDYLVGNKLSRADISL
                     VELLYYVEELDSSLISNFPLLKALKTRISNLPTVKKFLQPGSPRKPPADAKALEEARK
                     IFRF"
     exon            167..218
                     /gene="GSTA3"
                     /gene_synonym="GSTA3-3; GTA3"
                     /inference="alignment:Splign:2.1.0"
     exon            219..351
                     /gene="GSTA3"
                     /gene_synonym="GSTA3-3; GTA3"
                     /inference="alignment:Splign:2.1.0"
     exon            352..493
                     /gene="GSTA3"
                     /gene_synonym="GSTA3-3; GTA3"
                     /inference="alignment:Splign:2.1.0"
     exon            494..625
                     /gene="GSTA3"
                     /gene_synonym="GSTA3-3; GTA3"
                     /inference="alignment:Splign:2.1.0"
     exon            626..908
                     /gene="GSTA3"
                     /gene_synonym="GSTA3-3; GTA3"
                     /inference="alignment:Splign:2.1.0"
     regulatory      883..888
                     /regulatory_class="polyA_signal_sequence"
                     /gene="GSTA3"
                     /gene_synonym="GSTA3-3; GTA3"
                     /note="hexamer: AATAAA"
     polyA_site      908
                     /gene="GSTA3"
                     /gene_synonym="GSTA3-3; GTA3"
                     /note="major polyA site"
ORIGIN      
        1 atacacatca ggaggtggcc ttgagaagct gagcggagac cggctagact ttactcaaag
       61 aaaccaagag actgttacca tggcagggaa gcccaagctt cactacttca atggacgggg
      121 cagaatggag cccatccggt ggctcttggc tgcagctgga gtggagtttg aagagaaatt
      181 tataggatct gcagaagatt tgggaaagtt aagaaatgat gggagtttga tgttccagca
      241 agtaccaatg gttgagattg atgggatgaa gttggtacag accagagcca ttctcaacta
      301 cattgccagc aaatacaacc tctacgggaa agacataaag gagagagccc taattgatat
      361 gtatacagaa ggtatggcag atttgaatga aatgatcctt cttctgccct tatgtcgacc
      421 tgaggaaaaa gatgccaaga ttgccttgat caaagagaaa acaaaaagtc gctatttccc
      481 tgccttcgaa aaagtgttac agagccatgg acaagactac cttgttggca acaagctgag
      541 ccgggctgac attagcctgg tggaacttct ctactatgtg gaagagcttg actccagcct
      601 tatctccaac ttccctctgc tgaaggccct gaaaaccaga atcagcaacc tgcccacggt
      661 gaagaagttt ctacagcctg gcagcccaag gaagcctccc gcagatgcaa aagctttaga
      721 agaagccaga aagattttca ggttttaata aagcagccat ggaggctaag aacatgcaag
      781 accaatattc taaagttttg caacaatgaa gtgctttact taagtgttga ttgtgcctgt
      841 tgtaaagcta atgaaccctt tccaattata tgctaattaa ataataaaaa ctcctatttg
      901 ctaactta
//
