ID GSTA3_HUMAN Reviewed; 222 AA. AC Q16772; O43468; Q8WWA8; Q9H415; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2002, sequence version 3. DT 07-JUL-2009, entry version 88. DE RecName: Full=Glutathione S-transferase A3; DE EC=2.5.1.18; DE AltName: Full=Glutathione S-transferase A3-3; DE AltName: Full=GST class-alpha member 3; GN Name=GSTA3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=94140370; PubMed=8307579; DOI=10.1016/S0888-7543(05)80373-8; RA Suzuki T., Johnston P.N., Board P.G.; RT "Structure and organization of the human alpha class glutathione S- RT transferase genes and related pseudogenes."; RL Genomics 18:680-686(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RX MEDLINE=21413882; PubMed=11418619; DOI=10.1074/jbc.M104539200; RA Johansson A.-S., Mannervik B.; RT "Human glutathione transferase A3-3, a highly efficient catalyst of RT double-bond isomerization in the biosynthetic pathway of steroid RT hormones."; RL J. Biol. Chem. 276:33061-33065(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-222, AND VARIANT LEU-71. RX MEDLINE=98149759; PubMed=9480897; RA Board P.G.; RT "Identification of cDNAs encoding two human alpha class glutathione RT transferases (GSTA3 and GSTA4) and the heterologous expression of RT GSTA4-4."; RL Biochem. J. 330:827-831(1998). CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of CC exogenous and endogenous hydrophobic electrophiles. Catalyzes CC isomerization reactions that contribute to the biosynthesis of CC steroid hormones. Efficiently catalyze obligatory double-bond CC isomerizations of delta(5)-androstene-3,17-dione and delta(5)- CC pregnene-3,20-dione, precursors to testosterone and progesterone, CC respectively. CC -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family. CC -!- SIMILARITY: Contains 1 GST C-terminal domain. CC -!- SIMILARITY: Contains 1 GST N-terminal domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L13275; AAA74634.1; ALT_INIT; Genomic_DNA. DR EMBL; L13270; AAA74634.1; JOINED; Genomic_DNA. DR EMBL; L13271; AAA74634.1; JOINED; Genomic_DNA. DR EMBL; L13272; AAA74634.1; JOINED; Genomic_DNA. DR EMBL; L13273; AAA74634.1; JOINED; Genomic_DNA. DR EMBL; L13274; AAA74634.1; JOINED; Genomic_DNA. DR EMBL; AF508266; AAM33360.1; -; mRNA. DR EMBL; AL121969; CAC10389.1; -; Genomic_DNA. DR EMBL; BC020619; AAH20619.1; -; mRNA. DR EMBL; AF020919; AAD04712.1; ALT_INIT; mRNA. DR IPI; IPI00003929; -. DR PIR; A49365; A49365. DR RefSeq; NP_000838.3; -. DR UniGene; Hs.102484; -. DR PDB; 1TDI; X-ray; 2.40 A; A/B=1-222. DR PDB; 2VCV; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-222. DR PDBsum; 1TDI; -. DR PDBsum; 2VCV; -. DR PRIDE; Q16772; -. DR Ensembl; ENSG00000174156; Homo sapiens. DR GeneID; 2940; -. DR KEGG; hsa:2940; -. DR UCSC; uc003pbb.1; human. DR GeneCards; GC06M052869; -. DR H-InvDB; HIX0005957; -. DR HGNC; HGNC:4628; GSTA3. DR HPA; HPA004342; -. DR MIM; 605449; gene. DR PharmGKB; PA29018; -. DR HOGENOM; Q16772; -. DR HOVERGEN; Q16772; -. DR OMA; Q16772; QSHGQDY. DR BRENDA; 2.5.1.18; 247. DR Reactome; REACT_13433; Biological oxidations. DR DrugBank; DB00143; Glutathione. DR NextBio; 11651; -. DR ArrayExpress; Q16772; -. DR Bgee; Q16772; -. DR CleanEx; HS_GSTA3; -. DR GermOnline; ENSG00000174156; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004364; F:glutathione transferase activity; TAS:ProtInc. DR GO; GO:0008152; P:metabolic process; IEA:InterPro. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR017933; Glutathione_S_Trfase/Cl_chnl_C. DR InterPro; IPR003080; GST_alpha. DR InterPro; IPR004046; GST_C. DR InterPro; IPR012335; Thioredoxin_fold. DR Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1. DR PANTHER; PTHR11571:SF4; GST_alpha; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR PRINTS; PR01266; GSTRNSFRASEA. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Polymorphism; Transferase. FT CHAIN 1 222 Glutathione S-transferase A3. FT /FTId=PRO_0000185785. FT DOMAIN 3 83 GST N-terminal. FT DOMAIN 85 207 GST C-terminal. FT VARIANT 71 71 I -> L (in dbSNP:rs1052661). FT /FTId=VAR_049484. FT VARIANT 73 73 N -> D (in dbSNP:rs41273858). FT /FTId=VAR_049485. FT CONFLICT 63 63 M -> I (in Ref. 4; AAH20619). FT CONFLICT 113 114 RP -> PA (in Ref. 1; AAA74634). FT CONFLICT 128 128 T -> I (in Ref. 1; AAA74634). FT STRAND 6 9 FT TURN 14 16 FT HELIX 17 25 FT STRAND 31 34 FT HELIX 38 46 FT STRAND 57 60 FT STRAND 63 67 FT HELIX 68 78 FT HELIX 86 108 FT HELIX 109 111 FT HELIX 114 130 FT HELIX 132 143 FT STRAND 146 149 FT HELIX 155 170 FT TURN 172 177 FT HELIX 179 189 FT HELIX 192 198 FT HELIX 210 220 SQ SEQUENCE 222 AA; 25302 MW; 904AA17519B5343C CRC64; MAGKPKLHYF NGRGRMEPIR WLLAAAGVEF EEKFIGSAED LGKLRNDGSL MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYTEGMA DLNEMILLLP LCRPEEKDAK IALIKEKTKS RYFPAFEKVL QSHGQDYLVG NKLSRADISL VELLYYVEEL DSSLISNFPL LKALKTRISN LPTVKKFLQP GSPRKPPADA KALEEARKIF RF //