GSTEE_DROME
ID GSTEE_DROME Reviewed; 232 AA.
AC Q7JYX0;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Glutathione S-transferase E14 {ECO:0000303|PubMed:22082028};
DE EC=2.5.1.18 {ECO:0000269|PubMed:22082028};
DE AltName: Full=Protein noppera-bo {ECO:0000303|PubMed:25300303};
GN Name=GstE14 {ECO:0000312|FlyBase:FBgn0033817};
GN Synonyms=GSTD14-14 {ECO:0000312|FlyBase:FBgn0033817},
GN nobo {ECO:0000303|PubMed:25300303};
GN ORFNames=CG4688 {ECO:0000312|FlyBase:FBgn0033817};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAL49335.1};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL49335.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22082028; DOI=10.1042/bj20111747;
RA Saisawang C., Wongsantichon J., Ketterman A.J.;
RT "A preliminary characterization of the cytosolic glutathione transferase
RT proteome from Drosophila melanogaster.";
RL Biochem. J. 442:181-190(2012).
RN [5] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=25344753; DOI=10.1038/ncb3052;
RA Chanut-Delalande H., Hashimoto Y., Pelissier-Monier A., Spokony R., Dib A.,
RA Kondo T., Bohere J., Niimi K., Latapie Y., Inagaki S., Dubois L.,
RA Valenti P., Polesello C., Kobayashi S., Moussian B., White K.P., Plaza S.,
RA Kageyama Y., Payre F.;
RT "Pri peptides are mediators of ecdysone for the temporal control of
RT development.";
RL Nat. Cell Biol. 16:1035-1044(2014).
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25300303; DOI=10.1038/srep06586;
RA Enya S., Ameku T., Igarashi F., Iga M., Kataoka H., Shinoda T., Niwa R.;
RT "A Halloween gene noppera-bo encodes a glutathione S-transferase essential
RT for ecdysteroid biosynthesis via regulating the behaviour of cholesterol in
RT Drosophila.";
RL Sci. Rep. 4:6586-6586(2014).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles (PubMed:22082028).
CC Essential for ecdysteroid biosynthesis (PubMed:25344753,
CC PubMed:25300303). May be involved in detoxification (PubMed:22082028).
CC {ECO:0000269|PubMed:22082028, ECO:0000269|PubMed:25300303,
CC ECO:0000269|PubMed:25344753}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:22082028};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.84 mM for glutathione {ECO:0000269|PubMed:22082028};
CC KM=0.28 mM for 1-chloro-2,4-dinitrobenzene
CC {ECO:0000269|PubMed:22082028};
CC Vmax=133 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as
CC substrate {ECO:0000269|PubMed:22082028};
CC Vmax=2.75 umol/min/mg enzyme with 4-hydroxy-2-nonenal as substrate
CC {ECO:0000269|PubMed:22082028};
CC Vmax=0.322 umol/min/mg enzyme with phenethyl isothiocyanate as
CC substrate {ECO:0000269|PubMed:22082028};
CC -!- TISSUE SPECIFICITY: Expressed in the adult ovary (at protein level).
CC {ECO:0000269|PubMed:25300303}.
CC -!- DEVELOPMENTAL STAGE: In early embryos expression is ubiquitous
CC (PubMed:25344753). From mid-embryogenesis (stage 16) and throughout
CC larval development, expressed in the prothoracic gland cells of the
CC ring gland (PubMed:25344753, PubMed:25300303). Weak expression in the
CC follicle cells of the ovarioles in developing egg chambers (at protein
CC level) (PubMed:25300303). {ECO:0000269|PubMed:25300303,
CC ECO:0000269|PubMed:25344753}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. Embryos display severe
CC developmental defects such as poorly differentiated cuticle, failure of
CC head involution, abnormal gut looping, and defective mouth hooks and
CC dorsal closure (PubMed:25344753, PubMed:25300303). Trichromes are
CC absent (PubMed:25344753). Embryos have a higher sterol content
CC (PubMed:25344753, PubMed:25300303). Embryonic lethality, defective
CC epidermal differentiation and trichome development can be rescued by
CC supplementing embryos with 20-hydroxyecdysone (20E), ecdysone or
CC cholesterol (PubMed:25344753). RNAi-mediated knockdown results in
CC larval lethality at the second instar stage, which can be rescued by
CC supplementing larvae with 20E, ecdysone or cholesterol
CC (PubMed:25300303). {ECO:0000269|PubMed:25300303,
CC ECO:0000269|PubMed:25344753}.
CC -!- MISCELLANEOUS: Member of the Halloween gene group.
CC {ECO:0000303|PubMed:25300303, ECO:0000303|PubMed:25344753}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Epsilon family.
CC {ECO:0000303|PubMed:22082028}.
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DR EMBL; AE013599; AAF58397.1; -; Genomic_DNA.
DR EMBL; AY071713; AAL49335.1; -; mRNA.
DR RefSeq; NP_610855.1; NM_137011.3.
DR PDB; 6KEL; X-ray; 1.40 A; AA/BA=1-232.
DR PDB; 6KEM; X-ray; 1.50 A; AA/BA=1-232.
DR PDB; 6KEN; X-ray; 1.75 A; AA/BA=1-232.
DR PDB; 6KEO; X-ray; 1.58 A; AA/BA=1-232.
DR PDB; 6KEP; X-ray; 1.55 A; AA/BA=1-232.
DR PDB; 6KEQ; X-ray; 1.84 A; AA/BA=1-232.
DR PDB; 6KER; X-ray; 1.84 A; AA/BA=1-232.
DR PDB; 6T2T; X-ray; 1.30 A; A=1-232.
DR PDB; 7DAX; X-ray; 1.70 A; A/B=1-232.
DR PDB; 7DAY; X-ray; 1.48 A; A/B=1-232.
DR PDB; 7DAZ; X-ray; 1.64 A; A/B=1-232.
DR PDB; 7DB0; X-ray; 1.66 A; A/B=1-232.
DR PDB; 7DB1; X-ray; 1.83 A; A/B=1-232.
DR PDB; 7DB2; X-ray; 1.40 A; A/B=1-232.
DR PDB; 7DB3; X-ray; 1.70 A; A/B=1-232.
DR PDB; 7DB4; X-ray; 1.54 A; A/B=1-232.
DR PDBsum; 6KEL; -.
DR PDBsum; 6KEM; -.
DR PDBsum; 6KEN; -.
DR PDBsum; 6KEO; -.
DR PDBsum; 6KEP; -.
DR PDBsum; 6KEQ; -.
DR PDBsum; 6KER; -.
DR PDBsum; 6T2T; -.
DR PDBsum; 7DAX; -.
DR PDBsum; 7DAY; -.
DR PDBsum; 7DAZ; -.
DR PDBsum; 7DB0; -.
DR PDBsum; 7DB1; -.
DR PDBsum; 7DB2; -.
DR PDBsum; 7DB3; -.
DR PDBsum; 7DB4; -.
DR AlphaFoldDB; Q7JYX0; -.
DR SMR; Q7JYX0; -.
DR IntAct; Q7JYX0; 1.
DR STRING; 7227.FBpp0086857; -.
DR PaxDb; Q7JYX0; -.
DR DNASU; 36467; -.
DR EnsemblMetazoa; FBtr0087744; FBpp0086857; FBgn0033817.
DR GeneID; 36467; -.
DR KEGG; dme:Dmel_CG4688; -.
DR UCSC; CG4688-RA; d. melanogaster.
DR CTD; 36467; -.
DR FlyBase; FBgn0033817; GstE14.
DR VEuPathDB; VectorBase:FBgn0033817; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_2_1_1; -.
DR InParanoid; Q7JYX0; -.
DR OMA; CLMLIKL; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q7JYX0; -.
DR SABIO-RK; Q7JYX0; -.
DR BioGRID-ORCS; 36467; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36467; -.
DR PRO; PR:Q7JYX0; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033817; Expressed in head capsule and 12 other tissues.
DR Genevisible; Q7JYX0; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:FlyBase.
DR GO; GO:0004769; F:steroid delta-isomerase activity; IDA:FlyBase.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:FlyBase.
DR GO; GO:0045456; P:ecdysteroid biosynthetic process; IMP:FlyBase.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:FlyBase.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Detoxification; Lipid biosynthesis; Lipid metabolism;
KW Reference proteome; Steroid biosynthesis; Transferase.
FT CHAIN 1..232
FT /note="Glutathione S-transferase E14"
FT /id="PRO_0000433644"
FT DOMAIN 4..85
FT /note="GST N-terminal"
FT DOMAIN 91..218
FT /note="GST C-terminal"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:6T2T"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:6T2T"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:6T2T"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6T2T"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6T2T"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:6T2T"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:6T2T"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6T2T"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:6T2T"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6T2T"
FT HELIX 92..107
FT /evidence="ECO:0007829|PDB:6T2T"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:6T2T"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6T2T"
FT HELIX 130..147
FT /evidence="ECO:0007829|PDB:6T2T"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6T2T"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:7DB4"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6T2T"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:6T2T"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:6T2T"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:6T2T"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:6T2T"
FT HELIX 199..216
FT /evidence="ECO:0007829|PDB:6T2T"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:7DAY"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:6T2T"
SQ SEQUENCE 232 AA; 26622 MW; 81BDFB41C6FBD87B CRC64;
MSQPKPILYY DERSPPVRSC LMLIKLLDID VELRFVNLFK GEQFQKDFLA LNPQHSVPTL
VHGDLVLTDS HAILIHLAEK FDEGGSLWPQ EHAERMKVLN LLLFECSFLF RRDSDFMSAT
VRQGFANVDV AHHERKLTEA YIIMERYLEN SDFMAGPQLT LADLSIVTTL STVNLMFPLS
QFPRLRRWFT AMQQLDAYEA NCSGLEKLRQ TMESVGSFQF PSSSAVVTEK VE
