GST1A_ANOGA
ID GST1A_ANOGA Reviewed; 186 AA.
AC O77462; Q5TTE8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Glutathione S-transferase 1, isoform A;
DE EC=2.5.1.18;
DE AltName: Full=AgGst1-alpha;
DE AltName: Full=Aggst1-3;
DE AltName: Full=GST class-theta;
GN Name=GstD1 {ECO:0000303|PubMed:9826692};
GN Synonyms=GST1a {ECO:0000312|EMBL:AAC79992.1}; ORFNames=AGAP004164;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC79999.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RC STRAIN=ZAN/U {ECO:0000312|EMBL:AAC79999.1};
RX PubMed=9826692; DOI=10.1073/pnas.95.24.14284;
RA Ranson H., Collins F.H., Hemingway J.;
RT "The role of alternative mRNA splicing in generating heterogeneity within
RT the Anopheles gambiae class I glutathione S-transferase family.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:14284-14289(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000250|UniProtKB:P30711}.
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:0000250|UniProtKB:P30711};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30711}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A {ECO:0000269|PubMed:9826692}; Synonyms=1-3
CC {ECO:0000269|PubMed:9826692};
CC IsoId=O77462-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:9826692}; Synonyms=1-4
CC {ECO:0000269|PubMed:9826692};
CC IsoId=O77473-1; Sequence=External;
CC Name=C {ECO:0000269|PubMed:9826692}; Synonyms=1-5
CC {ECO:0000269|PubMed:9826692};
CC IsoId=Q93112-1; Sequence=External;
CC Name=D {ECO:0000269|PubMed:9826692}; Synonyms=1-1, 1-6
CC {ECO:0000269|PubMed:9826692}, 2-1;
CC IsoId=Q93113-1; Sequence=External;
CC -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79992.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC79999.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF071160; AAC79992.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF071163; AAC79999.1; ALT_FRAME; mRNA.
DR EMBL; AAAB01008880; EAL40658.2; -; Genomic_DNA.
DR RefSeq; XP_562680.2; XM_562680.2.
DR AlphaFoldDB; O77462; -.
DR SMR; O77462; -.
DR GeneID; 1273988; -.
DR CTD; 1273988; -.
DR VEuPathDB; VectorBase:AGAP004164; -.
DR OrthoDB; 1231780at2759; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
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; IPR036249; Thioredoxin-like_sf.
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 2: Evidence at transcript level;
KW Alternative splicing; Reference proteome; Transferase.
FT CHAIN 1..186
FT /note="Glutathione S-transferase 1, isoform A"
FT /id="PRO_0000283092"
FT DOMAIN 1..81
FT /note="GST N-terminal"
FT DOMAIN 92..186
FT /note="GST C-terminal"
FT BINDING 9
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 50..52
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 65..67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT CONFLICT 170..171
FT /note="Missing (in Ref. 1; AAC79992/AAC79999)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 186 AA; 21255 MW; 82B9860A3DD57A81 CRC64;
MDFYYLPGSA PCRAVQMTAA AVGVELNLKL TDLMKGEHMK PEFLKLNPQH CIPTLVDEDG
FVLWESRAIQ IYLVEKYCAH DPALAERLYP GDPRRRAVVH QRLFFDVAIL YQRFAEYYYP
QIFGKKVAGD PDRLRSMEQA LEFLNTFLEG ERFVAGGDDP TIADFSILAC ILDCNVRRCR
VRSAAI
