GST1C_ANOGA
ID GST1C_ANOGA Reviewed; 209 AA.
AC Q93112; O76482; Q7PQM5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Glutathione S-transferase 1, isoform C;
DE EC=2.5.1.18;
DE EC=4.5.1.1;
DE AltName: Full=AgGst1-alpha;
DE AltName: Full=Aggst1-5;
DE AltName: Full=DDT-dehydrochlorinase;
DE AltName: Full=GST class-theta;
GN Name=GstD1; Synonyms=GST1a; 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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Zands; TISSUE=Larva;
RX PubMed=9038148; DOI=10.1074/jbc.272.9.5464;
RA Ranson H., Cornel A.J., Fournier D., Vaughan A., Collins F.H.,
RA Hemingway J.;
RT "Cloning and localization of a glutathione S-transferase class I gene from
RT Anopheles gambiae.";
RL J. Biol. Chem. 272:5464-5468(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=ZAN/U;
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 [3]
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).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Zands;
RX PubMed=9164846; DOI=10.1042/bj3240097;
RA Ranson H., Prapanthadara L., Hemingway J.;
RT "Cloning and characterization of two glutathione S-transferases from a DDT-
RT resistant strain of Anopheles gambiae.";
RL Biochem. J. 324:97-102(1997).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Has DDT
CC dehydrochlorinase activity. {ECO:0000269|PubMed:9164846}.
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:9164846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-
CC 2,2-bis(4-chlorophenyl)ethylene + chloride + H(+);
CC Xref=Rhea:RHEA:19217, ChEBI:CHEBI:15378, ChEBI:CHEBI:16130,
CC ChEBI:CHEBI:16598, ChEBI:CHEBI:17996; EC=4.5.1.1;
CC Evidence={ECO:0000269|PubMed:9164846};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=C; Synonyms=1-5;
CC IsoId=Q93112-1; Sequence=Displayed;
CC Name=A; Synonyms=1-3;
CC IsoId=O77462-1; Sequence=External;
CC Name=B; Synonyms=1-4;
CC IsoId=O77473-1; Sequence=External;
CC Name=D; Synonyms=1-1, 1-6, 2-1;
CC IsoId=Q93113-1; Sequence=External;
CC -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC {ECO:0000305}.
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DR EMBL; Z81291; CAB03592.1; -; mRNA.
DR EMBL; AF071160; AAC79993.1; -; Genomic_DNA.
DR EMBL; AAAB01008880; EAA08605.2; -; Genomic_DNA.
DR RefSeq; XP_313049.1; XM_313049.4.
DR AlphaFoldDB; Q93112; -.
DR SMR; Q93112; -.
DR GeneID; 1273988; -.
DR CTD; 1273988; -.
DR VEuPathDB; VectorBase:AGAP004164; -.
DR OMA; KYEVLQW; -.
DR OrthoDB; 1231780at2759; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0018833; F:DDT-dehydrochlorinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
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 SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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 Alternative splicing; Lyase; Reference proteome; Transferase.
FT CHAIN 1..209
FT /note="Glutathione S-transferase 1, isoform C"
FT /id="PRO_0000185961"
FT DOMAIN 1..80
FT /note="GST N-terminal"
FT DOMAIN 86..207
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 64..66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT CONFLICT 135
FT /note="G -> D (in Ref. 1; CAB03592)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="S -> T (in Ref. 1; CAB03592)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="A -> V (in Ref. 1; CAB03592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 23783 MW; ED01B322C2715409 CRC64;
MDFYYLPGSA PCRAVQMTAA AVGVELNLKL TDLMKGEHMK PEFLKINPQH CIPTLVDNGF
ALWESRAICT YLAEKYGKDD KLYPKDPQKR AVVNQRMYFD MGTLYQRFAD YYYPQIFAKQ
PANPENEQKM KDAVGFLNSF LDGHKYVAGD SLTIADLSIL ATISTYDVAG FDLAKYQHVA
AWYENIRKEA PGAAINQAGI EEFKKYFEK
