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 27-MAR-2024, entry version 138. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 STRING; 7165.Q93112; -. DR EnsemblMetazoa; AGAP004164-RA; AGAP004164-PA; AGAP004164. [Q93112-1] DR GeneID; 1273988; -. DR CTD; 1273988; -. DR VEuPathDB; VectorBase:AGAP004164; -. DR InParanoid; Q93112; -. DR OMA; RYTNEAR; -. DR OrthoDB; 2318861at2759; -. 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 CDD; cd03177; GST_C_Delta_Epsilon; 1. DR CDD; cd03045; GST_N_Delta_Epsilon; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. 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 PANTHER; PTHR43969; GLUTATHIONE S TRANSFERASE D10, ISOFORM A-RELATED; 1. DR PANTHER; PTHR43969:SF9; GLUTATHIONE S TRANSFERASE D10, ISOFORM A-RELATED; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG01153; Main.4:_Theta-like; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 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 //