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Protein

Glutathione S-transferase 1, isoform C

Gene

GstD1

Organism
Anopheles gambiae (African malaria mosquito)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has DDT dehydrochlorinase activity.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication
1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91GlutathioneBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 1, isoform C (EC:2.5.1.18, EC:4.5.1.1)
Alternative name(s):
AgGst1-alpha
Aggst1-5
DDT-dehydrochlorinase
GST class-theta
Gene namesi
Name:GstD1
Synonyms:GST1a
ORF Names:AGAP004164
OrganismiAnopheles gambiae (African malaria mosquito)
Taxonomic identifieri7165 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles
ProteomesiUP000007062 Componenti: Chromosome 2R

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 209209Glutathione S-transferase 1, isoform CPRO_0000185961Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ93112.
SMRiQ93112. Positions 1-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8080GST N-terminalAdd
BLAST
Domaini86 – 207122GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 523Glutathione bindingBy similarity
Regioni64 – 663Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Theta family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

HOGENOMiHOG000125741.
OMAiEANEDGC.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform C (identifier: Q93112-1) [UniParc]FASTAAdd to basket

Also known as: 1-5

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDFYYLPGSA PCRAVQMTAA AVGVELNLKL TDLMKGEHMK PEFLKINPQH
60 70 80 90 100
CIPTLVDNGF ALWESRAICT YLAEKYGKDD KLYPKDPQKR AVVNQRMYFD
110 120 130 140 150
MGTLYQRFAD YYYPQIFAKQ PANPENEQKM KDAVGFLNSF LDGHKYVAGD
160 170 180 190 200
SLTIADLSIL ATISTYDVAG FDLAKYQHVA AWYENIRKEA PGAAINQAGI

EEFKKYFEK
Length:209
Mass (Da):23,783
Last modified:May 16, 2006 - v2
Checksum:iED01B322C2715409
GO
Isoform A (identifier: O77462-1) [UniParc]FASTAAdd to basket

Also known as: 1-3

The sequence of this isoform can be found in the external entry O77462.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:186
Mass (Da):21,255
GO
Isoform B (identifier: O77473-1) [UniParc]FASTAAdd to basket

Also known as: 1-4

The sequence of this isoform can be found in the external entry O77473.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:216
Mass (Da):24,492
GO
Isoform D (identifier: Q93113-1) [UniParc]FASTAAdd to basket

Also known as: 1-1, 1-6, 2-1

The sequence of this isoform can be found in the external entry Q93113.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:209
Mass (Da):23,445
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351G → D in CAB03592 (PubMed:9038148).Curated
Sequence conflicti139 – 1391S → T in CAB03592 (PubMed:9038148).Curated
Sequence conflicti181 – 1811A → V in CAB03592 (PubMed:9038148).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z81291 mRNA. Translation: CAB03592.1.
AF071160 Genomic DNA. Translation: AAC79993.1.
AAAB01008880 Genomic DNA. Translation: EAA08605.2.
RefSeqiXP_313049.1. XM_313049.4.

Genome annotation databases

EnsemblMetazoaiAGAP004164-RA; AGAP004164-PA; AGAP004164. [Q93112-1]
GeneIDi1273988.
VectorBaseiAGAP004163. Anopheles gambiae.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z81291 mRNA. Translation: CAB03592.1.
AF071160 Genomic DNA. Translation: AAC79993.1.
AAAB01008880 Genomic DNA. Translation: EAA08605.2.
RefSeqiXP_313049.1. XM_313049.4.

3D structure databases

ProteinModelPortaliQ93112.
SMRiQ93112. Positions 1-207.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiAGAP004164-RA; AGAP004164-PA; AGAP004164. [Q93112-1]
GeneIDi1273988.
VectorBaseiAGAP004163. Anopheles gambiae.

Organism-specific databases

CTDi1273988.

Phylogenomic databases

HOGENOMiHOG000125741.
OMAiEANEDGC.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and localization of a glutathione S-transferase class I gene from Anopheles gambiae."
    Ranson H., Cornel A.J., Fournier D., Vaughan A., Collins F.H., Hemingway J.
    J. Biol. Chem. 272:5464-5468(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Zands.
    Tissue: Larva.
  2. "The role of alternative mRNA splicing in generating heterogeneity within the Anopheles gambiae class I glutathione S-transferase family."
    Ranson H., Collins F.H., Hemingway J.
    Proc. Natl. Acad. Sci. U.S.A. 95:14284-14289(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    Strain: ZAN/U.
  3. "The genome sequence of the malaria mosquito Anopheles gambiae."
    Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F.
    , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.
    Science 298:129-149(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PEST.
  4. "Cloning and characterization of two glutathione S-transferases from a DDT-resistant strain of Anopheles gambiae."
    Ranson H., Prapanthadara L., Hemingway J.
    Biochem. J. 324:97-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
    Strain: Zands.

Entry informationi

Entry nameiGST1C_ANOGA
AccessioniPrimary (citable) accession number: Q93112
Secondary accession number(s): O76482, Q7PQM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 16, 2006
Last modified: July 22, 2015
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.