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Reviewed, UniProtKB/Swiss-Prot Q93113 (GST1D_ANOGA)

Last modified November 24, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutathione S-transferase 1, isoform D
    EC=2.5.1.18
Alternative name(s):
    GST class-theta
    AgGst1-alpha
    Aggst1-1
    Aggst1-6
    Aggst2-1
Gene names
Name: GstD1
Synonyms: GST1a
ORF Names: AGAP004164
OrganismAnopheles gambiae (African malaria mosquito) [Complete proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Ref.1

Catalytic activity

RX + glutathione = HX + R-S-glutathione.

Enzyme regulation

Inhibited by S-hexylglutathione. Ref.4

Subunit structure

Homodimer. Binds one molecule of S-hexylglutathione inhibitor per subunit. Ref.4

Developmental stage

Expressed in larvae. Ref.1

Sequence similarities

Belongs to the GST superfamily. Theta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Molecular functionglutathione transferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform D (identifier: Q93113-1)

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

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.
Isoform A (identifier: O77462-1)

Also known as: 1-3;

The sequence of this isoform can be found in the external entry O77462-1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform B (identifier: O77473-1)

Also known as: 1-4;

The sequence of this isoform can be found in the external entry O77473-1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform C (identifier: Q93112-1)

Also known as: 1-5;

The sequence of this isoform can be found in the external entry Q93112-1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 209209Glutathione S-transferase 1, isoform D
PRO_0000185962

Regions

Domain1 – 8080GST N-terminal
Domain86 – 207122GST C-terminal
Region6 – 116S-hexylglutathione-binding
Region50 – 534S-hexylglutathione-binding
Region64 – 663S-hexylglutathione-binding
Region203 – 2075S-hexylglutathione-binding

Sites

Active site91 Probable
Binding site331S-hexylglutathione
Binding site381S-hexylglutathione
Binding site1011S-hexylglutathione
Binding site1051S-hexylglutathione
Binding site1131S-hexylglutathione

Experimental info

Sequence conflict241V → A in CAA96105. Ref.1

Secondary structure

................................. 209
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform D (1-1) (1-6) (2-1) [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 3B262EEE21FAA9D0

FASTA20923,445
        10         20         30         40         50         60 
MDFYYLPGSA PCRAVQMTAA AVGVELNLKL TDLMKGEHMK PEFLKLNPQH CIPTLVDNGF 

        70         80         90        100        110        120 
ALWESRAIQI YLAEKYGKDD KLYPKDPQKR AVVNQRLYFD MGTLYQRFAD YHYPQIFAKQ 

       130        140        150        160        170        180 
PANPENEKKM KDAVGFLNTF LEGQEYAAGN DLTIADLSLA ATIATYEVAG FDFAPYPNVA 

       190        200 
AWFARCKANA PGYALNQAGA DEFKAKFLS 

« Hide

Isoform A (1-3).

See O77462.

FASTA
Isoform B (1-4).

See O77473.

FASTA
Isoform C (1-5).

See Q93112.

FASTA

References

« Hide 'large scale' references
[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: 9038148] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
Strain: G3 and 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: 9826692] [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. expand/collapse author list , 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: 12364791] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PEST.
[4]"Structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae."
Chen L., Hall P.R., Zhou X.E., Ranson H., Hemingway J., Meehan E.J.
Acta Crystallogr. D 59:2211-2217(2003) [PubMed: 14646079] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH S-HEXYLGLUTATHIONE INHIBITOR, ENZYME REGULATION, SUBUNIT, ACTIVE SITE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z71481 mRNA. Translation: CAA96105.1.
Z81292 mRNA. Translation: CAB03593.1.
AF071160 Genomic DNA. Translation: AAC79995.1.
AAAB01008880 Genomic DNA. Translation: EAA44713.3.
RefSeqXP_313050.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PN9X-ray2.00A/B1-209[»]
ModBaseSearch...

Genome annotation databases

GeneID1273988.
VectorBaseAGAP004163. Anopheles gambiae.

Organism-specific databases

CTD1273988.

Phylogenomic databases

OMAANPENEK.

Enzyme and pathway databases

BRENDA2.5.1.18. 165157.

Family and domain databases

InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGST1D_ANOGA
AccessionPrimary (citable) accession number: Q93113
Secondary accession number(s): Q7PH24, Q94998
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 24, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents