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Q93112 (GST1C_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GstD1
Synonyms:GST1a
ORF Names:AGAP004164
OrganismAnopheles gambiae (African malaria mosquito) [Reference proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

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. Has DDT dehydrochlorinase activity. Ref.4

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.4

1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride. Ref.4

Subunit structure

Homodimer By similarity.

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 functionLyase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionDDT-dehydrochlorinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

glutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform C (identifier: Q93112-1)

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.
Isoform A (identifier: O77462-1)

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.
Isoform B (identifier: O77473-1)

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.
Isoform D (identifier: Q93113-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 209209Glutathione S-transferase 1, isoform C
PRO_0000185961

Regions

Domain1 – 8080GST N-terminal
Domain86 – 207122GST C-terminal
Region50 – 523Glutathione binding By similarity
Region64 – 663Glutathione binding By similarity

Sites

Binding site91Glutathione By similarity

Experimental info

Sequence conflict1351G → D in CAB03592. Ref.1
Sequence conflict1391S → T in CAB03592. Ref.1
Sequence conflict1811A → V in CAB03592. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform C (1-5) [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: ED01B322C2715409

FASTA20923,783
        10         20         30         40         50         60 
MDFYYLPGSA PCRAVQMTAA AVGVELNLKL TDLMKGEHMK PEFLKINPQH CIPTLVDNGF 

        70         80         90        100        110        120 
ALWESRAICT YLAEKYGKDD KLYPKDPQKR AVVNQRMYFD MGTLYQRFAD YYYPQIFAKQ 

       130        140        150        160        170        180 
PANPENEQKM KDAVGFLNSF LDGHKYVAGD SLTIADLSIL ATISTYDVAG FDLAKYQHVA 

       190        200 
AWYENIRKEA PGAAINQAGI EEFKKYFEK 

« Hide

Isoform A (1-3) [UniParc].

See O77462.

Isoform B (1-4) [UniParc].

See O77473.

Isoform D (1-1) (1-6) (2-1) [UniParc].

See Q93113.

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] [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. 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] [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z81291 mRNA. Translation: CAB03592.1.
AF071160 Genomic DNA. Translation: AAC79993.1.
AAAB01008880 Genomic DNA. Translation: EAA08605.2.

3D structure databases

ProteinModelPortalQ93112.
SMRQ93112. Positions 1-207.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB00143. Glutathione.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaAGAP004164-RA; AGAP004164-PA; AGAP004164. [Q93112-1]
KEGGaga:AgaP_AGAP004164.
VectorBaseAGAP004163. Anopheles gambiae.

Organism-specific databases

CTD1273988.

Phylogenomic databases

HOGENOMHOG000125741.
KOK00799.
OMAICAYLIN.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGST1C_ANOGA
AccessionPrimary (citable) accession number: Q93112
Secondary accession number(s): O76482, Q7PQM5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 16, 2006
Last modified: April 16, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families