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O77462 (GST1A_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. 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 A

EC=2.5.1.18
Alternative name(s):
AgGst1-alpha
Aggst1-3
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 length186 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles By similarity. UniProtKB P30711

Catalytic activity

RX + glutathione = HX + R-S-glutathione. UniProtKB P30711

Subunit structure

Homodimer By similarity. UniProtKB P30711

Sequence similarities

Belongs to the GST superfamily. Theta family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence caution

The sequence AAC79992.1 differs from that shown. Reason: Frameshift at position 172.

The sequence AAC79999.1 differs from that shown. Reason: Frameshift at position 172.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutathione metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionglutathione transferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform A Ref.1 (identifier: O77462-1)

Also known as: 1-3;

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 B Ref.1 (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 C Ref.1 (identifier: Q93112-1)

Also known as: 1-5;

The sequence of this isoform can be found in the external entry Q93112.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform D Ref.1 (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 – 186186Glutathione S-transferase 1, isoform A
PRO_0000283092

Regions

Domain1 – 8181GST N-terminal
Domain92 – 18695GST C-terminal
Region50 – 523Glutathione binding By similarity
Region65 – 673Glutathione binding By similarity

Sites

Binding site91Glutathione By similarity

Experimental info

Sequence conflict170 – 1712Missing in AAC79992. Ref.1
Sequence conflict170 – 1712Missing in AAC79999. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A (1-3) [UniParc].

Last modified April 18, 2012. Version 3.
Checksum: 82B9860A3DD57A81

FASTA18621,255
        10         20         30         40         50         60 
MDFYYLPGSA PCRAVQMTAA AVGVELNLKL TDLMKGEHMK PEFLKLNPQH CIPTLVDEDG 

        70         80         90        100        110        120 
FVLWESRAIQ IYLVEKYCAH DPALAERLYP GDPRRRAVVH QRLFFDVAIL YQRFAEYYYP 

       130        140        150        160        170        180 
QIFGKKVAGD PDRLRSMEQA LEFLNTFLEG ERFVAGGDDP TIADFSILAC ILDCNVRRCR 


VRSAAI 

« Hide

Isoform B (1-4) [UniParc].

See O77473.

Isoform C (1-5) [UniParc].

See Q93112.

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

See Q93113.

References

« Hide 'large scale' references
[1]"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 / MRNA], ALTERNATIVE SPLICING.
Strain: ZAN/U.
[2]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF071160 Genomic DNA. Translation: AAC79992.1. Frameshift.
AF071163 mRNA. Translation: AAC79999.1. Frameshift.
AAAB01008880 Genomic DNA. Translation: EAL40658.2.

3D structure databases

ProteinModelPortalO77462.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaAGAP004164-RD; AGAP004164-PD; AGAP004164. [O77462-1]
KEGGaga:AgaP_AGAP004164.
VectorBaseAGAP004164. Anopheles gambiae.

Organism-specific databases

CTD1273988.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125741.
InParanoidO77462.
KOK00799.
OrthoDBEOG7V1FRJ.

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.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF02798. 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 nameGST1A_ANOGA
AccessionPrimary (citable) accession number: O77462
Secondary accession number(s): Q5TTE8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 18, 2012
Last modified: April 16, 2014
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families