Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O77473 (GST1B_ANOGA)

Last modified March 3, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 B
    EC=2.5.1.18
Alternative name(s):
    GST class-theta
    AgGst1-alpha
    Aggst1-4
Gene names
Name: GstD1
Synonyms: GST1a
ORF Names: AGAP004164
OrganismAnopheles gambiae (African malaria mosquito) [Complete proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

Enzyme regulation

Inhibited by S-hexylglutathione By similarity.

Subunit structure

Homodimer. Binds one molecule of S-hexylglutathione inhibitor per subunit 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 functionTransferase
   Technical termComplete 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 B Ref.1 (identifier: O77473-1)

Also known as: 1-4;

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 Ref.1 (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 C Ref.1 (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.
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 Q93113-1.
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 – 216216Glutathione S-transferase 1, isoform B
PRO_0000283093

Regions

Domain1 – 8080GST N-terminal
Domain89 – 210122GST C-terminal
Region6 – 116S-hexylglutathione-binding By similarity
Region50 – 534S-hexylglutathione-binding By similarity
Region64 – 663S-hexylglutathione-binding By similarity
Region207 – 2115S-hexylglutathione-binding By similarity

Sites

Active site91 By similarity
Binding site331S-hexylglutathione By similarity
Binding site381S-hexylglutathione By similarity
Binding site1041S-hexylglutathione By similarity
Binding site1081S-hexylglutathione By similarity
Binding site1161S-hexylglutathione By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform B (1-4) [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: BC94517EEC7A7F1E

FASTA21624,435
        10         20         30         40         50         60 
MDFYYLPGSA PCRAVQMTAA AVGVELNLKL TDLMKGEHMK PEFLKLNPQH CVPTLVDSGF 

        70         80         90        100        110        120 
ALWESRAIMC YLVEKYGKPC NNDSLYPTDP QKRAIVNQRL YFDMGTLYQR FGDYYYPQIF 

       130        140        150        160        170        180 
EGAPANEANF AKIGEALAFL DTFLEGERFV AGGNGYSLAD ISLYATLTTF EVAGYDFSAY 

       190        200        210 
VNVLRWYKSM PELIPASDTN RSWAEAARPF FDKVKH 

« Hide

Isoform A (1-3).

See O77462.

FASTA
Isoform C (1-5).

See Q93112.

FASTA
Isoform D (1-1) (1-6) (2-1).

See Q93113.

FASTA

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: 9826692] [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: 12364791] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PEST.

Cross-references

Sequence databases

AF071162 mRNA. Translation: AAC79998.1.
AF071160 Genomic DNA. Translation: AAC79994.1.
AAAB01008880 Genomic DNA. No translation available.

3D structure databases

HSSPHSSP built from PDB template 1PN9 based on UniProtKB Q93113.
ModBaseSearch...

Genome annotation databases

EnsemblAGAP004164. Anopheles gambiae. [Contig view]

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.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 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 nameGST1B_ANOGA
AccessionPrimary (citable) accession number: O77473
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: November 1, 1998
Last modified: March 3, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

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