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Q9VG96

- GSTT4_DROME

UniProt

Q9VG96 - GSTT4_DROME

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Protein

Glutathione S-transferase D4

Gene
GstD4, gstD23, CG11512
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

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

GO - Molecular functioni

  1. glutathione transferase activity Source: FlyBase
  2. protein binding Source: IntAct

GO - Biological processi

  1. glutathione metabolic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase D4 (EC:2.5.1.18)
Short name:
DmGST23
Gene namesi
Name:GstD4
Synonyms:gstD23
ORF Names:CG11512
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0010040. GstD4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Glutathione S-transferase D4PRO_0000185956Add
BLAST

Proteomic databases

PaxDbiQ9VG96.
PRIDEiQ9VG96.

Expressioni

Gene expression databases

BgeeiQ9VG96.

Interactioni

Subunit structurei

Homodimer By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
GstD6Q9VG943EBI-117276,EBI-152218

Protein-protein interaction databases

BioGridi71334. 8 interactions.
DIPiDIP-19902N.
IntActiQ9VG96. 5 interactions.
MINTiMINT-793961.

Structurei

3D structure databases

ProteinModelPortaliQ9VG96.
SMRiQ9VG96. Positions 1-207.

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 binding By similarity
Regioni64 – 663Glutathione binding By similarity

Sequence similaritiesi

Belongs to the GST superfamily. Theta family.

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00540000069741.
InParanoidiQ9VG96.
KOiK00799.
OMAiNGFAIWE.
OrthoDBiEOG7V1FRJ.
PhylomeDBiQ9VG96.

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]

Sequencei

Sequence statusi: Complete.

Q9VG96-1 [UniParc]FASTAAdd to Basket

« Hide

MDFYYSPRSS GSRTIIMVAK ALGLELNKKQ LRITEGEHLK PEFLKLNPQH    50
TIPTLVDNGF AIWESRAIAV YLVEKYGKDD SLFPNDPQKR ALINQRLYFD 100
MGTLHDSFMK YYYPFIRTGQ LGNAENYKKV EAAFEFLDIF LEGQDYVAGS 150
QLTVADIAIL SSVSTFEVVE FDISKYPNVA RWYANAKKIT PGWDENWKGL 200
LQMKTMYEAQ KASLK 215
Length:215
Mass (Da):24,736
Last modified:May 1, 2000 - v1
Checksum:i9556E0A1A54BBE1F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1421E → V in M97702. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97702 Genomic DNA. No translation available.
AE014297 Genomic DNA. Translation: AAF54789.1.
AY071648 mRNA. Translation: AAL49270.1.
PIRiE46681.
RefSeqiNP_524913.1. NM_080174.3.
UniGeneiDm.1754.

Genome annotation databases

EnsemblMetazoaiFBtr0082571; FBpp0082043; FBgn0010040.
GeneIDi48337.
KEGGidme:Dmel_CG11512.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97702 Genomic DNA. No translation available.
AE014297 Genomic DNA. Translation: AAF54789.1 .
AY071648 mRNA. Translation: AAL49270.1 .
PIRi E46681.
RefSeqi NP_524913.1. NM_080174.3.
UniGenei Dm.1754.

3D structure databases

ProteinModelPortali Q9VG96.
SMRi Q9VG96. Positions 1-207.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 71334. 8 interactions.
DIPi DIP-19902N.
IntActi Q9VG96. 5 interactions.
MINTi MINT-793961.

Proteomic databases

PaxDbi Q9VG96.
PRIDEi Q9VG96.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0082571 ; FBpp0082043 ; FBgn0010040 .
GeneIDi 48337.
KEGGi dme:Dmel_CG11512.

Organism-specific databases

CTDi 48337.
FlyBasei FBgn0010040. GstD4.

Phylogenomic databases

eggNOGi COG0625.
GeneTreei ENSGT00540000069741.
InParanoidi Q9VG96.
KOi K00799.
OMAi NGFAIWE.
OrthoDBi EOG7V1FRJ.
PhylomeDBi Q9VG96.

Miscellaneous databases

GenomeRNAii 48337.
NextBioi 839335.

Gene expression databases

Bgeei Q9VG96.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster."
    Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.
    J. Biol. Chem. 268:9737-9746(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiGSTT4_DROME
AccessioniPrimary (citable) accession number: Q9VG96
Secondary accession number(s): Q541F8, Q9TX90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi