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UniProtKB/Swiss-Prot entry P41043


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GST1_DROME
Primary accession number P41043
Secondary accession numbers Q0E945 Q9V7Y4
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on January 27, 2003 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 73)
Name and origin of the protein
Protein name Glutathione S-transferase S1
Synonyms EC 2.5.1.18
GST class-sigma 1
Glutathione S-transferase 2
Gene name
Name: GstS1
Synonyms: GST2
ORFNames: CG8938
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1007/BF01037590; PubMed=1445191 [NCBI, ExPASy, EBI, Israel, Japan]
Beall C., Fyrberg C., Song S., Fyrberg E.;
"Isolation of a Drosophila gene encoding glutathione S-transferase.";
Biochem. Genet. 30:515-527(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Embryo;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M95198; AAA28596.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE013599; AAF57901.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY118328; AAM48357.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A48982; A48982.
RefSeq NP_523767.2; -.
NP_725653.1; -.
NP_725654.1; -.
UniGene Dm.19945
3D structure databases
PDB
1M0U; X-ray; 1.75 A; A/B=1-249.[ExPASy / RCSB / EBI]
PDBsum 1M0U; -.
ModBase P41043.
Protein-protein interaction databases
DIP DIP:21396N; -.
IntAct P41043; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-005099-MON; -.
DMEL-XXX-02:DMEL-XXX-02-005100-MON; -.
DMEL-XXX-02:DMEL-XXX-02-005101-MON; -.
Organism-specific databases
FlyBase FBgn0010226; GstS1.
Gene expression databases
ArrayExpress P41043; -.
GermOnline CG8938; Drosophila melanogaster.
Ontologies
GO
GO:0004602; Molecular function: glutathione peroxidase activity (inferred from direct assay from FlyBase).
GO:0004364; Molecular function: glutathione transferase activity (non-traceable author statement from UniProtKB).
GO:0008152; Biological process: metabolic process (inferred by curator from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR010987; Glutathione-S-Trfase_C-like.
IPR004046; GST_C.
IPR004045; GST_N.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1050.10; GST_C_like; 1.
Pfam PF00043; GST_C; 1.
PF02798; GST_N; 1.
Pfam graphical view of domain structure.
PROSITE PS50405; GST_CTER; 1.
PS50404; GST_NTER; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P41043.
Genome annotation databases
Ensembl CG8938; Drosophila melanogaster. [Contig view]
GeneID 36927; -.
KEGG dme:Dmel_CG8938; -.
Phylogenomic databases
HOGENOM P41043; -.
Other
NextBio 801072; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   249  249     Glutathione S-transferase S1. PRO_0000185917
DOMAIN   48   125  78     GST N-terminal. 
DOMAIN   127   249  123     GST C-terminal. 
CONFLICT   61    70        AEPLRYLFAY -> PSPCATCSD (in Ref. 1; AAA28596). 
CONFLICT   79    85        RVTRDEW -> AHPRRV (in Ref. 1; AAA28596). 
CONFLICT   224   224        L -> V (in Ref. 1; AAA28596). 
STRAND   50    58  9      
HELIX   59    61  3      
HELIX   62    71  10      
STRAND   76    80  5      
TURN   82    84  3      
HELIX   85    88  4      
HELIX   89    91  3      
HELIX   93    95  3      
STRAND   99   102  4      
STRAND   105   108  4      
HELIX   110   121  12      
HELIX   128   152  25      
HELIX   157   169  13      
HELIX   171   185  15      
STRAND   188   191  4      
HELIX   197   213  17      
TURN   217   220  4      
HELIX   222   232  11      
HELIX   235   243  9      
Sequence information
Length: 249 AA [This is the length of the unprocessed precursor] Molecular weight: 27614 Da [This is the MW of the unprocessed precursor] CRC64: 11AB417F550859BD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MADEAQAPPA EGAPPAEGEA PPPAEGAEGA VEGGEAAPPA EPAEPIKHSY TLFYFNVKAL 

        70         80         90        100        110        120 
AEPLRYLFAY GNQEYEDVRV TRDEWPALKP TMPMGQMPVL EVDGKRVHQS ISMARFLAKT 

       130        140        150        160        170        180 
VGLCGATPWE DLQIDIVVDT INDFRLKIAV VSYEPEDEIK EKKLVTLNAE VIPFYLEKLE 

       190        200        210        220        230        240 
QTVKDNDGHL ALGKLTWADV YFAGITDYMN YMVKRDLLEP YPALRGVVDA VNALEPIKAW 


IEKRPVTEV 

P41043 in FASTA format

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