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UniProtKB/Swiss-Prot entry P42760


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

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Entry information
Entry name GSTF1_ARATH
Primary accession number P42760
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 70)
Name and origin of the protein
Protein name Glutathione S-transferase 1
Synonyms EC 2.5.1.18
GST class-phi member 1
Gene name
Name: GST1
Synonyms: ERD11
OrderedLocusNames: At1g02930
ORFNames: F22D16.7
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
DOI=10.1016/0014-5793(93)80727-C; PubMed=8253194 [NCBI, ExPASy, EBI, Israel, Japan]
Kiyosue T., Yamaguchi-Shinozaki K., Shinozaki K.;
"Characterization of two cDNAs (ERD11 and ERD13) for dehydration-inducible genes that encode putative glutathione S-transferases in Arabidopsis thaliana L.";
FEBS Lett. 335:189-192(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Landsberg erecta;
Yang K.Y., Kim E.Y., Kim K.S., Choi S.N., Guh J.O., Kim K.C., Cho B.-H.;
"Characterization of a glutathione S-transferase gene ATGST1 in Arabidopsis thaliana.";
Plant Cell Rep. 17:700-704(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
Yu G.-L., Ausubel F.M.;
Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
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
D17672; BAA04553.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11727; CAA72413.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L12057; -; NOT_ANNOTATED_CDS; Genomic_RNA.[EMBL / GenBank / DDBJ]
AC009525; AAF02873.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY050332; AAK91349.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY097392; AAM19908.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G86159; G86159.
S39541; S39541.
RefSeq NP_171792.1; -.
UniGene At.20350
3D structure databases
HSSP P46422; 1GNW. [HSSP ENTRY / PDB]
SMR P42760; 3-207.
ModBase P42760.
2D gel databases
SWISS-2DPAGE P42760; -.
Organism-specific databases
TAIR At1g02930; -.
Gene expression databases
ArrayExpress P42760; -.
GermOnline AT1G02930; Arabidopsis thaliana.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004364; Molecular function: glutathione transferase activity (inferred from electronic annotation from EC).
GO:0006950; Biological process: response to stress (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR010987; Glutathione-S-Trfase_C-like.
IPR004046; GST_C.
IPR004045; GST_N.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1050.10; GST_C_like; 1.
G3DSA:3.40.30.10; Thioredoxin_fold; 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 P42760.
Genome annotation databases
GeneID 839515; -.
GenomeReviews CT485782_GR; AT1G02930.
KEGG ath:AT1G02930; -.
NMPDR fig|3702.1.peg.423; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Stress response; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
CHAIN   1   208  208     Glutathione S-transferase 1. PRO_0000185846
DOMAIN   2    83  82     GST N-terminal. 
DOMAIN   89   208  120     GST C-terminal. 
CONFLICT   12    12        S -> F (in Ref. 1; BAA04553). 
Sequence information
Length: 208 AA [This is the length of the unprocessed precursor] Molecular weight: 23486 Da [This is the MW of the unprocessed precursor] CRC64: 113CED008A11902F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAGIKVFGHP ASTATRRVLI ALHEKNVDFE FVHVELKDGE HKKEPFILRN PFGKVPAFED 

        70         80         90        100        110        120 
GDFKIFESRA ITQYIAHEFS DKGNNLLSTG KDMAIIAMGI EIESHEFDPV GSKLVWEQVL 

       130        140        150        160        170        180 
KPLYGMTTDK TVVEEEEAKL AKVLDVYEHR LGESKYLASD HFTLVDLHTI PVIQYLLGTP 

       190        200 
TKKLFDERPH VSAWVADITS RPSAQKVL 

P42760 in FASTA format

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