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Q9C6C8 (GSTFE_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase F14

Short name=AtGSTF14
EC=2.5.1.18
Alternative name(s):
GST class-phi member 14
Gene names
Name:GSTF14
Ordered Locus Names:At1g49860
ORF Names:F10F5.9
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides By similarity.

Catalytic activity

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

Subcellular location

Cytoplasmcytosol Probable.

Sequence similarities

Belongs to the GST superfamily. Phi family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Biological processDetoxification
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to toxic substance

Inferred from electronic annotation. Source: UniProtKB-KW

toxin catabolic process

Traceable author statement Ref.4. Source: TAIR

   Cellular_componentcytoplasm

Non-traceable author statement Ref.4. Source: TAIR

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 254254Glutathione S-transferase F14
PRO_0000413547

Regions

Domain4 – 8582GST N-terminal
Domain92 – 231140GST C-terminal
Region42 – 432Glutathione binding By similarity
Region56 – 572Glutathione binding By similarity
Region69 – 702Glutathione binding By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9C6C8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: C38D25BA560602D9

FASTA25428,819
        10         20         30         40         50         60 
MADSKMKLHC GFIWGNSAAL FCINEKGLDF ELVFVDWLAG EAKTKTFLST LNPFGEVPVL 

        70         80         90        100        110        120 
EDGDLKLFEP KAITRYLAEQ YKDVGTNLLP DDPKKRAIMS MWMEVDSNQF LPIASTLIKE 

       130        140        150        160        170        180 
LIINPYQGLA TDDTAVQENK EKLSEVLNIY ETRLGESPYL AGESFSLADL HHLAPIDYLL 

       190        200        210        220        230        240 
NTDEEELKNL IYSRPNVAAW VEKMKMRPAW LKTVVMKNHI VDLMKQRRLP IKLDSSCHES 

       250 
TVVAQKNAIA IENK 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
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. expand/collapse author list , 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.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Probing the diversity of the Arabidopsis glutathione S-transferase gene family."
Wagner U., Edwards R., Dixon D.P., Mauch F.
Plant Mol. Biol. 49:515-532(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC079674 Genomic DNA. Translation: AAG51779.1.
CP002684 Genomic DNA. Translation: AEE32484.1.
BT010408 mRNA. Translation: AAQ62409.1.
AK176306 mRNA. Translation: BAD44069.1.
PIRE96535.
RefSeqNP_175408.1. NM_103873.4.
UniGeneAt.38148.

3D structure databases

ProteinModelPortalQ9C6C8.
SMRQ9C6C8. Positions 6-213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid26634. 1 interaction.
IntActQ9C6C8. 1 interaction.
STRING3702.AT1G49860.1-P.

Proteomic databases

PaxDbQ9C6C8.
PRIDEQ9C6C8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G49860.1; AT1G49860.1; AT1G49860.
GeneID841409.
KEGGath:AT1G49860.

Organism-specific databases

TAIRAT1G49860.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125746.
InParanoidQ9C6C8.
KOK00799.
OMALNIYETR.
PhylomeDBQ9C6C8.
ProtClustDBCLSN2913624.

Enzyme and pathway databases

BioCycARA:AT1G49860-MONOMER.

Gene expression databases

GenevestigatorQ9C6C8.

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.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. 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 nameGSTFE_ARATH
AccessionPrimary (citable) accession number: Q9C6C8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: June 1, 2001
Last modified: March 19, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names