GSTFE_ARATH
ID GSTFE_ARATH Reviewed; 254 AA.
AC Q9C6C8;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Glutathione S-transferase F14 {ECO:0000303|PubMed:12090627};
DE Short=AtGSTF14 {ECO:0000303|PubMed:12090627};
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:O80852};
DE AltName: Full=GST class-phi member 14 {ECO:0000303|PubMed:12090627};
GN Name=GSTF14 {ECO:0000303|PubMed:12090627};
GN OrderedLocusNames=At1g49860 {ECO:0000312|Araport:AT1G49860};
GN ORFNames=F10F5.9 {ECO:0000312|EMBL:AAG51779.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12090627; DOI=10.1023/a:1015557300450;
RA Wagner U., Edwards R., Dixon D.P., Mauch F.;
RT "Probing the diversity of the Arabidopsis glutathione S-transferase gene
RT family.";
RL Plant Mol. Biol. 49:515-532(2002).
CC -!- FUNCTION: May be involved in the conjugation of reduced glutathione to
CC a wide number of exogenous and endogenous hydrophobic electrophiles and
CC have a detoxification role against certain herbicides.
CC {ECO:0000250|UniProtKB:O80852}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000250|UniProtKB:O80852};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR EMBL; AC079674; AAG51779.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32484.1; -; Genomic_DNA.
DR EMBL; BT010408; AAQ62409.1; -; mRNA.
DR EMBL; AK176306; BAD44069.1; -; mRNA.
DR PIR; E96535; E96535.
DR RefSeq; NP_175408.1; NM_103873.5.
DR AlphaFoldDB; Q9C6C8; -.
DR SMR; Q9C6C8; -.
DR BioGRID; 26634; 1.
DR IntAct; Q9C6C8; 1.
DR STRING; 3702.AT1G49860.1; -.
DR PaxDb; Q9C6C8; -.
DR PRIDE; Q9C6C8; -.
DR ProteomicsDB; 247189; -.
DR EnsemblPlants; AT1G49860.1; AT1G49860.1; AT1G49860.
DR GeneID; 841409; -.
DR Gramene; AT1G49860.1; AT1G49860.1; AT1G49860.
DR KEGG; ath:AT1G49860; -.
DR Araport; AT1G49860; -.
DR TAIR; locus:2007278; AT1G49860.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_5_4_1; -.
DR InParanoid; Q9C6C8; -.
DR OMA; FKFPKVH; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q9C6C8; -.
DR BioCyc; ARA:AT1G49860-MON; -.
DR PRO; PR:Q9C6C8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6C8; baseline and differential.
DR Genevisible; Q9C6C8; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043295; F:glutathione binding; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR CDD; cd03187; GST_C_Phi; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR034347; GST_Phi_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Detoxification; Reference proteome; Transferase.
FT CHAIN 1..254
FT /note="Glutathione S-transferase F14"
FT /id="PRO_0000413547"
FT DOMAIN 4..85
FT /note="GST N-terminal"
FT /evidence="ECO:0000255"
FT DOMAIN 92..231
FT /note="GST C-terminal"
FT /evidence="ECO:0000255"
FT BINDING 42..43
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 56..57
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 69..70
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
SQ SEQUENCE 254 AA; 28819 MW; C38D25BA560602D9 CRC64;
MADSKMKLHC GFIWGNSAAL FCINEKGLDF ELVFVDWLAG EAKTKTFLST LNPFGEVPVL
EDGDLKLFEP KAITRYLAEQ YKDVGTNLLP DDPKKRAIMS MWMEVDSNQF LPIASTLIKE
LIINPYQGLA TDDTAVQENK EKLSEVLNIY ETRLGESPYL AGESFSLADL HHLAPIDYLL
NTDEEELKNL IYSRPNVAAW VEKMKMRPAW LKTVVMKNHI VDLMKQRRLP IKLDSSCHES
TVVAQKNAIA IENK
