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   27-MAR-2024, entry version 151.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.Q9C6C8; -.
DR   PaxDb; 3702-AT1G49860-1; -.
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; AT1G49860; GSTF14.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_5_4_1; -.
DR   InParanoid; Q9C6C8; -.
DR   OMA; LECEYMS; -.
DR   OrthoDB; 639740at2759; -.
DR   PhylomeDB; Q9C6C8; -.
DR   BioCyc; ARA:AT1G49860-MONOMER; -.
DR   PRO; PR:Q9C6C8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C6C8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR   CDD; cd03187; GST_C_Phi; 1.
DR   CDD; cd03053; GST_N_Phi; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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   PANTHER; PTHR43900:SF43; GLUTATHIONE S-TRANSFERASE F14; 1.
DR   PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
DR   Genevisible; Q9C6C8; AT.
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
//