GSTF4_ARATH
ID GSTF4_ARATH Reviewed; 245 AA.
AC Q84TK0; Q9FPM2; Q9SRY7;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Glutathione S-transferase F4;
DE Short=AtGSTF4;
DE EC=2.5.1.18;
DE AltName: Full=GST class-phi member 4;
DE AltName: Full=Glutathione S-transferase 31;
GN Name=GSTF4; Synonyms=GST31; OrderedLocusNames=At1g02950; ORFNames=F22D16.5;
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 [MRNA] (ISOFORM 2), GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84TK0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84TK0-2; Sequence=VSP_041937;
CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF02871.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009525; AAF02871.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27500.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27501.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27502.1; -; Genomic_DNA.
DR EMBL; AF320055; AAG40875.1; -; mRNA.
DR EMBL; BT005712; AAO64132.1; -; mRNA.
DR EMBL; BT020399; AAV97790.1; -; mRNA.
DR EMBL; AK228359; BAF00298.1; -; mRNA.
DR PIR; A86160; A86160.
DR RefSeq; NP_001030937.1; NM_001035860.1. [Q84TK0-2]
DR RefSeq; NP_563670.1; NM_100176.4. [Q84TK0-2]
DR RefSeq; NP_849581.1; NM_179250.1. [Q84TK0-1]
DR AlphaFoldDB; Q84TK0; -.
DR SMR; Q84TK0; -.
DR STRING; 3702.AT1G02950.2; -.
DR iPTMnet; Q84TK0; -.
DR PaxDb; Q84TK0; -.
DR PRIDE; Q84TK0; -.
DR ProteomicsDB; 248494; -. [Q84TK0-1]
DR EnsemblPlants; AT1G02950.1; AT1G02950.1; AT1G02950. [Q84TK0-2]
DR EnsemblPlants; AT1G02950.2; AT1G02950.2; AT1G02950. [Q84TK0-1]
DR EnsemblPlants; AT1G02950.3; AT1G02950.3; AT1G02950. [Q84TK0-2]
DR GeneID; 838240; -.
DR Gramene; AT1G02950.1; AT1G02950.1; AT1G02950. [Q84TK0-2]
DR Gramene; AT1G02950.2; AT1G02950.2; AT1G02950. [Q84TK0-1]
DR Gramene; AT1G02950.3; AT1G02950.3; AT1G02950. [Q84TK0-2]
DR KEGG; ath:AT1G02950; -.
DR Araport; AT1G02950; -.
DR TAIR; locus:2024765; AT1G02950.
DR eggNOG; KOG0867; Eukaryota.
DR InParanoid; Q84TK0; -.
DR PhylomeDB; Q84TK0; -.
DR PRO; PR:Q84TK0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84TK0; baseline and differential.
DR Genevisible; Q84TK0; 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 Alternative splicing; Cytoplasm; Detoxification; Reference proteome;
KW Transferase.
FT CHAIN 1..245
FT /note="Glutathione S-transferase F4"
FT /id="PRO_0000413542"
FT DOMAIN 25..106
FT /note="GST N-terminal"
FT DOMAIN 114..244
FT /note="GST C-terminal"
FT BINDING 35..36
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 64..65
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 77..78
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 90..91
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT VAR_SEQ 24..25
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12090627,
FT ECO:0000303|PubMed:14593172, ECO:0000303|Ref.5"
FT /id="VSP_041937"
SQ SEQUENCE 245 AA; 28701 MW; A9075D1B448C4886 CRC64;
MDCLQMVFKL FPNWKREAEV KKLVAGYKVH GDPFSTNTRR VLAVLHEKRL SYEPITVKLQ
TGEHKTEPFL SLNPFGQVPV FEDGSVKLYE SRAITQYIAY VHSSRGTQLL NLRSHETMAT
LTMWMEIEAH QFDPPASKLT WEQVIKPIYG LETDQTIVKE NEAILEKVLN IYEKRLEESR
FLACNSFTLV DLHHLPNIQY LLGTPTKKLF EKRSKVRKWV DEITSREAWK MACDQEKSWF
NKPRN
