TCHQD_ARATH
ID TCHQD_ARATH Reviewed; 266 AA.
AC O80662;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Glutathione S-transferase TCHQD;
DE EC=2.5.1.18;
DE AltName: Full=Protein tetrachlorohydroquinone dehalogenase-homolog;
GN Name=TCHQD; OrderedLocusNames=At1g77290; ORFNames=T14N5.14;
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; TISSUE=Rosette leaf;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19174456; DOI=10.1093/jxb/ern365;
RA Dixon D.P., Hawkins T., Hussey P.J., Edwards R.;
RT "Enzyme activities and subcellular localization of members of the
RT Arabidopsis glutathione transferase superfamily.";
RL J. Exp. Bot. 60:1207-1218(2009).
CC -!- FUNCTION: May be involved in the conjugation of reduced glutathione to
CC a wide number of exogenous and endogenous hydrophobic electrophiles.
CC {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: Cell membrane {ECO:0000269|PubMed:19174456}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; AC004260; AAC34354.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35958.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35959.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60330.1; -; Genomic_DNA.
DR EMBL; AY064034; AAL36390.1; -; mRNA.
DR EMBL; AK317233; BAH19914.1; -; mRNA.
DR EMBL; BT015120; AAT71992.1; -; mRNA.
DR PIR; T00457; T00457.
DR RefSeq; NP_001031292.1; NM_001036215.2.
DR RefSeq; NP_001322626.1; NM_001334774.1.
DR RefSeq; NP_177853.1; NM_106378.3.
DR AlphaFoldDB; O80662; -.
DR SMR; O80662; -.
DR STRING; 3702.AT1G77290.1; -.
DR iPTMnet; O80662; -.
DR PaxDb; O80662; -.
DR PRIDE; O80662; -.
DR ProteomicsDB; 246467; -.
DR EnsemblPlants; AT1G77290.1; AT1G77290.1; AT1G77290.
DR EnsemblPlants; AT1G77290.2; AT1G77290.2; AT1G77290.
DR EnsemblPlants; AT1G77290.3; AT1G77290.3; AT1G77290.
DR GeneID; 844065; -.
DR Gramene; AT1G77290.1; AT1G77290.1; AT1G77290.
DR Gramene; AT1G77290.2; AT1G77290.2; AT1G77290.
DR Gramene; AT1G77290.3; AT1G77290.3; AT1G77290.
DR KEGG; ath:AT1G77290; -.
DR Araport; AT1G77290; -.
DR TAIR; locus:2195990; AT1G77290.
DR eggNOG; KOG4420; Eukaryota.
DR HOGENOM; CLU_011226_5_3_1; -.
DR InParanoid; O80662; -.
DR OMA; LHCEEYD; -.
DR OrthoDB; 1011771at2759; -.
DR PhylomeDB; O80662; -.
DR PRO; PR:O80662; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80662; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
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; IPR044617; TCHQD.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR45374; PTHR45374; 1.
DR Pfam; PF13417; GST_N_3; 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 Cell membrane; Detoxification; Membrane; Reference proteome; Transferase.
FT CHAIN 1..266
FT /note="Glutathione S-transferase TCHQD"
FT /id="PRO_0000413580"
FT DOMAIN 1..80
FT /note="GST N-terminal"
FT DOMAIN 120..250
FT /note="GST C-terminal"
FT BINDING 9..10
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 38..39
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 51..52
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"
SQ SEQUENCE 266 AA; 31506 MW; D66A2B257ABC495D CRC64;
MQLYHHPYSI DSQRVRLALE EKGIDYTSYH VNPITGKHMD PSFFRMNPNA KLPVFRNGSH
IILDTIEIIE YLERIAEVSS GIEDATFNRE VVEWMRKIRE WESKLFTLAH IPDNRRLYVS
KFLRMVVIAR MAESPDLASA YHRKLREAYD TEDKLKDPGA LRRSKDHLLR LLDEVETKLE
GTTYLAGNEF SMADVMLIPV LARLSLLDLE EEYISSRKNL AEYWALVRRR PSYKKVIGRY
FNGWRKYATL VKTWMFVRVR SLLRKY
