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GSTT3_ARATH
ID   GSTT3_ARATH             Reviewed;         590 AA.
AC   Q9FHE1; Q56WE4;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Glutathione S-transferase T3;
DE            Short=AtGSTT3;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-theta member 3;
DE   AltName: Full=Glutathione S-transferase 10C;
GN   Name=GSTT3; Synonyms=GST10C; OrderedLocusNames=At5g41220; ORFNames=K1O13.1;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(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] OF 249-590.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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).
RN   [5]
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. {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: Nucleus {ECO:0000269|PubMed:19174456}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {ECO:0000305}.
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DR   EMBL; AB019225; BAB11098.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94655.1; -; Genomic_DNA.
DR   EMBL; AK222098; BAD95009.1; -; mRNA.
DR   RefSeq; NP_198938.1; NM_123487.4.
DR   AlphaFoldDB; Q9FHE1; -.
DR   SMR; Q9FHE1; -.
DR   STRING; 3702.AT5G41220.1; -.
DR   PaxDb; Q9FHE1; -.
DR   PRIDE; Q9FHE1; -.
DR   ProteomicsDB; 247187; -.
DR   EnsemblPlants; AT5G41220.1; AT5G41220.1; AT5G41220.
DR   GeneID; 834124; -.
DR   Gramene; AT5G41220.1; AT5G41220.1; AT5G41220.
DR   KEGG; ath:AT5G41220; -.
DR   Araport; AT5G41220; -.
DR   TAIR; locus:2155090; AT5G41220.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_462617_0_0_1; -.
DR   InParanoid; Q9FHE1; -.
DR   OrthoDB; 1231780at2759; -.
DR   PhylomeDB; Q9FHE1; -.
DR   BioCyc; ARA:AT5G41220-MON; -.
DR   PRO; PR:Q9FHE1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FHE1; baseline and differential.
DR   Genevisible; Q9FHE1; AT.
DR   GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR   CDD; cd03183; GST_C_Theta; 1.
DR   CDD; cd03050; GST_N_Theta; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR040077; GST_C_Theta.
DR   InterPro; IPR040075; GST_N_Theta.
DR   InterPro; IPR043377; GSTT1/2/3.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44750; PTHR44750; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
DR   PROSITE; PS50090; MYB_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Detoxification; Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..590
FT                   /note="Glutathione S-transferase T3"
FT                   /id="PRO_0000413576"
FT   DOMAIN          1..82
FT                   /note="GST N-terminal"
FT   DOMAIN          89..232
FT                   /note="GST C-terminal"
FT   DOMAIN          265..336
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT   REGION          402..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         11..12
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         40..41
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         53..54
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..67
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   590 AA;  67555 MW;  E85F66525F6C7AF5 CRC64;
     MKLKVYADRM SQPSRAVLIF CKVNEIQFDE ILIYLANRQQ LSPEFKDINP MGKVPAIVDG
     KLKLSESHAI LIYLSSAYPS VVDHWYPTDL SKRARIHSVL DWHHTNLRPG AAGYVLNSVL
     GPALGLPLNP KAAAEAEQLL TKSLTTLDTF WLKGNAMFLL GSNQPSIADL SLVCELTQLQ
     VLDDKDRLRL LSPHKNVEQW IENTRKATMP HFDEVHEVLF RAKDRCQKQR EMATASKPGP
     QSKIIQFSTI GEKSDDPNLV QNTTDRRKHR RKWSRAEDAI LISAWLNTSK DPIVDNEHKA
     CAFWKRIGAY FNNSASLANL PKREPSHCKQ RWSKLNDKVC KFVGCYDQAL NQRSSGQSED
     DVFQVAYQVY TNNYKSNFTL EHAWRELRHS KKWCSLYPFE NSKGGGSSKR TKLNNGDRVY
     SSSSNPESVP IALDEEEQVM DLPLGVKSSK QKEKKVATII TIEEREADSG SRLENLWVLD
     EEEQVMDRPL GVKSLEQKEN KVAPKPTIEE REAADSRSRL ENLWALKEKE EREADSRSRL
     ENLWALKEKD IEEQKKLTRM EVLKSLLGRT TDQLSEKEDI LKNKLIDEML
 
 
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