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GSTU9_ARATH
ID   GSTU9_ARATH             Reviewed;         240 AA.
AC   Q9FUT0; Q9FE97;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Glutathione S-transferase U9;
DE            Short=AtGSTU9;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-tau member 9;
DE   AltName: Full=Glutathione S-transferase 14;
GN   Name=GSTU9; Synonyms=GST14, GST14B; OrderedLocusNames=At5g62480;
GN   ORFNames=K19B1.9;
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] (ISOFORMS 1 AND 2), GENE FAMILY, AND
RP   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=9872454; DOI=10.1093/dnares/5.5.297;
RA   Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT   features of the regions of 1,013,767 bp covered by sixteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:297-308(1998).
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] (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 (SEP-2004) 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=Q9FUT0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FUT0-2; Sequence=VSP_041940;
CC   -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}.
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DR   EMBL; AF288179; AAG30128.1; -; mRNA.
DR   EMBL; AF288180; AAG30129.1; -; mRNA.
DR   EMBL; AB015469; BAB11498.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97612.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97613.1; -; Genomic_DNA.
DR   EMBL; AK176211; BAD43974.1; -; mRNA.
DR   RefSeq; NP_568954.2; NM_125642.3. [Q9FUT0-2]
DR   RefSeq; NP_851249.1; NM_180918.3. [Q9FUT0-1]
DR   AlphaFoldDB; Q9FUT0; -.
DR   SMR; Q9FUT0; -.
DR   STRING; 3702.AT5G62480.1; -.
DR   PaxDb; Q9FUT0; -.
DR   ProteomicsDB; 248496; -. [Q9FUT0-1]
DR   EnsemblPlants; AT5G62480.1; AT5G62480.1; AT5G62480. [Q9FUT0-1]
DR   EnsemblPlants; AT5G62480.2; AT5G62480.2; AT5G62480. [Q9FUT0-2]
DR   GeneID; 836368; -.
DR   Gramene; AT5G62480.1; AT5G62480.1; AT5G62480. [Q9FUT0-1]
DR   Gramene; AT5G62480.2; AT5G62480.2; AT5G62480. [Q9FUT0-2]
DR   KEGG; ath:AT5G62480; -.
DR   Araport; AT5G62480; -.
DR   TAIR; locus:2154129; AT5G62480.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_18_0_1; -.
DR   InParanoid; Q9FUT0; -.
DR   OMA; CKAQEEV; -.
DR   OrthoDB; 1225872at2759; -.
DR   PhylomeDB; Q9FUT0; -.
DR   BioCyc; ARA:AT5G62480-MON; -.
DR   BRENDA; 2.5.1.18; 399.
DR   PRO; PR:Q9FUT0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FUT0; baseline and differential.
DR   Genevisible; Q9FUT0; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   GO; GO:0009407; P:toxin catabolic process; TAS:TAIR.
DR   CDD; cd03185; GST_C_Tau; 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; IPR045074; GST_C_Tau.
DR   InterPro; IPR045073; Omega/Tau-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11260; PTHR11260; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 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; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..240
FT                   /note="Glutathione S-transferase U9"
FT                   /id="PRO_0000413555"
FT   DOMAIN          7..86
FT                   /note="GST N-terminal"
FT   DOMAIN          92..226
FT                   /note="GST C-terminal"
FT   BINDING         17..18
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         43..44
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         57..58
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         70..71
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         161
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZW27"
FT   VAR_SEQ         65..90
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12090627"
FT                   /id="VSP_041940"
SQ   SEQUENCE   240 AA;  27612 MW;  D0872464356EA2FB CRC64;
     MDEEVENKVI LHGSFASPYS KRIELALRLK SIPYQFVQED LQNKSQTLLR YNPVHKKIPV
     LVHNGKPISE SLFIIEYIDE TWSNGPHILP EDPYRRSKVR FWANYIQLHL YDLVIKVVKS
     EGEEQKKALT EVKEKLSVIE KEGLKEIFSD TDGEPTVTNE TMSLVDIVMC TLLSPYKAHE
     EVLGLKIIDP EIVPGVYGWI NAINETSVVK DLSPPYEQIL EILRAFRQMS LSPVLETYQS
 
 
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