GRS10_ARATH
ID GRS10_ARATH Reviewed; 102 AA.
AC Q9LIF1; A0ME06;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Monothiol glutaredoxin-S10;
DE Short=AtGrxS10;
DE AltName: Full=Protein ROXY 3;
GN Name=GRXS10; Synonyms=ROXY3; OrderedLocusNames=At3g21460; ORFNames=MHC9.13;
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], AND GENE FAMILY.
RX PubMed=19218396; DOI=10.1105/tpc.108.064477;
RA Li S., Lauri A., Ziemann M., Busch A., Bhave M., Zachgo S.;
RT "Nuclear activity of ROXY1, a glutaredoxin interacting with TGA factors, is
RT required for petal development in Arabidopsis thaliana.";
RL Plant Cell 21:429-441(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15170506; DOI=10.1007/s00018-004-3410-y;
RA Rouhier N., Gelhaye E., Jacquot J.-P.;
RT "Plant glutaredoxins: still mysterious reducing systems.";
RL Cell. Mol. Life Sci. 61:1266-1277(2004).
RN [6]
RP GENE FAMILY.
RX PubMed=16720602; DOI=10.1093/jxb/erl001;
RA Rouhier N., Couturier J., Jacquot J.-P.;
RT "Genome-wide analysis of plant glutaredoxin systems.";
RL J. Exp. Bot. 57:1685-1696(2006).
CC -!- FUNCTION: May only reduce GSH-thiol disulfides, but not protein
CC disulfides. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CC-type subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28101.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; FJ611903; ACO50408.1; -; mRNA.
DR EMBL; AP001305; BAB03058.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76510.1; -; Genomic_DNA.
DR EMBL; DQ487674; ABF59441.1; -; Genomic_DNA.
DR EMBL; DQ652772; ABK28101.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001078198.1; NM_001084729.3.
DR AlphaFoldDB; Q9LIF1; -.
DR SMR; Q9LIF1; -.
DR BioGRID; 624229; 1.
DR STRING; 3702.AT3G21460.1; -.
DR PaxDb; Q9LIF1; -.
DR PRIDE; Q9LIF1; -.
DR EnsemblPlants; AT3G21460.1; AT3G21460.1; AT3G21460.
DR GeneID; 5008019; -.
DR Gramene; AT3G21460.1; AT3G21460.1; AT3G21460.
DR KEGG; ath:AT3G21460; -.
DR Araport; AT3G21460; -.
DR TAIR; locus:2089468; AT3G21460.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_026126_6_0_1; -.
DR InParanoid; Q9LIF1; -.
DR OMA; YDQGVSP; -.
DR OrthoDB; 1535999at2759; -.
DR PhylomeDB; Q9LIF1; -.
DR PRO; PR:Q9LIF1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIF1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:TAIR.
DR InterPro; IPR011905; GlrX-like_pln_2.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR10168; PTHR10168; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02189; GlrX-like_plant; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Nucleus;
KW Redox-active center; Reference proteome.
FT CHAIN 1..102
FT /note="Monothiol glutaredoxin-S10"
FT /id="PRO_0000398151"
FT DOMAIN 1..101
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT MOTIF 99..102
FT /note="Responsive for interaction with TGA factors"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255"
SQ SEQUENCE 102 AA; 11056 MW; AE80B8738CAB6797 CRC64;
MDVVARLASQ RAVVIFSKST CCMSHAIKRL FYEQGVSPAI VEIDQDMYGK DIEWALARLG
CSPTVPAVFV GGKFVGTANT VMTLHLNGSL KILLKEAGAL WL
