GRXS9_ARATH
ID GRXS9_ARATH Reviewed; 102 AA.
AC O04341; C1JGP8;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Monothiol glutaredoxin-S9;
DE Short=AtGrxS9;
DE AltName: Full=Protein ROXY 7;
GN Name=GRXS9; Synonyms=ROXY7; OrderedLocusNames=At2g30540; ORFNames=T6B20.11;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 -!- INTERACTION:
CC O04341; Q39237: TGA1; NbExp=3; IntAct=EBI-4450582, EBI-541351;
CC O04341; Q39234: TGA3; NbExp=4; IntAct=EBI-4450582, EBI-541366;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CC-type subfamily.
CC {ECO:0000305}.
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DR EMBL; FJ611907; ACO50412.1; -; mRNA.
DR EMBL; U93215; AAB63083.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08405.1; -; Genomic_DNA.
DR EMBL; AY127010; AAM83235.1; -; mRNA.
DR EMBL; BT001028; AAN46782.1; -; mRNA.
DR EMBL; AY087910; AAM65461.1; -; mRNA.
DR PIR; F84709; F84709.
DR RefSeq; NP_180612.1; NM_128606.3.
DR AlphaFoldDB; O04341; -.
DR SMR; O04341; -.
DR BioGRID; 2952; 8.
DR IntAct; O04341; 7.
DR STRING; 3702.AT2G30540.1; -.
DR PaxDb; O04341; -.
DR PRIDE; O04341; -.
DR ProteomicsDB; 222256; -.
DR EnsemblPlants; AT2G30540.1; AT2G30540.1; AT2G30540.
DR GeneID; 817603; -.
DR Gramene; AT2G30540.1; AT2G30540.1; AT2G30540.
DR KEGG; ath:AT2G30540; -.
DR Araport; AT2G30540; -.
DR TAIR; locus:2064327; AT2G30540.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_026126_6_0_1; -.
DR InParanoid; O04341; -.
DR OMA; NEIMSHR; -.
DR OrthoDB; 1492265at2759; -.
DR PhylomeDB; O04341; -.
DR PRO; PR:O04341; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O04341; baseline and differential.
DR Genevisible; O04341; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 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 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Redox-active center;
KW Reference proteome.
FT CHAIN 1..102
FT /note="Monothiol glutaredoxin-S9"
FT /id="PRO_0000268730"
FT DOMAIN 1..101
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
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; 11080 MW; 22A4513956689BA1 CRC64;
MDKVVRMSSE KGVVIFSKSS CCMSYAVQVL FQDLGVHPTV HEIDKDPECR EIEKALMRLG
CSTPVPAIFV GGKLIGSTNE VMSLHLSGSL VPLVKPFQAN LC
