GRXS7_ARATH
ID GRXS7_ARATH Reviewed; 102 AA.
AC Q6NLU2; C1JGQ5; O23418;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Monothiol glutaredoxin-S7;
DE Short=AtGrxS7;
DE AltName: Full=Protein ROXY 14;
GN Name=GRXS7; Synonyms=ROXY14; OrderedLocusNames=At4g15670;
GN ORFNames=dl3875w, FCAALL.355;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [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 (MAR-2004) 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 Q6NLU2; Q39237: TGA1; NbExp=3; IntAct=EBI-25521272, EBI-541351;
CC Q6NLU2; Q39234: TGA3; NbExp=3; IntAct=EBI-25521272, EBI-541366;
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=AAS47604.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS76724.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; FJ611914; ACO50419.1; -; mRNA.
DR EMBL; Z97339; CAB10345.1; -; Genomic_DNA.
DR EMBL; AL161542; CAB78609.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83634.1; -; Genomic_DNA.
DR EMBL; BT011598; AAS47604.1; ALT_INIT; mRNA.
DR EMBL; BT012237; AAS76724.1; ALT_INIT; mRNA.
DR PIR; G71421; G71421.
DR RefSeq; NP_193302.1; NM_117658.4.
DR AlphaFoldDB; Q6NLU2; -.
DR SMR; Q6NLU2; -.
DR BioGRID; 12538; 2.
DR IntAct; Q6NLU2; 2.
DR STRING; 3702.AT4G15670.1; -.
DR PaxDb; Q6NLU2; -.
DR PRIDE; Q6NLU2; -.
DR ProteomicsDB; 222312; -.
DR EnsemblPlants; AT4G15670.1; AT4G15670.1; AT4G15670.
DR GeneID; 827244; -.
DR Gramene; AT4G15670.1; AT4G15670.1; AT4G15670.
DR KEGG; ath:AT4G15670; -.
DR Araport; AT4G15670; -.
DR TAIR; locus:2130554; AT4G15670.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_026126_6_0_1; -.
DR InParanoid; Q6NLU2; -.
DR OMA; GHEIEAA; -.
DR OrthoDB; 1535999at2759; -.
DR PhylomeDB; Q6NLU2; -.
DR PRO; PR:Q6NLU2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q6NLU2; 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 InterPro; IPR011905; GlrX-like_pln_2.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR10168; PTHR10168; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
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; Nucleus;
KW Redox-active center; Reference proteome.
FT CHAIN 1..102
FT /note="Monothiol glutaredoxin-S7"
FT /id="PRO_0000268728"
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; 11244 MW; CBBCA2E407C18107 CRC64;
MEKLQKMTSE KSLVIFSKNS CCMSHTIKTL FLDLGVNPTI YELDEINRGK EIEQALAQLG
CSPTVPVVFI GGQLVGGANQ VMSLHLNRSL IPMLKRVGAL WL
