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GRS11_ARATH
ID   GRS11_ARATH             Reviewed;          99 AA.
AC   Q9M9Y9; C1JGP7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Monothiol glutaredoxin-S11;
DE            Short=AtGrxS11;
DE   AltName: Full=Protein ROXY 6;
GN   Name=GRXS11; Synonyms=ROXY6; OrderedLocusNames=At1g06830;
GN   ORFNames=F4H5.25, F4H5.9;
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], 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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. CC-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; FJ611906; ACO50411.1; -; mRNA.
DR   EMBL; AC011001; AAF63150.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28043.1; -; Genomic_DNA.
DR   EMBL; AY072366; AAL62358.1; -; mRNA.
DR   EMBL; AY114614; AAM47933.1; -; mRNA.
DR   EMBL; AY085047; AAM61604.1; -; mRNA.
DR   PIR; B86203; B86203.
DR   RefSeq; NP_172168.1; NM_100560.3.
DR   AlphaFoldDB; Q9M9Y9; -.
DR   SMR; Q9M9Y9; -.
DR   BioGRID; 22436; 1.
DR   STRING; 3702.AT1G06830.1; -.
DR   PaxDb; Q9M9Y9; -.
DR   PRIDE; Q9M9Y9; -.
DR   ProteomicsDB; 222249; -.
DR   EnsemblPlants; AT1G06830.1; AT1G06830.1; AT1G06830.
DR   GeneID; 837195; -.
DR   Gramene; AT1G06830.1; AT1G06830.1; AT1G06830.
DR   KEGG; ath:AT1G06830; -.
DR   Araport; AT1G06830; -.
DR   TAIR; locus:2033148; AT1G06830.
DR   eggNOG; KOG1752; Eukaryota.
DR   HOGENOM; CLU_026126_6_0_1; -.
DR   InParanoid; Q9M9Y9; -.
DR   OMA; MRMGING; -.
DR   OrthoDB; 1492265at2759; -.
DR   PhylomeDB; Q9M9Y9; -.
DR   PRO; PR:Q9M9Y9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9M9Y9; baseline and differential.
DR   Genevisible; Q9M9Y9; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0006995; P:cellular response to nitrogen starvation; IGI: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; Redox-active center;
KW   Reference proteome.
FT   CHAIN           1..99
FT                   /note="Monothiol glutaredoxin-S11"
FT                   /id="PRO_0000268731"
FT   DOMAIN          1..99
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   99 AA;  10890 MW;  9DB774E5A6807479 CRC64;
     MDKVMRMSSE KGVVIFTKSS CCLSYAVQVL FQDLGVNPKI HEIDKDPECR EIEKALMRLG
     CSKPVPAVFI GGKLVGSTNE VMSMHLSSSL VPLVKPYLC
 
 
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