GRC13_ARATH
ID GRC13_ARATH Reviewed; 102 AA.
AC O82255; C1JGQ0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glutaredoxin-C13;
DE Short=AtGrxC13;
DE AltName: Full=Protein ROXY 9;
GN Name=GRXC13; Synonyms=ROXY9; OrderedLocusNames=At2g47880;
GN ORFNames=F17A22.27, T9J23.13;
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=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;
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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: Has a glutathione-disulfide oxidoreductase activity in the
CC presence of NADPH and glutathione reductase. Reduces low molecular
CC weight disulfides and proteins (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O82255; Q9FVU9: CSN5B; NbExp=3; IntAct=EBI-4444060, EBI-697501;
CC O82255; Q39237: TGA1; NbExp=3; IntAct=EBI-4444060, EBI-541351;
CC O82255; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-4444060, EBI-4426557;
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; FJ611909; ACO50414.1; -; mRNA.
DR EMBL; AC005309; AAC63642.1; -; Genomic_DNA.
DR EMBL; AC006072; AAM15127.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10904.1; -; Genomic_DNA.
DR EMBL; AK221443; BAD94488.1; -; mRNA.
DR EMBL; BT025025; ABE02400.1; -; mRNA.
DR EMBL; AY086073; AAM63279.1; -; mRNA.
DR PIR; F84920; F84920.
DR RefSeq; NP_182309.1; NM_130355.5.
DR AlphaFoldDB; O82255; -.
DR SMR; O82255; -.
DR BioGRID; 4735; 4.
DR IntAct; O82255; 4.
DR STRING; 3702.AT2G47880.1; -.
DR PaxDb; O82255; -.
DR PRIDE; O82255; -.
DR ProteomicsDB; 220656; -.
DR EnsemblPlants; AT2G47880.1; AT2G47880.1; AT2G47880.
DR GeneID; 819400; -.
DR Gramene; AT2G47880.1; AT2G47880.1; AT2G47880.
DR KEGG; ath:AT2G47880; -.
DR Araport; AT2G47880; -.
DR TAIR; locus:2043423; AT2G47880.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_026126_6_0_1; -.
DR InParanoid; O82255; -.
DR OMA; RPMVHEI; -.
DR OrthoDB; 1492265at2759; -.
DR PhylomeDB; O82255; -.
DR PRO; PR:O82255; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82255; baseline and differential.
DR Genevisible; O82255; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
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; 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 Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..102
FT /note="Glutaredoxin-C13"
FT /id="PRO_0000268720"
FT DOMAIN 1..101
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT DISULFID 21..24
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 102 AA; 11275 MW; 931C4D1825C9868D CRC64;
MDKVMRMSSE KGVVIFTKSS CCLCYAVQIL FRDLRVQPTI HEIDNDPDCR EIEKALLRLG
CSTAVPAVFV GGKLVGSTNE VMSLHLSGSL VPLIKPYQSI LY
