GRXC9_ARATH
ID GRXC9_ARATH Reviewed; 137 AA.
AC Q9SGP6; C1JGQ9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glutaredoxin-C9;
DE Short=AtGrxC9;
DE AltName: Full=Protein ROXY 19;
GN Name=GRXC9; Synonyms=GRX480, ROXY19; OrderedLocusNames=At1g28480;
GN ORFNames=F3M18.8;
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 [GENOMIC DNA], INDUCTION, AND INTERACTION WITH TGA2 AND
RP TGA6.
RX PubMed=17397508; DOI=10.1111/j.1365-313x.2007.03039.x;
RA Ndamukong I., Abdallat A.A., Thurow C., Fode B., Zander M., Weigel R.,
RA Gatz C.;
RT "SA-inducible Arabidopsis glutaredoxin interacts with TGA factors and
RT suppresses JA-responsive PDF1.2 transcription.";
RL Plant J. 50:128-139(2007).
RN [2]
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 [3]
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 [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;
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 [6]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
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 -!- SUBUNIT: Interacts with TGA2 and TGA6. {ECO:0000269|PubMed:17397508}.
CC -!- INTERACTION:
CC Q9SGP6; P43273: TGA2; NbExp=6; IntAct=EBI-1545762, EBI-541307;
CC Q9SGP6; Q39234: TGA3; NbExp=3; IntAct=EBI-1545762, EBI-541366;
CC Q9SGP6; Q39140: TGA6; NbExp=4; IntAct=EBI-1545762, EBI-541321;
CC Q9SGP6; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-1545762, EBI-4426557;
CC Q9SGP6; Q9SQK1: TGA2.2; Xeno; NbExp=5; IntAct=EBI-1545762, EBI-1545751;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by salicylic acid (SA).
CC {ECO:0000269|PubMed:17397508}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CC-type subfamily.
CC {ECO:0000305}.
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DR EMBL; FJ611918; ACO50423.1; -; mRNA.
DR EMBL; AC010155; AAF16751.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30981.1; -; Genomic_DNA.
DR EMBL; AF325030; AAG40382.1; -; mRNA.
DR EMBL; AK229369; BAF01232.1; -; mRNA.
DR EMBL; BT029336; ABK32150.1; -; mRNA.
DR PIR; H86410; H86410.
DR RefSeq; NP_174170.1; NM_102616.2.
DR AlphaFoldDB; Q9SGP6; -.
DR SMR; Q9SGP6; -.
DR BioGRID; 24983; 8.
DR IntAct; Q9SGP6; 12.
DR STRING; 3702.AT1G28480.1; -.
DR PaxDb; Q9SGP6; -.
DR PRIDE; Q9SGP6; -.
DR EnsemblPlants; AT1G28480.1; AT1G28480.1; AT1G28480.
DR GeneID; 839748; -.
DR Gramene; AT1G28480.1; AT1G28480.1; AT1G28480.
DR KEGG; ath:AT1G28480; -.
DR Araport; AT1G28480; -.
DR TAIR; locus:2032574; AT1G28480.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_026126_6_2_1; -.
DR InParanoid; Q9SGP6; -.
DR OMA; FIGGRMF; -.
DR OrthoDB; 1598650at2759; -.
DR PhylomeDB; Q9SGP6; -.
DR PRO; PR:Q9SGP6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGP6; baseline and differential.
DR Genevisible; Q9SGP6; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR GO; GO:0009863; P:salicylic acid mediated signaling pathway; IMP: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 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Electron transport; Nucleus;
KW Redox-active center; Reference proteome; Transport.
FT CHAIN 1..137
FT /note="Glutaredoxin-C9"
FT /id="PRO_0000268716"
FT DOMAIN 32..136
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT MOTIF 134..137
FT /note="Responsive for interaction with TGA factors"
FT /evidence="ECO:0000250"
FT DISULFID 52..55
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 137 AA; 14758 MW; 3009870CF31CE3DE CRC64;
MQGTISCARN YNMTTTVGES LRPLSLKTQG NGERVRMVVE ENAVIVIGRR GCCMCHVVRR
LLLGLGVNPA VLEIDEERED EVLSELENIG VQGGGGTVKL PAVYVGGRLF GGLDRVMATH
ISGELVPILK EVGALWL
