ID   GRXC1_ARATH             Reviewed;         125 AA.
AC   Q8L8T2; Q8RXH1; Q9FM49;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Glutaredoxin-C1;
DE            Short=AtGrxC1;
GN   Name=GRXC1; OrderedLocusNames=At5g63030; ORFNames=MJH22.9;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [2]
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   [3]
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   [4]
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   [5]
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   [6]
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. CPYC subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB08846.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB009051; BAB08846.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED97688.1; -; Genomic_DNA.
DR   EMBL; AY081257; AAL91146.1; -; mRNA.
DR   EMBL; AY114565; AAM47884.1; -; mRNA.
DR   EMBL; AY088825; AAM67134.1; -; mRNA.
DR   RefSeq; NP_568962.1; NM_125697.3.
DR   AlphaFoldDB; Q8L8T2; -.
DR   SMR; Q8L8T2; -.
DR   BioGRID; 21666; 30.
DR   IntAct; Q8L8T2; 30.
DR   STRING; 3702.AT5G63030.1; -.
DR   iPTMnet; Q8L8T2; -.
DR   PaxDb; Q8L8T2; -.
DR   PRIDE; Q8L8T2; -.
DR   ProteomicsDB; 222278; -.
DR   EnsemblPlants; AT5G63030.1; AT5G63030.1; AT5G63030.
DR   GeneID; 836423; -.
DR   Gramene; AT5G63030.1; AT5G63030.1; AT5G63030.
DR   KEGG; ath:AT5G63030; -.
DR   Araport; AT5G63030; -.
DR   TAIR; locus:2166325; AT5G63030.
DR   eggNOG; KOG1752; Eukaryota.
DR   HOGENOM; CLU_026126_7_2_1; -.
DR   InParanoid; Q8L8T2; -.
DR   OMA; YCHKARA; -.
DR   OrthoDB; 1535999at2759; -.
DR   PhylomeDB; Q8L8T2; -.
DR   PRO; PR:Q8L8T2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8L8T2; baseline and differential.
DR   Genevisible; Q8L8T2; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR   GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR011899; Glutaredoxin_euk/vir.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR02180; GRX_euk; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..125
FT                   /note="Glutaredoxin-C1"
FT                   /id="PRO_0000268708"
FT   DOMAIN          19..119
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        39..42
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        91
FT                   /note="N -> K (in Ref. 4; AAM67134)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   125 AA;  13611 MW;  F6FA57B0F3448917 CRC64;
     MGSMFSGNRM SKEEMEVVVN KAKEIVSAYP VVVFSKTYCG YCQRVKQLLT QLGATFKVLE
     LDEMSDGGEI QSALSEWTGQ TTVPNVFIKG NHIGGCDRVM ETNKQGKLVP LLTEAGAIAD
     NSSQL