ID   GRXC2_ARATH             Reviewed;         111 AA.
AC   Q9FNE2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 140.
DE   RecName: Full=Glutaredoxin-C2;
DE            Short=AtGrxC2;
GN   Name=GRXC2; Synonyms=GRX370; OrderedLocusNames=At5g40370;
GN   ORFNames=MPO12.80;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA   Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT   features of the regions of 1,044,062 bp covered by thirteen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:291-300(1997).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9FNE2-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. CPYC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB006702; BAB11592.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94538.1; -; Genomic_DNA.
DR   EMBL; AY064153; AAL36059.1; -; mRNA.
DR   EMBL; AY072307; AAL61914.1; -; mRNA.
DR   EMBL; AY097411; AAM19927.1; -; mRNA.
DR   EMBL; AY114546; AAM47865.1; -; mRNA.
DR   EMBL; AY086319; AAM64389.1; -; mRNA.
DR   RefSeq; NP_198853.1; NM_123401.4. [Q9FNE2-1]
DR   AlphaFoldDB; Q9FNE2; -.
DR   SMR; Q9FNE2; -.
DR   STRING; 3702.AT5G40370.2; -.
DR   iPTMnet; Q9FNE2; -.
DR   PaxDb; Q9FNE2; -.
DR   PRIDE; Q9FNE2; -.
DR   ProteomicsDB; 222251; -. [Q9FNE2-1]
DR   EnsemblPlants; AT5G40370.1; AT5G40370.1; AT5G40370. [Q9FNE2-1]
DR   GeneID; 834035; -.
DR   Gramene; AT5G40370.1; AT5G40370.1; AT5G40370. [Q9FNE2-1]
DR   KEGG; ath:AT5G40370; -.
DR   Araport; AT5G40370; -.
DR   eggNOG; KOG1752; Eukaryota.
DR   HOGENOM; CLU_026126_7_2_1; -.
DR   InParanoid; Q9FNE2; -.
DR   OMA; GRTTFPQ; -.
DR   PhylomeDB; Q9FNE2; -.
DR   PRO; PR:Q9FNE2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FNE2; baseline and differential.
DR   Genevisible; Q9FNE2; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   InterPro; IPR011767; GLR_AS.
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; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Cytoplasm; Disulfide bond; Electron transport;
KW   Redox-active center; Reference proteome; Transport.
FT   CHAIN           1..111
FT                   /note="Glutaredoxin-C2"
FT                   /id="PRO_0000268709"
FT   DOMAIN          3..103
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        23..26
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   111 AA;  11756 MW;  9059BE52259C83C4 CRC64;
     MAMQKAKEIV NSESVVVFSK TYCPYCVRVK ELLQQLGAKF KAVELDTESD GSQIQSGLAE
     WTGQRTVPNV FIGGNHIGGC DATSNLHKDG KLVPLLTEAG AIAGKTATTS A