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GRXC3_ARATH
ID   GRXC3_ARATH             Reviewed;         130 AA.
AC   Q9FVX1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Glutaredoxin-C3;
DE            Short=AtGrxC3;
GN   Name=GRXC3; OrderedLocusNames=At1g77370; ORFNames=F2P24.8;
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 [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   [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   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   [5]
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}.
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DR   EMBL; AC078898; AAG29202.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35970.1; -; Genomic_DNA.
DR   EMBL; AY065377; AAL38818.1; -; mRNA.
DR   EMBL; AY096542; AAM20192.1; -; mRNA.
DR   PIR; G96802; G96802.
DR   RefSeq; NP_177861.1; NM_106386.5.
DR   AlphaFoldDB; Q9FVX1; -.
DR   SMR; Q9FVX1; -.
DR   BioGRID; 29292; 1.
DR   IntAct; Q9FVX1; 1.
DR   STRING; 3702.AT1G77370.1; -.
DR   PaxDb; Q9FVX1; -.
DR   PRIDE; Q9FVX1; -.
DR   ProteomicsDB; 222363; -.
DR   EnsemblPlants; AT1G77370.1; AT1G77370.1; AT1G77370.
DR   GeneID; 844073; -.
DR   Gramene; AT1G77370.1; AT1G77370.1; AT1G77370.
DR   KEGG; ath:AT1G77370; -.
DR   Araport; AT1G77370; -.
DR   TAIR; locus:2031452; AT1G77370.
DR   eggNOG; KOG1752; Eukaryota.
DR   HOGENOM; CLU_026126_7_2_1; -.
DR   InParanoid; Q9FVX1; -.
DR   OMA; EYACYEL; -.
DR   PhylomeDB; Q9FVX1; -.
DR   PRO; PR:Q9FVX1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FVX1; baseline and differential.
DR   Genevisible; Q9FVX1; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0000137; C:Golgi cis cisterna; HDA: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..130
FT                   /note="Glutaredoxin-C3"
FT                   /id="PRO_0000268710"
FT   DOMAIN          34..130
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        54..57
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   130 AA;  14247 MW;  FFD408106C5357E8 CRC64;
     MVDQSPRRVV VAALLLFVVL CDLSNSAGAA NSVSAFVQNA ILSNKIVIFS KSYCPYCLRS
     KRIFSQLKEE PFVVELDQRE DGDQIQYELL EFVGRRTVPQ VFVNGKHIGG SDDLGAALES
     GQLQKLLAAS
 
 
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