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GRS12_ORYSJ
ID   GRS12_ORYSJ             Reviewed;         285 AA.
AC   Q2QX01; A3CFF5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Monothiol glutaredoxin-S12, chloroplastic;
DE   Flags: Precursor;
GN   Name=GRXS12; OrderedLocusNames=Os12g0175500, LOC_Os12g07650;
GN   ORFNames=OsJ_35400 {ECO:0000312|EMBL:EAZ19818.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
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: May only reduce GSH-thiol disulfides, but not protein
CC       disulfides. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. CGFS subfamily.
CC       {ECO:0000305}.
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DR   EMBL; DP000011; ABA96598.1; -; Genomic_DNA.
DR   EMBL; AP008218; BAF29310.1; -; Genomic_DNA.
DR   EMBL; AP014968; BAT16102.1; -; Genomic_DNA.
DR   EMBL; CM000149; EAZ19818.1; -; Genomic_DNA.
DR   EMBL; AK060940; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015618330.1; XM_015762844.1.
DR   AlphaFoldDB; Q2QX01; -.
DR   SMR; Q2QX01; -.
DR   BioGRID; 820684; 1.
DR   STRING; 4530.OS12T0175500-01; -.
DR   PaxDb; Q2QX01; -.
DR   PRIDE; Q2QX01; -.
DR   EnsemblPlants; Os12t0175500-01; Os12t0175500-01; Os12g0175500.
DR   GeneID; 4351647; -.
DR   Gramene; Os12t0175500-01; Os12t0175500-01; Os12g0175500.
DR   KEGG; osa:4351647; -.
DR   eggNOG; KOG0911; Eukaryota.
DR   HOGENOM; CLU_070932_0_0_1; -.
DR   InParanoid; Q2QX01; -.
DR   OMA; AHEMSKH; -.
DR   OrthoDB; 1449534at2759; -.
DR   Proteomes; UP000000763; Chromosome 12.
DR   Proteomes; UP000007752; Chromosome 12.
DR   Proteomes; UP000059680; Chromosome 12.
DR   Genevisible; Q2QX01; OS.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006812; P:cation transport; IEA:EnsemblPlants.
DR   CDD; cd03028; GRX_PICOT_like; 1.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR033658; GRX_PICOT-like.
DR   InterPro; IPR004480; Monothiol_GRX-rel.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR10293; PTHR10293; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR00365; TIGR00365; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Chloroplast; Iron; Iron-sulfur; Metal-binding; Plastid;
KW   Redox-active center; Reference proteome; Transit peptide.
FT   TRANSIT         1..45
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           46..285
FT                   /note="Monothiol glutaredoxin-S12, chloroplastic"
FT                   /id="PRO_0000271281"
FT   DOMAIN          185..285
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..72
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         202
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         267..268
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        159
FT                   /note="T -> I (in Ref. 6; AK060940)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   285 AA;  30590 MW;  B3E9D6101DDA1524 CRC64;
     MATSSAAAAL RLPASQLPLS ARPSSSSTLR FPPRRPARRG GLAVSAFTKL SEASPVAIPP
     EPAQPLPDEE ALPPKPGVYG VYDPAGELQF VGISRNVRAS VEGHRRKVPA DLCGSVKVSI
     ADEETPDRTV LTNAWKSWLE EHITATGKAP PGNVAGNHTW VGPPQRPPDL RLTPGRHVQL
     TVPLEQLIDR LVKDNKVVAF IKGSRSAPQC GFSQRVVGIL ESHGVDFVTV DVLDEEHNHG
     LRETLKTYSN WPTFPQVFVG GELVGGCDIV SSMAEKGELA ALFKK
 
 
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