GRS15_ARATH
ID GRS15_ARATH Reviewed; 169 AA.
AC Q8LBK6; B9DGX1; Q9LW13;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Monothiol glutaredoxin-S15, mitochondrial {ECO:0000303|PubMed:15170506};
DE Short=AtGrxS15 {ECO:0000303|PubMed:15170506};
DE Flags: Precursor;
GN Name=GRXS15 {ECO:0000303|PubMed:15170506};
GN OrderedLocusNames=At3g15660 {ECO:0000312|Araport:AT3G15660};
GN ORFNames=MSJ11.6 {ECO:0000312|EMBL:BAB02297.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12954611; DOI=10.1074/jbc.m307525200;
RA Chew O., Whelan J., Millar A.H.;
RT "Molecular definition of the ascorbate-glutathione cycle in Arabidopsis
RT mitochondria reveals dual targeting of antioxidant defenses in plants.";
RL J. Biol. Chem. 278:46869-46877(2003).
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).
RN [10]
RP INTERACTION WITH SUFE1; BOLA1; BOLA2 AND BOLA4.
RX PubMed=24203231; DOI=10.1093/mp/sst156;
RA Couturier J., Wu H.C., Dhalleine T., Pegeot H., Sudre D., Gualberto J.M.,
RA Jacquot J.P., Gaymard F., Vignols F., Rouhier N.;
RT "Monothiol glutaredoxin-BolA interactions: redox control of Arabidopsis
RT thaliana BolA2 and SufE1.";
RL Mol. Plant 7:187-205(2014).
CC -!- FUNCTION: May only reduce GSH-thiol disulfides, but not protein
CC disulfides. Participates probably to the maturation of iron-sulfur
CC proteins and to the regulation of the redox state of the BOLA proteins.
CC {ECO:0000305}.
CC -!- SUBUNIT: [2Fe-2S]-bridged holo-homodimer (By similarity). Interacts in
CC vitro with SUFE1, BOLA1, BOLA2 and BOLA4 (PubMed:24203231). Interacts
CC in vivo only with BOLA4 (PubMed:24203231).
CC {ECO:0000250|UniProtKB:Q03835, ECO:0000269|PubMed:24203231}.
CC -!- INTERACTION:
CC Q8LBK6; Q17TI5: BRX; NbExp=3; IntAct=EBI-4427398, EBI-4426649;
CC Q8LBK6; Q8GTS1: BZIP24; NbExp=2; IntAct=EBI-4427398, EBI-2292496;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12954611}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CGFS subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB017071; BAB02297.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75710.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75711.1; -; Genomic_DNA.
DR EMBL; BT006396; AAP21204.1; -; mRNA.
DR EMBL; AK227628; BAE99619.1; -; mRNA.
DR EMBL; AK317312; BAH19988.1; -; mRNA.
DR EMBL; AY087154; AAM64712.1; -; mRNA.
DR RefSeq; NP_001030704.1; NM_001035627.3.
DR RefSeq; NP_566522.1; NM_112436.3.
DR AlphaFoldDB; Q8LBK6; -.
DR SMR; Q8LBK6; -.
DR BioGRID; 6143; 20.
DR IntAct; Q8LBK6; 15.
DR STRING; 3702.AT3G15660.1; -.
DR MetOSite; Q8LBK6; -.
DR PaxDb; Q8LBK6; -.
DR PRIDE; Q8LBK6; -.
DR ProteomicsDB; 222276; -.
DR EnsemblPlants; AT3G15660.1; AT3G15660.1; AT3G15660.
DR EnsemblPlants; AT3G15660.2; AT3G15660.2; AT3G15660.
DR GeneID; 820809; -.
DR Gramene; AT3G15660.1; AT3G15660.1; AT3G15660.
DR Gramene; AT3G15660.2; AT3G15660.2; AT3G15660.
DR KEGG; ath:AT3G15660; -.
DR Araport; AT3G15660; -.
DR TAIR; locus:2093297; AT3G15660.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_3_3_1; -.
DR InParanoid; Q8LBK6; -.
DR OMA; CAFSKRM; -.
DR OrthoDB; 1449534at2759; -.
DR PhylomeDB; Q8LBK6; -.
DR PRO; PR:Q8LBK6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LBK6; baseline and differential.
DR Genevisible; Q8LBK6; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:TAIR.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IGI:TAIR.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IDA:TAIR.
DR GO; GO:0009249; P:protein lipoylation; IMP:TAIR.
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 1: Evidence at protein level;
KW 2Fe-2S; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..169
FT /note="Monothiol glutaredoxin-S15, mitochondrial"
FT /id="PRO_0000268735"
FT DOMAIN 66..168
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT REGION 38..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT BINDING 91
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT BINDING 120
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000255"
FT BINDING 132
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT BINDING 145..146
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT CONFLICT 100
FT /note="V -> I (in Ref. 6; AAM64712)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 169 AA; 18734 MW; 02B44A1F8106473D CRC64;
MAASLSSRLI KGIANLKAVR SSRLTSASVY QNGMMRFSST VPSDSDTHDD FKPTQKVPPD
STDSLKDIVE NDVKDNPVMI YMKGVPESPQ CGFSSLAVRV LQQYNVPISS RNILEDQELK
NAVKSFSHWP TFPQIFIKGE FIGGSDIILN MHKEGELEQK LKDVSGNQD
