GRS14_ARATH
ID GRS14_ARATH Reviewed; 173 AA.
AC Q84Y95; Q9SV38;
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-S14, chloroplastic {ECO:0000303|PubMed:15170506};
DE Short=AtGRXcp {ECO:0000303|PubMed:16829529};
DE Short=AtGrxS14 {ECO:0000303|PubMed:15170506};
DE AltName: Full=CAX-interacting protein 1 {ECO:0000303|PubMed:12480930};
DE Short=CXIP1 {ECO:0000303|PubMed:12480930};
DE Flags: Precursor;
GN Name=GRXS14 {ECO:0000303|PubMed:15170506};
GN Synonyms=CXIP1 {ECO:0000303|PubMed:12480930},
GN GRX5P {ECO:0000303|PubMed:18044966}, GRXCP {ECO:0000303|PubMed:16829529};
GN OrderedLocusNames=At3g54900 {ECO:0000312|Araport:AT3G54900};
GN ORFNames=F28P10.120 {ECO:0000312|EMBL:CAB41094.1};
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 [MRNA], INTERACTION WITH CAX1, TISSUE SPECIFICITY,
RP INDUCTION, AND MUTAGENESIS OF 97-CYS--SER-100 AND 133-SER--THR-137.
RX PubMed=12480930; DOI=10.1074/jbc.m210883200;
RA Cheng N.-H., Hirschi K.D.;
RT "Cloning and characterization of CXIP1 A novel PICOT domain-containing
RT Arabidopsis protein that associates with CAX1.";
RL J. Biol. Chem. 278:6503-6509(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS
RP OF CYS-97 AND PHE-99, AND DISRUPTION PHENOTYPE.
RX PubMed=16829529; DOI=10.1074/jbc.m601354200;
RA Cheng N.-H., Liu J.-Z., Brock A., Nelson R.S., Hirschi K.D.;
RT "AtGRXcp, an Arabidopsis chloroplastic glutaredoxin, is critical for
RT protection against protein oxidative damage.";
RL J. Biol. Chem. 281:26280-26288(2006).
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).
RN [8]
RP FUNCTION, AND IRON-SULFUR CLUSTER BINDING.
RX PubMed=18044966; DOI=10.1021/bi7013272;
RA Picciocchi A., Saguez C., Boussac A., Cassier-Chauvat C., Chauvat F.;
RT "CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis
RT PCC6803 and other evolutionary distant model organisms possess a
RT glutathione-ligated [2Fe-2S] cluster.";
RL Biochemistry 46:15018-15026(2007).
RN [9]
RP INTERACTION WITH SUFE1; BOLA1; BOLA2 AND BOLA4, AND MUTAGENESIS OF CYS-97.
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).
RN [10]
RP FUNCTION, AND INTERACTION WITH BOLA1.
RX PubMed=24714563; DOI=10.4161/psb.28564;
RA Dhalleine T., Rouhier N., Couturier J.;
RT "Putative roles of glutaredoxin-BolA holo-heterodimers in plants.";
RL Plant Signal. Behav. 9:E28564-E28564(2014).
RN [11]
RP INTERACTION WITH SBP1.
RX PubMed=30824043; DOI=10.1016/j.plantsci.2019.01.021;
RA Valassakis C., Dervisi I., Agalou A., Papandreou N., Kapetsis G., Podia V.,
RA Haralampidis K., Iconomidou V.A., Spaink H.P., Roussis A.;
RT "Novel interactions of selenium binding protein family with the PICOT
RT containing proteins AtGRXS14 and AtGRXS16 in Arabidopsis thaliana.";
RL Plant Sci. 281:102-112(2019).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 65-173.
RX PubMed=20516625; DOI=10.1107/s0907444910013119;
RA Li L., Cheng N., Hirschi K.D., Wang X.;
RT "Structure of Arabidopsis chloroplastic monothiol glutaredoxin AtGRXcp.";
RL Acta Crystallogr. D 66:725-732(2010).
RN [13]
RP STRUCTURE BY NMR OF 67-173 IN COMPLEX WITH BOLA1, AND DOMAIN.
RX PubMed=25012657; DOI=10.1074/jbc.m114.572701;
RA Roret T., Tsan P., Couturier J., Zhang B., Johnson M.K., Rouhier N.,
RA Didierjean C.;
RT "Structural and spectroscopic insights into BolA-glutaredoxin complexes.";
RL J. Biol. Chem. 289:24588-24598(2014).
CC -!- FUNCTION: May only reduce GSH-thiol disulfides, but not protein
CC disulfides (Potential). Probably involved in the regulation of the
CC redox state of the BOLA proteins (Potential). May act as Fe-S cluster
CC donors to Fe-S cluster-requiring proteins (PubMed:18044966). May
CC protect cells against protein oxidative damage (PubMed:16829529). May
CC regulate CAX cation transporters (PubMed:16829529). The GRXS14-BOLA1
CC heterodimer binds a labile, oxygen sensitive Fe-S cluster
CC (PubMed:24714563). {ECO:0000269|PubMed:16829529,
CC ECO:0000269|PubMed:18044966, ECO:0000269|PubMed:24714563, ECO:0000305}.
CC -!- SUBUNIT: [2Fe-2S]-bridged holo-homodimer (By similarity). Interacts
CC with N-terminal part of CAX1 in yeast (PubMed:12480930). Interacts in
CC vitro with SUFE1, BOLA1, BOLA2 and BOLA4 (PubMed:24203231). Interacts
CC in vivo only with SUFE1, BOLA1 and BOLA4 (PubMed:24203231,
CC PubMed:24714563, PubMed:12480930) (By similarity). Interacts with SBP1
CC (PubMed:30824043). {ECO:0000250|UniProtKB:Q03835,
CC ECO:0000269|PubMed:12480930, ECO:0000269|PubMed:24203231,
CC ECO:0000269|PubMed:24714563, ECO:0000269|PubMed:30824043}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16829529}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves, at intermediate levels
CC in stems and at lower levels in roots and flowers.
CC {ECO:0000269|PubMed:12480930, ECO:0000269|PubMed:16829529}.
CC -!- INDUCTION: By sodium and magnesium chloride.
CC {ECO:0000269|PubMed:12480930, ECO:0000269|PubMed:16829529}.
CC -!- DOMAIN: The C-terminal region (79-168) is involved in BOLA recognition
CC in GRXS-BOLA apo-heterodimer. {ECO:0000269|PubMed:25012657}.
CC -!- DISRUPTION PHENOTYPE: Plants display high sensitivity to external
CC oxidants, and their content of protein carbonylation is higher than
CC wild-type plants. {ECO:0000269|PubMed:16829529}.
CC -!- MISCELLANEOUS: The GRXS14-BOLA1 apo-heterodimer model derived from NMR
CC data shows a domain arrangement totally different from the holo-
CC heterodimer showing evidence for a Rieske-type ligation of a [2Fe-2S]
CC cluster. {ECO:0000269|PubMed:25012657}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CGFS subfamily.
CC {ECO:0000305}.
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DR EMBL; AY157988; AAO19647.1; -; mRNA.
DR EMBL; AL049655; CAB41094.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79309.1; -; Genomic_DNA.
DR EMBL; AF385708; AAK60300.1; -; mRNA.
DR EMBL; AY078020; AAL77721.1; -; mRNA.
DR PIR; T06730; T06730.
DR RefSeq; NP_191050.1; NM_115347.4.
DR PDB; 2MMA; NMR; -; A=65-173.
DR PDB; 3IPZ; X-ray; 2.40 A; A=65-173.
DR PDBsum; 2MMA; -.
DR PDBsum; 3IPZ; -.
DR AlphaFoldDB; Q84Y95; -.
DR BMRB; Q84Y95; -.
DR SMR; Q84Y95; -.
DR BioGRID; 9971; 10.
DR IntAct; Q84Y95; 4.
DR STRING; 3702.AT3G54900.1; -.
DR PaxDb; Q84Y95; -.
DR PRIDE; Q84Y95; -.
DR ProteomicsDB; 222275; -.
DR EnsemblPlants; AT3G54900.1; AT3G54900.1; AT3G54900.
DR GeneID; 824655; -.
DR Gramene; AT3G54900.1; AT3G54900.1; AT3G54900.
DR KEGG; ath:AT3G54900; -.
DR Araport; AT3G54900; -.
DR TAIR; locus:2082647; AT3G54900.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_3_2_1; -.
DR InParanoid; Q84Y95; -.
DR OMA; YVEGEFF; -.
DR OrthoDB; 1449534at2759; -.
DR PhylomeDB; Q84Y95; -.
DR EvolutionaryTrace; Q84Y95; -.
DR PRO; PR:Q84Y95; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84Y95; baseline and differential.
DR Genevisible; Q84Y95; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
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:0015297; F:antiporter activity; IDA:TAIR.
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; IDA: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; 3D-structure; Chloroplast; Disulfide bond; Glutathionylation; Iron;
KW Iron-sulfur; Metal-binding; Plastid; Redox-active center;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..173
FT /note="Monothiol glutaredoxin-S14, chloroplastic"
FT /id="PRO_0000268734"
FT DOMAIN 72..173
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT REGION 97..100
FT /note="Required for CAX1 activation"
FT REGION 133..137
FT /note="Required for CAX1 activation"
FT BINDING 89
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT BINDING 97
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305|PubMed:18044966,
FT ECO:0000305|PubMed:20516625"
FT BINDING 99
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305|PubMed:18044966,
FT ECO:0000305|PubMed:20516625"
FT BINDING 126
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT BINDING 130
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000305|PubMed:20516625"
FT BINDING 138
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT BINDING 151..152
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT MOD_RES 97
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS18"
FT DISULFID 172
FT /note="Interchain"
FT /evidence="ECO:0000305|PubMed:20516625"
FT MUTAGEN 97..100
FT /note="CGFS->AAAA: Loss of CAX1 activation."
FT /evidence="ECO:0000269|PubMed:12480930"
FT MUTAGEN 97
FT /note="C->A: Decreases protein stability."
FT /evidence="ECO:0000269|PubMed:16829529"
FT MUTAGEN 97
FT /note="C->S: No effect on interactions with BOLA proteins,
FT but strongly reduced interaction with SUFE1."
FT /evidence="ECO:0000269|PubMed:24203231"
FT MUTAGEN 99
FT /note="F->A: No effect on protein stability."
FT /evidence="ECO:0000269|PubMed:16829529"
FT MUTAGEN 133..137
FT /note="SNWPT->AAAAA: Loss of CAX1 activation."
FT /evidence="ECO:0000269|PubMed:12480930"
FT CONFLICT 14
FT /note="S -> P (in Ref. 1; AAO19647)"
FT /evidence="ECO:0000305"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:3IPZ"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:3IPZ"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:3IPZ"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:3IPZ"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:3IPZ"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3IPZ"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:3IPZ"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3IPZ"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:3IPZ"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:3IPZ"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:3IPZ"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:3IPZ"
SQ SEQUENCE 173 AA; 19309 MW; 3C005CCD72742A09 CRC64;
MALRSVKTPT LITSVAVVSS SVTNKPHSIR FSLKPTSALV VHNHQLSFYG SNLKLKPTKF
RCSASALTPQ LKDTLEKLVN SEKVVLFMKG TRDFPMCGFS NTVVQILKNL NVPFEDVNIL
ENEMLRQGLK EYSNWPTFPQ LYIGGEFFGG CDITLEAFKT GELQEEVEKA MCS
