GRS17_ARATH
ID GRS17_ARATH Reviewed; 488 AA.
AC Q9ZPH2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Monothiol glutaredoxin-S17 {ECO:0000303|PubMed:15170506};
DE Short=AtGrxS17 {ECO:0000303|PubMed:15170506};
GN Name=GRXS17 {ECO:0000303|PubMed:15170506};
GN OrderedLocusNames=At4g04950 {ECO:0000312|Araport:AT4G04950};
GN ORFNames=T1J1.6 {ECO:0000312|EMBL:AAD17344.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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).
RN [6]
RP INTERACTION WITH SUFE1; BOLA1; BOLA2 AND BOLA4, AND DOMAIN.
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 [7]
RP FUNCTION, AND INTERACTION WITH BOLA2.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RGLG3 AND RGLG4, AND
RP UBIQUITINATION AT LYS-154.
RX PubMed=27497447; DOI=10.1093/pcp/pcw122;
RA Nagels Durand A., Inigo S., Ritter A., Iniesto E., De Clercq R., Staes A.,
RA Van Leene J., Rubio V., Gevaert K., De Jaeger G., Pauwels L., Goossens A.;
RT "The Arabidopsis iron-sulfur protein GRXS17 is a target of the ubiquitin E3
RT ligases RGLG3 and RGLG4.";
RL Plant Cell Physiol. 57:1801-1813(2016).
CC -!- FUNCTION: May only reduce GSH-thiol disulfides, but not protein
CC disulfides (Probable). Participates probably to the maturation of iron-
CC sulfur proteins and to the regulation of the redox state of the BOLA
CC proteins. The GRXS17-BOLA2 heterodimer binds a labile, oxygen sensitive
CC iron-sulfur cluster (PubMed:24714563). {ECO:0000269|PubMed:24714563,
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 BOLA2 (PubMed:24203231, PubMed:24714563). Interacts
CC with RGLG3 and RGLG4 (PubMed:27497447). {ECO:0000250|UniProtKB:Q03835,
CC ECO:0000269|PubMed:24203231, ECO:0000269|PubMed:24714563,
CC ECO:0000269|PubMed:27497447}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The Glutaredoxin 2 domain is sufficient for interaction with
CC all BOLA. {ECO:0000269|PubMed:24203231}.
CC -!- PTM: Ubiquitinated at Lys-154. Polyubiquitinated by RGLG3 and RGLG4.
CC Polyubiquitination of GRXS17 leads to its degradation by the
CC proteasome. {ECO:0000269|PubMed:27497447}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CGFS subfamily.
CC {ECO:0000305}.
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DR EMBL; AF128393; AAD17344.1; -; Genomic_DNA.
DR EMBL; AL161502; CAB81037.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82446.1; -; Genomic_DNA.
DR EMBL; AY058202; AAL25614.1; -; mRNA.
DR EMBL; AY142003; AAM98267.1; -; mRNA.
DR PIR; C85062; C85062.
DR RefSeq; NP_192404.1; NM_116733.4.
DR AlphaFoldDB; Q9ZPH2; -.
DR SMR; Q9ZPH2; -.
DR BioGRID; 11146; 43.
DR IntAct; Q9ZPH2; 7.
DR STRING; 3702.AT4G04950.1; -.
DR PaxDb; Q9ZPH2; -.
DR PRIDE; Q9ZPH2; -.
DR ProteomicsDB; 222362; -.
DR EnsemblPlants; AT4G04950.1; AT4G04950.1; AT4G04950.
DR GeneID; 825835; -.
DR Gramene; AT4G04950.1; AT4G04950.1; AT4G04950.
DR KEGG; ath:AT4G04950; -.
DR Araport; AT4G04950; -.
DR TAIR; locus:2135363; AT4G04950.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_12_2_1; -.
DR InParanoid; Q9ZPH2; -.
DR OMA; KPVMLFM; -.
DR OrthoDB; 1449534at2759; -.
DR PhylomeDB; Q9ZPH2; -.
DR PRO; PR:Q9ZPH2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZPH2; baseline and differential.
DR Genevisible; Q9ZPH2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; 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:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:TAIR.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0051726; P:regulation of cell cycle; IEP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR CDD; cd03028; GRX_PICOT_like; 3.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR033658; GRX_PICOT-like.
DR InterPro; IPR004480; Monothiol_GRX-rel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10293; PTHR10293; 4.
DR Pfam; PF00462; Glutaredoxin; 3.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR00365; TIGR00365; 3.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Redox-active center;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..488
FT /note="Monothiol glutaredoxin-S17"
FT /id="PRO_0000268737"
FT DOMAIN 2..107
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 154..256
FT /note="Glutaredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT DOMAIN 284..386
FT /note="Glutaredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT DOMAIN 391..488
FT /note="Glutaredoxin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 408
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT BINDING 416
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 445
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT BINDING 457
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT BINDING 470..471
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
SQ SEQUENCE 488 AA; 53115 MW; 09C3D80A78FDA016 CRC64;
MSGTVKDIVS KAELDNLRQS GAPVVLHFWA SWCDASKQMD QVFSHLATDF PRAHFFRVEA
EEHPEISEAY SVAAVPYFVF FKDGKTVDTL EGADPSSLAN KVGKVAGSST SAEPAAPASL
GLAAGPTILE TVKENAKASL QDRAQPVSTA DALKSRLEKL TNSHPVMLFM KGIPEEPRCG
FSRKVVDILK EVNVDFGSFD ILSDNEVREG LKKFSNWPTF PQLYCNGELL GGADIAIAMH
ESGELKDAFK DLGITTVGSK ESQDEAGKGG GVSSGNTGLS ETLRARLEGL VNSKPVMLFM
KGRPEEPKCG FSGKVVEILN QEKIEFGSFD ILLDDEVRQG LKVYSNWSSY PQLYVKGELM
GGSDIVLEMQ KSGELKKVLT EKGITGEQSL EDRLKALINS SEVMLFMKGS PDEPKCGFSS
KVVKALRGEN VSFGSFDILT DEEVRQGIKN FSNWPTFPQL YYKGELIGGC DIIMELSESG
DLKATLSE
