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Monothiol glutaredoxin-S17 (AtGrxS17)

 GRS17_ARATH             Reviewed;         488 AA.
Q9ZPH2;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-OCT-2017, entry version 120.
RecName: Full=Monothiol glutaredoxin-S17 {ECO:0000303|PubMed:15170506};
Short=AtGrxS17 {ECO:0000303|PubMed:15170506};
Name=GRXS17 {ECO:0000303|PubMed:15170506};
OrderedLocusNames=At4g04950 {ECO:0000312|Araport:AT4G04950};
ORFNames=T1J1.6 {ECO:0000312|EMBL:AAD17344.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15170506; DOI=10.1007/s00018-004-3410-y;
Rouhier N., Gelhaye E., Jacquot J.-P.;
"Plant glutaredoxins: still mysterious reducing systems.";
Cell. Mol. Life Sci. 61:1266-1277(2004).
[5]
GENE FAMILY.
PubMed=16720602; DOI=10.1093/jxb/erl001;
Rouhier N., Couturier J., Jacquot J.-P.;
"Genome-wide analysis of plant glutaredoxin systems.";
J. Exp. Bot. 57:1685-1696(2006).
[6]
INTERACTION WITH SUFE1; BOLA1; BOLA2 AND BOLA4, AND DOMAIN.
PubMed=24203231; DOI=10.1093/mp/sst156;
Couturier J., Wu H.C., Dhalleine T., Pegeot H., Sudre D.,
Gualberto J.M., Jacquot J.P., Gaymard F., Vignols F., Rouhier N.;
"Monothiol glutaredoxin-BolA interactions: redox control of
Arabidopsis thaliana BolA2 and SufE1.";
Mol. Plant 7:187-205(2014).
[7]
FUNCTION, AND INTERACTION WITH BOLA2.
PubMed=24714563; DOI=10.4161/psb.28564;
Dhalleine T., Rouhier N., Couturier J.;
"Putative roles of glutaredoxin-BolA holo-heterodimers in plants.";
Plant Signal. Behav. 9:E28564-E28564(2014).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RGLG3 AND RGLG4,
AND UBIQUITINATION AT LYS-154.
PubMed=27497447; DOI=10.1093/pcp/pcw122;
Nagels Durand A., Inigo S., Ritter A., Iniesto E., De Clercq R.,
Staes A., Van Leene J., Rubio V., Gevaert K., De Jaeger G.,
Pauwels L., Goossens A.;
"The Arabidopsis iron-sulfur protein GRXS17 is a target of the
ubiquitin E3 ligases RGLG3 and RGLG4.";
Plant Cell Physiol. 57:1801-1813(2016).
-!- FUNCTION: May only reduce GSH-thiol disulfides, but not protein
disulfides (Probable). Participates probably to the maturation of
iron-sulfur proteins and to the regulation of the redox state of
the BOLA proteins. The GRXS17-BOLA2 heterodimer binds a labile,
oxygen sensitive iron-sulfur cluster (PubMed:24714563).
{ECO:0000269|PubMed:24714563, ECO:0000305}.
-!- SUBUNIT: [2Fe-2S]-bridged holo-homodimer (By similarity).
Interacts in vitro with SUFE1, BOLA1, BOLA2 and BOLA4
(PubMed:24203231). Interacts in vivo only with BOLA2
(PubMed:24203231, PubMed:24714563). Interacts with RGLG3 and RGLG4
(PubMed:27497447). {ECO:0000250|UniProtKB:Q03835,
ECO:0000269|PubMed:24203231, ECO:0000269|PubMed:24714563,
ECO:0000269|PubMed:27497447}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- DOMAIN: The Glutaredoxin 2 domain is sufficient for interaction
with all BOLA. {ECO:0000269|PubMed:24203231}.
-!- PTM: Ubiquitinated at Lys-154. Polyubiquitinated by RGLG3 and
RGLG4. Polyubiquitination of GRXS17 leads to its degradation by
the proteasome. {ECO:0000269|PubMed:27497447}.
-!- SIMILARITY: Belongs to the glutaredoxin family. CGFS subfamily.
{ECO:0000305}.
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EMBL; AF128393; AAD17344.1; -; Genomic_DNA.
EMBL; AL161502; CAB81037.1; -; Genomic_DNA.
EMBL; CP002687; AEE82446.1; -; Genomic_DNA.
EMBL; AY058202; AAL25614.1; -; mRNA.
EMBL; AY142003; AAM98267.1; -; mRNA.
PIR; C85062; C85062.
RefSeq; NP_192404.1; NM_116733.4.
UniGene; At.4053; -.
ProteinModelPortal; Q9ZPH2; -.
SMR; Q9ZPH2; -.
BioGrid; 11146; 37.
IntAct; Q9ZPH2; 6.
STRING; 3702.AT4G04950.1; -.
PaxDb; Q9ZPH2; -.
PRIDE; Q9ZPH2; -.
EnsemblPlants; AT4G04950.1; AT4G04950.1; AT4G04950.
GeneID; 825835; -.
Gramene; AT4G04950.1; AT4G04950.1; AT4G04950.
KEGG; ath:AT4G04950; -.
Araport; AT4G04950; -.
TAIR; locus:2135363; AT4G04950.
eggNOG; KOG0911; Eukaryota.
eggNOG; COG0278; LUCA.
eggNOG; COG0526; LUCA.
HOGENOM; HOG000165751; -.
InParanoid; Q9ZPH2; -.
OMA; KPVMLFM; -.
OrthoDB; EOG093608AP; -.
PhylomeDB; Q9ZPH2; -.
PRO; PR:Q9ZPH2; -.
Proteomes; UP000006548; Chromosome 4.
Genevisible; Q9ZPH2; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:TAIR.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
GO; GO:0051726; P:regulation of cell cycle; IEP:TAIR.
GO; GO:0009408; P:response to heat; IMP:TAIR.
CDD; cd03028; GRX_PICOT_like; 3.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR033658; GRX_PICOT-like.
InterPro; IPR004480; Monothiol_GRX-rel.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
PANTHER; PTHR10293; PTHR10293; 3.
Pfam; PF00462; Glutaredoxin; 3.
Pfam; PF00085; Thioredoxin; 1.
SUPFAM; SSF52833; SSF52833; 4.
TIGRFAMs; TIGR00365; TIGR00365; 3.
PROSITE; PS51354; GLUTAREDOXIN_2; 3.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
2Fe-2S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
Metal-binding; Redox-active center; Reference proteome; Repeat;
Ubl conjugation.
CHAIN 1 488 Monothiol glutaredoxin-S17.
/FTId=PRO_0000268737.
DOMAIN 2 107 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 154 256 Glutaredoxin 1. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
DOMAIN 284 386 Glutaredoxin 2. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
DOMAIN 391 488 Glutaredoxin 3. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
REGION 470 471 Glutathione binding.
{ECO:0000250|UniProtKB:P0AC69}.
METAL 416 416 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000250|UniProtKB:P0AC69}.
BINDING 408 408 Glutathione.
{ECO:0000250|UniProtKB:P0AC69}.
BINDING 445 445 Glutathione.
{ECO:0000250|UniProtKB:P0AC69}.
BINDING 457 457 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P0AC69}.
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


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