GRS16_ARATH
ID GRS16_ARATH Reviewed; 293 AA.
AC Q8H7F6; O80451; Q8LD13;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Bifunctional monothiol glutaredoxin-S16, chloroplastic {ECO:0000303|PubMed:15170506};
DE Short=AtGrxS16 {ECO:0000303|PubMed:15170506};
DE AltName: Full=Atypical GIY-YIG endonuclease {ECO:0000303|PubMed:23690600};
DE EC=3.1.-.-;
DE AltName: Full=CAX-interacting protein 2 {ECO:0000303|PubMed:12480930};
DE AltName: Full=CAXIP1-like protein {ECO:0000303|PubMed:12480930};
DE Flags: Precursor;
GN Name=GRXS16 {ECO:0000303|PubMed:15170506};
GN Synonyms=CXIP2 {ECO:0000303|PubMed:12480930};
GN OrderedLocusNames=At2g38270 {ECO:0000312|Araport:AT2G38270};
GN ORFNames=F16M14.20 {ECO:0000312|EMBL:AAC27175.1};
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].
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 MRNA].
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
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 [7]
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 [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, AND MUTAGENESIS OF CYS-219.
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 [11]
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 [12]
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 [13]
RP STRUCTURE BY NMR OF 63-170, FUNCTION, DOMAIN, MUTAGENESIS OF TYR-90;
RP PHE-101; SER-111; HIS-115; CYS-123; TRP-143 AND ASN-161, SUBUNIT, DISULFIDE
RP BOND, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=23690600; DOI=10.1073/pnas.1306899110;
RA Liu X., Liu S., Feng Y., Liu J.Z., Chen Y., Pham K., Deng H., Hirschi K.D.,
RA Wang X., Cheng N.;
RT "Structural insights into the N-terminal GIY-YIG endonuclease activity of
RT Arabidopsis glutaredoxin AtGRXS16 in chloroplasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:9565-9570(2013).
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 (Probable). The GRXS16-BOLA1 heterodimer binds a labile,
CC oxygen sensitive iron-sulfur cluster (PubMed:24714563). Able to cleave
CC linearized DNA in vitro (PubMed:23690600).
CC {ECO:0000269|PubMed:23690600, ECO:0000269|PubMed:24714563,
CC ECO:0000305}.
CC -!- ACTIVITY REGULATION: The formation of an intramolecular disulfide bond
CC negatively regulates both the N-terminal endonuclease and the C-
CC terminal glutaredoxin activities. {ECO:0000269|PubMed:23690600}.
CC -!- SUBUNIT: [2Fe-2S]-bridged holo-homodimer (PubMed:23690600). Interacts
CC in vitro with SUFE1, BOLA1, BOLA2 and BOLA4 (PubMed:24203231).
CC Interacts in vivo only with SUFE1, BOLA1 and BOLA4 (PubMed:24203231,
CC PubMed:24714563, PubMed:23690600). Interacts with SBP1
CC (PubMed:30824043). {ECO:0000269|PubMed:23690600,
CC ECO:0000269|PubMed:24203231, ECO:0000269|PubMed:24714563,
CC ECO:0000269|PubMed:30824043}.
CC -!- INTERACTION:
CC Q8H7F6; Q9XFM0: IAA28; NbExp=3; IntAct=EBI-4424482, EBI-3133404;
CC Q8H7F6; O81313: IND; NbExp=4; IntAct=EBI-4424482, EBI-4446992;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:23690600}.
CC -!- DOMAIN: The N-terminal domain (NTD) (63-170) has an intrinsic Mg(2+)-
CC dependent endonuclease activity in vitro (PubMed:23690600). The
CC glutaredoxin (GRX) domain (194-293) alone is able to complement yeast
CC grx5 cells in vitro, but not the full-length GRXS16 protein.
CC {ECO:0000269|PubMed:23690600}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CGFS subfamily.
CC {ECO:0000305}.
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DR EMBL; AY157989; AAO19648.1; -; mRNA.
DR EMBL; AF083698; AAN60257.1; -; mRNA.
DR EMBL; AC003028; AAC27175.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09515.1; -; Genomic_DNA.
DR EMBL; AK117441; BAC42106.1; -; mRNA.
DR EMBL; BT004974; AAO50507.1; -; mRNA.
DR EMBL; AY086273; AAM64346.1; -; mRNA.
DR PIR; T01258; T01258.
DR RefSeq; NP_565885.1; NM_129383.3.
DR PDB; 2LWF; NMR; -; A=63-170.
DR PDBsum; 2LWF; -.
DR AlphaFoldDB; Q8H7F6; -.
DR BMRB; Q8H7F6; -.
DR SMR; Q8H7F6; -.
DR BioGRID; 3749; 14.
DR IntAct; Q8H7F6; 8.
DR STRING; 3702.AT2G38270.1; -.
DR PaxDb; Q8H7F6; -.
DR PRIDE; Q8H7F6; -.
DR ProteomicsDB; 222250; -.
DR EnsemblPlants; AT2G38270.1; AT2G38270.1; AT2G38270.
DR GeneID; 818407; -.
DR Gramene; AT2G38270.1; AT2G38270.1; AT2G38270.
DR KEGG; ath:AT2G38270; -.
DR Araport; AT2G38270; -.
DR TAIR; locus:2042887; AT2G38270.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_070932_0_0_1; -.
DR InParanoid; Q8H7F6; -.
DR OMA; GGCDILS; -.
DR OrthoDB; 1449534at2759; -.
DR PhylomeDB; Q8H7F6; -.
DR PRO; PR:Q8H7F6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8H7F6; baseline and differential.
DR Genevisible; Q8H7F6; AT.
DR GO; GO:0009507; C:chloroplast; 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:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006812; P:cation transport; IDA:TAIR.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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; Hydrolase; Iron;
KW Iron-sulfur; Metal-binding; Multifunctional enzyme; Plastid;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..293
FT /note="Bifunctional monothiol glutaredoxin-S16,
FT chloroplastic"
FT /id="PRO_0000268736"
FT DOMAIN 194..293
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 211
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT BINDING 219
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 251
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT BINDING 263
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT BINDING 276..277
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0AC69"
FT DISULFID 123..219
FT /evidence="ECO:0000269|PubMed:23690600"
FT MUTAGEN 90
FT /note="Y->F: Strongly reduced nuclease activity."
FT /evidence="ECO:0000269|PubMed:23690600"
FT MUTAGEN 101
FT /note="F->Y: Enhanced nuclease activity."
FT /evidence="ECO:0000269|PubMed:23690600"
FT MUTAGEN 111
FT /note="S->A: Strongly reduced nuclease activity."
FT /evidence="ECO:0000269|PubMed:23690600"
FT MUTAGEN 111
FT /note="S->R: Slightly reduced nuclease activity."
FT /evidence="ECO:0000269|PubMed:23690600"
FT MUTAGEN 115
FT /note="H->F: Strongly reduced nuclease activity."
FT /evidence="ECO:0000269|PubMed:23690600"
FT MUTAGEN 123
FT /note="C->S: Increased glutaredoxin activity."
FT /evidence="ECO:0000269|PubMed:23690600"
FT MUTAGEN 143
FT /note="W->A,E: Slightly reduced nuclease activity."
FT /evidence="ECO:0000269|PubMed:23690600"
FT MUTAGEN 161
FT /note="N->L: Slightly reduced nuclease activity."
FT /evidence="ECO:0000269|PubMed:23690600"
FT MUTAGEN 219
FT /note="C->S: Decreased interactions with BOLA proteins and
FT loss of interaction with SUFE1."
FT /evidence="ECO:0000269|PubMed:24203231"
FT CONFLICT 194
FT /note="E -> G (in Ref. 2; AAN60257)"
FT /evidence="ECO:0000305"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2LWF"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:2LWF"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2LWF"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:2LWF"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:2LWF"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:2LWF"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2LWF"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:2LWF"
FT HELIX 136..153
FT /evidence="ECO:0007829|PDB:2LWF"
FT TURN 159..163
FT /evidence="ECO:0007829|PDB:2LWF"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:2LWF"
SQ SEQUENCE 293 AA; 32206 MW; 6B2E6337F8C5F050 CRC64;
MAAITISSSL HASASPRVVR PHVSRNTPVI TLYSRFTPSF SFPSLSFTLR DTAPSRRRSF
FIASAVKSLT ETELLPITEA DSIPSASGVY AVYDKSDELQ FVGISRNIAA SVSAHLKSVP
ELCGSVKVGI VEEPDKAVLT QAWKLWIEEH IKVTGKVPPG NKSGNNTFVK QTPRKKSDIR
LTPGRHVELT VPLEELIDRL VKESKVVAFI KGSRSAPQCG FSQRVVGILE SQGVDYETVD
VLDDEYNHGL RETLKNYSNW PTFPQIFVKG ELVGGCDILT SMYENGELAN ILN
