GRS13_ARATH
ID GRS13_ARATH Reviewed; 150 AA.
AC Q84TF4; C1JGQ8; Q94CA3; Q9ZWA7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Monothiol glutaredoxin-S13;
DE Short=AtGrxS13;
DE AltName: Full=Protein ROXY 18;
GN Name=GRXS13; Synonyms=ROXY18; OrderedLocusNames=At1g03850;
GN ORFNames=F21M11.22;
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] (ISOFORM 2), AND GENE FAMILY.
RX PubMed=19218396; DOI=10.1105/tpc.108.064477;
RA Li S., Lauri A., Ziemann M., Busch A., Bhave M., Zachgo S.;
RT "Nuclear activity of ROXY1, a glutaredoxin interacting with TGA factors, is
RT required for petal development in Arabidopsis thaliana.";
RL Plant Cell 21:429-441(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORMS 1 AND 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 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 [8]
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).
CC -!- FUNCTION: May only reduce GSH-thiol disulfides, but not protein
CC disulfides. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84TF4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84TF4-2; Sequence=VSP_022001;
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CC-type subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10683.1; Type=Erroneous gene model prediction; Evidence={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; FJ611917; ACO50422.1; -; mRNA.
DR EMBL; AC003027; AAD10683.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27622.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27623.1; -; Genomic_DNA.
DR EMBL; AY035012; AAK59517.1; -; mRNA.
DR EMBL; AY063052; AAL34226.1; -; mRNA.
DR EMBL; BT005845; AAO64780.1; -; mRNA.
DR EMBL; AK227319; BAE99333.1; -; mRNA.
DR EMBL; AK228449; BAF00376.1; -; mRNA.
DR EMBL; AY086732; AAM63783.1; -; mRNA.
DR PIR; B86169; B86169.
DR RefSeq; NP_563691.1; NM_100265.3. [Q84TF4-1]
DR RefSeq; NP_849586.1; NM_179255.3. [Q84TF4-2]
DR AlphaFoldDB; Q84TF4; -.
DR SMR; Q84TF4; -.
DR BioGRID; 24627; 1.
DR IntAct; Q84TF4; 1.
DR STRING; 3702.AT1G03850.1; -.
DR PaxDb; Q84TF4; -.
DR PRIDE; Q84TF4; -.
DR EnsemblPlants; AT1G03850.1; AT1G03850.1; AT1G03850. [Q84TF4-2]
DR EnsemblPlants; AT1G03850.2; AT1G03850.2; AT1G03850. [Q84TF4-1]
DR GeneID; 839392; -.
DR Gramene; AT1G03850.1; AT1G03850.1; AT1G03850. [Q84TF4-2]
DR Gramene; AT1G03850.2; AT1G03850.2; AT1G03850. [Q84TF4-1]
DR KEGG; ath:AT1G03850; -.
DR Araport; AT1G03850; -.
DR TAIR; locus:2024162; AT1G03850.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_026126_6_2_1; -.
DR InParanoid; Q84TF4; -.
DR OMA; SWTNTIP; -.
DR OrthoDB; 1598650at2759; -.
DR PhylomeDB; Q84TF4; -.
DR PRO; PR:Q84TF4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84TF4; baseline and differential.
DR Genevisible; Q84TF4; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IEP:TAIR.
DR GO; GO:0080183; P:response to photooxidative stress; IEP:TAIR.
DR InterPro; IPR011905; GlrX-like_pln_2.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR10168; PTHR10168; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02189; GlrX-like_plant; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Alternative splicing; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Nucleus; Redox-active center; Reference proteome.
FT CHAIN 1..150
FT /note="Monothiol glutaredoxin-S13"
FT /id="PRO_0000268733"
FT DOMAIN 53..149
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT REGION 30..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 147..150
FT /note="Responsive for interaction with TGA factors"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255"
FT VAR_SEQ 136..150
FT /note="GDLVPTLRQAGALWL -> GHSIKIRTDTWSSFSVATVDRIRW (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:19218396, ECO:0000303|Ref.5"
FT /id="VSP_022001"
SQ SEQUENCE 150 AA; 16366 MW; F0F147384D65D3A8 CRC64;
MQKAIRPYES PWTKTVPGNS IFLLKNEDKP SSSSSSLSWL TSGSPKPTSI SNKRSSNLVV
MENAVVVFAR RGCCLGHVAK RLLLTHGVNP VVVEIGEEDN NNYDNIVSDK EKLPMMYIGG
KLFGGLENLM AAHINGDLVP TLRQAGALWL
