GRC10_ARATH
ID GRC10_ARATH Reviewed; 148 AA.
AC Q29PZ1; C1JGR0; Q9LYI0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Glutaredoxin-C10;
DE Short=AtGrxC10;
DE AltName: Full=Protein ROXY 20;
GN Name=GRXC10; Synonyms=ROXY20; OrderedLocusNames=At5g11930;
GN ORFNames=F14F18.100;
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], 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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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 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: Has a glutathione-disulfide oxidoreductase activity in the
CC presence of NADPH and glutathione reductase. Reduces low molecular
CC weight disulfides and proteins (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CC-type subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87666.1; Type=Erroneous initiation; 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; FJ611919; ACO50424.1; -; mRNA.
DR EMBL; AL163812; CAB87666.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED91741.1; -; Genomic_DNA.
DR EMBL; BT024765; ABD59103.1; -; mRNA.
DR PIR; T48552; T48552.
DR RefSeq; NP_196754.2; NM_121231.3.
DR AlphaFoldDB; Q29PZ1; -.
DR SMR; Q29PZ1; -.
DR BioGRID; 16344; 1.
DR STRING; 3702.AT5G11930.1; -.
DR PaxDb; Q29PZ1; -.
DR PRIDE; Q29PZ1; -.
DR EnsemblPlants; AT5G11930.1; AT5G11930.1; AT5G11930.
DR GeneID; 831066; -.
DR Gramene; AT5G11930.1; AT5G11930.1; AT5G11930.
DR KEGG; ath:AT5G11930; -.
DR Araport; AT5G11930; -.
DR TAIR; locus:2143004; AT5G11930.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_026126_6_2_1; -.
DR InParanoid; Q29PZ1; -.
DR OMA; RSSTCCM; -.
DR OrthoDB; 1447264at2759; -.
DR PhylomeDB; Q29PZ1; -.
DR PRO; PR:Q29PZ1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q29PZ1; baseline and differential.
DR Genevisible; Q29PZ1; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
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 Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..148
FT /note="Glutaredoxin-C10"
FT /id="PRO_0000268717"
FT DOMAIN 55..147
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT REGION 16..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 76..79
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 148 AA; 15709 MW; DA3B90A98ED274C8 CRC64;
MKTMRGLRNC SNDAVTLDLT VHPPPPPPLP PPAPSTVSSS TASTSLSFDE EETSESKIGR
LISEHPVIIF TRFSSCCMCH VMKKLLSTVG VHPTVIEIDD GEIAYLAVEA APVLFIGGTC
VGGFESLVAL HLSGQLIPRL VEVGALWA