GRXC6_ORYSJ
ID GRXC6_ORYSJ Reviewed; 112 AA.
AC P55142; A3AVF9; O04273; Q0JBV3; Q7FA28;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Glutaredoxin-C6;
DE AltName: Full=Glutaredoxin-C2 homolog 1;
GN Name=GRXC6; Synonyms=RASC8; OrderedLocusNames=Os04g0508300, LOC_Os04g42930;
GN ORFNames=OsJ_15409 {ECO:0000312|EMBL:EAZ31298.1}, OSJNBa0043L24.17;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Aleurone;
RX PubMed=8287970; DOI=10.1016/0014-5793(94)80264-5;
RA Minakuchi K., Yabushita T., Masumura T., Ichihara K., Tanaka K.;
RT "Cloning and sequence analysis of a cDNA encoding rice glutaredoxin.";
RL FEBS Lett. 337:157-160(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=9099854; DOI=10.1016/s0378-1119(96)00771-8;
RA Sha S., Yabushita T., Minakuchi K., Masumura T., Tanaka K.;
RT "Structure of the rice glutaredoxin (thioltransferase) gene.";
RL Gene 188:23-28(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [8]
RP PROTEIN SEQUENCE OF 8-106, AND CHARACTERIZATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=9192723; DOI=10.1093/oxfordjournals.jbchem.a021663;
RA Sha S., Minakuchi K., Higaki N., Sato K., Ohtsuki K., Kurata A.,
RA Yoshikawa H., Kotaru M., Masumura T., Ichihara K., Tanaka K.;
RT "Purification and characterization of glutaredoxin (thioltransferase) from
RT rice (Oryza sativa L.).";
RL J. Biochem. 121:842-848(1997).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-23.
RX PubMed=12207894; DOI=10.1016/s0006-291x(02)02047-8;
RA Lee K.O., Lee J.R., Yoo J.Y., Jang H.H., Moon J.C., Jung B.G., Chi Y.H.,
RA Park S.K., Lee S.S., Lim C.O., Yun D.-J., Cho M.J., Lee S.Y.;
RT "GSH-dependent peroxidase activity of the rice (Oryza sativa) glutaredoxin,
RT a thioltransferase.";
RL Biochem. Biophys. Res. Commun. 296:1152-1156(2002).
RN [10]
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. Possesses thioltransferase,
CC dehydroascorbate reductase and GSH-dependent peroxidase activities in
CC vitro. {ECO:0000269|PubMed:12207894, ECO:0000269|PubMed:8287970}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.58 mM for H(2)O(2) {ECO:0000269|PubMed:12207894};
CC KM=0.29 mM for cumene hydroperoxide {ECO:0000269|PubMed:12207894};
CC KM=0.31 mM for tert-butyl hydroperoxide
CC {ECO:0000269|PubMed:12207894};
CC Vmax=62.5 umol/min/mg enzyme for H(2)O(2)
CC {ECO:0000269|PubMed:12207894};
CC Vmax=38.5 umol/min/mg enzyme for cumene hydroperoxide
CC {ECO:0000269|PubMed:12207894};
CC Vmax=16.8 umol/min/mg enzyme for tert-butyl hydroperoxide
CC {ECO:0000269|PubMed:12207894};
CC Note=The highest catalytic efficiency is observed with cumene
CC hydroperoxide as substrate.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in aleurone layer.
CC {ECO:0000269|PubMed:8287970}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: The mutagenesis of Cys-26 into a serine residue does not
CC affect thioltransferase and GSH-dependent peroxidase activities.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CPYC subfamily.
CC {ECO:0000305}.
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DR EMBL; X77150; CAA54397.1; -; mRNA.
DR EMBL; D86744; BAA20071.1; -; Genomic_DNA.
DR EMBL; AL662969; CAE04729.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF15184.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS90009.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ31298.1; -; Genomic_DNA.
DR PIR; JC5445; JC5445.
DR AlphaFoldDB; P55142; -.
DR SMR; P55142; -.
DR STRING; 4530.OS04T0508300-01; -.
DR PaxDb; P55142; -.
DR PRIDE; P55142; -.
DR EnsemblPlants; Os04t0508300-01; Os04t0508300-01; Os04g0508300.
DR Gramene; Os04t0508300-01; Os04t0508300-01; Os04g0508300.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_026126_7_2_1; -.
DR InParanoid; P55142; -.
DR OMA; DSTHAQF; -.
DR SABIO-RK; P55142; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; P55142; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02180; GRX_euk; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; Electron transport;
KW Redox-active center; Reference proteome; Transport.
FT CHAIN 1..112
FT /note="Glutaredoxin-C6"
FT /id="PRO_0000141607"
FT DOMAIN 3..103
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT DISULFID 23..26
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT MUTAGEN 23
FT /note="C->S: Loss of thioltransferase and GSH-dependent
FT peroxidase activities."
FT /evidence="ECO:0000269|PubMed:12207894"
FT CONFLICT 34
FT /note="E -> G (in Ref. 1; CAA54397)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 112 AA; 11774 MW; A95814731C869D0A CRC64;
MALAKAKETV ASAPVVVYSK SYCPFCVRVK KLFEQLGATF KAIELDGESD GSELQSALAE
WTGQRTVPNV FINGKHIGGC DDTLALNNEG KLVPLLTEAG AIASSAKTTI TA
