RIR2C_ARATH
ID RIR2C_ARATH Reviewed; 332 AA.
AC Q9LSD0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ribonucleoside-diphosphate reductase small chain C;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleoside-diphosphate reductase TSO2 subunit;
DE AltName: Full=Ribonucleotide reductase small subunit C;
GN Name=TSO2; OrderedLocusNames=At3g27060; ORFNames=MOJ10.13;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
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 [3]
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 [4]
RP TISSUE SPECIFICITY, FUNCTION, MUTAGENESIS OF ASP-49; ARG-97 AND GLY-170,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=16399800; DOI=10.1105/tpc.105.037044;
RA Wang C., Liu Z.;
RT "Arabidopsis ribonucleotide reductases are critical for cell cycle
RT progression, DNA damage repair, and plant development.";
RL Plant Cell 18:350-365(2006).
RN [5]
RP INTERACTION WITH CSN7, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=21614643; DOI=10.1007/s11103-011-9795-8;
RA Halimi Y., Dessau M., Pollak S., Ast T., Erez T., Livnat-Levanon N.,
RA Karniol B., Hirsch J.A., Chamovitz D.A.;
RT "COP9 signalosome subunit 7 from Arabidopsis interacts with and regulates
RT the small subunit of ribonucleotide reductase (RNR2).";
RL Plant Mol. Biol. 77:77-89(2011).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. Involved in DNA damage repair and
CC programmed cell death inhibition. {ECO:0000269|PubMed:16399800}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10014};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Homodimer and heterodimer with RNR2A. Heterotetramer of two R1
CC and two R2 chains (By similarity). Interacts with CSN7 (via C-terminal
CC tail). {ECO:0000250, ECO:0000269|PubMed:21614643}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21614643}. Nucleus
CC {ECO:0000269|PubMed:21614643}. Note=Cytoplasmic in adult cells, and
CC nuclear in meristematic regions and in all tissues following DNA
CC damage. The nuclear exclusion is dependent on CSN7.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cauline and rosette leaves,
CC stems and flowers. {ECO:0000269|PubMed:16399800,
CC ECO:0000269|PubMed:21614643}.
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly at the S-phase of the cell
CC cycle. {ECO:0000269|PubMed:16399800}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality when homozygous.
CC {ECO:0000269|PubMed:21614643}.
CC -!- MISCELLANEOUS: 'TSO' means 'ugly' in Chinese.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
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DR EMBL; AB026649; BAB01087.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77261.1; -; Genomic_DNA.
DR EMBL; AY063837; AAL36193.1; -; mRNA.
DR EMBL; AY117212; AAM51287.1; -; mRNA.
DR RefSeq; NP_189342.1; NM_113620.4.
DR AlphaFoldDB; Q9LSD0; -.
DR SMR; Q9LSD0; -.
DR BioGRID; 7654; 1.
DR STRING; 3702.AT3G27060.1; -.
DR PaxDb; Q9LSD0; -.
DR PRIDE; Q9LSD0; -.
DR ProteomicsDB; 236867; -.
DR EnsemblPlants; AT3G27060.1; AT3G27060.1; AT3G27060.
DR GeneID; 822324; -.
DR Gramene; AT3G27060.1; AT3G27060.1; AT3G27060.
DR KEGG; ath:AT3G27060; -.
DR Araport; AT3G27060; -.
DR TAIR; locus:2092030; AT3G27060.
DR eggNOG; KOG1567; Eukaryota.
DR HOGENOM; CLU_035339_2_1_1; -.
DR InParanoid; Q9LSD0; -.
DR OMA; KVGEYQR; -.
DR OrthoDB; 680824at2759; -.
DR PhylomeDB; Q9LSD0; -.
DR BioCyc; ARA:AT3G27060-MON; -.
DR BRENDA; 1.17.4.1; 399.
DR BRENDA; 1.17.4.2; 399.
DR UniPathway; UPA00326; -.
DR PRO; PR:Q9LSD0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSD0; baseline and differential.
DR Genevisible; Q9LSD0; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; TAS:TAIR.
DR GO; GO:0006260; P:DNA replication; IMP:TAIR.
DR GO; GO:0012501; P:programmed cell death; IMP:TAIR.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:TAIR.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR030475; RNR_small_AS.
DR InterPro; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; PTHR23409; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Deoxyribonucleotide synthesis; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..332
FT /note="Ribonucleoside-diphosphate reductase small chain C"
FT /id="PRO_0000254195"
FT ACT_SITE 114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 76
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MUTAGEN 49
FT /note="D->N: In tso2-1,4; white sectors in green organs,
FT uneven thickness, rough surfaces, and irregular margins of
FT leaves or floral organs."
FT /evidence="ECO:0000269|PubMed:16399800"
FT MUTAGEN 97
FT /note="R->C: In tso2-3; white sectors in green organs,
FT uneven thickness, rough surfaces, and irregular margins of
FT leaves or floral organs."
FT /evidence="ECO:0000269|PubMed:16399800"
FT MUTAGEN 170
FT /note="G->S: In tso2-2; white sectors in green organs,
FT uneven thickness, rough surfaces, and irregular margins of
FT leaves or floral organs."
FT /evidence="ECO:0000269|PubMed:16399800"
SQ SEQUENCE 332 AA; 38034 MW; 9EADC6E82B4DFCE1 CRC64;
MPSMPEEPLL TPTPDRFCMF PIHYPQIWEM YKKAEASFWT AEEVDLSQDN RDWENSLNDG
ERHFIKHVLA FFAASDGIVL ENLASRFMSD VQVSEARAFY GFQIAIENIH SEMYSLLLDT
YIKDNKERDH LFRAIETIPC VAKKAQWAMK WIDGSQTFAE RIIAFACVEG IFFSGSFCSI
FWLKKRGLMP GLTFSNELIS RDEGLHCDFA CLLYTLLKTK LSEERVKSIV CDAVEIEREF
VCDALPCALV GMNRDLMSQY IEFVADRLLG ALGYGKVYGV TNPFDWMELI SLQGKTNFFE
KRVGDYQKAS VMSSVNGNGA FDNHVFSLDE DF
