RBG3_ARATH
ID RBG3_ARATH Reviewed; 309 AA.
AC Q9FNR1;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glycine-rich RNA-binding protein 3, mitochondrial {ECO:0000303|PubMed:11809873};
DE Short=AtGR-RBP3 {ECO:0000303|PubMed:11809873};
DE AltName: Full=AtRBG3 {ECO:0000303|PubMed:20009520};
DE AltName: Full=Mitochondrial RNA-binding protein 2a {ECO:0000303|PubMed:11972043};
DE Short=At-mRBP2a {ECO:0000303|PubMed:11972043};
DE AltName: Full=Organelle RRM domain-containing protein 3 {ECO:0000303|PubMed:25800738};
DE Flags: Precursor;
GN Name=RBG3 {ECO:0000303|PubMed:20009520};
GN Synonyms=GR-RBP3 {ECO:0000303|PubMed:11809873},
GN MRBP2A {ECO:0000303|PubMed:11972043}, ORRM3 {ECO:0000303|PubMed:25800738};
GN OrderedLocusNames=At5g61030 {ECO:0000312|Araport:AT5G61030};
GN ORFNames=MAF19_30 {ECO:0000312|EMBL:BAB10366.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY.
RX PubMed=11809873; DOI=10.1093/nar/30.3.623;
RA Lorkovic Z.J., Barta A.;
RT "Genome analysis: RNA recognition motif (RRM) and K homology (KH) domain
RT RNA-binding proteins from the flowering plant Arabidopsis thaliana.";
RL Nucleic Acids Res. 30:623-635(2002).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11972043; DOI=10.1073/pnas.092019599;
RA Vermel M., Guermann B., Delage L., Grienenberger J.M., Marechal-Drouard L.,
RA Gualberto J.M.;
RT "A family of RRM-type RNA-binding proteins specific to plant
RT mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5866-5871(2002).
RN [7]
RP INDUCTION BY COLD.
RX PubMed=16207746; DOI=10.1093/jxb/eri298;
RA Kwak K.J., Kim Y.O., Kang H.;
RT "Characterization of transgenic Arabidopsis plants overexpressing GR-RBP4
RT under high salinity, dehydration, or cold stress.";
RL J. Exp. Bot. 56:3007-3016(2005).
RN [8]
RP NOMENCLATURE.
RX PubMed=20009520; DOI=10.4161/psb.5.2.10336;
RA Mangeon A., Junqueira R.M., Sachetto-Martins G.;
RT "Functional diversity of the plant glycine-rich proteins superfamily.";
RL Plant Signal. Behav. 5:99-104(2010).
RN [9]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH ORRM2 AND MORF8/RIP1, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25800738; DOI=10.1093/nar/gkv245;
RA Shi X., Hanson M.R., Bentolila S.;
RT "Two RNA recognition motif-containing proteins are plant mitochondrial
RT editing factors.";
RL Nucleic Acids Res. 43:3814-3825(2015).
RN [10]
RP INTERACTION WITH RBG5/ORRM4, AND SUBCELLULAR LOCATION.
RX PubMed=26578708; DOI=10.1104/pp.15.01280;
RA Shi X., Germain A., Hanson M.R., Bentolila S.;
RT "RNA recognition motif-containing protein ORRM4 broadly affects
RT mitochondrial RNA editing and impacts plant development and flowering.";
RL Plant Physiol. 170:294-309(2016).
RN [11]
RP INTERACTION WITH RBG2/ORRM5.
RC STRAIN=cv. Columbia;
RX PubMed=28549172; DOI=10.1093/jxb/erx139;
RA Shi X., Castandet B., Germain A., Hanson M.R., Bentolila S.;
RT "ORRM5, an RNA recognition motif-containing protein, has a unique effect on
RT mitochondrial RNA editing.";
RL J. Exp. Bot. 68:2833-2847(2017).
CC -!- FUNCTION: Possibly has a role in RNA transcription or processing during
CC stress (By similarity). Involved in C-to-U editing of mitochondrial
CC RNA. Functions as minor mitochondrial editing factor. Controls 6
CC percent of the mitochondrial editing sites (PubMed:25800738).
CC {ECO:0000250|UniProtKB:Q9LIS2, ECO:0000269|PubMed:25800738}.
CC -!- SUBUNIT: Homodimer (PubMed:25800738). Interacts with ORRM2 and
CC MORF8/RIP1 (PubMed:25800738). Interacts with RBG5/ORRM4
CC (PubMed:26578708). Binds to RBG2/ORRM5 (PubMed:28549172).
CC {ECO:0000269|PubMed:25800738, ECO:0000269|PubMed:26578708,
CC ECO:0000269|PubMed:28549172}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11972043,
CC ECO:0000269|PubMed:26578708}.
CC -!- INDUCTION: Up-regulated by cold stress. {ECO:0000269|PubMed:16207746}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit severe editing defects in
CC mitochondrial transcripts. {ECO:0000269|PubMed:25800738}.
CC -!- SIMILARITY: Belongs to the GR-RBP family. {ECO:0000305}.
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DR EMBL; AB006696; BAB10366.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97414.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69243.1; -; Genomic_DNA.
DR EMBL; AY060565; AAL31194.1; -; mRNA.
DR EMBL; AY125548; AAM78058.1; -; mRNA.
DR EMBL; AB493804; BAH30642.1; -; mRNA.
DR RefSeq; NP_001330940.1; NM_001345440.1.
DR RefSeq; NP_200911.1; NM_125496.3.
DR AlphaFoldDB; Q9FNR1; -.
DR SMR; Q9FNR1; -.
DR STRING; 3702.AT5G61030.1; -.
DR iPTMnet; Q9FNR1; -.
DR MetOSite; Q9FNR1; -.
DR PaxDb; Q9FNR1; -.
DR PRIDE; Q9FNR1; -.
DR ProteomicsDB; 236519; -.
DR EnsemblPlants; AT5G61030.1; AT5G61030.1; AT5G61030.
DR EnsemblPlants; AT5G61030.2; AT5G61030.2; AT5G61030.
DR GeneID; 836224; -.
DR Gramene; AT5G61030.1; AT5G61030.1; AT5G61030.
DR Gramene; AT5G61030.2; AT5G61030.2; AT5G61030.
DR KEGG; ath:AT5G61030; -.
DR Araport; AT5G61030; -.
DR TAIR; locus:2159401; AT5G61030.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_13_0_1; -.
DR InParanoid; Q9FNR1; -.
DR OMA; YANDRTS; -.
DR OrthoDB; 1579773at2759; -.
DR PRO; PR:Q9FNR1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNR1; baseline and differential.
DR Genevisible; Q9FNR1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IDA:TAIR.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
DR GO; GO:0016554; P:cytidine to uridine editing; IMP:UniProtKB.
DR GO; GO:0080156; P:mitochondrial mRNA modification; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; mRNA processing; Reference proteome; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..309
FT /note="Glycine-rich RNA-binding protein 3, mitochondrial"
FT /id="PRO_0000421674"
FT DOMAIN 40..118
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 247..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 29985 MW; 9EF7C0EF9A4EA97B CRC64;
MAFLSKFGNI LKQTTNKQLN AQVSLSSPSL FQAIRCMSSS KLFIGGMAYS MDEDSLREAF
TKYGEVVDTR VILDRETGRS RGFGFVTFTS SEAASSAIQA LDGRDLHGRV VKVNYANDRT
SGGGFGGGGY GGGGGGYGGS GGYGGGAGGY GGSGGYGGGA GGYGGNSGGG YGGNAAGGYG
GSGAGGYGGD ATGHGGAGGG YGSSGGFGSS GNTYGEGSSA SAGAVGDYNG SSGYGSANTY
GSSNGGFAGD SQFGGSPVGN SSQFGGDNTQ FTAGGQFGGE DQFGSMEKSE TKMEDGPIGG
EFEDVAKRA
