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Glycine-rich RNA-binding protein 3, mitochondrial (AtGR-RBP3) (AtRBG3) (Mitochondrial RNA-binding protein 2a) (At-mRBP2a) (Organelle RRM domain-containing protein 3)

 RBG3_ARATH              Reviewed;         309 AA.
Q9FNR1;
06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
23-MAY-2018, entry version 117.
RecName: Full=Glycine-rich RNA-binding protein 3, mitochondrial;
Short=AtGR-RBP3;
AltName: Full=AtRBG3;
AltName: Full=Mitochondrial RNA-binding protein 2a;
Short=At-mRBP2a;
AltName: Full=Organelle RRM domain-containing protein 3 {ECO:0000303|PubMed:25800738};
Flags: Precursor;
Name=RBG3;
Synonyms=GR-RBP3, MRBP2A, ORRM3 {ECO:0000303|PubMed:25800738};
OrderedLocusNames=At5g61030; ORFNames=MAF19_30;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9405937; DOI=10.1093/dnares/4.4.291;
Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. II.
Sequence features of the regions of 1,044,062 bp covered by thirteen
physically assigned P1 clones.";
DNA Res. 4:291-300(1997).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N.,
Takiguchi Y., Takagi M.;
"ORF cloning and analysis of Arabidopsis transcription factor genes.";
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
[5]
GENE FAMILY.
PubMed=11809873; DOI=10.1093/nar/30.3.623;
Lorkovic Z.J., Barta A.;
"Genome analysis: RNA recognition motif (RRM) and K homology (KH)
domain RNA-binding proteins from the flowering plant Arabidopsis
thaliana.";
Nucleic Acids Res. 30:623-635(2002).
[6]
SUBCELLULAR LOCATION.
PubMed=11972043; DOI=10.1073/pnas.092019599;
Vermel M., Guermann B., Delage L., Grienenberger J.M.,
Marechal-Drouard L., Gualberto J.M.;
"A family of RRM-type RNA-binding proteins specific to plant
mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 99:5866-5871(2002).
[7]
INDUCTION BY COLD.
PubMed=16207746; DOI=10.1093/jxb/eri298;
Kwak K.J., Kim Y.O., Kang H.;
"Characterization of transgenic Arabidopsis plants overexpressing GR-
RBP4 under high salinity, dehydration, or cold stress.";
J. Exp. Bot. 56:3007-3016(2005).
[8]
NOMENCLATURE.
PubMed=20009520; DOI=10.4161/psb.5.2.10336;
Mangeon A., Junqueira R.M., Sachetto-Martins G.;
"Functional diversity of the plant glycine-rich proteins
superfamily.";
Plant Signal. Behav. 5:99-104(2010).
[9]
FUNCTION, HOMODIMERIZATION, INTERACTION WITH ORRM2 AND MORF8/RIP1, AND
DISRUPTION PHENOTYPE.
PubMed=25800738; DOI=10.1093/nar/gkv245;
Shi X., Hanson M.R., Bentolila S.;
"Two RNA recognition motif-containing proteins are plant mitochondrial
editing factors.";
Nucleic Acids Res. 43:3814-3825(2015).
[10]
INTERACTION WITH RBG5/ORRM4, AND SUBCELLULAR LOCATION.
PubMed=26578708; DOI=10.1104/pp.15.01280;
Shi X., Germain A., Hanson M.R., Bentolila S.;
"RNA recognition motif-containing protein ORRM4 broadly affects
mitochondrial RNA editing and impacts plant development and
flowering.";
Plant Physiol. 170:294-309(2016).
-!- FUNCTION: Possibly has a role in RNA transcription or processing
during stress (By similarity). Involved in C-to-U editing of
mitochondrial RNA. Functions as minor mitochondrial editing
factor. Controls 6 percent of the mitochondrial editing sites
(PubMed:25800738). {ECO:0000250|UniProtKB:Q9LIS2,
ECO:0000269|PubMed:25800738}.
-!- SUBUNIT: Homodimer. Interacts with ORRM2 and MORF8/RIP1
(PubMed:25800738). Interacts with RBG5/ORRM4 (PubMed:26578708).
{ECO:0000269|PubMed:25800738, ECO:0000269|PubMed:26578708}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11972043,
ECO:0000269|PubMed:26578708}.
-!- INDUCTION: Up-regulated by cold stress.
{ECO:0000269|PubMed:16207746}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but mutant plants exhibit severe editing defects in
mitochondrial transcripts. {ECO:0000269|PubMed:25800738}.
-!- SIMILARITY: Belongs to the GR-RBP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB006696; BAB10366.1; -; Genomic_DNA.
EMBL; CP002688; AED97414.1; -; Genomic_DNA.
EMBL; CP002688; ANM69243.1; -; Genomic_DNA.
EMBL; AY060565; AAL31194.1; -; mRNA.
EMBL; AY125548; AAM78058.1; -; mRNA.
EMBL; AB493804; BAH30642.1; -; mRNA.
RefSeq; NP_001330940.1; NM_001345440.1.
RefSeq; NP_200911.1; NM_125496.3.
UniGene; At.24064; -.
ProteinModelPortal; Q9FNR1; -.
SMR; Q9FNR1; -.
STRING; 3702.AT5G61030.1; -.
iPTMnet; Q9FNR1; -.
PaxDb; Q9FNR1; -.
PRIDE; Q9FNR1; -.
EnsemblPlants; AT5G61030.1; AT5G61030.1; AT5G61030.
EnsemblPlants; AT5G61030.2; AT5G61030.2; AT5G61030.
GeneID; 836224; -.
Gramene; AT5G61030.1; AT5G61030.1; AT5G61030.
Gramene; AT5G61030.2; AT5G61030.2; AT5G61030.
KEGG; ath:AT5G61030; -.
Araport; AT5G61030; -.
TAIR; locus:2159401; AT5G61030.
eggNOG; KOG0118; Eukaryota.
eggNOG; COG0724; LUCA.
HOGENOM; HOG000029199; -.
InParanoid; Q9FNR1; -.
KO; K12741; -.
OMA; SSQFGGD; -.
OrthoDB; EOG09360WQH; -.
PRO; PR:Q9FNR1; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FNR1; baseline and differential.
Genevisible; Q9FNR1; AT.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:TAIR.
GO; GO:0005507; F:copper ion binding; IDA:TAIR.
GO; GO:0003723; F:RNA binding; IDA:TAIR.
GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
GO; GO:0016554; P:cytidine to uridine editing; IMP:UniProtKB.
GO; GO:0080156; P:mitochondrial mRNA modification; IMP:TAIR.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0009409; P:response to cold; IEP:UniProtKB.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
Complete proteome; Mitochondrion; mRNA processing; Reference proteome;
RNA-binding; Transit peptide.
TRANSIT 1 37 Mitochondrion. {ECO:0000255}.
CHAIN 38 309 Glycine-rich RNA-binding protein 3,
mitochondrial.
/FTId=PRO_0000421674.
DOMAIN 40 118 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 122 300 Gly-rich.
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


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