RBG2_ARATH
ID RBG2_ARATH Reviewed; 158 AA.
AC Q9SVM8; A0A6B9JA45; Q39105; Q41988;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Glycine-rich RNA-binding protein 2, mitochondrial {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746};
DE Short=AtGR-RBP2 {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746};
DE AltName: Full=AtRBG2 {ECO:0000303|PubMed:20009520};
DE AltName: Full=Glycine-rich protein 2 {ECO:0000303|PubMed:20009520};
DE Short=AtGRP2 {ECO:0000303|PubMed:20009520};
DE AltName: Full=Mitochondrial RNA-binding protein 1a {ECO:0000303|PubMed:11972043};
DE Short=At-mRBP1a {ECO:0000303|PubMed:11972043};
DE AltName: Full=Organelle RNA recognition motif-containing protein 5 {ECO:0000303|PubMed:28549172};
DE AltName: Full=Small RNA binding protein 3 {ECO:0000303|PubMed:31812689};
DE Short=AtSRBP3 {ECO:0000303|PubMed:31812689};
DE Flags: Precursor;
GN Name=RBG2 {ECO:0000303|PubMed:20009520};
GN Synonyms=GR-RBP2 {ECO:0000303|PubMed:11809873,
GN ECO:0000303|PubMed:16207746}, GRP2 {ECO:0000303|PubMed:20009520},
GN MRBP1A {ECO:0000303|PubMed:11972043}, ORRM5 {ECO:0000303|PubMed:28549172},
GN SRBP3 {ECO:0000303|PubMed:31812689};
GN OrderedLocusNames=At4g13850 {ECO:0000312|Araport:AT4G13850};
GN ORFNames=F18A5.240 {ECO:0000312|EMBL:CAB36849.1};
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 [MRNA].
RA Macknight R., Love K., Dean C.;
RT "Identification of an Arabidopsis cDNA encoding a novel glycine rich RNA-
RT binding protein and mapping of the gene family onto the Arabidopsis
RT physical map.";
RL (er) Plant Gene Register PGR98-152(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, DOMAIN,
RP SUBUNIT, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=31812689; DOI=10.1016/j.molp.2019.12.001;
RA Yan Y., Ham B.-K., Chong Y.H., Yeh S.-D., Lucas W.J.;
RT "A plant SMALL RNA-BINDING PROTEIN 1 family mediates cell-to-cell
RT trafficking of RNAi signals.";
RL Mol. Plant 13:321-335(2020).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-158.
RC STRAIN=cv. C24; TISSUE=Flower;
RA Quigley F.R.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-85.
RC STRAIN=cv. C24; TISSUE=Flower bud;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [9]
RP PROTEIN SEQUENCE OF 35-48, AND SUBCELLULAR LOCATION.
RC TISSUE=Leaf, and Stem;
RX PubMed=11743114; DOI=10.1104/pp.010474;
RA Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT "Proteomic approach to identify novel mitochondrial proteins in
RT Arabidopsis.";
RL Plant Physiol. 127:1694-1710(2001).
RN [10]
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 [11]
RP SUBCELLULAR LOCATION, FUNCTION, AND INDUCTION BY COLD.
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [13]
RP INDUCTION BY COLD AND DEHYDRATION, AND FUNCTION.
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 [14]
RP INDUCTION BY COLD.
RX PubMed=17169986; DOI=10.1093/nar/gkl1076;
RA Kim J.S., Park S.J., Kwak K.J., Kim Y.O., Kim J.Y., Song J., Jang B.,
RA Jung C.-H., Kang H.;
RT "Cold shock domain proteins and glycine-rich RNA-binding proteins from
RT Arabidopsis thaliana can promote the cold adaptation process in Escherichia
RT coli.";
RL Nucleic Acids Res. 35:506-516(2007).
RN [15]
RP INDUCTION BY COLD, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17376161; DOI=10.1111/j.1365-313x.2007.03057.x;
RA Kim J.Y., Park S.J., Jang B., Jung C.-H., Ahn S.J., Goh C.-H., Cho K.,
RA Han O., Kang H.;
RT "Functional characterization of a glycine-rich RNA-binding protein 2 in
RT Arabidopsis thaliana under abiotic stress conditions.";
RL Plant J. 50:439-451(2007).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION BY HYDROGEN PEROXIDE.
RX PubMed=19672695; DOI=10.1007/s11033-009-9636-x;
RA Schmidt F., Marnef A., Cheung M.K., Wilson I., Hancock J., Staiger D.,
RA Ladomery M.;
RT "A proteomic analysis of oligo(dT)-bound mRNP containing oxidative stress-
RT induced Arabidopsis thaliana RNA-binding proteins ATGRP7 and ATGRP8.";
RL Mol. Biol. Rep. 37:839-845(2010).
RN [17]
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 [18]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, AND INTERACTION WITH ORRM2;
RP RBG3/ORRM3 AND RBG5/ORRM4.
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: Promotes the cis-splicing and editing of several
CC mitochondrial RNAs (including NAD5 transcripts) (PubMed:28549172).
CC Plays a role in RNA transcription or processing during stress. Binds
CC RNAs and DNAs sequence with a preference to single-stranded nucleic
CC acids. Displays strong affinity to poly(U) sequence. Exerts cold and
CC freezing tolerance, probably by exhibiting an RNA chaperone activity
CC during the cold and freezing adaptation process. Mediates cell-to-cell
CC trafficking of RNA interference (RNAi) signals (small RNAs (sRNA), e.g.
CC small interfering RNA (siRNA) and microRNA (miRNA)) which regulate
CC growth and development, as well as responses to environmental inputs,
CC including pathogen attack; can compromise zucchini yellow mosaic virus
CC (ZYMV) and tobacco rattle virus (TRV) infections at the early stage
CC (PubMed:31812689). {ECO:0000269|PubMed:11972043,
CC ECO:0000269|PubMed:16207746, ECO:0000269|PubMed:17376161,
CC ECO:0000269|PubMed:28549172, ECO:0000269|PubMed:31812689}.
CC -!- SUBUNIT: Binds to small phloem-mobile single-stranded RNAs (ss-sRNA,
CC e.g. small interfering RNA (siRNA) and microRNA (miRNA)) in the phloeme
CC exudate, including viral-derived sRNA (vsiRNA) (PubMed:31812689).
CC Interacts with ORRM2, RBG3/ORRM3 and RBG5/ORRM4 (PubMed:28549172).
CC {ECO:0000269|PubMed:28549172, ECO:0000269|PubMed:31812689}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11743114,
CC ECO:0000269|PubMed:11972043, ECO:0000269|PubMed:14671022}. Secreted
CC {ECO:0000269|PubMed:31812689}. Note=Observed in the phloem
CC translocation stream. {ECO:0000269|PubMed:31812689}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SVM8-1; Sequence=Displayed;
CC -!- INDUCTION: Up-regulated by cold stress and down-regulated by
CC dehydration stress. Induced by hydrogen peroxide (at the protein
CC level). {ECO:0000269|PubMed:11972043, ECO:0000269|PubMed:16207746,
CC ECO:0000269|PubMed:17169986, ECO:0000269|PubMed:17376161,
CC ECO:0000269|PubMed:19672695}.
CC -!- DOMAIN: The glycine-rich (GR) domain is necessary and sufficient for
CC cell-to-cell movement and to interefere with zucchini yellow mosaic
CC virus (ZYMV) infection. {ECO:0000269|PubMed:31812689}.
CC -!- DOMAIN: The RRM domain is required to promote mitochondrial RNA
CC processing. {ECO:0000269|PubMed:28549172}.
CC -!- DISRUPTION PHENOTYPE: Defects in seed germination under salt or cold
CC stress (PubMed:17376161). Altered seedling growth under cold stress
CC (PubMed:17376161). Delayed growth and late flowering associated with
CC reduced mitochondrial RNA editing efficiency, including the cis-
CC splicing of the first intron of the NAD5 transcript (PubMed:28549172).
CC The triple mutant srbp1 srbp2 srbp3 is more susceptible to tobacco
CC rattle virus (TRV) (PubMed:31812689). {ECO:0000269|PubMed:17376161,
CC ECO:0000269|PubMed:28549172, ECO:0000269|PubMed:31812689}.
CC -!- MISCELLANEOUS: Plants overexpressing RBG2 confer freezing tolerance.
CC -!- SIMILARITY: Belongs to the GR-RBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA05727.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AJ002892; CAA05727.1; ALT_SEQ; mRNA.
DR EMBL; MN064665; QGZ19400.1; -; mRNA.
DR EMBL; AL035528; CAB36849.1; -; Genomic_DNA.
DR EMBL; AL161537; CAB78427.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83333.1; -; Genomic_DNA.
DR EMBL; AY072361; AAL62353.1; -; mRNA.
DR EMBL; BT002197; AAN72208.1; -; mRNA.
DR EMBL; AY085621; AAM62842.1; -; mRNA.
DR EMBL; X69377; CAA49174.1; -; mRNA.
DR EMBL; Z18189; CAA79126.1; -; mRNA.
DR PIR; S31443; S31443.
DR PIR; T05254; T05254.
DR RefSeq; NP_193121.1; NM_117459.4. [Q9SVM8-1]
DR AlphaFoldDB; Q9SVM8; -.
DR SMR; Q9SVM8; -.
DR BioGRID; 12316; 3.
DR IntAct; Q9SVM8; 3.
DR STRING; 3702.AT4G13850.1; -.
DR iPTMnet; Q9SVM8; -.
DR MetOSite; Q9SVM8; -.
DR SwissPalm; Q9SVM8; -.
DR PaxDb; Q9SVM8; -.
DR PRIDE; Q9SVM8; -.
DR ProteomicsDB; 225908; -. [Q9SVM8-1]
DR EnsemblPlants; AT4G13850.1; AT4G13850.1; AT4G13850. [Q9SVM8-1]
DR GeneID; 827019; -.
DR Gramene; AT4G13850.1; AT4G13850.1; AT4G13850. [Q9SVM8-1]
DR KEGG; ath:AT4G13850; -.
DR Araport; AT4G13850; -.
DR TAIR; locus:2119495; AT4G13850.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; Q9SVM8; -.
DR OMA; FNAIRCM; -.
DR PhylomeDB; Q9SVM8; -.
DR PRO; PR:Q9SVM8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SVM8; baseline and differential.
DR Genevisible; Q9SVM8; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:TAIR.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0034336; F:misfolded RNA binding; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0035197; F:siRNA binding; IDA:UniProtKB.
DR GO; GO:0009631; P:cold acclimation; IMP:UniProtKB.
DR GO; GO:0006858; P:extracellular transport; IDA:UniProtKB.
DR GO; GO:1990428; P:miRNA transport; IDA:UniProtKB.
DR GO; GO:0090615; P:mitochondrial mRNA processing; IMP:UniProtKB.
DR GO; GO:0060567; P:negative regulation of DNA-templated transcription, termination; IDA:UniProtKB.
DR GO; GO:0050688; P:regulation of defense response to virus; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0050658; P:RNA transport; IDA:UniProtKB.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
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 Alternative splicing; Chaperone; Direct protein sequencing; Mitochondrion;
KW Phosphoprotein; Reference proteome; RNA-binding; Secreted; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:11743114"
FT CHAIN 35..158
FT /note="Glycine-rich RNA-binding protein 2, mitochondrial"
FT /id="PRO_0000031018"
FT DOMAIN 35..113
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 122..157
FT /note="Glycine-rich (GR) required for cell-to-cell
FT movement"
FT /evidence="ECO:0000305|PubMed:31812689"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8RWN5"
SQ SEQUENCE 158 AA; 15702 MW; 67B24DFEE76125E6 CRC64;
MAFCNKLGGL LRQNISSNGN VPVTSMLGSL RLMSTKLFIG GLSWGTDDAS LRDAFAHFGD
VVDAKVIVDR ETGRSRGFGF VNFNDEGAAT AAISEMDGKE LNGRHIRVNP ANDRPSAPRA
YGGGGGYSGG GGGYGGGGGG YGGGGGGYGG GGDGGGGF
