RBG4_ARATH
ID RBG4_ARATH Reviewed; 136 AA.
AC Q9LIS2; A0A6B9JFL3; Q8LDS0;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Glycine-rich RNA-binding protein 4, mitochondrial {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746};
DE Short=AtGR-RBP4 {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746};
DE AltName: Full=AtRBG4 {ECO:0000303|PubMed:20009520};
DE AltName: Full=Glycine-rich protein 4 {ECO:0000303|PubMed:17169986};
DE Short=AtGRP4 {ECO:0000303|PubMed:17169986};
DE AltName: Full=Mitochondrial RNA-binding protein 1b {ECO:0000303|PubMed:11972043};
DE Short=At-mRBP1b {ECO:0000303|PubMed:11972043};
DE AltName: Full=Small RNA binding protein 4 {ECO:0000303|PubMed:31812689};
DE Short=AtSRBP4 {ECO:0000303|PubMed:31812689};
DE Flags: Precursor;
GN Name=RBG4 {ECO:0000303|PubMed:20009520};
GN Synonyms=GR-RBP4 {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746,
GN ECO:0000303|PubMed:20009520}, GRP4 {ECO:0000303|PubMed:17169986,
GN ECO:0000303|PubMed:20009520}, MRBP1B {ECO:0000303|PubMed:11972043},
GN SRBP4 {ECO:0000303|PubMed:31812689};
GN OrderedLocusNames=At3g23830 {ECO:0000312|Araport:AT3G23830};
GN ORFNames=F14O13.2 {ECO:0000312|EMBL:BAB03001.1};
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], FUNCTION, DOMAIN, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP TISSUE SPECIFICITY, INDUCTION BY COLD; DEHYDRATION AND SALT, 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 [9]
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 [10]
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).
CC -!- FUNCTION: Possibly has a role in RNA transcription or processing during
CC stress (PubMed:16207746). Binds sequence non-specifically to RNAs and
CC DNAs (PubMed:16207746). Mediates cell-to-cell trafficking of RNA
CC interference (RNAi) signals (small RNAs (sRNA), e.g. small interfering
CC RNA (siRNA) and microRNA (miRNA)) which regulate growth and
CC development, as well as responses to environmental inputs, including
CC pathogen attack; can compromise zucchini yellow mosaic virus (ZYMV) and
CC tobacco rattle virus (TRV) infections at the early stage
CC (PubMed:31812689). {ECO:0000269|PubMed:16207746,
CC 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).
CC {ECO:0000269|PubMed:31812689}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11972043}.
CC Secreted {ECO:0000269|PubMed:31812689}. Note=Observed in the phloem
CC translocation stream. {ECO:0000269|PubMed:31812689}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in young plants, root tips,
CC and flowers, but weakly in mature leaves and stems, implying highly
CC expression in actively proliferating organs.
CC {ECO:0000269|PubMed:16207746}.
CC -!- INDUCTION: Up-regulated by cold stress and down-regulated by salt
CC stress and dehydration stress. {ECO:0000269|PubMed:16207746,
CC ECO:0000269|PubMed:17169986}.
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 -!- MISCELLANEOUS: Plants overexpressing RBG4 display retarded germination
CC under salt and dehydration stress.
CC -!- SIMILARITY: Belongs to the GR-RBP family. {ECO:0000305}.
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DR EMBL; MN064666; QGZ19401.1; -; mRNA.
DR EMBL; AP001297; BAB03001.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76819.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76820.1; -; Genomic_DNA.
DR EMBL; AY070755; AAL50093.1; -; mRNA.
DR EMBL; AY097374; AAM19890.1; -; mRNA.
DR EMBL; AY085838; AAM63053.1; -; mRNA.
DR RefSeq; NP_189025.1; NM_113288.3.
DR RefSeq; NP_850629.1; NM_180298.4.
DR AlphaFoldDB; Q9LIS2; -.
DR SMR; Q9LIS2; -.
DR STRING; 3702.AT3G23830.2; -.
DR SwissPalm; Q9LIS2; -.
DR PaxDb; Q9LIS2; -.
DR PRIDE; Q9LIS2; -.
DR ProteomicsDB; 236520; -.
DR EnsemblPlants; AT3G23830.1; AT3G23830.1; AT3G23830.
DR EnsemblPlants; AT3G23830.2; AT3G23830.2; AT3G23830.
DR GeneID; 821966; -.
DR Gramene; AT3G23830.1; AT3G23830.1; AT3G23830.
DR Gramene; AT3G23830.2; AT3G23830.2; AT3G23830.
DR KEGG; ath:AT3G23830; -.
DR Araport; AT3G23830; -.
DR TAIR; locus:2076096; AT3G23830.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_28_4_1; -.
DR InParanoid; Q9LIS2; -.
DR OMA; FANDKPR; -.
DR OrthoDB; 1579773at2759; -.
DR PhylomeDB; Q9LIS2; -.
DR PRO; PR:Q9LIS2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIS2; baseline and differential.
DR Genevisible; Q9LIS2; 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:0003690; F:double-stranded DNA binding; IDA:TAIR.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:TAIR.
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:0006858; P:extracellular transport; IDA:UniProtKB.
DR GO; GO:1990428; P:miRNA transport; IDA:UniProtKB.
DR GO; GO:1900864; P:mitochondrial RNA modification; IGI:TAIR.
DR GO; GO:0050688; P:regulation of defense response to virus; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0050658; P:RNA transport; IDA: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; Phosphoprotein; Reference proteome; RNA-binding; Secreted;
KW Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..136
FT /note="Glycine-rich RNA-binding protein 4, mitochondrial"
FT /id="PRO_0000421675"
FT DOMAIN 35..113
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 113..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..135
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"
FT CONFLICT 17
FT /note="Q -> H (in Ref. 5; AAM63053)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 136 AA; 14129 MW; 1BE69CF10A48607D CRC64;
MAFCNKLSGI LRQGVSQSSN GPVTSMLGSL RYMSSKLFVG GLSWGTDDSS LKQAFTSFGE
VTEATVIADR ETGRSRGFGF VSFSCEDSAN NAIKEMDGKE LNGRQIRVNL ATERSSAPRS
SFGGGGGYGG GGGGGY