RBG7_ARATH
ID RBG7_ARATH Reviewed; 176 AA.
AC Q03250; A0A6B9JEL0; C0Z304; Q8LEV4; Q94B62;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Glycine-rich RNA-binding protein 7 {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746};
DE Short=AtGR-RBP7 {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746};
DE AltName: Full=AtRBG7 {ECO:0000303|PubMed:20009520};
DE AltName: Full=Glycine-rich protein 7 {ECO:0000303|PubMed:20009520};
DE Short=AtGRP7 {ECO:0000303|PubMed:20009520};
DE AltName: Full=Protein COLD, CIRCADIAN RHYTHM, AND RNA BINDING 2 {ECO:0000303|PubMed:7513083};
DE Short=Protein CCR2 {ECO:0000303|PubMed:7513083};
DE AltName: Full=Small RNA binding protein 1 {ECO:0000303|PubMed:31812689};
DE Short=AtSRBP1 {ECO:0000303|PubMed:31812689};
GN Name=RBG7 {ECO:0000303|PubMed:20009520};
GN Synonyms=CCR2 {ECO:0000303|PubMed:7513083},
GN GR-RBP7 {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746},
GN GRP7 {ECO:0000303|PubMed:20009520}, SRBP1 {ECO:0000303|PubMed:31812689};
GN OrderedLocusNames=At2g21660 {ECO:0000312|Araport:AT2G21660};
GN ORFNames=F2G1.7 {ECO:0000312|EMBL:AAD23639.1};
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] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8448367; DOI=10.1007/bf00014552;
RA van Nocker S., Vierstra R.D.;
RT "Two cDNAs from Arabidopsis thaliana encode putative RNA binding proteins
RT containing glycine-rich domains.";
RL Plant Mol. Biol. 21:695-699(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, INDUCTION BY
RP COLD AND CIRCADIAN RHYTHM, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=7513083; DOI=10.1104/pp.104.3.1015;
RA Carpenter C.D., Kreps J.A., Simon A.E.;
RT "Genes encoding glycine-rich Arabidopsis thaliana proteins with RNA-binding
RT motifs are influenced by cold treatment and an endogenous circadian
RT rhythm.";
RL Plant Physiol. 104:1015-1025(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE,
RP 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP INDUCTION BY CIRCADIAN RHYTHM, AND FUNCTION.
RX PubMed=9238008; DOI=10.1073/pnas.94.16.8515;
RA Heintzen C., Nater M., Apel K., Staiger D.;
RT "AtGRP7, a nuclear RNA-binding protein as a component of a circadian-
RT regulated negative feedback loop in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8515-8520(1997).
RN [10]
RP FUNCTION, AND REVIEW.
RX PubMed=11710982; DOI=10.1098/rstb.2001.0964;
RA Staiger D.;
RT "RNA-binding proteins and circadian rhythms in Arabidopsis thaliana.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1755-1759(2001).
RN [11]
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 [12]
RP FUNCTION, AND ALTERNATIVE SPLICING.
RX PubMed=12535349; DOI=10.1046/j.1365-313x.2003.01629.x;
RA Staiger D., Zecca L., Wieczorek Kirk D.A., Apel K., Eckstein L.;
RT "The circadian clock regulated RNA-binding protein AtGRP7 autoregulates its
RT expression by influencing alternative splicing of its own pre-mRNA.";
RL Plant J. 33:361-371(2003).
RN [13]
RP SUBCELLULAR LOCATION, INTERACTION WITH TRN1, AND NUCLEAR LOCALIZATION
RP SIGNAL.
RX PubMed=14756317; DOI=10.1023/b:plan.0000009288.46713.1f;
RA Ziemienowicz A., Haasen D., Staiger D., Merkle T.;
RT "Arabidopsis transportin1 is the nuclear import receptor for the circadian
RT clock-regulated RNA-binding protein AtGRP7.";
RL Plant Mol. Biol. 53:201-212(2003).
RN [14]
RP 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 [15]
RP INDUCTION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17001447; DOI=10.2478/s11658-006-0042-2;
RA Cao S., Jiang L., Song S., Jing R., Xu G.;
RT "AtGRP7 is involved in the regulation of abscisic acid and stress responses
RT in Arabidopsis.";
RL Cell. Mol. Biol. Lett. 11:526-535(2006).
RN [16]
RP DISRUPTION PHENOTYPE, ADP-RIBOSYLATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, MUTAGENESIS OF ARG-47 AND ARG-49, AND SUBCELLULAR LOCATION.
RX PubMed=17450127; DOI=10.1038/nature05737;
RA Fu Z.Q., Guo M., Jeong B.R., Tian F., Elthon T.E., Cerny R.L., Staiger D.,
RA Alfano J.R.;
RT "A type III effector ADP-ribosylates RNA-binding proteins and quells plant
RT immunity.";
RL Nature 447:284-288(2007).
RN [17]
RP INDUCTION BY COLD, AND FUNCTION.
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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [19]
RP MUTAGENESIS OF ARG-49, AND FUNCTION.
RX PubMed=17924945; DOI=10.1111/j.1365-313x.2007.03302.x;
RA Schoening J.C., Streitner C., Page D.R., Hennig S., Uchida K., Wolf E.,
RA Furuya M., Staiger D.;
RT "Auto-regulation of the circadian slave oscillator component AtGRP7 and
RT regulation of its targets is impaired by a single RNA recognition motif
RT point mutation.";
RL Plant J. 52:1119-1130(2007).
RN [20]
RP RNA-BINDING.
RX PubMed=18576621; DOI=10.1021/ja801994z;
RA Schuettpelz M., Schoening J.C., Doose S., Neuweiler H., Peters E.,
RA Staiger D., Sauer M.;
RT "Changes in conformational dynamics of mRNA upon AtGRP7 binding studied by
RT fluorescence correlation spectroscopy.";
RL J. Am. Chem. Soc. 130:9507-9513(2008).
RN [21]
RP FUNCTION, ALTERNATIVE SPLICING, AND INDUCTION BY COLD.
RX PubMed=18987006; DOI=10.1093/nar/gkn847;
RA Schoening J.C., Streitner C., Meyer I.M., Gao Y., Staiger D.;
RT "Reciprocal regulation of glycine-rich RNA-binding proteins via an
RT interlocked feedback loop coupling alternative splicing to nonsense-
RT mediated decay in Arabidopsis.";
RL Nucleic Acids Res. 36:6977-6987(2008).
RN [22]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18410480; DOI=10.1111/j.1365-313x.2008.03518.x;
RA Kim J.S., Jung H.J., Lee H.J., Kim K.A., Goh C.H., Woo Y., Oh S.H.,
RA Han Y.S., Kang H.;
RT "Glycine-rich RNA-binding protein 7 affects abiotic stress responses by
RT regulating stomata opening and closing in Arabidopsis thaliana.";
RL Plant J. 55:455-466(2008).
RN [23]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18573194; DOI=10.1111/j.1365-313x.2008.03591.x;
RA Streitner C., Danisman S., Wehrle F., Schoening J.C., Alfano J.R.,
RA Staiger D.;
RT "The small glycine-rich RNA binding protein AtGRP7 promotes floral
RT transition in Arabidopsis thaliana.";
RL Plant J. 56:239-250(2008).
RN [24]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=19083177; DOI=10.1007/978-1-59745-289-2_21;
RA Schoening J.C., Staiger D.;
RT "RNA-protein interaction mediating post-transcriptional regulation in the
RT circadian system.";
RL Methods Mol. Biol. 479:337-351(2009).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION BY HYDROGEN PEROXIDE, AND
RP RNA-BINDING.
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 [27]
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 [28]
RP FUNCTION, INTERACTION WITH HOPU1, MUTAGENESIS OF ARG-49, ADP-RIBOSYLATION
RP AT ARG-49, AND DISRUPTION PHENOTYPE.
RX PubMed=22013065; DOI=10.1074/jbc.m111.290122;
RA Jeong B.R., Lin Y., Joe A., Guo M., Korneli C., Yang H., Wang P., Yu M.,
RA Cerny R.L., Staiger D., Alfano J.R., Xu Y.;
RT "Structure function analysis of an ADP-ribosyltransferase type III effector
RT and its RNA-binding target in plant immunity.";
RL J. Biol. Chem. 286:43272-43281(2011).
RN [29]
RP FUNCTION, AND DOMAIN.
RX PubMed=21511907; DOI=10.1093/jxb/err101;
RA Kwak K.J., Park S.J., Han J.H., Kim M.K., Oh S.H., Han Y.S., Kang H.;
RT "Structural determinants crucial to the RNA chaperone activity of glycine-
RT rich RNA-binding proteins 4 and 7 in Arabidopsis thaliana during the cold
RT adaptation process.";
RL J. Exp. Bot. 62:4003-4011(2011).
RN [30]
RP SUBCELLULAR LOCATION.
RX PubMed=21453442; DOI=10.1111/j.1600-0854.2011.01180.x;
RA Lummer M., Humpert F., Steuwe C., Caesar K., Schuettpelz M., Sauer M.,
RA Staiger D.;
RT "Reversible photoswitchable DRONPA-s monitors nucleocytoplasmic transport
RT of an RNA-binding protein in transgenic plants.";
RL Traffic 12:693-702(2011).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [33]
RP FUNCTION, AND MUTAGENESIS OF ARG-49.
RX PubMed=23042250; DOI=10.1093/nar/gks873;
RA Streitner C., Koester T., Simpson C.G., Shaw P., Danisman S., Brown J.W.,
RA Staiger D.;
RT "An hnRNP-like RNA-binding protein affects alternative splicing by in vivo
RT interaction with transcripts in Arabidopsis thaliana.";
RL Nucleic Acids Res. 40:11240-11255(2012).
RN [34]
RP FUNCTION, INDUCTION BY PATHOGEN, AND DISRUPTION PHENOTYPE.
RX PubMed=22902796; DOI=10.1016/j.plaphy.2012.07.020;
RA Lee H.J., Kim J.S., Yoo S.J., Kang E.Y., Han S.H., Yang K.Y., Kim Y.C.,
RA McSpadden Gardener B., Kang H.;
RT "Different roles of glycine-rich RNA-binding protein7 in plant defense
RT against Pectobacterium carotovorum, Botrytis cinerea, and tobacco mosaic
RT viruses.";
RL Plant Physiol. Biochem. 60:46-52(2012).
CC -!- FUNCTION: Plays a role in RNA transcription or processing during
CC stress. Binds RNAs and DNAs sequence with a preference to single-
CC stranded nucleic acids. Displays strong affinity to poly(U) and poly(G)
CC sequence. Involved in mRNA alternative splicing of numerous targets by
CC modulating splice site selection. Negatively regulates the circadian
CC oscillations of its own transcript as well as RBG8 transcript. Forms an
CC interlocked post-transcriptional negative feedback loop with the RBG8
CC autoregulatory circuit. Both proteins negatively autoregulate and
CC reciprocally crossregulate by binding to their pre-mRNAs and promoting
CC unproductive splicing coupled to degradation via the NMD pathway.
CC Involved in the regulation of abscisic acid and stress responses.
CC Affects the growth and stress tolerance under high salt and dehydration
CC stress conditions, and also confers freezing tolerance, particularly
CC via the regulation of stomatal opening and closing in the guard cells.
CC Exhibits RNA chaperone activity during the cold adaptation process.
CC Involved in the export of mRNAs from the nucleus to the cytoplasm under
CC cold stress conditions. Target of the Pseudomonas syringae type III
CC effector HopU1, which could probably be involved in plant innate
CC immunity. Component of the flowering autonomous pathway which promotes
CC floral transition, at least partly by down-regulating FLC. Mediates
CC cell-to-cell trafficking of RNA interference (RNAi) signals (small RNAs
CC (sRNA), e.g. small interfering RNA (siRNA) and microRNA (miRNA)) which
CC regulate growth and development, as well as responses to environmental
CC inputs, including pathogen attack; can compromise zucchini yellow
CC mosaic virus (ZYMV) and tobacco rattle virus (TRV) infections at the
CC early stage (PubMed:31812689). {ECO:0000269|PubMed:11710982,
CC ECO:0000269|PubMed:12535349, ECO:0000269|PubMed:16207746,
CC ECO:0000269|PubMed:17001447, ECO:0000269|PubMed:17169986,
CC ECO:0000269|PubMed:17924945, ECO:0000269|PubMed:18410480,
CC ECO:0000269|PubMed:18573194, ECO:0000269|PubMed:18987006,
CC ECO:0000269|PubMed:19083177, ECO:0000269|PubMed:21511907,
CC ECO:0000269|PubMed:22013065, ECO:0000269|PubMed:22902796,
CC ECO:0000269|PubMed:23042250, ECO:0000269|PubMed:31812689,
CC ECO:0000269|PubMed:9238008}.
CC -!- SUBUNIT: Interacts with TRN1 (PubMed:14756317). Interacts with the
CC Pseudomonas syringae type III effector HopU1 (PubMed:22013065). Binds
CC to small phloem-mobile single-stranded RNAs (ss-sRNA, e.g. small
CC interfering RNA (siRNA) and microRNA (miRNA)) in the phloeme exudate,
CC including viral-derived sRNA (vsiRNA) (PubMed:31812689).
CC {ECO:0000269|PubMed:14756317, ECO:0000269|PubMed:22013065,
CC ECO:0000269|PubMed:31812689}.
CC -!- INTERACTION:
CC Q03250; C0LGT6: EFR; NbExp=4; IntAct=EBI-1393626, EBI-8801168;
CC Q03250; Q9FL28: FLS2; NbExp=4; IntAct=EBI-1393626, EBI-1799448;
CC Q03250; Q88A91: hopU1; Xeno; NbExp=2; IntAct=EBI-1393626, EBI-8802399;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Secreted
CC {ECO:0000269|PubMed:31812689}. Note=Shuttling between nucleus and
CC cytoplasm. Relocalization from the cytoplasm into the nucleus is
CC mediated by TRN1. Observed in the phloem translocation stream
CC (PubMed:31812689). {ECO:0000269|PubMed:31812689}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q03250-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03250-2; Sequence=VSP_045855, VSP_045856;
CC -!- TISSUE SPECIFICITY: Ubiquitous with strong expression in guard cell.
CC {ECO:0000269|PubMed:18410480, ECO:0000269|PubMed:7513083}.
CC -!- INDUCTION: Up-regulated by cold stress and down-regulated by
CC dehydration stress, salt stress, abscisic acid (ABA) and mannitol.
CC Circadian regulation. Induced by hydrogen peroxide (at the protein
CC level). Up-regulated under P.carotovorum SCC1 (Pec) infection.
CC {ECO:0000269|PubMed:16207746, ECO:0000269|PubMed:17001447,
CC ECO:0000269|PubMed:17169986, ECO:0000269|PubMed:18987006,
CC ECO:0000269|PubMed:19672695, ECO:0000269|PubMed:22902796,
CC ECO:0000269|PubMed:7513083, ECO:0000269|PubMed:9238008}.
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: N-terminal part of the protein is one of the crucial
CC determinant to confer RNA chaperone activity during cold adaptation
CC process. {ECO:0000269|PubMed:21511907}.
CC -!- PTM: ADP-ribosylated by the Pseudomonas syringae type III effector
CC HopU1. ADP-ribosylation reduces the ability of the protein to bind RNA.
CC {ECO:0000269|PubMed:17450127}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitive responses to ABA in both seed
CC germination and root growth. Late-flowering. Increased germination rate
CC and seedling growth under salt and dehydration stress. Impaired mRNA
CC export under cold stress conditions. Defective in PAMP-triggered
CC immunity (PTI) responses and high susceptibility to P.syringae and
CC P.carotovorum SCC1 (Pec). Increased sensitivity to tobacco rattle virus
CC (TRV) (PubMed:31812689). The triple mutant srbp1 srbp2 srbp3 is more
CC susceptible to TRV (PubMed:31812689). {ECO:0000269|PubMed:17001447,
CC ECO:0000269|PubMed:17450127, ECO:0000269|PubMed:18410480,
CC ECO:0000269|PubMed:18573194, ECO:0000269|PubMed:22013065,
CC ECO:0000269|PubMed:22902796, ECO:0000269|PubMed:31812689}.
CC -!- MISCELLANEOUS: Plants overexpressing RBG7 display retarded germination
CC and affected seedling growth under salt and dehydration stress
CC conditions, confer freezing tolerance and also possess enhanced
CC resistance to P.syringae.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GR-RBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK68766.1; Type=Miscellaneous discrepancy; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=AAL66938.1; Type=Miscellaneous discrepancy; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=BAH57083.1; Type=Miscellaneous discrepancy; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=L04172; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z14987; CAA78711.1; -; mRNA.
DR EMBL; L00648; AAA32853.1; -; mRNA.
DR EMBL; L04172; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; MN064663; QGZ19398.1; -; mRNA.
DR EMBL; AC007119; AAD23639.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07209.1; -; Genomic_DNA.
DR EMBL; AF428381; AAL16149.1; -; mRNA.
DR EMBL; AY054284; AAL06943.1; -; mRNA.
DR EMBL; AY042826; AAK68766.1; ALT_SEQ; mRNA.
DR EMBL; AY072523; AAL66938.1; ALT_SEQ; mRNA.
DR EMBL; AK318968; BAH57083.1; ALT_SEQ; mRNA.
DR EMBL; AY085214; AAM62447.1; -; mRNA.
DR PIR; S30147; S30147.
DR RefSeq; NP_179760.1; NM_127738.5. [Q03250-1]
DR AlphaFoldDB; Q03250; -.
DR SMR; Q03250; -.
DR BioGRID; 2058; 8.
DR IntAct; Q03250; 41.
DR MINT; Q03250; -.
DR STRING; 3702.AT2G21660.1; -.
DR iPTMnet; Q03250; -.
DR MetOSite; Q03250; -.
DR SwissPalm; Q03250; -.
DR PaxDb; Q03250; -.
DR PRIDE; Q03250; -.
DR ProMEX; Q03250; -.
DR ProteomicsDB; 225967; -. [Q03250-1]
DR EnsemblPlants; AT2G21660.1; AT2G21660.1; AT2G21660. [Q03250-1]
DR GeneID; 816705; -.
DR Gramene; AT2G21660.1; AT2G21660.1; AT2G21660. [Q03250-1]
DR KEGG; ath:AT2G21660; -.
DR Araport; AT2G21660; -.
DR TAIR; locus:2049359; AT2G21660.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_28_1_1; -.
DR InParanoid; Q03250; -.
DR OMA; MANCKVF; -.
DR OrthoDB; 1579773at2759; -.
DR PRO; PR:Q03250; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q03250; baseline and differential.
DR Genevisible; Q03250; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; 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: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:0000380; P:alternative mRNA splicing, via spliceosome; IMP:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:TAIR.
DR GO; GO:0006858; P:extracellular transport; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:TAIR.
DR GO; GO:1990428; P:miRNA transport; IDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:TAIR.
DR GO; GO:0050688; P:regulation of defense response to virus; IDA:UniProtKB.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
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; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
DR GO; GO:0010501; P:RNA secondary structure unwinding; IDA:TAIR.
DR GO; GO:0050658; P:RNA transport; IDA:UniProtKB.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; 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 Acetylation; ADP-ribosylation; Alternative splicing; Chaperone; Cytoplasm;
KW Immunity; Innate immunity; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Plant defense; Reference proteome; RNA-binding; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..176
FT /note="Glycine-rich RNA-binding protein 7"
FT /id="PRO_0000081599"
FT DOMAIN 8..86
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 2..41
FT /note="Required for RNA chaperone activity"
FT REGION 83..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..175
FT /note="Glycine-rich (GR) required for cell-to-cell
FT movement"
FT /evidence="ECO:0000305|PubMed:31812689"
FT REGION 97..148
FT /note="Nuclear targeting sequence (M9)"
FT REGION 131..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 49
FT /note="ADP-ribosylarginine; by HopU1"
FT /evidence="ECO:0000269|PubMed:22013065"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT VAR_SEQ 39..48
FT /note="IINDRETGRS -> VCYTPRSDSE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:19423640, ECO:0000303|PubMed:7513083"
FT /id="VSP_045855"
FT VAR_SEQ 49..176
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:19423640, ECO:0000303|PubMed:7513083"
FT /id="VSP_045856"
FT MUTAGEN 47
FT /note="R->K: Abolishes ADP-ribosylation by HopU1."
FT /evidence="ECO:0000269|PubMed:17450127"
FT MUTAGEN 49
FT /note="R->K: Abolishes ADP-ribosylation by HopU1. Enable to
FT complement the rbg7 mutant."
FT /evidence="ECO:0000269|PubMed:17450127,
FT ECO:0000269|PubMed:17924945, ECO:0000269|PubMed:22013065,
FT ECO:0000269|PubMed:23042250"
FT MUTAGEN 49
FT /note="R->Q: Impairs RNA-binding and consequently impairs
FT the regulation of its pre-mRNA and its downstream pre-mRNA
FT target RBG8. Affects the alternative splicing of numerous
FT targets."
FT /evidence="ECO:0000269|PubMed:17450127,
FT ECO:0000269|PubMed:17924945, ECO:0000269|PubMed:22013065,
FT ECO:0000269|PubMed:23042250"
FT CONFLICT 133
FT /note="Missing (in Ref. 8; AAM62447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 16890 MW; 3E1025477F9CF4C4 CRC64;
MASGDVEYRC FVGGLAWATD DRALETAFAQ YGDVIDSKII NDRETGRSRG FGFVTFKDEK
AMKDAIEGMN GQDLDGRSIT VNEAQSRGSG GGGGHRGGGG GGYRSGGGGG YSGGGGSYGG
GGGRREGGGG YSGGGGGYSS RGGGGGSYGG GRREGGGGYG GGEGGGYGGS GGGGGW
