RBG8_ARATH
ID RBG8_ARATH Reviewed; 169 AA.
AC Q03251; A0A178UVJ6; B9DFJ8; Q94CB0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Glycine-rich RNA-binding protein 8 {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746};
DE Short=AtGR-RBP8 {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746};
DE AltName: Full=AtRBG8 {ECO:0000303|PubMed:20009520};
DE AltName: Full=Glycine-rich protein 8 {ECO:0000303|PubMed:20009520};
DE Short=AtGRP8 {ECO:0000303|PubMed:20009520};
DE AltName: Full=Protein COLD, CIRCADIAN RHYTHM, AND RNA BINDING 1 {ECO:0000303|PubMed:7513083};
DE Short=Protein CCR1 {ECO:0000303|PubMed:7513083};
DE AltName: Full=Small RNA binding protein 2 {ECO:0000303|PubMed:31812689};
DE Short=AtSRBP2 {ECO:0000303|PubMed:31812689};
GN Name=RBG8 {ECO:0000303|PubMed:20009520};
GN Synonyms=CCR1 {ECO:0000303|PubMed:7513083},
GN GR-RBP8 {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746},
GN GRP8 {ECO:0000303|PubMed:20009520}, SRBP2 {ECO:0000303|PubMed:31812689};
GN OrderedLocusNames=At4g39260 {ECO:0000312|Araport:AT4G39260};
GN ORFNames=T22F8.160 {ECO:0000312|EMBL:CAB43641.1};
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 1), 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=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 [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] (ISOFORM 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 1).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
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 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 [9]
RP 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 [10]
RP INTERACTION WITH TRN1, AND NUCLEAR LOCALIZATION 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 [11]
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 [12]
RP ADP-RIBOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR
RP 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 [13]
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 [14]
RP FUNCTION, ALTERNATIVE SPLICING, MUTAGENESIS OF ARG-47, AND INDUCTION BY
RP 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 [15]
RP RNA-BINDING, AND FUNCTION.
RX PubMed=19527663; DOI=10.1016/j.bpj.2009.03.022;
RA Fuhrmann A., Schoening J.C., Anselmetti D., Staiger D., Ros R.;
RT "Quantitative analysis of single-molecule RNA-protein interaction.";
RL Biophys. J. 96:5030-5039(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [17]
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 [18]
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 [19]
RP FUNCTION.
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).
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. Involved in mRNA alternative splicing of
CC numerous targets by modulating splice site selection. Negatively
CC regulates the circadian oscillations of its own transcript as well as
CC RBG7 transcript. Forms an interlocked post-transcriptional negative
CC feedback loop with the RBG7 autoregulatory circuit. Both proteins
CC negatively autoregulate and reciprocally crossregulate by binding to
CC their pre-mRNAs and promoting unproductive splicing coupled to
CC degradation via the NMD pathway. Target of the Pseudomonas syringae
CC type III effector HopU1. 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:18987006,
CC ECO:0000269|PubMed:19527663, ECO:0000269|PubMed:23042250,
CC ECO:0000269|PubMed:31812689}.
CC -!- SUBUNIT: Interacts with TRN1 (PubMed:14756317). Binds to small phloem-
CC mobile single-stranded RNAs (ss-sRNA, e.g. small interfering RNA
CC (siRNA) and microRNA (miRNA)) in the phloeme exudate, including viral-
CC derived sRNA (vsiRNA) (PubMed:31812689). {ECO:0000269|PubMed:14756317,
CC ECO:0000269|PubMed:31812689}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17450127}. Nucleus
CC {ECO:0000250}. Secreted {ECO:0000269|PubMed:31812689}. Note=Shuttling
CC between nucleus and cytoplasm. Relocalization from the cytoplasm into
CC the nucleus is mediated by TRN1 (By similarity). Observed in the phloem
CC translocation stream (PubMed:31812689). {ECO:0000250,
CC ECO:0000269|PubMed:31812689}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q03251-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03251-2; Sequence=VSP_045857, VSP_045858;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7513083}.
CC -!- INDUCTION: Up-regulated by cold stress. Circadian regulation. Induced
CC by hydrogen peroxide (at the protein level).
CC {ECO:0000269|PubMed:16207746, ECO:0000269|PubMed:18987006,
CC ECO:0000269|PubMed:19672695, ECO:0000269|PubMed:7513083}.
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 -!- 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: The triple mutant srbp1 srbp2 srbp3 is more
CC susceptible to tobacco rattle virus (TRV).
CC {ECO:0000269|PubMed:31812689}.
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=AAK59502.1; Type=Miscellaneous discrepancy; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; Z14988; CAA78712.1; -; mRNA.
DR EMBL; L00649; AAA32854.1; -; mRNA.
DR EMBL; L04171; AAA20201.1; -; mRNA.
DR EMBL; MN064664; QGZ19399.1; -; mRNA.
DR EMBL; AL050351; CAB43641.1; -; Genomic_DNA.
DR EMBL; AL161594; CAB80589.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87044.1; -; Genomic_DNA.
DR EMBL; AY034997; AAK59502.1; ALT_SEQ; mRNA.
DR EMBL; AY063005; AAL34179.1; -; mRNA.
DR EMBL; AK316798; BAH19515.1; -; mRNA.
DR PIR; S30148; S30148.
DR RefSeq; NP_195637.1; NM_120087.4. [Q03251-1]
DR AlphaFoldDB; Q03251; -.
DR SMR; Q03251; -.
DR BioGRID; 15362; 5.
DR STRING; 3702.AT4G39260.1; -.
DR iPTMnet; Q03251; -.
DR MetOSite; Q03251; -.
DR PaxDb; Q03251; -.
DR PRIDE; Q03251; -.
DR ProteomicsDB; 236509; -. [Q03251-1]
DR EnsemblPlants; AT4G39260.1; AT4G39260.1; AT4G39260. [Q03251-1]
DR GeneID; 830082; -.
DR Gramene; AT4G39260.1; AT4G39260.1; AT4G39260. [Q03251-1]
DR KEGG; ath:AT4G39260; -.
DR Araport; AT4G39260; -.
DR TAIR; locus:2136298; AT4G39260.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_28_1_1; -.
DR InParanoid; Q03251; -.
DR OrthoDB; 1579773at2759; -.
DR PRO; PR:Q03251; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q03251; baseline and differential.
DR Genevisible; Q03251; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA: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: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: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:0050688; P:regulation of defense response to virus; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
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 ADP-ribosylation; Alternative splicing; Cytoplasm; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Secreted.
FT CHAIN 1..169
FT /note="Glycine-rich RNA-binding protein 8"
FT /id="PRO_0000081600"
FT DOMAIN 6..84
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 80..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..168
FT /note="Glycine-rich (GR) required for cell-to-cell
FT movement"
FT /evidence="ECO:0000305|PubMed:31812689"
FT REGION 95..143
FT /note="Nuclear targeting sequence (M9)"
FT REGION 130..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="ADP-ribosylarginine; by HopU1"
FT /evidence="ECO:0000250"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT VAR_SEQ 37..51
FT /note="IINDRESGRSRGFGF -> VCYTRDRSPGSSRFR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_045857"
FT VAR_SEQ 52..169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_045858"
FT MUTAGEN 47
FT /note="R->Q: Impairs RNA-binding and consequently impairs
FT the regulation of its pre-mRNA and its downstream pre-mRNA
FT target RBG7."
FT /evidence="ECO:0000269|PubMed:18987006"
SQ SEQUENCE 169 AA; 16579 MW; 31C4C246D247EB0D CRC64;
MSEVEYRCFV GGLAWATNDE DLQRTFSQFG DVIDSKIIND RESGRSRGFG FVTFKDEKAM
RDAIEEMNGK ELDGRVITVN EAQSRGSGGG GGGRGGSGGG YRSGGGGGYS GGGGGGYSGG
GGGGYERRSG GYGSGGGGGG RGYGGGGRRE GGGYGGGDGG SYGGGGGGW
