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Glycine-rich RNA-binding protein 8 (AtGR-RBP8) (AtRBG8) (Glycine-rich protein 8) (AtGRP8) (Protein COLD, CIRCADIAN RHYTHM, AND RNA BINDING 1) (Protein CCR1)

 RBG8_ARATH              Reviewed;         169 AA.
Q03251; Q94CB0;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
25-APR-2018, entry version 134.
RecName: Full=Glycine-rich RNA-binding protein 8;
Short=AtGR-RBP8;
AltName: Full=AtRBG8;
AltName: Full=Glycine-rich protein 8;
Short=AtGRP8;
AltName: Full=Protein COLD, CIRCADIAN RHYTHM, AND RNA BINDING 1;
Short=Protein CCR1;
Name=RBG8; Synonyms=CCR1, GR-RBP8, GRP8; OrderedLocusNames=At4g39260;
ORFNames=T22F8.160;
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 [MRNA] (ISOFORM 1).
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=8448367; DOI=10.1007/BF00014552;
van Nocker S., Vierstra R.D.;
"Two cDNAs from Arabidopsis thaliana encode putative RNA binding
proteins containing glycine-rich domains.";
Plant Mol. Biol. 21:695-699(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING,
INDUCTION BY COLD AND CIRCADIAN RHYTHM, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=7513083; DOI=10.1104/pp.104.3.1015;
Carpenter C.D., Kreps J.A., Simon A.E.;
"Genes encoding glycine-rich Arabidopsis thaliana proteins with RNA-
binding motifs are influenced by cold treatment and an endogenous
circadian rhythm.";
Plant Physiol. 104:1015-1025(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[6]
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).
[7]
ALTERNATIVE SPLICING.
PubMed=12535349; DOI=10.1046/j.1365-313X.2003.01629.x;
Staiger D., Zecca L., Wieczorek Kirk D.A., Apel K., Eckstein L.;
"The circadian clock regulated RNA-binding protein AtGRP7
autoregulates its expression by influencing alternative splicing of
its own pre-mRNA.";
Plant J. 33:361-371(2003).
[8]
INTERACTION WITH TRN1, AND NUCLEAR LOCALIZATION SIGNAL.
PubMed=14756317; DOI=10.1023/B:PLAN.0000009288.46713.1f;
Ziemienowicz A., Haasen D., Staiger D., Merkle T.;
"Arabidopsis transportin1 is the nuclear import receptor for the
circadian clock-regulated RNA-binding protein AtGRP7.";
Plant Mol. Biol. 53:201-212(2003).
[9]
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).
[10]
ADP-RIBOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR
LOCATION.
PubMed=17450127; DOI=10.1038/nature05737;
Fu Z.Q., Guo M., Jeong B.R., Tian F., Elthon T.E., Cerny R.L.,
Staiger D., Alfano J.R.;
"A type III effector ADP-ribosylates RNA-binding proteins and quells
plant immunity.";
Nature 447:284-288(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17951448; DOI=10.1105/tpc.107.050989;
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T.,
Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
targeting peptides, metabolic pathways, and defense mechanisms.";
Plant Cell 19:3170-3193(2007).
[12]
FUNCTION, ALTERNATIVE SPLICING, MUTAGENESIS OF ARG-47, AND INDUCTION
BY COLD.
PubMed=18987006; DOI=10.1093/nar/gkn847;
Schoening J.C., Streitner C., Meyer I.M., Gao Y., Staiger D.;
"Reciprocal regulation of glycine-rich RNA-binding proteins via an
interlocked feedback loop coupling alternative splicing to nonsense-
mediated decay in Arabidopsis.";
Nucleic Acids Res. 36:6977-6987(2008).
[13]
RNA-BINDING, AND FUNCTION.
PubMed=19527663; DOI=10.1016/j.bpj.2009.03.022;
Fuhrmann A., Schoening J.C., Anselmetti D., Staiger D., Ros R.;
"Quantitative analysis of single-molecule RNA-protein interaction.";
Biophys. J. 96:5030-5039(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION BY HYDROGEN PEROXIDE,
AND RNA-BINDING.
PubMed=19672695; DOI=10.1007/s11033-009-9636-x;
Schmidt F., Marnef A., Cheung M.K., Wilson I., Hancock J., Staiger D.,
Ladomery M.;
"A proteomic analysis of oligo(dT)-bound mRNP containing oxidative
stress-induced Arabidopsis thaliana RNA-binding proteins ATGRP7 and
ATGRP8.";
Mol. Biol. Rep. 37:839-845(2010).
[16]
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).
[17]
FUNCTION.
PubMed=23042250; DOI=10.1093/nar/gks873;
Streitner C., Koester T., Simpson C.G., Shaw P., Danisman S.,
Brown J.W., Staiger D.;
"An hnRNP-like RNA-binding protein affects alternative splicing by in
vivo interaction with transcripts in Arabidopsis thaliana.";
Nucleic Acids Res. 40:11240-11255(2012).
-!- FUNCTION: Plays a role in RNA transcription or processing during
stress. Binds RNAs and DNAs sequence with a preference to single-
stranded nucleic acids. Involved in mRNA alternative splicing of
numerous targets by modulating splice site selection. Negatively
regulates the circadian oscillations of its own transcript as well
as RBG7 transcript. Forms an interlocked post-transcriptional
negative feedback loop with the RBG7 autoregulatory circuit. Both
proteins negatively autoregulate and reciprocally crossregulate by
binding to their pre-mRNAs and promoting unproductive splicing
coupled to degradation via the NMD pathway. Target of the
Pseudomonas syringae type III effector HopU1.
{ECO:0000269|PubMed:18987006, ECO:0000269|PubMed:19527663,
ECO:0000269|PubMed:23042250}.
-!- SUBUNIT: Interacts with TRN1. {ECO:0000269|PubMed:14756317}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17450127}.
Nucleus {ECO:0000250}. Note=Shuttling between nucleus and
cytoplasm. Relocalization from the cytoplasm into the nucleus is
mediated by TRN1 (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q03251-1; Sequence=Displayed;
Name=2;
IsoId=Q03251-2; Sequence=VSP_045857, VSP_045858;
Note=May be due to a competing donor splice site. No
experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7513083}.
-!- INDUCTION: Up-regulated by cold stress. Circadian regulation.
Induced by hydrogen peroxide (at the protein level).
{ECO:0000269|PubMed:16207746, ECO:0000269|PubMed:18987006,
ECO:0000269|PubMed:19672695, ECO:0000269|PubMed:7513083}.
-!- PTM: ADP-ribosylated by the Pseudomonas syringae type III effector
HopU1. ADP-ribosylation reduces the ability of the protein to bind
RNA. {ECO:0000269|PubMed:17450127}.
-!- SIMILARITY: Belongs to the GR-RBP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK59502.1; Type=Miscellaneous discrepancy; Note=Wrong choice of frame.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; Z14988; CAA78712.1; -; mRNA.
EMBL; L00649; AAA32854.1; -; mRNA.
EMBL; L04171; AAA20201.1; -; mRNA.
EMBL; AL050351; CAB43641.1; -; Genomic_DNA.
EMBL; AL161594; CAB80589.1; -; Genomic_DNA.
EMBL; CP002687; AEE87044.1; -; Genomic_DNA.
EMBL; AY034997; AAK59502.1; ALT_SEQ; mRNA.
EMBL; AY063005; AAL34179.1; -; mRNA.
PIR; S30148; S30148.
RefSeq; NP_195637.1; NM_120087.4. [Q03251-1]
UniGene; At.23968; -.
ProteinModelPortal; Q03251; -.
SMR; Q03251; -.
BioGrid; 15362; 5.
STRING; 3702.AT4G39260.1; -.
iPTMnet; Q03251; -.
PaxDb; Q03251; -.
PRIDE; Q03251; -.
EnsemblPlants; AT4G39260.1; AT4G39260.1; AT4G39260. [Q03251-1]
EnsemblPlants; AT4G39260.3; AT4G39260.3; AT4G39260.
GeneID; 830082; -.
Gramene; AT4G39260.1; AT4G39260.1; AT4G39260. [Q03251-1]
Gramene; AT4G39260.3; AT4G39260.3; AT4G39260.
KEGG; ath:AT4G39260; -.
Araport; AT4G39260; -.
TAIR; locus:2136298; AT4G39260.
eggNOG; ENOG410IQXM; Eukaryota.
eggNOG; ENOG41121QZ; LUCA.
HOGENOM; HOG000276232; -.
InParanoid; Q03251; -.
OMA; TIRIDYS; -.
OrthoDB; EOG09360WUX; -.
PRO; PR:Q03251; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q03251; baseline and differential.
Genevisible; Q03251; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0005730; C:nucleolus; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0003729; F:mRNA binding; IDA:TAIR.
GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:TAIR.
GO; GO:0045087; P:innate immune response; IDA:TAIR.
GO; GO:0009737; P:response to abscisic acid; IDA:TAIR.
GO; GO:0009409; P:response to cold; IEP:UniProtKB.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
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;
ADP-ribosylation; Alternative splicing; Complete proteome; Cytoplasm;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding.
CHAIN 1 169 Glycine-rich RNA-binding protein 8.
/FTId=PRO_0000081600.
DOMAIN 6 84 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 95 143 Nuclear targeting sequence (M9).
COMPBIAS 86 168 Gly-rich.
MOD_RES 47 47 ADP-ribosylarginine; by HopU1.
{ECO:0000250}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000244|PubMed:19245862}.
VAR_SEQ 37 51 IINDRESGRSRGFGF -> VCYTRDRSPGSSRFR (in
isoform 2).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_045857.
VAR_SEQ 52 169 Missing (in isoform 2).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_045858.
MUTAGEN 47 47 R->Q: Impairs RNA-binding and
consequently impairs the regulation of
its pre-mRNA and its downstream pre-mRNA
target RBG7.
{ECO:0000269|PubMed:18987006}.
SEQUENCE 169 AA; 16579 MW; 31C4C246D247EB0D CRC64;
MSEVEYRCFV GGLAWATNDE DLQRTFSQFG DVIDSKIIND RESGRSRGFG FVTFKDEKAM
RDAIEEMNGK ELDGRVITVN EAQSRGSGGG GGGRGGSGGG YRSGGGGGYS GGGGGGYSGG
GGGGYERRSG GYGSGGGGGG RGYGGGGRRE GGGYGGGDGG SYGGGGGGW


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