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Glycine-rich RNA-binding protein 7 (AtGR-RBP7) (AtRBG7) (Glycine-rich protein 7) (AtGRP7) (Protein COLD, CIRCADIAN RHYTHM, AND RNA BINDING 2) (Protein CCR2)

 RBG7_ARATH              Reviewed;         176 AA.
Q03250; C0Z304; Q8LEV4; Q94B62;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
25-APR-2018, entry version 143.
RecName: Full=Glycine-rich RNA-binding protein 7;
Short=AtGR-RBP7;
AltName: Full=AtRBG7;
AltName: Full=Glycine-rich protein 7;
Short=AtGRP7;
AltName: Full=Protein COLD, CIRCADIAN RHYTHM, AND RNA BINDING 2;
Short=Protein CCR2;
Name=RBG7; Synonyms=CCR2, GR-RBP7, GRP7; OrderedLocusNames=At2g21660;
ORFNames=F2G1.7;
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 2), 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=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(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] (ISOFORMS 1 AND 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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
INDUCTION BY CIRCADIAN RHYTHM, AND FUNCTION.
PubMed=9238008; DOI=10.1073/pnas.94.16.8515;
Heintzen C., Nater M., Apel K., Staiger D.;
"AtGRP7, a nuclear RNA-binding protein as a component of a circadian-
regulated negative feedback loop in Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 94:8515-8520(1997).
[9]
FUNCTION, AND REVIEW.
PubMed=11710982; DOI=10.1098/rstb.2001.0964;
Staiger D.;
"RNA-binding proteins and circadian rhythms in Arabidopsis thaliana.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1755-1759(2001).
[10]
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).
[11]
FUNCTION, AND 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).
[12]
SUBCELLULAR LOCATION, 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).
[13]
INDUCTION BY COLD; DEHYDRATION AND SALT, AND FUNCTION.
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).
[14]
INDUCTION, DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=17001447; DOI=10.2478/s11658-006-0042-2;
Cao S., Jiang L., Song S., Jing R., Xu G.;
"AtGRP7 is involved in the regulation of abscisic acid and stress
responses in Arabidopsis.";
Cell. Mol. Biol. Lett. 11:526-535(2006).
[15]
DISRUPTION PHENOTYPE, ADP-RIBOSYLATION, IDENTIFICATION BY MASS
SPECTROMETRY, MUTAGENESIS OF ARG-47 AND ARG-49, 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).
[16]
INDUCTION BY COLD, AND FUNCTION.
PubMed=17169986; DOI=10.1093/nar/gkl1076;
Kim J.S., Park S.J., Kwak K.J., Kim Y.O., Kim J.Y., Song J., Jang B.,
Jung C.-H., Kang H.;
"Cold shock domain proteins and glycine-rich RNA-binding proteins from
Arabidopsis thaliana can promote the cold adaptation process in
Escherichia coli.";
Nucleic Acids Res. 35:506-516(2007).
[17]
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).
[18]
MUTAGENESIS OF ARG-49, AND FUNCTION.
PubMed=17924945; DOI=10.1111/j.1365-313X.2007.03302.x;
Schoening J.C., Streitner C., Page D.R., Hennig S., Uchida K.,
Wolf E., Furuya M., Staiger D.;
"Auto-regulation of the circadian slave oscillator component AtGRP7
and regulation of its targets is impaired by a single RNA recognition
motif point mutation.";
Plant J. 52:1119-1130(2007).
[19]
RNA-BINDING.
PubMed=18576621; DOI=10.1021/ja801994z;
Schuettpelz M., Schoening J.C., Doose S., Neuweiler H., Peters E.,
Staiger D., Sauer M.;
"Changes in conformational dynamics of mRNA upon AtGRP7 binding
studied by fluorescence correlation spectroscopy.";
J. Am. Chem. Soc. 130:9507-9513(2008).
[20]
FUNCTION, ALTERNATIVE SPLICING, 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).
[21]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=18410480; DOI=10.1111/j.1365-313X.2008.03518.x;
Kim J.S., Jung H.J., Lee H.J., Kim K.A., Goh C.H., Woo Y., Oh S.H.,
Han Y.S., Kang H.;
"Glycine-rich RNA-binding protein 7 affects abiotic stress responses
by regulating stomata opening and closing in Arabidopsis thaliana.";
Plant J. 55:455-466(2008).
[22]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18573194; DOI=10.1111/j.1365-313X.2008.03591.x;
Streitner C., Danisman S., Wehrle F., Schoening J.C., Alfano J.R.,
Staiger D.;
"The small glycine-rich RNA binding protein AtGRP7 promotes floral
transition in Arabidopsis thaliana.";
Plant J. 56:239-250(2008).
[23]
FUNCTION, AND RNA-BINDING.
PubMed=19083177; DOI=10.1007/978-1-59745-289-2_21;
Schoening J.C., Staiger D.;
"RNA-protein interaction mediating post-transcriptional regulation in
the circadian system.";
Methods Mol. Biol. 479:337-351(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[25]
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).
[26]
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).
[27]
FUNCTION, INTERACTION WITH HOPU1, MUTAGENESIS OF ARG-49,
ADP-RIBOSYLATION AT ARG-49, AND DISRUPTION PHENOTYPE.
PubMed=22013065; DOI=10.1074/jbc.M111.290122;
Jeong B.R., Lin Y., Joe A., Guo M., Korneli C., Yang H., Wang P.,
Yu M., Cerny R.L., Staiger D., Alfano J.R., Xu Y.;
"Structure function analysis of an ADP-ribosyltransferase type III
effector and its RNA-binding target in plant immunity.";
J. Biol. Chem. 286:43272-43281(2011).
[28]
FUNCTION, AND DOMAIN.
PubMed=21511907; DOI=10.1093/jxb/err101;
Kwak K.J., Park S.J., Han J.H., Kim M.K., Oh S.H., Han Y.S., Kang H.;
"Structural determinants crucial to the RNA chaperone activity of
glycine-rich RNA-binding proteins 4 and 7 in Arabidopsis thaliana
during the cold adaptation process.";
J. Exp. Bot. 62:4003-4011(2011).
[29]
SUBCELLULAR LOCATION.
PubMed=21453442; DOI=10.1111/j.1600-0854.2011.01180.x;
Lummer M., Humpert F., Steuwe C., Caesar K., Schuettpelz M., Sauer M.,
Staiger D.;
"Reversible photoswitchable DRONPA-s monitors nucleocytoplasmic
transport of an RNA-binding protein in transgenic plants.";
Traffic 12:693-702(2011).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22092075; DOI=10.1021/pr200917t;
Aryal U.K., Krochko J.E., Ross A.R.;
"Identification of phosphoproteins in Arabidopsis thaliana leaves
using polyethylene glycol fractionation, immobilized metal-ion
affinity chromatography, two-dimensional gel electrophoresis and mass
spectrometry.";
J. Proteome Res. 11:425-437(2012).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[32]
FUNCTION, AND MUTAGENESIS OF ARG-49.
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).
[33]
FUNCTION, INDUCTION BY PATHOGEN, AND DISRUPTION PHENOTYPE.
PubMed=22902796; DOI=10.1016/j.plaphy.2012.07.020;
Lee H.J., Kim J.S., Yoo S.J., Kang E.Y., Han S.H., Yang K.Y.,
Kim Y.C., McSpadden Gardener B., Kang H.;
"Different roles of glycine-rich RNA-binding protein7 in plant defense
against Pectobacterium carotovorum, Botrytis cinerea, and tobacco
mosaic viruses.";
Plant Physiol. Biochem. 60:46-52(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. Displays strong affinity to poly(U) and
poly(G) sequence. 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 RBG8 transcript. Forms an interlocked post-transcriptional
negative feedback loop with the RBG8 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. Involved in the
regulation of abscisic acid and stress responses. Affects the
growth and stress tolerance under high salt and dehydration stress
conditions, and also confers freezing tolerance, particularly via
the regulation of stomatal opening and closing in the guard cells.
Exhibits RNA chaperone activity during the cold adaptation
process. Involved in the export of mRNAs from the nucleus to the
cytoplasm under cold stress conditions. Target of the Pseudomonas
syringae type III effector HopU1, which could probably be involved
in plant innate immunity. Component of the flowering autonomous
pathway which promotes floral transition, at least partly by down-
regulating FLC. {ECO:0000269|PubMed:11710982,
ECO:0000269|PubMed:12535349, ECO:0000269|PubMed:16207746,
ECO:0000269|PubMed:17001447, ECO:0000269|PubMed:17169986,
ECO:0000269|PubMed:17924945, ECO:0000269|PubMed:18410480,
ECO:0000269|PubMed:18573194, ECO:0000269|PubMed:18987006,
ECO:0000269|PubMed:19083177, ECO:0000269|PubMed:21511907,
ECO:0000269|PubMed:22013065, ECO:0000269|PubMed:22902796,
ECO:0000269|PubMed:23042250, ECO:0000269|PubMed:9238008}.
-!- SUBUNIT: Interacts with TRN1. Interacts with the Pseudomonas
syringae type III effector HopU1. {ECO:0000269|PubMed:14756317,
ECO:0000269|PubMed:22013065}.
-!- INTERACTION:
C0LGT6:EFR; NbExp=4; IntAct=EBI-1393626, EBI-8801168;
Q9FL28:FLS2; NbExp=4; IntAct=EBI-1393626, EBI-1799448;
Q88A91:hopU1 (xeno); NbExp=2; IntAct=EBI-1393626, EBI-8802399;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttling between
nucleus and cytoplasm. Relocalization from the cytoplasm into the
nucleus is mediated by TRN1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q03250-1; Sequence=Displayed;
Name=2;
IsoId=Q03250-2; Sequence=VSP_045855, VSP_045856;
Note=May be due to a competing donor splice site. No
experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous with strong expression in guard
cell. {ECO:0000269|PubMed:18410480, ECO:0000269|PubMed:7513083}.
-!- INDUCTION: Up-regulated by cold stress and down-regulated by
dehydration stress, salt stress, abscisic acid (ABA) and mannitol.
Circadian regulation. Induced by hydrogen peroxide (at the protein
level). Up-regulated under P.carotovorum SCC1 (Pec) infection.
{ECO:0000269|PubMed:16207746, ECO:0000269|PubMed:17001447,
ECO:0000269|PubMed:17169986, ECO:0000269|PubMed:18987006,
ECO:0000269|PubMed:19672695, ECO:0000269|PubMed:22902796,
ECO:0000269|PubMed:7513083, ECO:0000269|PubMed:9238008}.
-!- DOMAIN: N-terminal part of the protein is one of the crucial
determinant to confer RNA chaperone activity during cold
adaptation process. {ECO:0000269|PubMed:21511907}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: Hypersensitive responses to ABA in both seed
germination and root growth. Late-flowering. Increased germination
rate and seedling growth under salt and dehydration stress.
Impaired mRNA export under cold stress conditions. Defective in
PAMP-triggered immunity (PTI) responses and high susceptibility to
P.syringae and P.carotovorum SCC1 (Pec).
{ECO:0000269|PubMed:17001447, ECO:0000269|PubMed:17450127,
ECO:0000269|PubMed:18410480, ECO:0000269|PubMed:18573194,
ECO:0000269|PubMed:22013065, ECO:0000269|PubMed:22902796}.
-!- MISCELLANEOUS: Plants overexpressing RBG7 display retarded
germination and affected seedling growth under salt and
dehydration stress conditions, confer freezing tolerance and also
possess enhanced resistance to P.syringae.
-!- SIMILARITY: Belongs to the GR-RBP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK68766.1; Type=Miscellaneous discrepancy; Note=Wrong choice of frame.; Evidence={ECO:0000305};
Sequence=AAL66938.1; Type=Miscellaneous discrepancy; Note=Wrong choice of frame.; Evidence={ECO:0000305};
Sequence=BAH57083.1; Type=Miscellaneous discrepancy; Note=Wrong choice of frame.; Evidence={ECO:0000305};
Sequence=L04172; Type=Frameshift; Positions=11; Evidence={ECO:0000305};
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EMBL; Z14987; CAA78711.1; -; mRNA.
EMBL; L00648; AAA32853.1; -; mRNA.
EMBL; L04172; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC007119; AAD23639.1; -; Genomic_DNA.
EMBL; CP002685; AEC07209.1; -; Genomic_DNA.
EMBL; AF428381; AAL16149.1; -; mRNA.
EMBL; AY054284; AAL06943.1; -; mRNA.
EMBL; AY042826; AAK68766.1; ALT_SEQ; mRNA.
EMBL; AY072523; AAL66938.1; ALT_SEQ; mRNA.
EMBL; AK318968; BAH57083.1; ALT_SEQ; mRNA.
EMBL; AY085214; AAM62447.1; -; mRNA.
PIR; S30147; S30147.
RefSeq; NP_179760.1; NM_127738.5. [Q03250-1]
UniGene; At.22672; -.
UniGene; At.23628; -.
UniGene; At.24279; -.
UniGene; At.72988; -.
ProteinModelPortal; Q03250; -.
SMR; Q03250; -.
BioGrid; 2058; 8.
IntAct; Q03250; 41.
MINT; Q03250; -.
STRING; 3702.AT2G21660.1; -.
iPTMnet; Q03250; -.
SwissPalm; Q03250; -.
PaxDb; Q03250; -.
PRIDE; Q03250; -.
ProMEX; Q03250; -.
EnsemblPlants; AT2G21660.1; AT2G21660.1; AT2G21660. [Q03250-1]
EnsemblPlants; AT2G21660.2; AT2G21660.2; AT2G21660.
GeneID; 816705; -.
Gramene; AT2G21660.1; AT2G21660.1; AT2G21660. [Q03250-1]
Gramene; AT2G21660.2; AT2G21660.2; AT2G21660.
KEGG; ath:AT2G21660; -.
Araport; AT2G21660; -.
TAIR; locus:2049359; AT2G21660.
eggNOG; KOG0118; Eukaryota.
eggNOG; COG0724; LUCA.
HOGENOM; HOG000276232; -.
InParanoid; Q03250; -.
OMA; MGEACKV; -.
OrthoDB; EOG09360WUX; -.
PRO; PR:Q03250; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q03250; baseline and differential.
Genevisible; Q03250; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0003690; F:double-stranded DNA binding; IDA:TAIR.
GO; GO:0003729; F:mRNA binding; IDA:TAIR.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:TAIR.
GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
GO; GO:0032508; P:DNA duplex unwinding; IDA:TAIR.
GO; GO:0045087; P:innate immune response; IDA:TAIR.
GO; GO:0006406; P:mRNA export from nucleus; IMP:TAIR.
GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009409; P:response to cold; IEP:UniProtKB.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
GO; GO:0010501; P:RNA secondary structure unwinding; IDA:TAIR.
GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP: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;
Acetylation; ADP-ribosylation; Alternative splicing; Chaperone;
Complete proteome; Cytoplasm; Immunity; Innate immunity;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Plant defense; Reference proteome; RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 176 Glycine-rich RNA-binding protein 7.
/FTId=PRO_0000081599.
DOMAIN 8 86 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 2 41 Required for RNA chaperone activity.
REGION 97 148 Nuclear targeting sequence (M9).
COMPBIAS 88 175 Gly-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 49 49 ADP-ribosylarginine; by HopU1.
{ECO:0000269|PubMed:22013065}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000244|PubMed:19376835}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000244|PubMed:22092075}.
VAR_SEQ 39 48 IINDRETGRS -> VCYTPRSDSE (in isoform 2).
{ECO:0000303|PubMed:14593172,
ECO:0000303|PubMed:19423640,
ECO:0000303|PubMed:7513083}.
/FTId=VSP_045855.
VAR_SEQ 49 176 Missing (in isoform 2).
{ECO:0000303|PubMed:14593172,
ECO:0000303|PubMed:19423640,
ECO:0000303|PubMed:7513083}.
/FTId=VSP_045856.
MUTAGEN 47 47 R->K: Abolishes ADP-ribosylation by
HopU1. {ECO:0000269|PubMed:17450127}.
MUTAGEN 49 49 R->K: Abolishes ADP-ribosylation by
HopU1. Enable to complement the rbg7
mutant. {ECO:0000269|PubMed:17450127,
ECO:0000269|PubMed:17924945,
ECO:0000269|PubMed:22013065,
ECO:0000269|PubMed:23042250}.
MUTAGEN 49 49 R->Q: Impairs RNA-binding and
consequently impairs the regulation of
its pre-mRNA and its downstream pre-mRNA
target RBG8. Affects the alternative
splicing of numerous targets.
{ECO:0000269|PubMed:17450127,
ECO:0000269|PubMed:17924945,
ECO:0000269|PubMed:22013065,
ECO:0000269|PubMed:23042250}.
CONFLICT 133 133 Missing (in Ref. 7; AAM62447).
{ECO:0000305}.
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


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