RGGA_ARATH
ID RGGA_ARATH Reviewed; 355 AA.
AC O23523; A8MQG3; A8MQJ5;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=RGG repeats nuclear RNA binding protein A {ECO:0000303|PubMed:11905967};
DE Short=AtRGGA {ECO:0000303|PubMed:25783413};
GN Name=RGGA {ECO:0000303|PubMed:11905967};
GN OrderedLocusNames=At4g16830 {ECO:0000312|Araport:AT4G16830};
GN ORFNames=dl4440w {ECO:0000312|EMBL:CAB10456.1},
GN FCAALL.13 {ECO:0000312|EMBL:CAB80954.1};
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=11905967; DOI=10.1023/a:1014089531125;
RA Landsberger M., Lorkovic Z.J., Oelmuller R.;
RT "Molecular characterization of nucleus-localized RNA-binding proteins from
RT higher plants.";
RL Plant Mol. Biol. 48:413-421(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, 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 [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION BY SALT;
RP ABSCISIC ACID AND OSMOTIC STRESS, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=25783413; DOI=10.1104/pp.114.255802;
RA Ambrosone A., Batelli G., Nurcato R., Aurilia V., Punzo P.,
RA Bangarusamy D.K., Ruberti I., Sassi M., Leone A., Costa A., Grillo S.;
RT "The Arabidopsis RNA-binding protein AtRGGA regulates tolerance to salt and
RT drought stress.";
RL Plant Physiol. 168:292-306(2015).
CC -!- FUNCTION: Binds RNA. Regulates responses to abscisic acid (ABA).
CC Promotes stomata closure in drought conditions. Involved in resistance
CC to salt and drought stresses via the accumulation of Pro.
CC {ECO:0000269|PubMed:25783413}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:25783413}. Nucleus {ECO:0000250|UniProtKB:Q9SQ56,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O23523-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O23523-2; Sequence=VSP_058643;
CC Name=3;
CC IsoId=O23523-3; Sequence=VSP_058644;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, roots,
CC inflorescences, and siliques (PubMed:25783413). Constitutively
CC expressed in seedlings and roots (PubMed:11905967).
CC {ECO:0000269|PubMed:11905967, ECO:0000269|PubMed:25783413}.
CC -!- DEVELOPMENTAL STAGE: In leaves, especially present in stomata guard
CC cells. In reproductive organs, expressed in pollen grains and tubes of
CC germinating pollen, as well as in funiculi attaching seeds to siliques.
CC {ECO:0000269|PubMed:25783413}.
CC -!- INDUCTION: By abscisic acid (ABA), and osmotic stress (e.g.
CC polyethylene glycol PEG). Slight transient repression by salt (NaCl).
CC {ECO:0000269|PubMed:25783413}.
CC -!- DISRUPTION PHENOTYPE: Larger rosettes and delayed flowering in long
CC days (16 h of light/8 h of darkness). Higher sensitivity to salt
CC (NaCl). Hypersensitivity to the presence of abscisic acid (ABA).
CC {ECO:0000269|PubMed:25783413}.
CC -!- SIMILARITY: Belongs to the RGGA protein family. {ECO:0000305}.
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DR EMBL; AF110227; AAF14243.1; -; Genomic_DNA.
DR EMBL; Z97342; CAB10456.1; -; Genomic_DNA.
DR EMBL; AL161545; CAB80954.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83809.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83810.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83811.1; -; Genomic_DNA.
DR EMBL; AY063896; AAL36252.1; -; mRNA.
DR EMBL; AY096500; AAM20150.1; -; mRNA.
DR EMBL; AY127018; AAM83242.1; -; mRNA.
DR EMBL; BT000559; AAN18128.1; -; mRNA.
DR PIR; F71435; F71435.
DR RefSeq; NP_001078399.1; NM_001084930.1. [O23523-2]
DR RefSeq; NP_001078400.1; NM_001084931.1. [O23523-3]
DR RefSeq; NP_193416.1; NM_117785.5. [O23523-1]
DR AlphaFoldDB; O23523; -.
DR SMR; O23523; -.
DR STRING; 3702.AT4G16830.1; -.
DR iPTMnet; O23523; -.
DR MetOSite; O23523; -.
DR PaxDb; O23523; -.
DR PRIDE; O23523; -.
DR ProteomicsDB; 236886; -. [O23523-1]
DR EnsemblPlants; AT4G16830.1; AT4G16830.1; AT4G16830. [O23523-1]
DR EnsemblPlants; AT4G16830.2; AT4G16830.2; AT4G16830. [O23523-2]
DR EnsemblPlants; AT4G16830.3; AT4G16830.3; AT4G16830. [O23523-3]
DR GeneID; 827389; -.
DR Gramene; AT4G16830.1; AT4G16830.1; AT4G16830. [O23523-1]
DR Gramene; AT4G16830.2; AT4G16830.2; AT4G16830. [O23523-2]
DR Gramene; AT4G16830.3; AT4G16830.3; AT4G16830. [O23523-3]
DR KEGG; ath:AT4G16830; -.
DR Araport; AT4G16830; -.
DR TAIR; locus:2129191; AT4G16830.
DR eggNOG; KOG2945; Eukaryota.
DR HOGENOM; CLU_033492_0_0_1; -.
DR InParanoid; O23523; -.
DR OMA; QNRKREF; -.
DR OrthoDB; 1266627at2759; -.
DR PhylomeDB; O23523; -.
DR PRO; PR:O23523; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23523; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:TAIR.
DR GO; GO:0071472; P:cellular response to salt stress; IMP:TAIR.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR InterPro; IPR039764; HABP4/SERBP1.
DR InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR InterPro; IPR019084; Stm1-like_N.
DR PANTHER; PTHR12299; PTHR12299; 1.
DR Pfam; PF04774; HABP4_PAI-RBP1; 1.
DR Pfam; PF09598; Stm1_N; 1.
DR SMART; SM01233; HABP4_PAI-RBP1; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Acetylation; Alternative splicing;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..355
FT /note="RGG repeats nuclear RNA binding protein A"
FT /id="PRO_0000438316"
FT DOMAIN 234..289
FT /note="FF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01013"
FT REGION 26..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 132..139
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 145..155
FT /note="Arginine-rich RNA-binding motif E-R-P-R-R-X-[F/Y]-
FT [E/D]-R-R-S"
FT /evidence="ECO:0000303|PubMed:11905967"
FT COMPBIAS 139..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O23593"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 1..140
FT /note="MATLNPFDLLDDDAEDPSQLAVAIEKIDKSKKSGQVSSLPAKSAPKLPSKPL
FT PPAQAVREARSDAPRGGGGRGGFNRGRGGYNRDDGNNGYSGGYTKPSGEGDVSKSSYER
FT RGGGGAPRGSFRGEGGGPGGGRRGGFSNE -> MLHVVVEAVEDLTVVVVVTTVMMVTM
FT DIQGDTLNPQVKEMFQSLLTRGVA (in isoform 2)"
FT /id="VSP_058643"
FT VAR_SEQ 2..57
FT /note="ATLNPFDLLDDDAEDPSQLAVAIEKIDKSKKSGQVSSLPAKSAPKLPSKPLP
FT PAQA -> MMLRIQASSLLPSRRLISPRNLDRFRACLLSQLLSFHRSHFLLLKP (in
FT isoform 3)"
FT /id="VSP_058644"
SQ SEQUENCE 355 AA; 37468 MW; A7F1D63DA96B7C2C CRC64;
MATLNPFDLL DDDAEDPSQL AVAIEKIDKS KKSGQVSSLP AKSAPKLPSK PLPPAQAVRE
ARSDAPRGGG GRGGFNRGRG GYNRDDGNNG YSGGYTKPSG EGDVSKSSYE RRGGGGAPRG
SFRGEGGGPG GGRRGGFSNE GGDGERPRRA FERRSGTGRG SDFKRDGSGR GNWGTPGEEI
AAETEAVAGV ETEKDVGEKP AVDDVAADAN KEDTVVEEKE PEDKEMTLDE YEKILEEKKK
ALQSLTTSER KVDTKVFESM QQLSNKKSND EIFIKLGSDK DKRKDDKEEK AKKAVSINEF
LKPAEGGNYY RGGRGGRGRG GRGRGGVSSG ESGGYRNEAA PAIGDAAQFP SLGGK
