MRG1_ARATH
ID MRG1_ARATH Reviewed; 320 AA.
AC Q94C32; O23159;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Protein MRG1 {ECO:0000303|PubMed:25211338};
DE AltName: Full=MRG family protein 1 {ECO:0000303|PubMed:25211338};
DE AltName: Full=Morf Related Gene 1 {ECO:0000303|PubMed:25211338};
GN Name=MRG1 {ECO:0000303|PubMed:25211338};
GN OrderedLocusNames=At4g37280 {ECO:0000312|Araport:AT4G37280};
GN ORFNames=C7A10.80 {ECO:0000312|EMBL:CAB16772.1};
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 {ECO:0000312|EMBL:AAK59778.1};
RN [1]
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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH HAM1 AND HAM2.
RC STRAIN=cv. Columbia;
RX PubMed=25183522; DOI=10.1093/nar/gku781;
RA Xu Y., Gan E.S., Zhou J., Wee W.Y., Zhang X., Ito T.;
RT "Arabidopsis MRG domain proteins bridge two histone modifications to
RT elevate expression of flowering genes.";
RL Nucleic Acids Res. 42:10960-10974(2014).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=25211338; DOI=10.1371/journal.pgen.1004617;
RA Bu Z., Yu Y., Li Z., Liu Y., Jiang W., Huang Y., Dong A.W.;
RT "Regulation of arabidopsis flowering by the histone mark readers MRG1/2 via
RT interaction with CONSTANS to modulate FT expression.";
RL PLoS Genet. 10:E1004617-E1004617(2014).
RN [7]
RP IDENTIFICATION IN THE NUA4 COMPLEX.
RX DOI=10.1186/s12870-015-0461-1;
RA Bieluszewski T., Galganski L., Sura W., Bieluszewska A., Abram M.,
RA Ludwikow A., Ziolkowski P., Sadowski J.;
RT "AtEAF1 is a potential platform protein for Arabidopsis NuA4
RT acetyltransferase complex.";
RL BMC Plant Biol. 15:0-0(2015).
CC -!- FUNCTION: Chromatin remodeling factor. Acts as a 'reader' protein by
CC binding to H3K36me3 and H3K36me3 to control histone H4 acetylation.
CC Increases the transcriptional levels of the flowering time genes FLC
CC and FT (PubMed:25183522, PubMed:25211338). Binds the chromatin at the
CC FT promoter upon interaction with CO (Probable).
CC {ECO:0000269|PubMed:25183522, ECO:0000269|PubMed:25211338,
CC ECO:0000305|PubMed:25211338}.
CC -!- SUBUNIT: Interacts with HAM1 and HAM2 (PubMed:25183522). Interacts (via
CC MRG domain) with CO (Probable). Component of the NuA4 histone
CC acetyltransferase complex (Ref.7). {ECO:0000269|PubMed:25183522,
CC ECO:0000269|Ref.7, ECO:0000305|PubMed:25211338}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25183522}.
CC Note=Localized only in the euchromatic regions.
CC {ECO:0000269|PubMed:25183522}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Mainly expressed in the vasculature of
CC cotyledons and leaves, and in roots and inflorescences
CC (PubMed:25211338). {ECO:0000269|PubMed:25183522,
CC ECO:0000269|PubMed:25211338}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC MRG2. Mrg1 and mrg2 double mutants are late-flowering under long-day
CC growth conditions. {ECO:0000269|PubMed:25183522,
CC ECO:0000269|PubMed:25211338}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB16772.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80394.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z99707; CAB16772.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161591; CAB80394.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86776.1; -; Genomic_DNA.
DR EMBL; AY037193; AAK59778.1; -; mRNA.
DR EMBL; AY142038; AAM98302.1; -; mRNA.
DR PIR; E85440; E85440.
DR RefSeq; NP_568021.1; NM_119891.4.
DR AlphaFoldDB; Q94C32; -.
DR SMR; Q94C32; -.
DR IntAct; Q94C32; 1.
DR STRING; 3702.AT4G37280.1; -.
DR iPTMnet; Q94C32; -.
DR PaxDb; Q94C32; -.
DR PRIDE; Q94C32; -.
DR ProteomicsDB; 239078; -.
DR EnsemblPlants; AT4G37280.1; AT4G37280.1; AT4G37280.
DR GeneID; 829882; -.
DR Gramene; AT4G37280.1; AT4G37280.1; AT4G37280.
DR KEGG; ath:AT4G37280; -.
DR Araport; AT4G37280; -.
DR TAIR; locus:2114980; AT4G37280.
DR eggNOG; KOG3001; Eukaryota.
DR HOGENOM; CLU_039566_1_0_1; -.
DR InParanoid; Q94C32; -.
DR OMA; GLQTYFD; -.
DR OrthoDB; 1624495at2759; -.
DR PhylomeDB; Q94C32; -.
DR PRO; PR:Q94C32; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94C32; baseline and differential.
DR Genevisible; Q94C32; AT.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; IDA:TAIR.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IPI:TAIR.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0048586; P:regulation of long-day photoperiodism, flowering; IGI:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.274.30; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR008676; MRG.
DR InterPro; IPR038217; MRG_C_sf.
DR InterPro; IPR026541; MRG_dom.
DR InterPro; IPR025995; Tudor-knot.
DR PANTHER; PTHR10880; PTHR10880; 1.
DR Pfam; PF05712; MRG; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR PIRSF; PIRSF038133; HAT_Nua4_EAF3/MRG15; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS51640; MRG; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..320
FT /note="Protein MRG1"
FT /id="PRO_0000432989"
FT DOMAIN 30..80
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 150..318
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 320 AA; 36383 MW; B913517C35AFC078 CRC64;
MGSSSKEETA SDGDTASGGA SPSNDGRLFS EGERVLAYHG PRVYGAKVQK VELRKKEWKY
FVHYLGWNKN WDEWVSADRL LKHTEENLVK QKALDKKQGV EKGTKSGRSA QTKTRSSADT
KADKDDTKTN AAKGKKRKHE SGNEKDNVTA EKLMKIQIPA SLKKQLTDDW EYIAQKDKVV
KLPRSPNVDE ILSKYLEFKT KKDGMVTDSV AEILKGIRSY FDKALPVMLL YKKERRQYQE
SIVDDTSPST VYGAEHLLRL FVKLPDLFSY VNMEEETWSR MQQTLSDFLK FIQKNQSTFL
LPSAYDSDKV SDGKGKGKDD
