MRG2_ARATH
ID MRG2_ARATH Reviewed; 327 AA.
AC Q4V3E2; Q9SRX0;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein MRG2 {ECO:0000303|PubMed:25211338};
DE AltName: Full=MRG family protein 2 {ECO:0000303|PubMed:25211338};
DE AltName: Full=Morf Related Gene 2 {ECO:0000303|PubMed:25211338};
GN Name=MRG2 {ECO:0000303|PubMed:25211338};
GN OrderedLocusNames=At1g02740 {ECO:0000312|Araport:AT1G02740};
GN ORFNames=F22D16.25 {ECO:0000312|EMBL:AAF02891.1};
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:AAY56405.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP 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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INTERACTION WITH CO,
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 53-123 IN COMPLEX WITH
RP TRIMETHYLATED HISTONE H3 PEPTIDES, AND MUTAGENESIS OF TYR-87.
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).
CC -!- FUNCTION: Chromatin remodeling factor. Acts as a 'reader' protein by
CC binding to H3K4me3 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 (PubMed:25211338).
CC {ECO:0000269|PubMed:25183522, ECO:0000269|PubMed:25211338}.
CC -!- SUBUNIT: Interacts with HAM1 and HAM2 (PubMed:25183522). Interacts (via
CC MRG domain) with CO (PubMed:25211338). Component of the NuA4 histone
CC acetyltransferase complex (By similarity).
CC {ECO:0000250|UniProtKB:Q94C32, ECO:0000269|PubMed:25183522,
CC ECO:0000269|PubMed:25211338}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:25183522). Mainly expressed in
CC the vasculature of cotyledons and leaves, and in roots and
CC inflorescences (PubMed:25211338). {ECO:0000269|PubMed:25183522,
CC ECO:0000269|PubMed:25211338}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC MRG1. 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=AAF02891.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009525; AAF02891.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27465.1; -; Genomic_DNA.
DR EMBL; BT023414; AAY56405.1; -; mRNA.
DR PIR; E86157; E86157.
DR RefSeq; NP_171774.2; NM_100154.4.
DR PDB; 4PL6; X-ray; 1.68 A; A/B=51-123.
DR PDB; 4PLI; X-ray; 1.65 A; A/B=51-123.
DR PDB; 4PLL; X-ray; 2.60 A; A/B=51-123.
DR PDBsum; 4PL6; -.
DR PDBsum; 4PLI; -.
DR PDBsum; 4PLL; -.
DR AlphaFoldDB; Q4V3E2; -.
DR SMR; Q4V3E2; -.
DR STRING; 3702.AT1G02740.1; -.
DR iPTMnet; Q4V3E2; -.
DR PaxDb; Q4V3E2; -.
DR PRIDE; Q4V3E2; -.
DR ProteomicsDB; 250859; -.
DR EnsemblPlants; AT1G02740.1; AT1G02740.1; AT1G02740.
DR GeneID; 839455; -.
DR Gramene; AT1G02740.1; AT1G02740.1; AT1G02740.
DR KEGG; ath:AT1G02740; -.
DR Araport; AT1G02740; -.
DR TAIR; locus:2024725; AT1G02740.
DR eggNOG; KOG3001; Eukaryota.
DR HOGENOM; CLU_039566_1_0_1; -.
DR InParanoid; Q4V3E2; -.
DR OMA; SDCFYEA; -.
DR OrthoDB; 1624495at2759; -.
DR PhylomeDB; Q4V3E2; -.
DR PRO; PR:Q4V3E2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q4V3E2; baseline and differential.
DR Genevisible; Q4V3E2; AT.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990188; F:euchromatin binding; IDA:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA:TAIR.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IPI:TAIR.
DR GO; GO:0043621; F:protein self-association; 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:0043967; P:histone H4 acetylation; IMP:UniProtKB.
DR GO; GO:0048586; P:regulation of long-day photoperiodism, flowering; IGI:TAIR.
DR GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.274.30; -; 1.
DR InterPro; IPR014002; Agenet_dom_plant.
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; SM00743; Agenet; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS51640; MRG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..327
FT /note="Protein MRG2"
FT /id="PRO_0000432990"
FT DOMAIN 52..101
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 162..327
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 87
FT /note="Y->A: Loss of H3K4me3/H3K36me3 binding capacity and
FT loss of activity."
FT /evidence="ECO:0000269|PubMed:25211338"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4PLI"
FT STRAND 65..77
FT /evidence="ECO:0007829|PDB:4PLI"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:4PLI"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4PLI"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:4PLI"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4PLI"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4PLL"
SQ SEQUENCE 327 AA; 37629 MW; 951BE90E4D7B1912 CRC64;
MGSPNAAAET DLTTDDFIGD TRRDSGSDTE TNTDCDGEDL PLLLLPAPPG HFEEGERVLA
KHSDCFYEAK VLKVEFKDNE WKYFVHYIGW NKSWDEWIRL DCLLKHSDEN IEKQKEQGLK
QQGIKSAMAW KVSKMKPRSP NVARGRKRKQ DSVDTEKNVL PSDNLLSFNI PPALRKQLLD
DFEFVTQMQK LVQLPRSPNV DGILKKYIDS QMKKHGRVTD SLEEILKGLR CYFDKALPVM
LLYNNERKQY EESVSGGVSP STVYGAEHLL RLFVKLPELL VHVNMAEETL KELQDNFVDI
LRFLRKNQSV LFVSTYKAVE EMEKKEG
