WDR5A_ARATH
ID WDR5A_ARATH Reviewed; 317 AA.
AC Q9M2Z2;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=COMPASS-like H3K4 histone methylase component WDR5A {ECO:0000303|PubMed:19567704};
DE Short=AtWDR5A {ECO:0000303|PubMed:19567704};
GN Name=WDR5A {ECO:0000303|PubMed:19567704};
GN OrderedLocusNames=At3g49660 {ECO:0000312|Araport:AT3G49660};
GN ORFNames=T16K5.10 {ECO:0000312|EMBL:CAB66904.1};
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|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP HISTONE H3 AND ATX1.
RX PubMed=19567704; DOI=10.1105/tpc.109.067967;
RA Jiang D., Gu X., He Y.;
RT "Establishment of the winter-annual growth habit via FRIGIDA-mediated
RT histone methylation at FLOWERING LOCUS C in Arabidopsis.";
RL Plant Cell 21:1733-1746(2009).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH RBL; SDG14 AND SDG16, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21423667; DOI=10.1371/journal.pgen.1001330;
RA Jiang D., Kong N.C., Gu X., Li Z., He Y.;
RT "Arabidopsis COMPASS-like complexes mediate histone H3 lysine-4
RT trimethylation to control floral transition and plant development.";
RL PLoS Genet. 7:E1001330-E1001330(2011).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH ATX1.
RC STRAIN=cv. Wassilewskija;
RX PubMed=23284292; DOI=10.1371/journal.pgen.1003111;
RA Ding Y., Ndamukong I., Xu Z., Lapko H., Fromm M., Avramova Z.;
RT "ATX1-generated H3K4me3 is required for efficient elongation of
RT transcription, not initiation, at ATX1-regulated genes.";
RL PLoS Genet. 8:E1003111-E1003111(2012).
CC -!- FUNCTION: Forms multiple COMPASS-like complexes involved in histone
CC methylation by interacting with different histone H3 'Lys-4'
CC methyltransferases such as ATX1, SDG14 or SDG16 (PubMed:21423667).
CC Binds to target loci chromatin, increasing H3K4 trimethylation and
CC causing activation of the gene (PubMed:19567704). Up-regulates FLC and
CC MAF4 expression to delay flowering (PubMed:19567704). Present at the
CC promoters and at the transcription start sites (TSS) regions of WRKY70
CC and LTP7; this occupancy is ATX1-dependent (PubMed:23284292). Involved
CC in the transition from transcription initiation to transcription
CC elongation (PubMed:23284292). {ECO:0000269|PubMed:19567704,
CC ECO:0000269|PubMed:21423667, ECO:0000269|PubMed:23284292}.
CC -!- SUBUNIT: Part of a complex composed of TRO, RBL and WDR5A
CC (PubMed:21423667). This complex is formed during both vegetative and
CC reproductive development (PubMed:21423667). Interacts with SDG14,
CC SDG16, RBL, but not with TRO (PubMed:21423667). Interacts with ATX1 and
CC K4-methylated H3 tails (PubMed:19567704). {ECO:0000269|PubMed:19567704,
CC ECO:0000269|PubMed:21423667, ECO:0000269|PubMed:23284292}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19567704,
CC ECO:0000269|PubMed:21423667}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in developing embryos and
CC endosperms (PubMed:21423667). Expressed in shoot and root apical
CC regions, and in vasculature (PubMed:19567704).
CC {ECO:0000269|PubMed:19567704, ECO:0000269|PubMed:21423667}.
CC -!- DISRUPTION PHENOTYPE: Eearly flowering (PubMed:23284292). Decreased
CC TATA-binding protein (TBP) levels lower Ser5P Pol II levels near the
CC transcription start sites (TSSs) of target genes and of Pol II at the
CC genes 3'-ends thus affecting the transition from transcription
CC initiation to transcription elongation (PubMed:23284292). Significantly
CC reduced trimethylated 'Lys-4' of histone H3 (H3K4me3) levels at the 5'-
CC ends of WRKY70 and LTP7 genes leading to reduced transcript
CC accumulation (PubMed:23284292). {ECO:0000269|PubMed:23284292}.
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DR EMBL; AL132965; CAB66904.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78573.1; -; Genomic_DNA.
DR PIR; T46032; T46032.
DR RefSeq; NP_190535.1; NM_114826.4.
DR AlphaFoldDB; Q9M2Z2; -.
DR SMR; Q9M2Z2; -.
DR STRING; 3702.AT3G49660.1; -.
DR PaxDb; Q9M2Z2; -.
DR PRIDE; Q9M2Z2; -.
DR ProteomicsDB; 242573; -.
DR EnsemblPlants; AT3G49660.1; AT3G49660.1; AT3G49660.
DR GeneID; 824128; -.
DR Gramene; AT3G49660.1; AT3G49660.1; AT3G49660.
DR KEGG; ath:AT3G49660; -.
DR Araport; AT3G49660; -.
DR TAIR; locus:2097435; AT3G49660.
DR eggNOG; KOG0266; Eukaryota.
DR HOGENOM; CLU_000288_57_1_1; -.
DR InParanoid; Q9M2Z2; -.
DR OMA; RLWNYHT; -.
DR OrthoDB; 957291at2759; -.
DR PhylomeDB; Q9M2Z2; -.
DR PRO; PR:Q9M2Z2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2Z2; baseline and differential.
DR Genevisible; Q9M2Z2; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IPI:TAIR.
DR GO; GO:0042393; F:histone binding; IDA:TAIR.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IMP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Nucleus; Reference proteome; Repeat; Transferase;
KW WD repeat.
FT CHAIN 1..317
FT /note="COMPASS-like H3K4 histone methylase component WDR5A"
FT /id="PRO_0000431782"
FT REPEAT 22..61
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 69..108
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 111..152
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 153..192
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 196..235
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 238..280
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 283..317
FT /note="WD 7"
FT /evidence="ECO:0000255"
SQ SEQUENCE 317 AA; 34820 MW; 70BED05EF6DB7DB0 CRC64;
MAEEIPATAS FTPYVHSQTL TSHNRAVSSV KFSSDGRLLA SASADKTIRT YTINTINDPI
AEPVQEFTGH ENGISDVAFS SDARFIVSAS DDKTLKLWDV ETGSLIKTLI GHTNYAFCVN
FNPQSNMIVS GSFDETVRIW DVTTGKCLKV LPAHSDPVTA VDFNRDGSLI VSSSYDGLCR
IWDSGTGHCV KTLIDDENPP VSFVRFSPNG KFILVGTLDN TLRLWNISSA KFLKTYTGHV
NAQYCISSAF SVTNGKRIVS GSEDNCVHMW ELNSKKLLQK LEGHTETVMN VACHPTENLI
ASGSLDKTVR IWTQKKE
