MSI5_ARATH
ID MSI5_ARATH Reviewed; 487 AA.
AC Q9SU78; Q6NQ53;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=WD-40 repeat-containing protein MSI5 {ECO:0000305};
DE AltName: Full=Protein MULTICOPY SUPPRESSOR OF IRA1 5 {ECO:0000303|PubMed:23394836};
DE Short=AtMSI5 {ECO:0000303|PubMed:23394836};
GN Name=MSI5 {ECO:0000303|PubMed:23394836};
GN OrderedLocusNames=At4g29730 {ECO:0000312|Araport:AT4G29730};
GN ORFNames=T16L4.240 {ECO:0000312|EMBL:CAB45333.1};
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 [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 [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].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DWD MOTIF.
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
RN [6]
RP INTERACTION WITH AHL16.
RX PubMed=23394836; DOI=10.1016/j.cub.2013.01.030;
RA Xu Y., Wang Y., Stroud H., Gu X., Sun B., Gan E.S., Ng K.H., Jacobsen S.E.,
RA He Y., Ito T.;
RT "A matrix protein silences transposons and repeats through interaction with
RT retinoblastoma-associated proteins.";
RL Curr. Biol. 23:345-350(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH LHP1; PDP2; PDP3 AND PDP6,
RP AND SUBUNIT.
RX PubMed=29314758; DOI=10.1111/jipb.12630;
RA Zhou J.X., Liu Z.W., Li Y.Q., Li L., Wang B., Chen S., He X.J.;
RT "Arabidopsis PWWP domain proteins mediate H3K27 trimethylation on FLC and
RT regulate flowering time.";
RL J. Integr. Plant Biol. 60:362-368(2018).
CC -!- FUNCTION: Core histone-binding subunit that may target chromatin
CC assembly factors, chromatin remodeling factors and histone deacetylases
CC to their histone substrates in a manner that is regulated by
CC nucleosomal DNA (By similarity). Acts together with PDP1 and MSI4/FVE
CC to regulate the function of the PRC2 complex on FLC (PubMed:29314758).
CC {ECO:0000250|UniProtKB:O22607, ECO:0000269|PubMed:29314758}.
CC -!- SUBUNIT: Interacts with AHL16 (PubMed:23394836). Interacts with LHP1,
CC PDP2, PDP3 and PDP6 (PubMed:29314758). Component of the PRC2 (polycomb
CC repressive complex 2) complex which regulates histone methylation on
CC histone H3K27 (PubMed:29314758). {ECO:0000269|PubMed:23394836,
CC ECO:0000269|PubMed:29314758}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O22607,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- DOMAIN: The DWD box is required for interaction with DDB1A.
CC {ECO:0000250|UniProtKB:O22607}.
CC -!- DISRUPTION PHENOTYPE: Reduced H3K27me3 level but increased levels of
CC histone H3 acetylation and H3K4me3 on FLC in the fve msi5 double
CC mutant. {ECO:0000269|PubMed:29314758}.
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45333.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79731.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL079344; CAB45333.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161575; CAB79731.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85666.1; -; Genomic_DNA.
DR EMBL; BT010610; AAQ89632.1; -; mRNA.
DR EMBL; AK176425; BAD44188.1; -; mRNA.
DR PIR; T09936; T09936.
DR RefSeq; NP_194702.2; NM_119118.3.
DR AlphaFoldDB; Q9SU78; -.
DR SMR; Q9SU78; -.
DR BioGRID; 14381; 12.
DR STRING; 3702.AT4G29730.1; -.
DR PaxDb; Q9SU78; -.
DR PRIDE; Q9SU78; -.
DR ProteomicsDB; 250786; -.
DR EnsemblPlants; AT4G29730.1; AT4G29730.1; AT4G29730.
DR GeneID; 829094; -.
DR Gramene; AT4G29730.1; AT4G29730.1; AT4G29730.
DR KEGG; ath:AT4G29730; -.
DR Araport; AT4G29730; -.
DR TAIR; locus:2134408; AT4G29730.
DR eggNOG; KOG0264; Eukaryota.
DR HOGENOM; CLU_020445_2_0_1; -.
DR InParanoid; Q9SU78; -.
DR OMA; HQPRSTE; -.
DR OrthoDB; 831322at2759; -.
DR PhylomeDB; Q9SU78; -.
DR PRO; PR:Q9SU78; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SU78; baseline and differential.
DR Genevisible; Q9SU78; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; IMP:UniProtKB.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IMP:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
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; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; Nucleus; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; WD repeat.
FT CHAIN 1..487
FT /note="WD-40 repeat-containing protein MSI5"
FT /id="PRO_0000051084"
FT REPEAT 142..182
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 197..237
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 270..310
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 315..355
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 364..404
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 419..466
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..21
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 288..303
FT /note="DWD box"
FT /evidence="ECO:0000255"
FT COMPBIAS 236..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O22607"
SQ SEQUENCE 487 AA; 53995 MW; 87BAF58C946ABF6A CRC64;
MESEAAATVQ ATRPRRAPRT PVTAILTDKR RRKPKSNNES QLPFLLQQSQ KATVDDTYSQ
WKTLLPILYD SFVNHTLVWP SLSCRWGPQL EQAGSKTQRL YLSEQTNGSV PNTLVIANCE
TVNRQLNEKA HSPFVKKYKT IIHPGEVNRI RELPQNSKIV ATHTDSPDIL IWNTETQPDR
YAVLGAPDSR PDLLLIGHQD DAEFALAMCP TEPFVLSGGK DKSVILWNIQ DHITMAGSDS
KSPGSSFKQT GEGSDKTGGP SVGPRGIYNG HKDTVEDVAF CPSSAQEFCS VGDDSCLMLW
DARTGTSPAM KVEKAHDADL HCVDWNPHDN NLILTGSADN TVRVFDRRNL TSNGVGSPVY
KFEGHRAAVL CVQWSPDKSS VFGSSAEDGL LNIWDCDRVG KKSERATKTP DGLFFQHAGH
RDKVVDFHWS LLNPWTIVSV SDNCESIGGG GTLQIWRMSD LIYRPEDEVL TELEKFKSHV
FTCTSKS
