PDP2_ARATH
ID PDP2_ARATH Reviewed; 726 AA.
AC Q9SF36; Q0WMU6;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=PWWP domain-containing protein 2 {ECO:0000303|PubMed:29314758};
GN Name=PDP2 {ECO:0000303|PubMed:29314758};
GN OrderedLocusNames=At3g09670 {ECO:0000312|Araport:AT3G09670};
GN ORFNames=F11F8.26 {ECO:0000312|EMBL:AAF23297.1};
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=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 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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [5]
RP INTERACTION WITH DEK3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=25387881; DOI=10.1105/tpc.114.129254;
RA Waidmann S., Kusenda B., Mayerhofer J., Mechtler K., Jonak C.;
RT "A DEK domain-containing protein modulates chromatin structure and function
RT in Arabidopsis.";
RL Plant Cell 26:4328-4344(2014).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MSI4/FVE AND MSI5,
RP SUBUNIT, GENE FAMILY, AND NOMENCLATURE.
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: Together with PDP1, PDP3 and PDP6, interacts with MSI4/FVE
CC and MSI5 to suppress FLC, MAF4 and MAF5 expression by regulating the
CC function of the PRC2 complex and modulating H3K27me3 level, thereby
CC promoting flowering. {ECO:0000269|PubMed:29314758}.
CC -!- SUBUNIT: Interacts with DEK3 (PubMed:25387881). Binds to MSI4/FVE and
CC MSI5 (PubMed:29314758). Component of the PRC2 (polycomb repressive
CC complex 2) complex which regulates histone methylation on histone H3K27
CC (By similarity). {ECO:0000250|UniProtKB:Q9FNE4,
CC ECO:0000269|PubMed:25387881, ECO:0000269|PubMed:29314758}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- DISRUPTION PHENOTYPE: Delayed flowering associated with reduced
CC H3K27me3 level on FLC (PubMed:29314758). The triple mutant pdp1 pdp2
CC pdp3 has increased levels of FLC, MAF4 and MAF5 expression, but
CC decreased expression of FT (PubMed:29314758).
CC {ECO:0000269|PubMed:29314758}.
CC -!- SIMILARITY: Belongs to the PDP family. {ECO:0000305}.
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DR EMBL; AC016661; AAF23297.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74795.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74796.1; -; Genomic_DNA.
DR EMBL; AK229716; BAF01554.1; -; mRNA.
DR RefSeq; NP_001078128.1; NM_001084659.1.
DR RefSeq; NP_187578.1; NM_111801.5.
DR AlphaFoldDB; Q9SF36; -.
DR SMR; Q9SF36; -.
DR IntAct; Q9SF36; 1.
DR STRING; 3702.AT3G09670.2; -.
DR PaxDb; Q9SF36; -.
DR PRIDE; Q9SF36; -.
DR ProteomicsDB; 189808; -.
DR EnsemblPlants; AT3G09670.1; AT3G09670.1; AT3G09670.
DR EnsemblPlants; AT3G09670.2; AT3G09670.2; AT3G09670.
DR GeneID; 820124; -.
DR Gramene; AT3G09670.1; AT3G09670.1; AT3G09670.
DR Gramene; AT3G09670.2; AT3G09670.2; AT3G09670.
DR KEGG; ath:AT3G09670; -.
DR Araport; AT3G09670; -.
DR TAIR; locus:2074944; AT3G09670.
DR eggNOG; ENOG502QTFR; Eukaryota.
DR HOGENOM; CLU_023067_0_0_1; -.
DR InParanoid; Q9SF36; -.
DR OMA; VNCKEAN; -.
DR OrthoDB; 192789at2759; -.
DR PhylomeDB; Q9SF36; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SF36; baseline and differential.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IMP:UniProtKB.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR InterPro; IPR000313; PWWP_dom.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 1: Evidence at protein level;
KW Flowering; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..726
FT /note="PWWP domain-containing protein 2"
FT /id="PRO_0000453270"
FT DOMAIN 199..260
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 460..467
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 495..502
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 392..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 309
FT /note="N -> Y (in Ref. 3; BAF01554)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 726 AA; 79272 MW; 2D7CE175454037E7 CRC64;
MSTESERIES VSEANASSLE VGNDQMSEAL AGQAQELKTI GDDKEGCGNF ASAGDNGMEK
VNGFTNLVKE TESVNGELDL GTRTENVGGE SNQSDKKVLV DSEEVMMVEK RGLLVEKEVE
PDMVCSHGAD LSDVKVSDGR LDSEDLVQDR KPDGLEKQGT KVEDLDVVCF MGLEPHESKD
ESILDDEIAH VAAKVKISDS DLVWAKVRSH PWWPGQVFDA SAATDKAKKH FKKGSFLVTY
FGDCTFAWNE ASRIKPFRQH FSQMAKQSSL PDFIDAIDFA LEEVSRRIEF GLACSCISEE
VYQKIKTQNV INPGIREDSS SIHGGDKVSS AVFFEPANLV GYVKRLACSP SYDATDALQL
VSQRAQLLAF NRWKGYTDLP EFMTLQGSVE SAPKISPAEE QSSLVEVSDP EPTKSKQVYT
KRRKTNLQTE QSSLVEVSDP DKGDCKHDGV FEYEETIVPK KKEKTLAEFI AEKRVSRHNG
NTSHEKSGNV PHCEKKRKVV QSKVPKSTKK IKANLQTEDP GSPVSPKNDR KNNLSAGDKI
TPQKARKSFG IGASILKVAN QMHCSTPTRL LPCSDSTSKK AAKSNGSGKS LQEKPKAEAL
SAREISPSTT LSSPHAASVT KTTSGKSNSV SLDHNLSGEL DQVRKEAPST NLVEDPMLES
RDLKDSSKEQ VVHEDKKEAA NVADEKSIMD SNLTGEKISG LDLREQPSNK NCSGGSDSCK
EDVSAE
