PDP1_ARATH
ID PDP1_ARATH Reviewed; 1072 AA.
AC F4K4D6; C0SVR2;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=PWWP domain-containing protein 1 {ECO:0000303|PubMed:29314758};
GN Name=PDP1 {ECO:0000303|PubMed:29314758};
GN OrderedLocusNames=At5g27650 {ECO:0000312|Araport:AT5G27650};
GN ORFNames=T1G16.4 {ECO:0000312|EMBL:AED93711.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 [MRNA] OF 10-1072.
RA Fujita M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MSI4/FVE, SUBUNIT, GENE
RP 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 PDP2, 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 MSI4/FVE (PubMed:29314758). Component of the
CC PRC2 (polycomb repressive complex 2) complex which regulates histone
CC methylation on histone H3K27 (By similarity).
CC {ECO:0000250|UniProtKB:Q9FNE4, 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; AC069556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93711.1; -; Genomic_DNA.
DR EMBL; AB493765; BAH30603.1; -; mRNA.
DR RefSeq; NP_198117.2; NM_122647.3.
DR AlphaFoldDB; F4K4D6; -.
DR STRING; 3702.AT5G27650.1; -.
DR iPTMnet; F4K4D6; -.
DR PaxDb; F4K4D6; -.
DR PRIDE; F4K4D6; -.
DR ProteomicsDB; 216517; -.
DR EnsemblPlants; AT5G27650.1; AT5G27650.1; AT5G27650.
DR GeneID; 832827; -.
DR Gramene; AT5G27650.1; AT5G27650.1; AT5G27650.
DR KEGG; ath:AT5G27650; -.
DR Araport; AT5G27650; -.
DR TAIR; locus:2143631; AT5G27650.
DR eggNOG; ENOG502QQX0; Eukaryota.
DR HOGENOM; CLU_006566_0_0_1; -.
DR InParanoid; F4K4D6; -.
DR OMA; YVFQKRA; -.
DR OrthoDB; 982164at2759; -.
DR PhylomeDB; F4K4D6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K4D6; 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..1072
FT /note="PWWP domain-containing protein 1"
FT /id="PRO_0000453269"
FT DOMAIN 173..234
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 21..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 402..409
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 596..603
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 705..712
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 733..740
FT /note="Nuclear localization signal 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 65..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..119
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 118096 MW; 242302BF28DEAEA1 CRC64;
MYKTKLIPVM NEDAVIVQQT DSIQDPKVTP DDTVVDSSGD VHEAIDDDVE ASSPMELDSA
VTNDARVLES ERSEKDGVVG SEEEDEIKSE DVLIDKDDES SEVKEEEEEE DGSDDQSSEL
GSEADEKELD LGLKEEKKGV SDYKSLLSEF DDYVASEKMG SGVSRALSYG FEVGDLVWGK
VKSHPWWPGH IFNEAFASPS VRRMRRIDHV LVAFFGDSSY GWFDPAELIP FEPNLEEKSQ
QTVSKHFVRA VEEAKDEASR RSALGLTCKC RNPYNFRPSN VEDYFAVDVP DYELQAVYSV
DQIKNSRDKF LPAETISFVK QLALAPQECD PDSLKFMKKK AVVFAFRKSV FEEFDETYAQ
AFGTKSPRSS VSTLEPHNRA PPRAPLSGPL VIAETLGDLK SSKKPTKVKV SKKKDKYLLK
RRDEAGDKSV QFGEIEASSE ASHIQGIDGS LDGDFGLQRR APTLQTPMKD EKSGIVSMDF
ASSNTAIPGK EFSASKPSLD EEKGLAEKSK ERMEERAAVL PEHGKSEAMA SLKPKEEAGT
DLGSAGSSLQ PLLESHTSAS EGKSSTGSVI KKVKVAKRSS SEMSSENPPS EPKKKKKKKK
EPDSDHPVKR KNLYSGEAGA KKLSQLGSAH LQTYMEADVP QLLSHLQDLS LDPFHGLSVA
SFGTARKFFL RFRSLNYQKS LSVSSSDATV ENARDTKPSK PVKTVKRTED PSKAGKKRLS
SDRQDEIPSA KKLKKTNQLK SMASEKKIIR EAKDSIKPIR EPSRVVQAKP ARGQTGKKTA
PSVKVVEPTM LVMKFPPGTS LPSAALLKAR FGRFGLLDQS AIRVFWKSST CRVVFLYKAD
AQTAFRYATG NNTLFGNVNV KYFLRDVDAP KAEPREPENT KEDDEPQSQW LDQAPPLHQP
TLPPPNVNLK SCLKKPVDDP SSSSNNGNGN RAAVRVKFML GGEENSSKAN TEPPQVTMTL
NRNSGPSSSS SSVPMEFVSK KFQNVVHHQQ LPPSTLPPIL PLPPQYTKPQ QLPIKPVDHV
EPPMPPSRNF RGPIPAVSAG DISHQMLNLL SKCNEVVANV TGLLGYVPYH PL
