PDP3_ARATH
ID PDP3_ARATH Reviewed; 1008 AA.
AC Q9FNE4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=PWWP domain-containing protein 3 {ECO:0000303|PubMed:29314758};
GN Name=PDP3 {ECO:0000303|PubMed:29314758};
GN OrderedLocusNames=At5g40340 {ECO:0000312|Araport:AT5G40340};
GN ORFNames=MPO12.6 {ECO:0000312|EMBL:BAB11589.1};
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH LHP1; 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, PDP2 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 LHP1, MSI4/FVE
CC and MSI5 (PubMed:29314758). Component of the PRC2 (polycomb repressive
CC complex 2) complex which regulates histone methylation on histone H3K27
CC (PubMed:29314758). {ECO:0000269|PubMed:25387881,
CC 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; AB006702; BAB11589.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94535.1; -; Genomic_DNA.
DR RefSeq; NP_198850.1; NM_123398.3.
DR AlphaFoldDB; Q9FNE4; -.
DR IntAct; Q9FNE4; 1.
DR STRING; 3702.AT5G40340.1; -.
DR PaxDb; Q9FNE4; -.
DR PRIDE; Q9FNE4; -.
DR ProteomicsDB; 177474; -.
DR EnsemblPlants; AT5G40340.1; AT5G40340.1; AT5G40340.
DR GeneID; 834032; -.
DR Gramene; AT5G40340.1; AT5G40340.1; AT5G40340.
DR Araport; AT5G40340; -.
DR TAIR; locus:2170563; AT5G40340.
DR eggNOG; ENOG502QQX0; Eukaryota.
DR HOGENOM; CLU_007246_0_0_1; -.
DR InParanoid; Q9FNE4; -.
DR OrthoDB; 1167092at2759; -.
DR PhylomeDB; Q9FNE4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNE4; baseline and differential.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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 Coiled coil; Flowering; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1008
FT /note="PWWP domain-containing protein 3"
FT /id="PRO_0000453271"
FT DOMAIN 127..188
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 84..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 78..122
FT /evidence="ECO:0000255"
FT COILED 804..824
FT /evidence="ECO:0000255"
FT MOTIF 786..793
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 809..816
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 841..848
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 87..124
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..492
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1008 AA; 114239 MW; 3645210B6225D09D CRC64;
MEIEVVLGIG EDAGPKPCSA EIESAEKTLK DDGVVQENGV RVSDNGEKKS DVVVDVDEKN
EKNLNESGVI EDCVMNGVSS LLKLKEDVEE EEEEEEEEEE EEEDGEDEEE EEEEEEEEEE
EEHGYCVGDF VWGKIKNHPW WPGQIYDPSD ASDLALKIKQ KGKLLVACFG DGTFAWCGAS
QLKPFAESFK ECSKVSNSRS FLGAVEEAVE EIGRHIERVL VCDCAEEKKH EFDSPLVNNA
GIKEGVLVRD VRREMISSLL IGKHGEILKD VKSFAETVSF SGLLELEILK RKVSAFYRSN
RGYGLTEYHE PQSVPGLEDK NNDDDDDDEE KNVNDGLQWR AKRSRVEEVA ALDHEESSSL
QRSLEKCSGF PDHRLPHRRK EKSITEIIEK ESAAKVRFET EPADGDVKSN VKSGRKKTKR
HDEVNGDLEN VTTTALWRRR KSEVATIEDG GNKQVVESSK GKTSRKKKKM DVDDGDDDGS
GDKEESEEKE ISDLEINIDS TSLASLRKKV RFDDSVVERS TENGETATQT SKRERKKSKY
LSPDFLSDFS RKGRKKSTIE SESSKVSSQS QVDERVTDAS DSLMEVEEDT LDKPCEPSSD
NGLGQEELSR ELSNAVDFLR LGATPKEMQD LIRVAALGTQ YPKDSSSRDM VREFMTIYRS
FTYHDGANHK FLGSYDSSDK EKEELSEMGK PVTKGKEKKD KKGKAKQKAE EIEVTGKEEN
ETDKHGKMKK ERKRKKSESK KEGGEGEETQ KEANESTKKE RKRKKSESKK QSDGEEETQK
EPSESTKKER KRKNPESKKK AEAVEEEETR KESVESTKKE RKRKKPKHDE EEVPNETEKP
EKKKKKKREG KSKKKETETE FSGAELYVTF GPGSSLPKKE DLIEIYEKFG ALDKERTDTV
DNNFSAHVAF LDVADGEKAF ESSLEKCPFT SNSTVKFRLK YPNERTEEKK TEAEVAETTM
EVEYLKKKLD EMKLLLDGCE GGMTEEVKVK LEGEMVNLLE KVIEMRSS
