TFDP1_CAEEL
ID TFDP1_CAEEL Reviewed; 598 AA.
AC Q22703;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Transcription factor dpl-1;
GN Name=dpl-1 {ECO:0000303|PubMed:11463372, ECO:0000312|WormBase:T23G7.1};
GN ORFNames=T23G7.1 {ECO:0000312|WormBase:T23G7.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EFL-1 AND LIN-35,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11463372; DOI=10.1016/s1097-2765(01)00194-0;
RA Ceol C.J., Horvitz H.R.;
RT "dpl-1 DP and efl-1 E2F act with lin-35 Rb to antagonize Ras signaling in
RT C.elegans vulval development.";
RL Mol. Cell 7:461-473(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12062054; DOI=10.1016/s0960-9822(02)00844-8;
RA Boxem M., van den Heuvel S.;
RT "C. elegans class B synthetic multivulva genes act in G(1) regulation.";
RL Curr. Biol. 12:906-911(2002).
RN [4]
RP FUNCTION, AND IDENTIFICATION IN THE DRM COMPLEX.
RX PubMed=17075059; DOI=10.1073/pnas.0608461103;
RA Harrison M.M., Ceol C.J., Lu X., Horvitz H.R.;
RT "Some C. elegans class B synthetic multivulva proteins encode a conserved
RT LIN-35 Rb-containing complex distinct from a NuRD-like complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16782-16787(2006).
RN [5]
RP FUNCTION.
RX PubMed=17466069; DOI=10.1186/1471-213x-7-38;
RA Ouellet J., Roy R.;
RT "The lin-35/Rb and RNAi pathways cooperate to regulate a key cell cycle
RT transition in C. elegans.";
RL BMC Dev. Biol. 7:38-38(2007).
RN [6]
RP FUNCTION.
RX PubMed=17881492; DOI=10.1242/dev.004606;
RA Schertel C., Conradt B.;
RT "C. elegans orthologs of components of the RB tumor suppressor complex have
RT distinct pro-apoptotic functions.";
RL Development 134:3691-3701(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17237514; DOI=10.1534/genetics.106.068148;
RA Reddien P.W., Andersen E.C., Huang M.C., Horvitz H.R.;
RT "DPL-1 DP, LIN-35 Rb and EFL-1 E2F act with the MCD-1 zinc-finger protein
RT to promote programmed cell death in Caenorhabditis elegans.";
RL Genetics 175:1719-1733(2007).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=23347407; DOI=10.1186/gb-2013-14-1-r5;
RA Kudron M., Niu W., Lu Z., Wang G., Gerstein M., Snyder M., Reinke V.;
RT "Tissue-specific direct targets of Caenorhabditis elegans Rb/E2F dictate
RT distinct somatic and germline programs.";
RL Genome Biol. 14:R5.1-R5.17(2013).
RN [9]
RP FUNCTION.
RX PubMed=24752899; DOI=10.1128/mcb.01532-13;
RA Lascarez-Lagunas L.I., Silva-Garcia C.G., Dinkova T.D., Navarro R.E.;
RT "LIN-35/Rb causes starvation-induced germ cell apoptosis via CED-9/Bcl2
RT downregulation in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 34:2499-2516(2014).
CC -!- FUNCTION: Synthetic multivulva class B (synMuvB) protein
CC (PubMed:11463372, PubMed:17075059). SynMuvB proteins are required to
CC repress the induction of vulval development by Ras signaling and
CC probably act by forming the multiprotein DRM complex that represses
CC transcription (PubMed:11463372, PubMed:17075059). May also negatively
CC regulate vulval development in association with other SynMuv class B
CC proteins such as lin-15A (PubMed:11463372). Can stimulate E2F-dependent
CC transcription (PubMed:17075059). Plays a role in negatively regulating
CC the progression through the G1 phase of the cell cycle during
CC postembryonic development, most likely by acting as a transcriptional
CC repressor in association with the cell cycle regulatory factor efl-1
CC and the transcriptional repressor lin-35, but may also act as a
CC positive regulator of cell cycle entry (PubMed:12062054). Involved in
CC the regulation of intestinal cell division during postembryonic
CC development, most likely in complex with efl-1 and lin-35
CC (PubMed:17466069). Promotes germ cell programmed cell death, probably
CC together with efl-1, by positively regulating the expression of the
CC apoptosis proteins ced-3 and ced-4 (PubMed:17881492, PubMed:24752899).
CC In particular, positively regulates the expression of ced-4 in response
CC to starvation (PubMed:24752899). Its role in programmed cell death may
CC be in conjunction with cell cycle regulatory factor efl-1 and the
CC synthetic multivulva class B proteins lin-35, lin-37 and lin-52, and is
CC independent of the ced-1, ced-8 and ced-9 pathways (PubMed:17237514).
CC {ECO:0000269|PubMed:11463372, ECO:0000269|PubMed:12062054,
CC ECO:0000269|PubMed:17075059, ECO:0000269|PubMed:17237514,
CC ECO:0000269|PubMed:17466069, ECO:0000269|PubMed:17881492,
CC ECO:0000269|PubMed:24752899}.
CC -!- SUBUNIT: Component of the DRM complex, at least composed of lin-9, lin-
CC 35, lin-37, lin-52, lin-53, lin-54- dpl-1 and efl-1 (PubMed:17075059).
CC Interacts (via N-terminus) with efl-1 (PubMed:11463372). Interacts (via
CC C-terminus) with lin-35 (via C-terminus) (PubMed:11463372).
CC {ECO:0000269|PubMed:11463372, ECO:0000269|PubMed:17075059}.
CC -!- INTERACTION:
CC Q22703; G5EF11: efl-1; NbExp=2; IntAct=EBI-324825, EBI-331564;
CC Q22703; G5EDT1: lin-35; NbExp=2; IntAct=EBI-324825, EBI-321470;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11463372,
CC ECO:0000269|PubMed:23347407}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development. Highly expressed
CC in somatic nuclei, as well as in immature germ cell and oocyte nuclei.
CC {ECO:0000269|PubMed:11463372}.
CC -!- DISRUPTION PHENOTYPE: Uncoordinated movements, also known as an Unc
CC phenotype, most likely due to defective cell cycle progression defects
CC in the Pn.a neuroblast lineage (PubMed:11463372). No obvious vulval
CC development defects (PubMed:11463372). Programmed cell death defect in
CC a ced-3 n2427 mutant background (PubMed:17237514). Double knockout with
CC the n433 mutant of the synthetic multivulva class A protein lin-15A
CC results in a multiple vulva (Muv) phenotype (PubMed:11463372). RNAi-
CC mediated knockdown results in reduced postembryonic intestinal cell
CC divisions (PubMed:12062054). {ECO:0000269|PubMed:11463372,
CC ECO:0000269|PubMed:12062054, ECO:0000269|PubMed:17237514}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR EMBL; AY028165; AAK19021.1; -; mRNA.
DR EMBL; Z68319; CAA92699.1; -; Genomic_DNA.
DR PIR; T25207; T25207.
DR RefSeq; NP_495957.1; NM_063556.5.
DR AlphaFoldDB; Q22703; -.
DR SMR; Q22703; -.
DR BioGRID; 39783; 14.
DR ComplexPortal; CPX-1100; DRM complex.
DR ComplexPortal; CPX-1138; RB1-E2F1-TFDP1 transcription repressor complex.
DR ComplexPortal; CPX-1145; E2F2-DP1 transcription factor complex.
DR ComplexPortal; CPX-1146; RB1-E2F2-TFDP1 transcription repressor complex.
DR ComplexPortal; CPX-965; E2F1-DP1 Transcription factor complex.
DR DIP; DIP-26129N; -.
DR IntAct; Q22703; 10.
DR MINT; Q22703; -.
DR STRING; 6239.T23G7.1; -.
DR iPTMnet; Q22703; -.
DR EPD; Q22703; -.
DR PaxDb; Q22703; -.
DR PeptideAtlas; Q22703; -.
DR EnsemblMetazoa; T23G7.1.1; T23G7.1.1; WBGene00001061.
DR EnsemblMetazoa; T23G7.1.2; T23G7.1.2; WBGene00001061.
DR GeneID; 174458; -.
DR KEGG; cel:CELE_T23G7.1; -.
DR UCSC; T23G7.1; c. elegans.
DR CTD; 174458; -.
DR WormBase; T23G7.1; CE21197; WBGene00001061; dpl-1.
DR eggNOG; KOG2829; Eukaryota.
DR GeneTree; ENSGT00940000169233; -.
DR HOGENOM; CLU_464018_0_0_1; -.
DR InParanoid; Q22703; -.
DR OMA; DIRWIGL; -.
DR OrthoDB; 1074923at2759; -.
DR Reactome; R-CEL-1538133; G0 and Early G1.
DR Reactome; R-CEL-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR SignaLink; Q22703; -.
DR PRO; PR:Q22703; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001061; Expressed in embryo and 5 other tissues.
DR GO; GO:0070176; C:DRM complex; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0035189; C:Rb-E2F complex; IDA:ComplexPortal.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0008406; P:gonad development; IGI:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:ComplexPortal.
DR GO; GO:1903507; P:negative regulation of nucleic acid-templated transcription; IC:ComplexPortal.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:WormBase.
DR GO; GO:0040027; P:negative regulation of vulval development; IDA:ComplexPortal.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; IMP:WormBase.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051302; P:regulation of cell division; IGI:UniProtKB.
DR GO; GO:0042659; P:regulation of cell fate specification; IMP:WormBase.
DR GO; GO:0046599; P:regulation of centriole replication; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:ComplexPortal.
DR CDD; cd14458; DP_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.20.140.80; -; 1.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR InterPro; IPR038168; TF_DP_C_sf.
DR InterPro; IPR014889; Transc_factor_DP_C.
DR InterPro; IPR015648; Transcrpt_fac_DP.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12548; PTHR12548; 1.
DR Pfam; PF08781; DP; 1.
DR Pfam; PF02319; E2F_TDP; 1.
DR SMART; SM01138; DP; 1.
DR SMART; SM01372; E2F_TDP; 1.
DR SUPFAM; SSF144074; SSF144074; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..598
FT /note="Transcription factor dpl-1"
FT /id="PRO_0000219480"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 67930 MW; A79692087FF3D2AE CRC64;
MNPTNYDPRI GQPAQSRPQV SLSMGRRIVQ MPTGLPRSYQ DESHNEPVGW DEPSGVGGSS
GAGGQQSDKP TGLRHFSTKV CEKVKEKGLT NYNEVADELV ADYFQNNLIK QIDVVKQEYD
MKNIRRRVYD ALNVLLAMNI ITKSKKDIRW IGLPASASQE ISRLEEEKSR REASISSKKQ
ALEEMVLQIV SYKNLVERNR KNEHKNGRPE NDTVLHLPFL IINTDKEANV ECSVSSDKSE
FLFSFDKKFE IHDDFEILKK LNLACSLETT NPTAEEVKTA KSFLPTLHQH YVDEIIANRK
KVEAEKEEKR KQQQLIADQM SMNLSQAQYV EPTSSLAQMS YSSRFNRQLQ EHLINDGSED
RSAAAGIMER DYDMDKNVNQ GSASRGPMYN TYSPQKIRAQ VNTPLQVPPV TKRYYVQKTQ
GPMKHDMTPV VRTVNRPYST VPPDRRLSTG ATSVNSGPVK YYVPQGHQPM HQPVGQRYRV
RPQQPQMSHM GQPHQVQQRV VYPAGSISGH QLQPGQRIVT QRIVAPGGPH PPGTIVRKVI
RKIVVNNPKQ SPAQQVIQKK MMEQDMCTFE RKTEQPMTSA QAAALIQHPQ PEEYDYFQ
