TFDP1_BOVIN
ID TFDP1_BOVIN Reviewed; 410 AA.
AC Q17QZ4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Transcription factor Dp-1;
GN Name=TFDP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Can stimulate E2F-dependent transcription. Binds DNA
CC cooperatively with E2F family members through the E2 recognition site,
CC 5'-TTTC[CG]CGC-3', found in the promoter region of a number of genes
CC whose products are involved in cell cycle regulation or in DNA
CC replication. The E2F1:DP complex appears to mediate both cell
CC proliferation and apoptosis. Blocks adipocyte differentiation by
CC repressing CEBPA binding to its target gene promoters (By similarity).
CC {ECO:0000250|UniProtKB:Q14186}.
CC -!- SUBUNIT: Component of the E2F:DP transcription factor complex. Forms
CC heterodimers with E2F family members. The complex can interact with
CC hypophosphorylated retinoblastoma protein RB1 and related proteins
CC (RBL1 and RBL2) that inhibit the E2F transactivation domain. This
CC repression involves recruitment of histone deacetylase (HDAC). During
CC the cell cycle, from mid-to-late G1 phase, RB family members become
CC phosphorylated, detach from the DRTF1/E2F complex to render E2F
CC transcriptionally active. Part of the E2F6.com-1 complex in G0 phase is
CC composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2,
CC MBLR, L3MBTL2 YAF2. Component of the DREAM complex (also named LINC
CC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54,
CC MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in
CC quiescent cells where it represses cell cycle-dependent genes. It
CC dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a
CC subcomplex that binds to MYBL2. The complex TFDP1:E2F1 interacts with
CC CEBPA; the interaction prevents CEBPA binding to target gene promoters
CC and represses its transcriptional activity (By similarity).
CC {ECO:0000250|UniProtKB:Q14186}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q08639}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q08639}. Note=Shuttles between the cytoplasm and
CC nucleus and translocates into the nuclear compartment upon
CC heterodimerization with E2F1. {ECO:0000250|UniProtKB:Q08639}.
CC -!- PTM: Ubiquitinated by the BCR(KBTBD5) complex, leading to its
CC subsequent degradation. {ECO:0000250|UniProtKB:Q08639}.
CC -!- PTM: Phosphorylation by E2F1-bound cyclin A-CDK2, in the S phase,
CC inhibits E2F-mediated DNA binding and transactivation.
CC {ECO:0000250|UniProtKB:Q14186}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR EMBL; BC118103; AAI18104.1; -; mRNA.
DR RefSeq; NP_001069497.1; NM_001076029.1.
DR AlphaFoldDB; Q17QZ4; -.
DR SMR; Q17QZ4; -.
DR STRING; 9913.ENSBTAP00000026175; -.
DR PaxDb; Q17QZ4; -.
DR PRIDE; Q17QZ4; -.
DR Ensembl; ENSBTAT00000026175; ENSBTAP00000026175; ENSBTAG00000019645.
DR Ensembl; ENSBTAT00000073887; ENSBTAP00000067273; ENSBTAG00000019645.
DR Ensembl; ENSBTAT00000084839; ENSBTAP00000070624; ENSBTAG00000019645.
DR GeneID; 534579; -.
DR KEGG; bta:534579; -.
DR CTD; 7027; -.
DR VEuPathDB; HostDB:ENSBTAG00000019645; -.
DR VGNC; VGNC:107256; TFDP1.
DR eggNOG; KOG2829; Eukaryota.
DR GeneTree; ENSGT00940000154652; -.
DR HOGENOM; CLU_039874_3_1_1; -.
DR InParanoid; Q17QZ4; -.
DR OMA; FSTTDNH; -.
DR OrthoDB; 1046304at2759; -.
DR TreeFam; TF314396; -.
DR Reactome; R-BTA-1538133; G0 and Early G1.
DR Reactome; R-BTA-69231; Cyclin D associated events in G1.
DR Reactome; R-BTA-8953750; Transcriptional Regulation by E2F6.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000019645; Expressed in retina and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035189; C:Rb-E2F complex; IEA:Ensembl.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0043276; P:anoikis; IEA:Ensembl.
DR GO; GO:0008544; P:epidermis development; IEA:Ensembl.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0070345; P:negative regulation of fat cell proliferation; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd14458; DP_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.20.140.80; -; 1.
DR InterPro; IPR028313; DP-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 PANTHER; PTHR12548:SF4; PTHR12548:SF4; 1.
DR Pfam; PF08781; DP; 1.
DR Pfam; PF02319; E2F_TDP; 1.
DR PIRSF; PIRSF009404; Transcription_factor_DP; 1.
DR SMART; SM01138; DP; 1.
DR SMART; SM01372; E2F_TDP; 1.
DR SUPFAM; SSF144074; SSF144074; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Cell cycle; Cytoplasm; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..410
FT /note="Transcription factor Dp-1"
FT /id="PRO_0000305939"
FT DNA_BIND 113..195
FT /evidence="ECO:0000255"
FT REGION 77..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..127
FT /note="Interaction with CEBPA"
FT /evidence="ECO:0000250|UniProtKB:Q14186"
FT REGION 204..277
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 211..327
FT /note="Enhances binding of RB protein to E2F"
FT REGION 214..246
FT /note="DCB1"
FT REGION 259..315
FT /note="DCB2"
FT REGION 370..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 161..195
FT /note="DEF box"
FT COMPBIAS 78..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..410
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14186"
FT MOD_RES 23
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:Q14186, ECO:0000255"
SQ SEQUENCE 410 AA; 44926 MW; A8D2A37139EB7997 CRC64;
MAKDAGLIEA NGELKVFIDQ NLSPGKGVVS LVAVHPSTVN SLGKQLLPKT FGQSNVNITQ
QVVIGTPQRP AAPNTIVVGS PHTPNTHFVS QNQPSDPSPW SAGKRNRKGE KNGKGLRHFS
MKVCEKVQRK GTTSYNEVAD ELVAEFSAAD SHILPSESAY DQKNIRRRVY DALNVLMAMN
IISKEKKEIK WIGLPTNSAQ ECQSLEVERQ RRLERIKQKQ SQLQELILQQ IAFKNLVQRN
RQVEQQASRP PPPNSVIHLP FIIVNTSKKT VIDCSISNDK FEYLFNFDNT FEIHDDIEVL
KRMGMACGLE SGSCSPEDLR VARSLVPKAL EPYVTEMAQG SLGGVFVASA VSTSNGTRLS
ASDLANGADG ALATSSSGSQ YSGSRVETPV SCVGEDDEDD EDFNENEEED
