DPF3_DANRE
ID DPF3_DANRE Reviewed; 391 AA.
AC A9LMC0; Q5RIJ2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Zinc finger protein DPF3;
GN Name=dpf3; ORFNames=si:ch211-268e23.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=18765789; DOI=10.1101/gad.471408;
RA Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C.,
RA Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H.,
RA Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.;
RT "Regulation of muscle development by DPF3, a novel histone acetylation and
RT methylation reader of the BAF chromatin remodeling complex.";
RL Genes Dev. 22:2370-2384(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Muscle-specific component of the BAF complex, a multiprotein
CC complex involved in transcriptional activation and repression of select
CC genes by chromatin remodeling (alteration of DNA-nucleosome topology).
CC Specifically binds acetylated lysines on histone 3 and 4. In the
CC complex, it acts as a tissue-specific anchor between histone
CC acetylations and methylations and chromatin remodeling. Belongs to the
CC neuron-specific chromatin remodeling complex (nBAF complex) and may
CC play a role in neural development (By similarity). Plays an essential
CC role in heart and skeletal muscle development. {ECO:0000250,
CC ECO:0000269|PubMed:18765789}.
CC -!- SUBUNIT: Component of the BAF complex. Interacts with acetylated
CC histones H3 and H4. Component of neuron-specific chromatin remodeling
CC complex (nBAF complex), a subfamily of ATP-dependent SWI/SNF chromatin
CC remodeling complexes (By similarity). {ECO:0000250|UniProtKB:P58269,
CC ECO:0000250|UniProtKB:Q92784}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92784}.
CC -!- TISSUE SPECIFICITY: Expressed in the heart and somites.
CC {ECO:0000269|PubMed:18765789}.
CC -!- DOMAIN: The PHD-type zinc fingers mediate the binding to acetylated
CC histones. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI11958.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU245032; ABX10892.1; -; mRNA.
DR EMBL; BX255881; CAI11958.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001104639.1; NM_001111169.1.
DR AlphaFoldDB; A9LMC0; -.
DR SMR; A9LMC0; -.
DR STRING; 7955.ENSDARP00000109205; -.
DR PaxDb; A9LMC0; -.
DR Ensembl; ENSDART00000034245; ENSDARP00000032706; ENSDARG00000025309.
DR GeneID; 562738; -.
DR KEGG; dre:562738; -.
DR CTD; 8110; -.
DR ZFIN; ZDB-GENE-041014-190; dpf3.
DR eggNOG; KOG1244; Eukaryota.
DR GeneTree; ENSGT00940000159153; -.
DR InParanoid; A9LMC0; -.
DR OrthoDB; 708781at2759; -.
DR PhylomeDB; A9LMC0; -.
DR TreeFam; TF318971; -.
DR PRO; PR:A9LMC0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000025309; Expressed in retina and 17 other tissues.
DR ExpressionAtlas; A9LMC0; baseline.
DR GO; GO:0071565; C:nBAF complex; IBA:GO_Central.
DR GO; GO:0016514; C:SWI/SNF complex; ISS:ZFIN.
DR GO; GO:0042393; F:histone binding; ISS:ZFIN.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:ZFIN.
DR GO; GO:0006338; P:chromatin remodeling; ISS:ZFIN.
DR GO; GO:0048644; P:muscle organ morphogenesis; IMP:ZFIN.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:ZFIN.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR025750; DPF1-3_N.
DR InterPro; IPR038047; DPF3.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10615:SF120; PTHR10615:SF120; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF14051; Requiem_N; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 2: Evidence at transcript level;
KW Activator; Chromatin regulator; Metal-binding; Neurogenesis; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..391
FT /note="Zinc finger protein DPF3"
FT /id="PRO_0000355186"
FT ZN_FING 198..235
FT /note="C2H2-type"
FT ZN_FING 273..333
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 330..380
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 152..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 44635 MW; DDFCA1C6238B1A1D CRC64;
MATVIQNPLK ALGDQFYREA IEHCRSYNAR LCAERSVRMP FLDSQTGVAQ NNCYIWMEKR
HRGPGMAAGQ MYTYPARCWR KKRRLHTPLD PQLRLCELRL EAELMAKREA PQTEATALEA
LLRGDGILDK RNNNAKEEET LLEIQRVLEA DENGDGFHDD EDFEVDTPKR KHRNKGRGRG
SGRRRTEAVA NDDQDKPYVC DNRYKQKHNS KTADSVCGKR YKNRPGLSYH YAHTHLAEEE
GEEERETEIP QSPPVHHENH KPQKAPDGSI IPNDYCDFCL GDSGSNRKTG QAEELVSCSD
CGRSGHPSCL QFTDNMMQAV RTYQWQCIEC KSCSLCGTSE NDDQLLFCDD CDRGYHMYCL
KPPMTQPPEG SWSCHLCQNL LKDKASGVED P
