DPF3_CHICK
ID DPF3_CHICK Reviewed; 427 AA.
AC P58270;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Zinc finger protein DPF3;
DE AltName: Full=Zinc finger protein cer-d4;
GN Name=DPF3; Synonyms=CERD4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=11845289; DOI=10.1007/s00335-001-3039-1;
RA Ninkina N.N., Mertsalov I.B., Kulikova D.A., Alimova-Kost M.V.,
RA Simonova O.B., Korochkin L.I., Kiselev S.L., Buchman V.L.;
RT "Cerd4, third member of the d4 gene family: expression and organization of
RT genomic locus.";
RL Mamm. Genome 12:862-866(2001).
RN [2]
RP FUNCTION.
RX PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H.,
RA Aebersold R., Graef I.A., Crabtree G.R.;
RT "An essential switch in subunit composition of a chromatin remodeling
RT complex during neural development.";
RL Neuron 55:201-215(2007).
RN [3]
RP TISSUE SPECIFICITY.
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).
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. It thereby
CC probably plays an essential role in heart and skeletal muscle
CC development. Belongs to the neuron-specific chromatin remodeling
CC complex (nBAF complex) and plays a role in neural development.
CC {ECO:0000269|PubMed:17640523}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P58270-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P58270-2; Sequence=VSP_005614, VSP_005615;
CC Name=3;
CC IsoId=P58270-3; Sequence=VSP_005614, VSP_005616;
CC Name=4;
CC IsoId=P58270-4; Sequence=VSP_005614, VSP_005615, VSP_005616;
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 -!- SIMILARITY: Belongs to the requiem/DPF family. {ECO:0000305}.
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DR EMBL; AF362754; AAK51968.1; -; mRNA.
DR EMBL; AF362753; AAK51967.1; -; mRNA.
DR EMBL; AF362756; AAK51970.1; -; mRNA.
DR EMBL; AF362755; AAK51969.1; -; mRNA.
DR RefSeq; NP_989970.1; NM_204639.2. [P58270-1]
DR RefSeq; XP_015142411.1; XM_015286925.1. [P58270-2]
DR AlphaFoldDB; P58270; -.
DR SMR; P58270; -.
DR STRING; 9031.ENSGALP00000015213; -.
DR PaxDb; P58270; -.
DR GeneID; 395351; -.
DR KEGG; gga:395351; -.
DR CTD; 8110; -.
DR VEuPathDB; HostDB:geneid_395351; -.
DR eggNOG; KOG1244; Eukaryota.
DR InParanoid; P58270; -.
DR OrthoDB; 708781at2759; -.
DR PhylomeDB; P58270; -.
DR PRO; PR:P58270; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0071565; C:nBAF complex; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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 Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR025750; DPF1-3_N.
DR InterPro; IPR038047; DPF3.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
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 SMART; SM00355; ZnF_C2H2; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; Chromatin regulator; Metal-binding;
KW Neurogenesis; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..427
FT /note="Zinc finger protein DPF3"
FT /id="PRO_0000168156"
FT ZN_FING 247..270
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 308..368
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 365..415
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 182..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 102..137
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11845289"
FT /id="VSP_005614"
FT VAR_SEQ 212..224
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11845289"
FT /id="VSP_005615"
FT VAR_SEQ 340..427
FT /note="GHPTCLQFTTNMTEAVKTYQWQCIECKSCSLCGTSENDDQLLFCDDCDRGYH
FT MYCLNPPVFEPPEGSWSCHLCRELLRERASAFGFQA -> AHLGREGRRDEAAPTRTTE
FT DLFGSTSESDTSTFHGFDEDDAEEPLSSRGGGCGGSSPSADKKGGC (in isoform
FT 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11845289"
FT /id="VSP_005616"
SQ SEQUENCE 427 AA; 48930 MW; B22DB85D1E714152 CRC64;
MATVIHNPLK ALGDQFYKEA IEHCRSYNSR LCAERSVRLP FLDSQTGVAQ NNCYIWMEKR
HRGPGLAPGQ LYTYPARCWR KKRRLHPPED SRLKLLEIKP ETSHLPGKTE LITETEFITK
MSVDLRRFLS CKLYTSEVDL PLKKDGFTSE STTLEALLRG EGIEKKMDTK EEDPIQEIQR
VLENDENADE VNEEEDLEED IPKRKNRPRG RPKTPTWKKI FQKNARGSGG GRRRNDAASQ
DDHDKPYVCD ICGKRYKNRP GLSYHYAHTH LASEEGDEAR EQETRSSPVH RNENHKPQKG
PDGVIIPNNY CDFCLGGSNM NKKSGRPEEL VSCSDCGRSG HPTCLQFTTN MTEAVKTYQW
QCIECKSCSL CGTSENDDQL LFCDDCDRGY HMYCLNPPVF EPPEGSWSCH LCRELLRERA
SAFGFQA
