DPF1_MOUSE
ID DPF1_MOUSE Reviewed; 387 AA.
AC Q9QX66; Q9QX65; Q9QYA4;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Zinc finger protein neuro-d4 {ECO:0000305};
DE AltName: Full=BRG1-associated factor 45B;
DE Short=BAF45B;
DE AltName: Full=D4, zinc and double PHD fingers family 1;
GN Name=Dpf1 {ECO:0000312|MGI:MGI:1352748}; Synonyms=Baf45b, Neud4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=CD-1;
RX PubMed=10602997; DOI=10.1007/s003350010014;
RA Mertsalov I.B., Kulikova D.A., Alimova-Kost M.V., Ninkina N.N.,
RA Korochkin L.I., Buchman V.L.;
RT "Structure and expression of two members of the d4 gene family in mouse.";
RL Mamm. Genome 11:72-74(2000).
RN [2]
RP FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
RP SPECTROMETRY, IDENTIFICATION IN THE NBAF COMPLEX, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
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).
CC -!- FUNCTION: May have an important role in developing neurons by
CC participating in regulation of cell survival, possibly as a
CC neurospecific transcription factor. Belongs to the neuron-specific
CC chromatin remodeling complex (nBAF complex). During neural development
CC a switch from a stem/progenitor to a postmitotic chromatin remodeling
CC mechanism occurs as neurons exit the cell cycle and become committed to
CC their adult state. The transition from proliferating neural
CC stem/progenitor cells to postmitotic neurons requires a switch in
CC subunit composition of the npBAF and nBAF complexes. As neural
CC progenitors exit mitosis and differentiate into neurons, npBAF
CC complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged
CC for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C
CC subunits in neuron-specific complexes (nBAF). The npBAF complex is
CC essential for the self-renewal/proliferative capacity of the
CC multipotent neural stem cells. The nBAF complex along with CREST plays
CC a role regulating the activity of genes essential for dendrite growth.
CC {ECO:0000269|PubMed:17640523}.
CC -!- SUBUNIT: Component of neuron-specific chromatin remodeling complex
CC (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B,
CC SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
CC SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57,
CC SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin.
CC {ECO:0000269|PubMed:17640523}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9QX66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QX66-2; Sequence=VSP_005608;
CC Name=3;
CC IsoId=Q9QX66-3; Sequence=VSP_005609;
CC -!- TISSUE SPECIFICITY: At embryonic stages, predominant expression in the
CC nervous system. Expressed specifically in postmitotic neurons (at
CC protein level). {ECO:0000269|PubMed:17640523}.
CC -!- DEVELOPMENTAL STAGE: Low levels at embryonic day 9.5, and then sharp
CC increase since embryonic day 12. In the developing forebrain and
CC cerebellar primordium, strictly expressed in postmitotic neurons.
CC {ECO:0000269|PubMed:17640523}.
CC -!- SIMILARITY: Belongs to the requiem/DPF family. {ECO:0000305}.
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DR EMBL; U48238; AAF21455.1; -; mRNA.
DR EMBL; U48239; AAF21456.1; -; mRNA.
DR EMBL; AF108133; AAF21305.1; -; Genomic_DNA.
DR CCDS; CCDS21071.1; -. [Q9QX66-2]
DR CCDS; CCDS90198.1; -. [Q9QX66-1]
DR RefSeq; NP_038902.1; NM_013874.2. [Q9QX66-2]
DR AlphaFoldDB; Q9QX66; -.
DR SMR; Q9QX66; -.
DR BioGRID; 205927; 2.
DR ComplexPortal; CPX-1256; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1257; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1258; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1259; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR STRING; 10090.ENSMUSP00000054385; -.
DR iPTMnet; Q9QX66; -.
DR PhosphoSitePlus; Q9QX66; -.
DR MaxQB; Q9QX66; -.
DR PaxDb; Q9QX66; -.
DR PRIDE; Q9QX66; -.
DR ProteomicsDB; 279803; -. [Q9QX66-1]
DR ProteomicsDB; 279804; -. [Q9QX66-2]
DR ProteomicsDB; 279805; -. [Q9QX66-3]
DR Antibodypedia; 16434; 179 antibodies from 28 providers.
DR DNASU; 29861; -.
DR Ensembl; ENSMUST00000049977; ENSMUSP00000054385; ENSMUSG00000030584. [Q9QX66-2]
DR Ensembl; ENSMUST00000065181; ENSMUSP00000070539; ENSMUSG00000030584. [Q9QX66-1]
DR GeneID; 29861; -.
DR KEGG; mmu:29861; -.
DR CTD; 8193; -.
DR MGI; MGI:1352748; Dpf1.
DR VEuPathDB; HostDB:ENSMUSG00000030584; -.
DR eggNOG; KOG1244; Eukaryota.
DR GeneTree; ENSGT00940000160692; -.
DR InParanoid; Q9QX66; -.
DR OrthoDB; 708781at2759; -.
DR TreeFam; TF318971; -.
DR BioGRID-ORCS; 29861; 1 hit in 77 CRISPR screens.
DR PRO; PR:Q9QX66; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9QX66; protein.
DR Bgee; ENSMUSG00000030584; Expressed in cortical plate and 156 other tissues.
DR ExpressionAtlas; Q9QX66; baseline and differential.
DR Genevisible; Q9QX66; MM.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038046; DPF1.
DR InterPro; IPR025750; DPF1-3_N.
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:SF12; PTHR10615:SF12; 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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Isopeptide bond; Metal-binding;
KW Neurogenesis; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..387
FT /note="Zinc finger protein neuro-d4"
FT /id="PRO_0000168146"
FT ZN_FING 195..218
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 271..328
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 325..375
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92782"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92782"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92782"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10602997"
FT /id="VSP_005609"
FT VAR_SEQ 1..9
FT /note="MATVIPSPL -> MATAIQNPLK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10602997"
FT /id="VSP_005608"
FT VARIANT 314
FT /note="A -> P"
SQ SEQUENCE 387 AA; 44239 MW; 9FC2F75EFB38CFF4 CRC64;
MATVIPSPLS LGEDFYREAI EHCRSYNARL CAERSLRLPF LDSQTGVAQN NCYIWMEKTH
RGPGLAPGQI YTYPARCWRK KRRLNILEDP RLRPCEYKID CEAPLKKEGG LPEGPVLEAL
LCAETGEKKV ELKEEETIMD CQKQQLLEFP HDLEVEDLEE DIPRRKNRAR GKAYGIGGLR
KRQDTASLED RDKPYVCDIC GKRYKNRPGL SYHYTHTHLA EEEGEEHTER HALPFHRKNN
HKQFYKELAW VPEAQRKHTA KKAPDGTVIP NGYCDFCLGG SKKTGCPEDL ISCADCGRSG
HPSCLQFTVN MTAAVRTYRW QCIECKSCSL CGTSENDDQL LFCDDCDRGY HMYCLSPPMA
EPPEGSWSCH LCLRHLKEKA SAYITLT
