ID   DPF1_HUMAN              Reviewed;         353 AA.
AC   Q92782;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   09-FEB-2010, entry version 78.
DE   RecName: Full=Zinc finger protein neuro-d4;
DE   AltName: Full=D4, zinc and double PHD fingers family 1;
DE   AltName: Full=BRG1-associated factor 45B;
DE            Short=BAF45B;
GN   Name=DPF1; Synonyms=BAF45B, NEUD4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
RX   MEDLINE=96411662; PubMed=8812431; DOI=10.1006/geno.1996.0440;
RA   Chestkov A.V., Baka I.D., Kost M.V., Georgiev G.P., Buchman V.L.;
RT   "The d4 gene family in the human genome.";
RL   Genomics 36:174-177(1996).
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
CC       development a switch from a stem/progenitor to a post-mitotic
CC       chromatin remodeling mechanism occurs as neurons exit the cell
CC       cycle and become committed to their adult state. The transition
CC       from proliferating neural stem/progenitor cells to post-mitotic
CC       neurons requires a switch in subunit composition of the npBAF and
CC       nBAF complexes. As neural progenitors exit mitosis and
CC       differentiate into neurons, npBAF complexes which contain
CC       ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous
CC       alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits
CC       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
CC       plays a role regulating the activity of genes essential for
CC       dendrite growth (By similarity).
CC   -!- SUBUNIT: Component of neuron-specific chromatin remodeling complex
CC       (nBAF complex) composed of at least, ARID1A/BAF250A or
CC       ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
CC       SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC       SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
CC       DPF3/BAF45C, ACTL6B/BAF53B and actin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q92782-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q92782-2; Sequence=VSP_005607;
CC   -!- SIMILARITY: Belongs to the requiem/DPF family.
CC   -!- SIMILARITY: Contains 2 PHD-type zinc fingers.
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DR   EMBL; U43843; AAC50685.1; -; mRNA.
DR   IPI; IPI00216452; -.
DR   IPI; IPI00291761; -.
DR   RefSeq; NP_001128628.1; -.
DR   RefSeq; NP_004638.2; -.
DR   UniGene; Hs.631576; -.
DR   SMR; Q92782; 223-340.
DR   IntAct; Q92782; 1.
DR   STRING; Q92782; -.
DR   PhosphoSite; Q92782; -.
DR   Ensembl; ENST00000420980; ENSP00000397354; ENSG00000011332; Homo sapiens.
DR   Ensembl; ENST00000434076; ENSP00000413691; ENSG00000011332; Homo sapiens.
DR   GeneID; 8193; -.
DR   UCSC; uc002ohl.1; human.
DR   CTD; 8193; -.
DR   GeneCards; GC19M043394; -.
DR   H-InvDB; HIX0015085; -.
DR   HGNC; HGNC:20225; DPF1.
DR   MIM; 601670; gene.
DR   PharmGKB; PA134879894; -.
DR   HOVERGEN; Q92782; -.
DR   InParanoid; Q92782; -.
DR   NextBio; 30890; -.
DR   ArrayExpress; Q92782; -.
DR   Bgee; Q92782; -.
DR   CleanEx; HS_DPF1; -.
DR   Genevestigator; Q92782; -.
DR   GermOnline; ENSG00000011332; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006917; P:induction of apoptosis; TAS:ProtInc.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00184; RING; 2.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; Cytoplasm; Metal-binding;
KW   Neurogenesis; Nucleus; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    353       Zinc finger protein neuro-d4.
FT                                /FTId=PRO_0000168145.
FT   ZN_FING     227    284       PHD-type 1.
FT   ZN_FING     281    341       PHD-type 2.
FT   VAR_SEQ     294    303       Missing (in isoform 2).
FT                                /FTId=VSP_005607.
SQ   SEQUENCE   353 AA;  39876 MW;  137D8310E77FB111 CRC64;
     MATVIPSPLS LGEDFYREAI EHCRSYNARL CAERSLRLPF LDSQTGVAQN NCYIWMEKTH
     RGPGLAPGQI YTYPARCWRK KRRLNILEDP RLRPCEYKID CEAPLKKEGG LPEGPVLEAL
     LCAETGEKKI ELKEEETIMD CQKQQLLEFP HDLEVEDLED DIPRRKNRAK GKAYGIGGLR
     KRQDTASLED RDKPYVCDKF YKELAWVPEA QRKHTAKKAP DGTVIPNGYC DFCLGGSKKT
     GCPEDLISCA DCGRSGHPSC LQFTVNMTAA VRTYRWQCIE CKSCSLCGTS ENDGASWAGL
     TPQDQLLFCD DCDRGYHMYC LSPPMAEPPE GSWSCHLCLR HLKEKASAYI TLT
//