DPF1_RAT
ID DPF1_RAT Reviewed; 397 AA.
AC P56163;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
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|RGD:61868}; Synonyms=Baf45b, Neud4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND VARIANT HIS-363.
RC TISSUE=Brain cortex;
RX PubMed=1454523; DOI=10.1093/nar/20.21.5579;
RA Buchman V.L., Ninkina N.N., Bogdanov Y.D., Bortvin A.L., Akopian H.N.,
RA Kiselev S.L., Krylova O.Y., Anokhin K.V., Georgiev G.P.;
RT "Differential splicing creates a diversity of transcripts from a
RT neurospecific developmentally regulated gene encoding a protein with new
RT zinc-finger motifs.";
RL Nucleic Acids Res. 20:5579-5585(1992).
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 (By similarity). {ECO:0000250}.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P56163-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P56163-2; Sequence=VSP_005611, VSP_005613;
CC Name=3;
CC IsoId=P56163-3; Sequence=VSP_005612, VSP_005613;
CC Name=4;
CC IsoId=P56163-4; Sequence=VSP_005610, VSP_005613;
CC -!- TISSUE SPECIFICITY: Expression restricted to neurons. High levels in
CC hippocampus and cerebral cortex, lower in other localizations in the
CC central nervous system and in peripheral nervous system (dorsal root
CC ganglia).
CC -!- DEVELOPMENTAL STAGE: Higher expression in developing than in mature
CC central nervous system with a maxima at postnatal day 4.
CC -!- SIMILARITY: Belongs to the requiem/DPF family. {ECO:0000305}.
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DR EMBL; X66022; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S26731; S26731.
DR AlphaFoldDB; P56163; -.
DR SMR; P56163; -.
DR STRING; 10116.ENSRNOP00000028091; -.
DR PaxDb; P56163; -.
DR PRIDE; P56163; -.
DR UCSC; RGD:61868; rat. [P56163-1]
DR RGD; 61868; Dpf1.
DR eggNOG; KOG1244; Eukaryota.
DR HOGENOM; CLU_038980_0_1_1; -.
DR InParanoid; P56163; -.
DR PhylomeDB; P56163; -.
DR TreeFam; TF318971; -.
DR PRO; PR:P56163; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P56163; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IDA:RGD.
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; 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 2: Evidence at transcript 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..397
FT /note="Zinc finger protein neuro-d4"
FT /id="PRO_0000168147"
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..385
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 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 382
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..199
FT /note="MATVIPSPLSLGEDFYREAIEHCRSYNARLCAERSLRLPFLDSQTGVAQNNC
FT YIWMEKTHRGPGLAPGQIYTYPARCWRKKRRLNILEDPRLRPCEYKIDCEAPLKKEGGL
FT PEGPVLEALLCAETGEKKVELKEEETIMDCQKQQLLEFPHDLEVEDLEEDIPRRKNRAK
FT GKAYGIGGLRKRQDNASLEDRDKPYVCDI -> MALEVSGNARTTHPWRTETSL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:1454523"
FT /id="VSP_005611"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1454523"
FT /id="VSP_005610"
FT VAR_SEQ 143..172
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1454523"
FT /id="VSP_005612"
FT VAR_SEQ 338..347
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:1454523"
FT /id="VSP_005613"
FT VARIANT 363
FT /note="Y -> H"
FT /evidence="ECO:0000269|PubMed:1454523"
SQ SEQUENCE 397 AA; 45193 MW; A2FE8CD0B49D0A42 CRC64;
MATVIPSPLS LGEDFYREAI EHCRSYNARL CAERSLRLPF LDSQTGVAQN NCYIWMEKTH
RGPGLAPGQI YTYPARCWRK KRRLNILEDP RLRPCEYKID CEAPLKKEGG LPEGPVLEAL
LCAETGEKKV ELKEEETIMD CQKQQLLEFP HDLEVEDLEE DIPRRKNRAK GKAYGIGGLR
KRQDNASLED RDKPYVCDIC GKRYKNRPGL SYHYTHTHLA EEEGEEHTER HALPFHRKNN
HKQFYKELAW VPEAQRKHTA KKAPDGTVIP NGYCDFCLGG SKKTGCPEDL ISCADCGRSG
HPSCLQFTVN MTAAVRTYRW QCIECKSCSL CGTSENDGAS WAGLTPQDQL LFCDDCDRGY
HMYCLSPPMA EPPEGSWSCH LCLRHLKEKA SAYITLT
