PHF10_BOVIN
ID PHF10_BOVIN Reviewed; 410 AA.
AC Q2T9V9;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=PHD finger protein 10;
DE AltName: Full=BRG1-associated factor 45a;
DE Short=BAF45a;
GN Name=PHF10; Synonyms=BAF45A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in transcription activity regulation by chromatin
CC remodeling. Belongs to the neural progenitors-specific chromatin
CC remodeling complex (npBAF complex) and is required for the
CC proliferation of neural progenitors. During neural development a switch
CC from a stem/progenitor to a post-mitotic chromatin remodeling mechanism
CC occurs as neurons exit the cell cycle and become committed to their
CC adult state. The transition from proliferating neural stem/progenitor
CC cells to post-mitotic neurons requires a switch in subunit composition
CC of the npBAF and nBAF complexes. As neural progenitors exit mitosis and
CC differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A
CC and PHF10/BAF45A, are exchanged for homologous alternative
CC ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-
CC specific complexes (nBAF). The npBAF complex is essential for the self-
CC renewal/proliferative capacity of the multipotent neural stem cells.
CC The nBAF complex along with CREST plays a role regulating the activity
CC of genes essential for dendrite growth (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of neural progenitors-specific chromatin remodeling
CC complex (npBAF complex) composed of at least, ARID1A/BAF250A or
CC ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
CC SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57,
CC SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Interacts with
CC ACTL6A/BAF53A, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A and
CC PBRM1/BAF180 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SAYP family. {ECO:0000305}.
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DR EMBL; BC111243; AAI11244.1; -; mRNA.
DR RefSeq; NP_001033141.1; NM_001038052.1.
DR AlphaFoldDB; Q2T9V9; -.
DR SMR; Q2T9V9; -.
DR STRING; 9913.ENSBTAP00000005130; -.
DR PaxDb; Q2T9V9; -.
DR PRIDE; Q2T9V9; -.
DR GeneID; 507648; -.
DR KEGG; bta:507648; -.
DR CTD; 55274; -.
DR eggNOG; KOG1512; Eukaryota.
DR HOGENOM; CLU_028634_2_0_1; -.
DR InParanoid; Q2T9V9; -.
DR OrthoDB; 708781at2759; -.
DR TreeFam; TF318971; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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; IPR038045; PHF10.
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:SF174; PTHR10615:SF174; 1.
DR Pfam; PF00628; PHD; 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 Isopeptide bond; Metal-binding; Neurogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..410
FT /note="PHD finger protein 10"
FT /id="PRO_0000391319"
FT ZN_FING 291..348
FT /note="PHD-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 350..393
FT /note="PHD-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..207
FT /note="SAY"
FT REGION 1..97
FT /note="Essential to induce neural progenitor proliferation"
FT /evidence="ECO:0000250"
FT REGION 199..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..246
FT /note="Essential to induce neural progenitor proliferation"
FT /evidence="ECO:0000250"
FT COMPBIAS 252..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUB8"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUB8"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUB8"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUB8"
FT CROSSLNK 153
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WUB8"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WUB8"
SQ SEQUENCE 410 AA; 46437 MW; 70F3B5FDB9824313 CRC64;
MLQEQVSEYL GVTSFKRKYP DLERRDLSHK EKLYLRELNV ITETQCTLGL TALRSDEVID
LMIKEYPAKH AEYSVILQEK ERQRITDHYK EYSQMQQQNT QKVEASKVPE YIKKAAKKAA
EFNSNLNRER MEERRAYFDL QTHVIQVPQG KYKVLPTERT KVSSYPVALI PGQFQEYYKR
YSPDELRYLP LNTALYEPPL DPELPALESD GDSDDAEDGR GDEKGKSKGT SDSSSGNVSE
GEGLPEGQEE PLPGRQRPRD KAAAPRKDAP KRSALSKAVP GHKPKVIPNA LCGICLKGKE
SSRRGKAEPL VHCSQCDNSG HPSCLDMTME LVSMIKTYPW QCMECKTCII CGQPHHEEEM
MFCDVCDRGY HTFCVGLGAI PSGRWICDCC QRAPPTPRKV GRRGKNSKEG
