PO3F2_MOUSE
ID PO3F2_MOUSE Reviewed; 445 AA.
AC P31360; A2AJY1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=POU domain, class 3, transcription factor 2;
DE AltName: Full=Brain-specific homeobox/POU domain protein 2;
DE Short=Brain-2;
DE Short=Brn-2;
DE AltName: Full=Nervous system-specific octamer-binding transcription factor N-Oct-3;
DE AltName: Full=Octamer-binding protein 7;
DE Short=Oct-7;
DE AltName: Full=Octamer-binding transcription factor 7;
DE Short=OTF-7;
GN Name=Pou3f2; Synonyms=Brn-2, Brn2, Otf7;
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].
RC TISSUE=Brain;
RX PubMed=1565620; DOI=10.1073/pnas.89.8.3280;
RA Hara Y., Rovescalli C., Kim Y., Nirenberg M.;
RT "Structure and evolution of four POU domain genes expressed in mouse
RT brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3280-3284(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION.
RX PubMed=18505825; DOI=10.1128/mcb.00338-08;
RA Hoser M., Potzner M.R., Koch J.M., Boesl M.R., Wegner M., Sock E.;
RT "Sox12 deletion in the mouse reveals nonreciprocal redundancy with the
RT related Sox4 and Sox11 transcription factors.";
RL Mol. Cell. Biol. 28:4675-4687(2008).
RN [4]
RP FUNCTION.
RX PubMed=18403418; DOI=10.1093/nar/gkn162;
RA Dy P., Penzo-Mendez A., Wang H., Pedraza C.E., Macklin W.B., Lefebvre V.;
RT "The three SoxC proteins--Sox4, Sox11 and Sox12--exhibit overlapping
RT expression patterns and molecular properties.";
RL Nucleic Acids Res. 36:3101-3117(2008).
RN [5]
RP FUNCTION.
RX PubMed=20107439; DOI=10.1038/nature08797;
RA Vierbuchen T., Ostermeier A., Pang Z.P., Kokubu Y., Suedhof T.C.,
RA Wernig M.;
RT "Direct conversion of fibroblasts to functional neurons by defined
RT factors.";
RL Nature 463:1035-1041(2010).
RN [6]
RP FUNCTION.
RX PubMed=24243019; DOI=10.1016/j.cell.2013.09.028;
RA Wapinski O.L., Vierbuchen T., Qu K., Lee Q.Y., Chanda S., Fuentes D.R.,
RA Giresi P.G., Ng Y.H., Marro S., Neff N.F., Drechsel D., Martynoga B.,
RA Castro D.S., Webb A.E., Suedhof T.C., Brunet A., Guillemot F., Chang H.Y.,
RA Wernig M.;
RT "Hierarchical mechanisms for direct reprogramming of fibroblasts to
RT neurons.";
RL Cell 155:621-635(2013).
RN [7]
RP INTERACTION WITH ISL1.
RX PubMed=24643061; DOI=10.1371/journal.pone.0092105;
RA Li R., Wu F., Ruonala R., Sapkota D., Hu Z., Mu X.;
RT "Isl1 and Pou4f2 form a complex to regulate target genes in developing
RT retinal ganglion cells.";
RL PLoS ONE 9:E92105-E92105(2014).
RN [8]
RP FUNCTION.
RX PubMed=27281220; DOI=10.1038/nature18323;
RA Treutlein B., Lee Q.Y., Camp J.G., Mall M., Koh W., Shariati S.A., Sim S.,
RA Neff N.F., Skotheim J.M., Wernig M., Quake S.R.;
RT "Dissecting direct reprogramming from fibroblast to neuron using single-
RT cell RNA-seq.";
RL Nature 534:391-395(2016).
CC -!- FUNCTION: Transcription factor that plays a key role in neuronal
CC differentiation (PubMed:24243019). Binds preferentially to the
CC recognition sequence which consists of two distinct half-sites,
CC ('GCAT') and ('TAAT'), separated by a non-conserved spacer region of 0,
CC 2, or 3 nucleotides (By similarity). Acts as a transcriptional
CC activator when binding cooperatively with SOX4, SOX11, or SOX12 to gene
CC promoters (PubMed:18505825, PubMed:18403418). The combination of three
CC transcription factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to
CC reprogram fibroblasts and other somatic cells into induced neuronal
CC (iN) cells in vitro (PubMed:20107439, PubMed:24243019,
CC PubMed:27281220). Acts downstream of ASCL1, accessing chromatin that
CC has been opened by ASCL1, and promotes transcription of neuronal genes
CC (PubMed:24243019). {ECO:0000250|UniProtKB:P56222,
CC ECO:0000269|PubMed:18403418, ECO:0000269|PubMed:18505825,
CC ECO:0000269|PubMed:20107439, ECO:0000269|PubMed:24243019,
CC ECO:0000269|PubMed:27281220}.
CC -!- SUBUNIT: Interacts with PQBP1 (By similarity). Interaction with ISL1
CC (PubMed:24643061). {ECO:0000250|UniProtKB:P20265,
CC ECO:0000269|PubMed:24643061}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the neuroectodermal cell
CC lineage.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-3
CC subfamily. {ECO:0000305}.
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DR EMBL; M88300; AAA39961.1; -; Genomic_DNA.
DR EMBL; AL772230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18005.1; -.
DR PIR; S31224; S31224.
DR RefSeq; NP_032925.1; NM_008899.2.
DR AlphaFoldDB; P31360; -.
DR SMR; P31360; -.
DR BioGRID; 202306; 1.
DR STRING; 10090.ENSMUSP00000136147; -.
DR iPTMnet; P31360; -.
DR PhosphoSitePlus; P31360; -.
DR MaxQB; P31360; -.
DR PaxDb; P31360; -.
DR PeptideAtlas; P31360; -.
DR PRIDE; P31360; -.
DR ProteomicsDB; 289649; -.
DR Antibodypedia; 18892; 371 antibodies from 42 providers.
DR DNASU; 18992; -.
DR Ensembl; ENSMUST00000178174; ENSMUSP00000136147; ENSMUSG00000095139.
DR GeneID; 18992; -.
DR KEGG; mmu:18992; -.
DR UCSC; uc008sdp.2; mouse.
DR CTD; 5454; -.
DR MGI; MGI:101895; Pou3f2.
DR VEuPathDB; HostDB:ENSMUSG00000095139; -.
DR eggNOG; KOG3802; Eukaryota.
DR GeneTree; ENSGT00940000162208; -.
DR HOGENOM; CLU_013065_1_2_1; -.
DR InParanoid; P31360; -.
DR OMA; QHHGGEH; -.
DR OrthoDB; 752252at2759; -.
DR PhylomeDB; P31360; -.
DR TreeFam; TF316413; -.
DR BioGRID-ORCS; 18992; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Pou3f2; mouse.
DR PRO; PR:P31360; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P31360; protein.
DR Bgee; ENSMUSG00000095139; Expressed in ventricular zone and 103 other tissues.
DR Genevisible; P31360; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0071837; F:HMG box domain binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0014002; P:astrocyte development; IMP:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IGI:MGI.
DR GO; GO:0008544; P:epidermis development; IMP:MGI.
DR GO; GO:0021869; P:forebrain ventricular zone progenitor cell division; IGI:MGI.
DR GO; GO:0021979; P:hypothalamus cell differentiation; IMP:MGI.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IGI:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
DR GO; GO:0007399; P:nervous system development; IDA:UniProtKB.
DR GO; GO:0061101; P:neuroendocrine cell differentiation; IMP:MGI.
DR GO; GO:0021985; P:neurohypophysis development; IMP:MGI.
DR GO; GO:0048666; P:neuron development; IDA:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IDA:UniProtKB.
DR GO; GO:0048663; P:neuron fate commitment; IDA:UniProtKB.
DR GO; GO:0048665; P:neuron fate specification; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0050770; P:regulation of axonogenesis; IMP:MGI.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0014044; P:Schwann cell development; IGI:MGI.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013847; POU.
DR InterPro; IPR000327; POU_dom.
DR InterPro; IPR016362; TF_POU_3.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR PIRSF; PIRSF002629; Transcription_factor_POU; 1.
DR PRINTS; PR00028; POUDOMAIN.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00352; POU; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00035; POU_1; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 1: Evidence at protein level;
KW Activator; Differentiation; DNA-binding; Homeobox; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..445
FT /note="POU domain, class 3, transcription factor 2"
FT /id="PRO_0000100723"
FT DOMAIN 264..338
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 356..415
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 64..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..254
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20265"
SQ SEQUENCE 445 AA; 47149 MW; 1A47F10950EECE8A CRC64;
MATAASNHYS LLTSSASIVH AEPPGGMQQG AGGYREAQSL VQGDYGALQS NGHPLSHAHQ
WITALSHGGG GGGGGGGGGG GGGGGGGGDG SPWSTSPLGQ PDIKPSVVVQ QGGRGDELHG
PGALQQQHQQ QQQQQQQQQQ QQQQQQQQQQ QRPPHLVHHA ANHHPGPGAW RSAAAAAHLP
PSMGASNGGL LYSQPSFTVN GMLGAGGQPA GLHHHGLRDA HDEPHHADHH PHPHSHPHQQ
PPPPPPPQGP PGHPGAHHDP HSDEDTPTSD DLEQFAKQFK QRRIKLGFTQ ADVGLALGTL
YGNVFSQTTI CRFEALQLSF KNMCKLKPLL NKWLEEADSS SGSPTSIDKI AAQGRKRKKR
TSIEVSVKGA LESHFLKCPK PSAQEITSLA DSLQLEKEVV RVWFCNRRQK EKRMTPPGGT
LPGAEDVYGG SRDTPPHHGV QTPVQ
