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PO3F2_RAT
ID   PO3F2_RAT               Reviewed;         445 AA.
AC   P56222;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 146.
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=Brn2, Otf7;
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], AND FUNCTION.
RC   TISSUE=Brain;
RX   PubMed=8276233; DOI=10.1101/gad.7.12b.2483;
RA   Li P., He X., Gerrero M.R., Mok M., Aggarwal A., Rosenfeld M.G.;
RT   "Spacing and orientation of bipartite DNA-binding motifs as potential
RT   functional determinants for POU domain factors.";
RL   Genes Dev. 7:2483-2496(1993).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Transcription factor that plays a key role in neuronal
CC       differentiation (By similarity). 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 (PubMed:8276233). Acts as a transcriptional
CC       activator when binding cooperatively with SOX4, SOX11, or SOX12 to gene
CC       promoters (By similarity). The combination of three transcription
CC       factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to reprogram
CC       fibroblasts and other somatic cells into induced neuronal (iN) cells in
CC       vitro (By similarity). Acts downstream of ASCL1, accessing chromatin
CC       that has been opened by ASCL1, and promotes transcription of neuronal
CC       genes (By similarity). {ECO:0000250|UniProtKB:P31360,
CC       ECO:0000269|PubMed:8276233}.
CC   -!- SUBUNIT: Interacts with PQBP1. Interaction with ISL1.
CC       {ECO:0000250|UniProtKB:P20265, ECO:0000250|UniProtKB:P31360}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed specifically at high levels in the brain.
CC   -!- SIMILARITY: Belongs to the POU transcription factor family. Class-3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L27663; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A49447; A49447.
DR   AlphaFoldDB; P56222; -.
DR   SMR; P56222; -.
DR   STRING; 10116.ENSRNOP00000009043; -.
DR   PhosphoSitePlus; P56222; -.
DR   PaxDb; P56222; -.
DR   UCSC; RGD:61946; rat.
DR   RGD; 61946; Pou3f2.
DR   eggNOG; KOG3802; Eukaryota.
DR   InParanoid; P56222; -.
DR   PhylomeDB; P56222; -.
DR   PRO; PR:P56222; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; IDA:RGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:RGD.
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; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0014002; P:astrocyte development; ISO:RGD.
DR   GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
DR   GO; GO:0021799; P:cerebral cortex radially oriented cell migration; ISO:RGD.
DR   GO; GO:0008544; P:epidermis development; ISO:RGD.
DR   GO; GO:0021869; P:forebrain ventricular zone progenitor cell division; ISO:RGD.
DR   GO; GO:0021979; P:hypothalamus cell differentiation; ISO:RGD.
DR   GO; GO:0022011; P:myelination in peripheral nervous system; ISO:RGD.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR   GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR   GO; GO:0021985; P:neurohypophysis development; ISO:RGD.
DR   GO; GO:0048666; P:neuron development; ISS:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0048663; P:neuron fate commitment; ISS:UniProtKB.
DR   GO; GO:0048665; P:neuron fate specification; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0050770; P:regulation of axonogenesis; ISO:RGD.
DR   GO; GO:0045595; P:regulation of cell differentiation; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:RGD.
DR   GO; GO:0014044; P:Schwann cell development; ISO:RGD.
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_0000100724"
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          63..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          336..361
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..156
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   COMPBIAS        336..350
FT                   /note="Polar 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;  47172 MW;  9D2729E34E359FD3 CRC64;
     MATAASNHYS LLTSSASIVH AEPPGGMQQG AGGYREAQSL QVQGDYGALQ SNGHPLSHAH
     WITALSHGGS GGGGGGGGGG GGGGGGGGDG SPWSTSPLGQ PDIKPSVVVQ QGGRGDELHG
     PGALQQQHQQ QQQQQQQQQQ QQQQQQQQQQ QRPPHLVHHA ANNHPGPGAW RSAAAAAHLP
     PSMGASNGGL LYSQPSFTVN GMLGAGGQPA GLHHHGLRDA HDEPHHADHH PHPHSHPHQQ
     PPPPPPPQGP PGHPGAHHDP HSDEDTPTSD DLEQFAKQFK QRRIKLGFTQ ADVGLALGTL
     YGNVFSQTTI CRFEALQLSF KNMCKLKPLL NKWLEEADSS SGSPTSIDKI ASQGRKRKKR
     TSIEVSVKGA LESHFLKCPK PSAQEITSLA DSLQLEKEVV RVWFCNRRQK EKRMTPPGGT
     LPGAEDVYGG SRDTPPHHGV QTPVQ
 
 
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