PO3F3_RAT
ID PO3F3_RAT Reviewed; 497 AA.
AC Q63262;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=POU domain, class 3, transcription factor 3;
DE AltName: Full=Brain-specific homeobox/POU domain protein 1;
DE Short=Brain-1;
DE Short=Brn-1;
GN Name=Pou3f3; Synonyms=Brn-1, Brn1, Rhs2;
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].
RX PubMed=9405434; DOI=10.1074/jbc.272.51.32286;
RA Schreiber J., Enderich J., Sock E., Schmidt C., Richter-Landsberg C.,
RA Wegner M.;
RT "Redundancy of class III POU proteins in the oligodendrocyte lineage.";
RL J. Biol. Chem. 272:32286-32293(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 325-449.
RC TISSUE=Hypothalamus;
RX PubMed=1348858; DOI=10.1073/pnas.89.8.3285;
RA le Moine C., Young W.S.;
RT "RHS2, a POU domain-containing gene, and its expression in developing and
RT adult rat.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3285-3289(1992).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 450-TRP-PHE-451.
RX PubMed=9632656; DOI=10.1074/jbc.273.26.16050;
RA Kuhlbrodt K., Herbarth B., Sock E., Enderich J., Hermans-Borgmeyer I.,
RA Wegner M.;
RT "Cooperative function of POU proteins and SOX proteins in glial cells.";
RL J. Biol. Chem. 273:16050-16057(1998).
CC -!- FUNCTION: Transcription factor that acts synergistically with SOX11 and
CC SOX4. Plays a role in neuronal development. Is implicated in an
CC enhancer activity at the embryonic met-mesencephalic junction; the
CC enhancer element contains the octamer motif (5'-ATTTGCAT-3') (By
CC similarity). {ECO:0000250|UniProtKB:P31361,
CC ECO:0000269|PubMed:9632656}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P20264}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000255|PROSITE-ProRule:PRU00530, ECO:0000269|PubMed:9632656}.
CC -!- TISSUE SPECIFICITY: Brain.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryonic day 11.5 into adulthood.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-3
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ001641; CAA04893.1; -; mRNA.
DR EMBL; M84644; AAA42041.1; -; mRNA.
DR RefSeq; NP_620192.1; NM_138837.1.
DR AlphaFoldDB; Q63262; -.
DR SMR; Q63262; -.
DR STRING; 10116.ENSRNOP00000040234; -.
DR iPTMnet; Q63262; -.
DR PhosphoSitePlus; Q63262; -.
DR PaxDb; Q63262; -.
DR GeneID; 192109; -.
DR KEGG; rno:192109; -.
DR UCSC; RGD:619768; rat.
DR CTD; 5455; -.
DR RGD; 619768; Pou3f3.
DR eggNOG; KOG3802; Eukaryota.
DR InParanoid; Q63262; -.
DR OrthoDB; 752252at2759; -.
DR PhylomeDB; Q63262; -.
DR PRO; PR:Q63262; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
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; IDA:MGI.
DR GO; GO:0071837; F:HMG box domain binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; ISO:RGD.
DR GO; GO:0048878; P:chemical homeostasis; ISO:RGD.
DR GO; GO:0021869; P:forebrain ventricular zone progenitor cell division; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0072218; P:metanephric ascending thin limb development; ISS:UniProtKB.
DR GO; GO:0072240; P:metanephric DCT cell differentiation; ISS:UniProtKB.
DR GO; GO:0072236; P:metanephric loop of Henle development; ISS:UniProtKB.
DR GO; GO:0072227; P:metanephric macula densa development; ISS:UniProtKB.
DR GO; GO:0072233; P:metanephric thick ascending limb development; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0071918; P:urea transmembrane transport; 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 Developmental protein; DNA-binding; Homeobox; Neurogenesis; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..497
FT /note="POU domain, class 3, transcription factor 3"
FT /id="PRO_0000100730"
FT DOMAIN 311..385
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 403..462
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 31..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..147
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 450..451
FT /note="WF->CS: Abolishes synergistic action with SOX11."
FT /evidence="ECO:0000269|PubMed:9632656"
SQ SEQUENCE 497 AA; 50226 MW; 00640505E343ABC2 CRC64;
MATAASNPYL PGNSLLAAGS IVHSDAAGAG GGGGGGGGGG GGAGGGGGGM QPGSAAVTSG
AYRGDPSSVK MVQSDFMQGA MAASNGGHML SHAHQWVTAL PHAAAAAAAA AAAAVEASSP
WSGSAVGMAG SPQQPPRPPP PPPQGPDVKG GVGREDLHAG TALHHRGPPH LGPPPPPPHQ
GHPGGWGAAA AAAAAAAAAA AAAHLPSMAG GQQPPPQSLL YSQPGGFTVN GMLSAPPGPG
GGGGGAGGGA QSLVHPGLVR GDTPELAEHH HHHHHHAHPH PPHPHHAQGP PHHGGGGAGP
GLNSHDPHSD EDTPTSDDLE QFAKQFKQRR IKLGFTQADV GLALGTLYGN VFSQTTICRF
EALQLSFKNM CKLKPLLNKW LEEADSSTGS PTSIDKIAAQ GRKRKKRTSI EVSVKGALES
HFLKCPKPSA QEITNLADSL QLEKEVVRVW FCNRRQKEKR MTPPGIQQQT PDDVYSQVGT
VSADTPPPHH GLQTSVQ
