PO4F1_MOUSE
ID PO4F1_MOUSE Reviewed; 421 AA.
AC P17208; E9QPT6;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=POU domain, class 4, transcription factor 1;
DE AltName: Full=Brain-specific homeobox/POU domain protein 3A;
DE Short=Brain-3A;
DE Short=Brn-3A;
DE AltName: Full=Brn-3.0;
GN Name=Pou4f1; Synonyms=Brn-3, Brn3, Brn3a;
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], AND TISSUE SPECIFICITY.
RX PubMed=8162704; DOI=10.1159/000133709;
RA Theil T., Zechner U., Klett C., Adolph S., Moeroey T.;
RT "Chromosomal localization and sequences of the murine Brn-3 family of
RT developmental control genes.";
RL Cytogenet. Cell Genet. 66:267-271(1994).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 286-401.
RC STRAIN=T6 / TW1; TISSUE=Testis;
RX PubMed=1970171; DOI=10.1093/nar/18.6.1634;
RA Goldsborough A., Ashworth A., Willison K.R.;
RT "Cloning and sequencing of POU-boxes expressed in mouse testis.";
RL Nucleic Acids Res. 18:1634-1634(1990).
RN [4]
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8290353; DOI=10.1093/nar/21.25.5921;
RA Theil T., McLean-Hunter S., Zoernig M., Moeroey T.;
RT "Mouse Brn-3 family of POU transcription factors: a new aminoterminal
RT domain is crucial for the oncogenic activity of Brn-3a.";
RL Nucleic Acids Res. 21:5921-5929(1993).
RN [5]
RP INTERACTION WITH POU4F2 (ISOFORM 1).
RX PubMed=8537352; DOI=10.1074/jbc.270.52.30958;
RA Theil T., Roedel B., Spiegelhalter F., Moeroey T.;
RT "Short isoform of POU factor Brn-3b can form a heterodimer with Brn-3a that
RT is inactive for octamer motif binding.";
RL J. Biol. Chem. 270:30958-30964(1995).
RN [6]
RP FUNCTION, DOMAIN, AND DNA-BINDING.
RX PubMed=8621561; DOI=10.1074/jbc.271.15.9108;
RA Budhram-Mahadeo V., Morris P.J., Lakin N.D., Dawson S.J., Latchman D.S.;
RT "The different activities of the two activation domains of the Brn-3a
RT transcription factor are dependent on the context of the binding site.";
RL J. Biol. Chem. 271:9108-9113(1996).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=8637595; DOI=10.1038/381603a0;
RA Erkman L., McEvilly R.J., Luo L., Ryan A.K., Hooshmand F., O'Connell S.M.,
RA Keithley E.M., Rapaport D.H., Ryan A.F., Rosenfeld M.G.;
RT "Role of transcription factors Brn-3.1 and Brn-3.2 in auditory and visual
RT system development.";
RL Nature 381:603-606(1996).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8876243; DOI=10.1073/pnas.93.21.11950;
RA Xiang M., Gan L., Zhou L., Klein W.H., Nathans J.;
RT "Targeted deletion of the mouse POU domain gene Brn-3a causes selective
RT loss of neurons in the brainstem and trigeminal ganglion, uncoordinated
RT limb movement, and impaired suckling.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:11950-11955(1996).
RN [9]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF VAL-378.
RX PubMed=8972215; DOI=10.1128/mcb.17.1.345;
RA Smith M.D., Dawson S.J., Latchman D.S.;
RT "The Brn-3a transcription factor induces neuronal process outgrowth and the
RT coordinate expression of genes encoding synaptic proteins.";
RL Mol. Cell. Biol. 17:345-354(1997).
RN [10]
RP FUNCTION, AND INTERACTION WITH ESR1 (ISOFORM 1).
RX PubMed=9448000; DOI=10.1128/mcb.18.2.1029;
RA Budhram-Mahadeo V., Parker M., Latchman D.S.;
RT "POU transcription factors Brn-3a and Brn-3b interact with the estrogen
RT receptor and differentially regulate transcriptional activity via an
RT estrogen response element.";
RL Mol. Cell. Biol. 18:1029-1041(1998).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF VAL-378.
RX PubMed=9694219; DOI=10.1097/00001756-199807130-00029;
RA Dawson S.J., Palmer R.D., Morris P.J., Latchman D.S.;
RT "Functional role of position 22 in the homeodomain of Brn-3 transcription
RT factors.";
RL NeuroReport 9:2305-2309(1998).
RN [12]
RP FUNCTION, FUNCTION (ISOFORM 2), DOMAIN, AND MUTAGENESIS OF VAL-378.
RX PubMed=9722627; DOI=10.1093/nar/26.18.4100;
RA Smith M.D., Dawson S.J., Boxer L.M., Latchman D.S.;
RT "The N-terminal domain unique to the long form of the Brn-3a transcription
RT factor is essential to protect neuronal cells from apoptosis and for the
RT activation of Bbcl-2 gene expression.";
RL Nucleic Acids Res. 26:4100-4107(1998).
RN [13]
RP FUNCTION.
RX PubMed=10640682; DOI=10.1016/s0169-328x(99)00271-5;
RA Smith M.D., Ensor E.A., Stohl L., Wagner J.A., Latchman D.S.;
RT "Regulation of NGFI-A (Egr-1) gene expression by the POU domain
RT transcription factor Brn-3a.";
RL Brain Res. Mol. Brain Res. 74:117-125(1999).
RN [14]
RP FUNCTION.
RX PubMed=12441296; DOI=10.1242/dev.00194;
RA Trieu M., Ma A., Eng S.R., Fedtsova N., Turner E.E.;
RT "Direct autoregulation and gene dosage compensation by POU-domain
RT transcription factor Brn3a.";
RL Development 130:111-121(2003).
RN [15]
RP FUNCTION, FUNCTION (ISOFORM 2), AND INTERACTION WITH RIT2.
RX PubMed=12934100; DOI=10.1038/sj.onc.1206635;
RA Calissano M., Latchman D.S.;
RT "Functional interaction between the small GTP-binding protein Rin and the
RT N-terminal of Brn-3a transcription factor.";
RL Oncogene 22:5408-5414(2003).
RN [16]
RP FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=17668438; DOI=10.1002/jcb.21257;
RA Schulze-Spaete U., Battaglino R., Fu J., Sharma A., Vokes M., Stashenko P.;
RT "Brn3 transcription factors control terminal osteoclastogenesis.";
RL J. Cell. Biochem. 102:1-12(2007).
RN [17]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=22326227; DOI=10.1016/j.ydbio.2012.01.021;
RA Zou M., Li S., Klein W.H., Xiang M.;
RT "Brn3a/Pou4f1 regulates dorsal root ganglion sensory neuron specification
RT and axonal projection into the spinal cord.";
RL Dev. Biol. 364:114-127(2012).
CC -!- FUNCTION: Multifunctional transcription factor with different regions
CC mediating its different effects (PubMed:10640682, PubMed:8621561,
CC PubMed:9694219, PubMed:9722627). Acts by binding (via its C-terminal
CC domain) to sequences related to the consensus octamer motif 5'-
CC ATGCAAAT-3' in the regulatory regions of its target genes
CC (PubMed:8621561, PubMed:17668438). Regulates the expression of specific
CC genes involved in differentiation and survival within a subset of
CC neuronal lineages. It has been shown that activation of some of these
CC genes requires its N-terminal domain, maybe through a neuronal-specific
CC cofactor (PubMed:12934100). Ativates BCL2 expression and protects
CC neuronal cells from apoptosis (via the N-terminal domain)
CC (PubMed:9722627). Induces neuronal process outgrowth and the coordinate
CC expression of genes encoding synaptic proteins (PubMed:8972215). Exerts
CC its major developmental effects in somatosensory neurons and in
CC brainstem nuclei involved in motor control. Stimulates the binding
CC affinity of the nuclear estrogene receptor ESR1 to DNA estrogen
CC response element (ERE), and hence modulates ESR1-induced
CC transcriptional activity (PubMed:9448000). May positively regulate
CC POU4F2 and POU4F3 (PubMed:8876243). Regulates dorsal root ganglion
CC sensory neuron specification and axonal projection into the spinal cord
CC (PubMed:22326227). Plays a role in TNFSF11-mediated terminal osteoclast
CC differentiation (PubMed:17668438). Negatively regulates its own
CC expression interacting directly with a highly conserved autoregulatory
CC domain surrounding the transcription initiation site (PubMed:12441296).
CC {ECO:0000269|PubMed:10640682, ECO:0000269|PubMed:12441296,
CC ECO:0000269|PubMed:12934100, ECO:0000269|PubMed:17668438,
CC ECO:0000269|PubMed:22326227, ECO:0000269|PubMed:8621561,
CC ECO:0000269|PubMed:8876243, ECO:0000269|PubMed:8972215,
CC ECO:0000269|PubMed:9448000, ECO:0000269|PubMed:9694219,
CC ECO:0000269|PubMed:9722627}.
CC -!- FUNCTION: [Isoform 2]: Able to act as transcription factor, cannot
CC regulate the expression of the same subset of genes than isoform 1
CC (PubMed:12934100). Does not have antiapoptotic effect on neuronal cells
CC (PubMed:9722627). {ECO:0000269|PubMed:12934100,
CC ECO:0000269|PubMed:9722627}.
CC -!- SUBUNIT: Interacts (via N-terminus) with RIT2; the interaction controls
CC POU4F1 transactivation activity on some neuronal target genes
CC (PubMed:12934100). Isoform 1 interacts with POU4F2 isoform 2; this
CC interaction inhibits both POU4F1 DNA-binding and transcriptional
CC activities (PubMed:8537352). Isoform 1 interacts (C-terminus) with ESR1
CC (via DNA-binding domain); this interaction decreases the estrogen
CC receptor ESR1 transcriptional activity in a DNA- and ligand 17-beta-
CC estradiol-independent manner (PubMed:9448000).
CC {ECO:0000269|PubMed:12934100, ECO:0000269|PubMed:8537352,
CC ECO:0000269|PubMed:9448000}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17668438}. Cytoplasm
CC {ECO:0000269|PubMed:17668438}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Brn-3A-Long {ECO:0000303|PubMed:8290353};
CC IsoId=P17208-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:8290353}; Synonyms=Brn-3A-Short
CC {ECO:0000303|PubMed:8290353};
CC IsoId=P17208-2; Sequence=VSP_058637;
CC -!- TISSUE SPECIFICITY: Expressed in mature osteoclasts (at protein level)
CC (PubMed:17668438). Brain, peripheral sensory nervous system and retina
CC (PubMed:8162704). In the adult nervous system, predominates in the
CC medial habenula, superficial gray of the superior colliculus, red
CC nucleus, mesencephalic nucleus of the trigeminal ganglion, nucleus
CC ambiguus, inferior olivary nucleus, and peripheral sensory ganglia
CC (PubMed:8290353). {ECO:0000269|PubMed:17668438,
CC ECO:0000269|PubMed:8162704, ECO:0000269|PubMed:8290353}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the spinal cord from 11 dpc to the
CC adult stage (PubMed:8290353). As early as 10.5 dpc to 15.5 dpc,
CC strongly expressed in all dorsal root ganglion neurons
CC (PubMed:22326227). In retinal ganglion cells, expression starts at 15.5
CC dpc and exhibits a slow decrease with moderate levels detectable at P8
CC (PubMed:8637595). {ECO:0000269|PubMed:22326227,
CC ECO:0000269|PubMed:8290353, ECO:0000269|PubMed:8637595}.
CC -!- INDUCTION: Up-regulated by the osteoclast differentiation factor
CC TNFSF11 (PubMed:17668438). {ECO:0000269|PubMed:17668438}.
CC -!- DOMAIN: The C-terminal domain is able to act as both DNA-binding domain
CC and a transcriptional activator. The N-terminal domain is also required
CC for transactivation activity on some target genes acting as a discrete
CC activation domain (PubMed:8621561, PubMed:9722627). Neurite outgrowth
CC and expression of genes required for synapse formation are primarily
CC dependent on the C-terminal domain, however the N-terminal domain is
CC required for maximal induction (PubMed:8972215).
CC {ECO:0000269|PubMed:8621561, ECO:0000269|PubMed:8972215,
CC ECO:0000269|PubMed:9722627}.
CC -!- DISRUPTION PHENOTYPE: Mutants have defective suckling and uncoordinated
CC limb and trunk movements, leading to early postnatal death. They show a
CC loss of neurons in the trigerminal ganglia, the medial habenula, the
CC red nucleus and the caudal region of the inferior olivary nucleus
CC (PubMed:8876243). Mutant dorsal root ganglions are defective in sensory
CC neuron specification, and sensory afferent axons fail to form normal
CC trajectories in the spinal cord (PubMed:22326227).
CC {ECO:0000269|PubMed:22326227, ECO:0000269|PubMed:8876243}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-4
CC subfamily. {ECO:0000305}.
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DR EMBL; S69350; AAB30577.2; -; Genomic_DNA.
DR EMBL; AC121997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X51959; CAA36218.1; -; mRNA.
DR CCDS; CCDS27319.1; -. [P17208-1]
DR RefSeq; NP_035273.3; NM_011143.4. [P17208-1]
DR RefSeq; XP_006518768.1; XM_006518705.3. [P17208-1]
DR RefSeq; XP_006518769.1; XM_006518706.3. [P17208-1]
DR AlphaFoldDB; P17208; -.
DR SMR; P17208; -.
DR BioGRID; 202310; 2.
DR STRING; 10090.ENSMUSP00000060798; -.
DR PhosphoSitePlus; P17208; -.
DR PaxDb; P17208; -.
DR PRIDE; P17208; -.
DR Antibodypedia; 24689; 156 antibodies from 31 providers.
DR DNASU; 18996; -.
DR Ensembl; ENSMUST00000053016; ENSMUSP00000060798; ENSMUSG00000048349. [P17208-1]
DR GeneID; 18996; -.
DR KEGG; mmu:18996; -.
DR UCSC; uc007uxb.2; mouse. [P17208-1]
DR CTD; 5457; -.
DR MGI; MGI:102525; Pou4f1.
DR VEuPathDB; HostDB:ENSMUSG00000048349; -.
DR eggNOG; KOG1168; Eukaryota.
DR GeneTree; ENSGT00940000162154; -.
DR HOGENOM; CLU_013065_0_0_1; -.
DR InParanoid; P17208; -.
DR OMA; HPHMHSL; -.
DR OrthoDB; 929123at2759; -.
DR PhylomeDB; P17208; -.
DR TreeFam; TF316413; -.
DR Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR BioGRID-ORCS; 18996; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pou4f1; mouse.
DR PRO; PR:P17208; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P17208; protein.
DR Bgee; ENSMUSG00000048349; Expressed in trigeminal ganglion and 131 other tissues.
DR Genevisible; P17208; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:ARUK-UCL.
DR GO; GO:0003682; F:chromatin binding; IGI:ParkinsonsUK-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IGI:ARUK-UCL.
DR GO; GO:0051020; F:GTPase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ARUK-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0021535; P:cell migration in hindbrain; IMP:MGI.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
DR GO; GO:0021953; P:central nervous system neuron differentiation; IMP:MGI.
DR GO; GO:0021986; P:habenula development; IMP:MGI.
DR GO; GO:0007507; P:heart development; IGI:ARUK-UCL.
DR GO; GO:0060384; P:innervation; IMP:MGI.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:BHF-UCL.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IDA:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IGI:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0048665; P:neuron fate specification; IMP:BHF-UCL.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
DR GO; GO:0048935; P:peripheral nervous system neuron development; IMP:BHF-UCL.
DR GO; GO:0048934; P:peripheral nervous system neuron differentiation; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IGI:MGI.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:UniProtKB.
DR GO; GO:0051355; P:proprioception involved in equilibrioception; IMP:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0048880; P:sensory system development; IMP:BHF-UCL.
DR GO; GO:0001967; P:suckling behavior; IMP:MGI.
DR GO; GO:0021559; P:trigeminal nerve development; IMP:BHF-UCL.
DR GO; GO:0003223; P:ventricular compact myocardium morphogenesis; IMP:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
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; IPR015584; POU4-TF1.
DR InterPro; IPR000327; POU_dom.
DR PANTHER; PTHR11636:SF42; PTHR11636:SF42; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; 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 Alternative splicing; Cytoplasm; Developmental protein; DNA-binding;
KW Homeobox; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..421
FT /note="POU domain, class 4, transcription factor 1"
FT /id="PRO_0000100737"
FT DOMAIN 262..339
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 357..416
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 94..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 57..66
FT /note="POU-IV box"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_058637"
FT MUTAGEN 378
FT /note="V->I: Abolishes transcriptional activity. Increases
FT transcriptional repression. Disrupts induction of neurite
FT outgrowth and expression of synaptic genes. No effect on
FT transactivation of BCL2 expression."
FT /evidence="ECO:0000269|PubMed:8972215,
FT ECO:0000269|PubMed:9694219, ECO:0000269|PubMed:9722627"
FT CONFLICT 179
FT /note="G -> A (in Ref. 1; AAB30577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 42767 MW; 64EC98E5C0CF79E2 CRC64;
MMSMNSKQPH FAMHPTLPEH KYPSLHSSSE AIRRACLPTP PLQSNLFASL DETLLARAEA
LAAVDIAVSQ GKSHPFKPDA TYHTMNSVPC TSTSTVPLAH HHHHHHHHQA LEPGDLLDHI
SSPSLALMAG AGGAGAAGGG GGAHDGPGGG GGPGGGGGPG GGGPGGGGGG GGPGGGGGGP
GGGLLGGSAH PHPHMHGLGH LSHPAAAAAM NMPSGLPHPG LVAAAAHHGA AAAAAAAAAG
QVAAASAAAA VVGAAGLASI CDSDTDPREL EAFAERFKQR RIKLGVTQAD VGSALANLKI
PGVGSLSQST ICRFESLTLS HNNMIALKPI LQAWLEEAEG AQREKMNKPE LFNGGEKKRK
RTSIAAPEKR SLEAYFAVQP RPSSEKIAAI AEKLDLKKNV VRVWFCNQRQ KQKRMKFSAT
Y
