NPAS4_MOUSE
ID NPAS4_MOUSE Reviewed; 802 AA.
AC Q8BGD7; Q3V3U3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Neuronal PAS domain-containing protein 4 {ECO:0000305};
DE Short=Neuronal PAS4 {ECO:0000305};
DE AltName: Full=HLH-PAS transcription factor NXF {ECO:0000303|PubMed:14701734};
DE AltName: Full=Limbic-enhanced PAS protein {ECO:0000303|PubMed:15363889};
DE Short=LE-PAS {ECO:0000303|PubMed:15363889};
GN Name=Npas4 {ECO:0000312|MGI:MGI:2664186};
GN Synonyms=Nxf {ECO:0000303|PubMed:14701734};
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 / MRNA], FUNCTION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/SvJ, and C57BL/6J; TISSUE=Brain;
RX PubMed=14701734; DOI=10.1128/mcb.24.2.608-616.2004;
RA Ooe N., Saito K., Mikami N., Nakatuka I., Kaneko H.;
RT "Identification of a novel basic helix-loop-helix-PAS factor, NXF, reveals
RT a Sim2 competitive, positive regulatory role in dendritic-cytoskeleton
RT modulator drebrin gene expression.";
RL Mol. Cell. Biol. 24:608-616(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster;
RX PubMed=15363889; DOI=10.1016/j.molbrainres.2004.06.023;
RA Moser M., Knoth R., Bode C., Patterson C.;
RT "LE-PAS, a novel Arnt-dependent HLH-PAS protein, is expressed in limbic
RT tissues and transactivates the CNS midline enhancer element.";
RL Brain Res. Mol. Brain Res. 128:141-149(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 274-802.
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18815592; DOI=10.1038/nature07319;
RA Lin Y., Bloodgood B.L., Hauser J.L., Lapan A.D., Koon A.C., Kim T.K.,
RA Hu L.S., Malik A.N., Greenberg M.E.;
RT "Activity-dependent regulation of inhibitory synapse development by
RT Npas4.";
RL Nature 455:1198-1204(2008).
RN [5]
RP SUBUNIT.
RX PubMed=19284974; DOI=10.1016/j.bbagrm.2009.01.003;
RA Ooe N., Saito K., Kaneko H.;
RT "Characterization of functional heterodimer partners in brain for a bHLH-
RT PAS factor NXF.";
RL Biochim. Biophys. Acta 1789:192-197(2009).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=19001414; DOI=10.1074/jbc.m805196200;
RA Ooe N., Motonaga K., Kobayashi K., Saito K., Kaneko H.;
RT "Functional characterization of basic helix-loop-helix-PAS type
RT transcription factor NXF in vivo: putative involvement in an 'on demand'
RT neuroprotection system.";
RL J. Biol. Chem. 284:1057-1063(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, DNA-BINDING, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=22194569; DOI=10.1126/science.1208049;
RA Ramamoorthi K., Fropf R., Belfort G.M., Fitzmaurice H.L., McKinney R.M.,
RA Neve R.L., Otto T., Lin Y.;
RT "Npas4 regulates a transcriptional program in CA3 required for contextual
RT memory formation.";
RL Science 334:1669-1675(2011).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=23029555; DOI=10.1371/journal.pone.0046604;
RA Coutellier L., Beraki S., Ardestani P.M., Saw N.L., Shamloo M.;
RT "Npas4: a neuronal transcription factor with a key role in social and
RT cognitive functions relevant to developmental disorders.";
RL PLoS ONE 7:E46604-E46604(2012).
RN [9]
RP FUNCTION.
RX PubMed=23172225; DOI=10.1074/jbc.m112.413310;
RA Yun J., Nagai T., Furukawa-Hibi Y., Kuroda K., Kaibuchi K., Greenberg M.E.,
RA Yamada K.;
RT "Neuronal Per Arnt Sim (PAS) domain protein 4 (NPAS4) regulates neurite
RT outgrowth and phosphorylation of synapsin I.";
RL J. Biol. Chem. 288:2655-2664(2013).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=24201284; DOI=10.1038/nature12743;
RA Bloodgood B.L., Sharma N., Browne H.A., Trepman A.Z., Greenberg M.E.;
RT "The activity-dependent transcription factor NPAS4 regulates domain-
RT specific inhibition.";
RL Nature 503:121-125(2013).
RN [11]
RP INDUCTION.
RX PubMed=24291638; DOI=10.1016/j.bbagrm.2013.11.004;
RA Bersten D.C., Wright J.A., McCarthy P.J., Whitelaw M.L.;
RT "Regulation of the neuronal transcription factor NPAS4 by REST and
RT microRNAs.";
RL Biochim. Biophys. Acta 1839:13-24(2014).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=24855953; DOI=10.1016/j.cell.2014.03.058;
RA Spiegel I., Mardinly A.R., Gabel H.W., Bazinet J.E., Couch C.H.,
RA Tzeng C.P., Harmin D.A., Greenberg M.E.;
RT "Npas4 regulates excitatory-inhibitory balance within neural circuits
RT through cell-type-specific gene programs.";
RL Cell 157:1216-1229(2014).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25088421; DOI=10.1016/j.celrep.2014.06.056;
RA Yoshihara S., Takahashi H., Nishimura N., Kinoshita M., Asahina R.,
RA Kitsuki M., Tatsumi K., Furukawa-Hibi Y., Hirai H., Nagai T., Yamada K.,
RA Tsuboi A.;
RT "Npas4 regulates Mdm2 and thus Dcx in experience-dependent dendritic spine
RT development of newborn olfactory bulb interneurons.";
RL Cell Rep. 8:843-857(2014).
RN [14]
RP DISRUPTION PHENOTYPE.
RX PubMed=25549857; DOI=10.1016/j.bbr.2014.12.044;
RA Jaehne E.J., Klaric T.S., Koblar S.A., Baune B.T., Lewis M.D.;
RT "Effects of Npas4 deficiency on anxiety, depression-like, cognition and
RT sociability behaviour.";
RL Behav. Brain Res. 281:276-282(2015).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=25911220; DOI=10.1016/j.bbr.2015.04.027;
RA Coutellier L., Gilbert V., Shepard R.;
RT "Npas4 deficiency increases vulnerability to juvenile stress in mice.";
RL Behav. Brain Res. 295:17-25(2015).
RN [16]
RP FUNCTION, AND INDUCTION.
RX PubMed=27238022; DOI=10.1016/j.cell.2016.05.010;
RA Ye L., Allen W.E., Thompson K.R., Tian Q., Hsueh B., Ramakrishnan C.,
RA Wang A.C., Jennings J.H., Adhikari A., Halpern C.H., Witten I.B.,
RA Barth A.L., Luo L., McNab J.A., Deisseroth K.;
RT "Wiring and molecular features of prefrontal ensembles representing
RT distinct experiences.";
RL Cell 165:1776-1788(2016).
RN [17]
RP INTERACTION WITH ARNT AND ARNT2.
RX PubMed=27782878; DOI=10.7554/elife.18790;
RA Wu D., Su X., Potluri N., Kim Y., Rastinejad F.;
RT "NPAS1-ARNT and NPAS3-ARNT crystal structures implicate the bHLH-PAS family
RT as multi-ligand binding transcription factors.";
RL Elife 5:0-0(2016).
RN [18]
RP TISSUE SPECIFICITY, INDUCTION, AND UBIQUITINATION.
RX PubMed=26663079; DOI=10.1074/jbc.m115.704098;
RA Speckmann T., Sabatini P.V., Nian C., Smith R.G., Lynn F.C.;
RT "Npas4 transcription factor expression is regulated by calcium signaling
RT pathways and prevents tacrolimus-induced cytotoxicity in pancreatic beta
RT cells.";
RL J. Biol. Chem. 291:2682-2695(2016).
RN [19]
RP INDUCTION.
RX PubMed=27189618; DOI=10.1007/s12035-016-9912-4;
RA Choy F.C., Klaric T.S., Koblar S.A., Lewis M.D.;
RT "miR-744 and miR-224 downregulate Npas4 and affect lineage differentiation
RT potential and neurite development during neural differentiation of mouse
RT embryonic stem cells.";
RL Mol. Neurobiol. 54:3528-3541(2017).
CC -!- FUNCTION: Transcription factor expressed in neurons of the brain that
CC regulates the excitatory-inhibitory balance within neural circuits and
CC is required for contextual memory in the hippocampus (PubMed:18815592,
CC PubMed:22194569, PubMed:23029555, PubMed:24201284, PubMed:24855953).
CC Plays a key role in the structural and functional plasticity of neurons
CC (PubMed:23172225). Acts as an early-response transcription factor in
CC both excitatory and inhibitory neurons, where it induces distinct but
CC overlapping sets of late-response genes in these two types of neurons,
CC allowing the synapses that form on inhibitory and excitatory neurons to
CC be modified by neuronal activity in a manner specific to their function
CC within a circuit, thereby facilitating appropriate circuit responses to
CC sensory experience (PubMed:24201284, PubMed:24855953). In excitatory
CC neurons, activates transcription of BDNF, which in turn controls the
CC number of GABA-releasing synapses that form on excitatory neurons,
CC thereby promoting an increased number of inhibitory synapses on
CC excitatory neurons (PubMed:18815592, PubMed:22194569, PubMed:24201284).
CC In inhibitory neurons, regulates a distinct set of target genes that
CC serve to increase excitatory input onto somatostatin neurons, probably
CC resulting in enhanced feedback inhibition within cortical circuits
CC (PubMed:24855953). The excitatory and inhibitory balance in neurons
CC affects a number of processes, such as short-term and long-term memory,
CC acquisition of experience, fear memory, response to stress and social
CC behavior (PubMed:18815592, PubMed:22194569, PubMed:23029555,
CC PubMed:24201284, PubMed:27238022). Acts as a regulator of dendritic
CC spine development in olfactory bulb granule cells in a sensory-
CC experience-dependent manner by regulating expression of MDM2
CC (PubMed:25088421). Efficient DNA binding requires dimerization with
CC another bHLH protein, such as ARNT, ARNT2 or BMAL1 (PubMed:14701734,
CC PubMed:15363889, PubMed:19284974). Can activate the CME (CNS midline
CC enhancer) element (PubMed:14701734, PubMed:15363889).
CC {ECO:0000269|PubMed:14701734, ECO:0000269|PubMed:15363889,
CC ECO:0000269|PubMed:18815592, ECO:0000269|PubMed:22194569,
CC ECO:0000269|PubMed:23029555, ECO:0000269|PubMed:23172225,
CC ECO:0000269|PubMed:24201284, ECO:0000269|PubMed:24855953,
CC ECO:0000269|PubMed:25088421, ECO:0000269|PubMed:27238022}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein (PubMed:14701734, PubMed:15363889, PubMed:19284974).
CC Heterodimer; forms a heterodimer with ARNT, ARNT2 or BMAL1
CC (PubMed:14701734, PubMed:15363889, PubMed:19284974).
CC {ECO:0000269|PubMed:14701734, ECO:0000269|PubMed:15363889,
CC ECO:0000269|PubMed:19284974, ECO:0000269|PubMed:27782878}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:15363889, ECO:0000269|PubMed:24201284}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain (PubMed:14701734,
CC PubMed:15363889). Expressed in the limbic system and olfactory bulb
CC (PubMed:15363889, PubMed:25088421). Specifically expressed in CA1 and
CC CA3 region of the hippocampus after contextual learning (at protein
CC level) (PubMed:22194569, PubMed:23029555). Also expressed in pancreatic
CC beta cells (PubMed:26663079). {ECO:0000269|PubMed:14701734,
CC ECO:0000269|PubMed:15363889, ECO:0000269|PubMed:22194569,
CC ECO:0000269|PubMed:23029555, ECO:0000269|PubMed:25088421,
CC ECO:0000269|PubMed:26663079}.
CC -!- INDUCTION: Induced upon calcium influx (PubMed:26663079). Expression is
CC regulated by neuronal activity (at protein level) (PubMed:18815592,
CC PubMed:22194569, PubMed:24201284, PubMed:24855953). Induced in CA3
CC region of the hippocampus after contextual learning (PubMed:22194569).
CC Induced following sensory input in newborn olfactory bulb interneurons
CC (PubMed:25088421). Induced in the medial prefrontal cortex cells of the
CC brain following experiences with positive valence (PubMed:27238022).
CC Induced in pancreatic beta cells in response to calcium influx
CC (PubMed:26663079). Down-regulated by REST (PubMed:24291638).
CC Transcripts are regulated by a subset of miRNAs, such as miR-203, miR-
CC 224 and miR-744, that bind to its 3'-UTR region and down-regulate its
CC expression (PubMed:24291638, PubMed:27189618).
CC {ECO:0000269|PubMed:18815592, ECO:0000269|PubMed:22194569,
CC ECO:0000269|PubMed:24201284, ECO:0000269|PubMed:24291638,
CC ECO:0000269|PubMed:24855953, ECO:0000269|PubMed:25088421,
CC ECO:0000269|PubMed:26663079, ECO:0000269|PubMed:27189618,
CC ECO:0000269|PubMed:27238022}.
CC -!- PTM: Ubiquitinated, leading to degradation by the proteosome.
CC {ECO:0000269|PubMed:26663079}.
CC -!- DISRUPTION PHENOTYPE: Mice appear anxious and hyperactive, are prone to
CC seizures and have a shortened lifespan compared with their wild-type
CC littermates (PubMed:18815592, PubMed:19001414, PubMed:23029555,
CC PubMed:25549857). Mice show learning and memory deficits: while having
CC intact memories 5 minutes after training, memory is significantly
CC reduced one hour or 24 hours following training, suggesting that both
CC short-term memory and long-term memory are impaired (PubMed:22194569).
CC Mice show social and cognitive defects: they are hyperactive in a novel
CC environment, spend less time exploring, show higher social dominance
CC than their wild-type littermates and display pre-pulse inhibition,
CC working memory, long-term memory and cognitive flexibility deficits
CC (PubMed:23029555). When exposed to an enriched environment, a
CC significantly less frequent and slightly smaller amplitude inhibitory
CC postsynaptic current is observed (PubMed:24201284). Mice show a
CC reduction in the dendritic spine density in olfactory bulb granule
CC cells, leading to impaired odor discrimination learning
CC (PubMed:25088421). Mice also show increased vulnerability to juvenile
CC stress: mice exposed to chronic mild stress during adolescence, but not
CC during adulthood, develop prefrontal cortex-dependent cognitive
CC deficits in adulthood (PubMed:25911220). {ECO:0000269|PubMed:18815592,
CC ECO:0000269|PubMed:19001414, ECO:0000269|PubMed:22194569,
CC ECO:0000269|PubMed:23029555, ECO:0000269|PubMed:24201284,
CC ECO:0000269|PubMed:25088421, ECO:0000269|PubMed:25549857,
CC ECO:0000269|PubMed:25911220}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE20480.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB049835; BAC19831.1; -; mRNA.
DR EMBL; AB054577; BAC53755.1; -; Genomic_DNA.
DR EMBL; AY730724; AAV28629.1; -; mRNA.
DR EMBL; AK032607; BAE20480.1; ALT_FRAME; mRNA.
DR CCDS; CCDS29445.1; -.
DR RefSeq; NP_705781.1; NM_153553.5.
DR RefSeq; XP_006531783.1; XM_006531720.3.
DR RefSeq; XP_006531784.1; XM_006531721.3.
DR RefSeq; XP_011246921.1; XM_011248619.2.
DR AlphaFoldDB; Q8BGD7; -.
DR SMR; Q8BGD7; -.
DR BioGRID; 230436; 2.
DR STRING; 10090.ENSMUSP00000062992; -.
DR PhosphoSitePlus; Q8BGD7; -.
DR PaxDb; Q8BGD7; -.
DR PRIDE; Q8BGD7; -.
DR ProteomicsDB; 293945; -.
DR ABCD; Q8BGD7; 3 sequenced antibodies.
DR Antibodypedia; 30154; 209 antibodies from 31 providers.
DR DNASU; 225872; -.
DR Ensembl; ENSMUST00000056129; ENSMUSP00000062992; ENSMUSG00000045903.
DR GeneID; 225872; -.
DR KEGG; mmu:225872; -.
DR UCSC; uc008gbu.2; mouse.
DR CTD; 266743; -.
DR MGI; MGI:2664186; Npas4.
DR VEuPathDB; HostDB:ENSMUSG00000045903; -.
DR eggNOG; ENOG502QRXX; Eukaryota.
DR GeneTree; ENSGT00530000064165; -.
DR HOGENOM; CLU_013890_0_0_1; -.
DR InParanoid; Q8BGD7; -.
DR OMA; KTYFTQE; -.
DR OrthoDB; 219290at2759; -.
DR PhylomeDB; Q8BGD7; -.
DR TreeFam; TF319684; -.
DR BioGRID-ORCS; 225872; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Npas4; mouse.
DR PRO; PR:Q8BGD7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8BGD7; protein.
DR Bgee; ENSMUSG00000045903; Expressed in islet of Langerhans and 39 other tissues.
DR ExpressionAtlas; Q8BGD7; baseline and differential.
DR Genevisible; Q8BGD7; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071386; P:cellular response to corticosterone stimulus; IDA:MGI.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:UniProtKB.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; IMP:UniProtKB.
DR GO; GO:1904862; P:inhibitory synapse assembly; IMP:UniProtKB.
DR GO; GO:0007612; P:learning; IMP:UniProtKB.
DR GO; GO:0007616; P:long-term memory; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007614; P:short-term memory; IMP:UniProtKB.
DR GO; GO:0035176; P:social behavior; IMP:UniProtKB.
DR CDD; cd00130; PAS; 2.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR Pfam; PF08447; PAS_3; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55785; SSF55785; 2.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 2.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; Differentiation; DNA-binding; Neurogenesis;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..802
FT /note="Neuronal PAS domain-containing protein 4"
FT /id="PRO_0000248223"
FT DOMAIN 1..53
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 70..144
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 203..275
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 280..319
FT /note="PAC"
FT REGION 1..13
FT /note="Basic motif; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 14..53
FT /note="Helix-loop-helix motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 470..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..38
FT /evidence="ECO:0000255"
FT COILED 624..648
FT /evidence="ECO:0000255"
FT COMPBIAS 470..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 87286 MW; A38663C689FBEAB5 CRC64;
MYRSTKGASK ARRDQINAEI RNLKELLPLA EADKVRLSYL HIMSLACIYT RKGVFFAGGT
PLAGPTGLLS AQELEDIVAA LPGFLLVFTA EGKLLYLSES VSEHLGHSMV DLVAQGDSIY
DIIDPADHLT VRQQLTMPSA LDADRLFRCR FNTSKSLRRQ SSGNKLVLIR GRFHAHPPGA
YWAGNPVFTA FCAPLEPRPR PGPGPGPGPG PASLFLAMFQ SRHAKDLALL DVSESVLIYL
GFERSELLCK SWYGLLHPED LAQASSQHYR LLAESGDIQA EMVVRLQAKH GGWTWIYCML
YSEGPEGPFT ANNYPISDTE AWSLRQQLNS EDTQAAYVLG TPAVLPSFSE NVFSQEQCSN
PLFTPSLGTP RSASFPRAPE LGVISTPEEL PQPSKELDFS YLPFPARPEP SLQADLSKDL
VCTPPYTPHQ PGGCAFLFSL HEPFQTHLPP PSSSLQEQLT PSTVTFSEQL TPSSATFPDP
LTSSLQGQLT ESSARSFEDQ LTPCTSSFPD QLLPSTATFP EPLGSPAHEQ LTPPSTAFQA
HLNSPSQTFP EQLSPNPTKT YFAQEGCSFL YEKLPPSPSS PGNGDCTLLA LAQLRGPLSV
DVPLVPEGLL TPEASPVKQS FFHYTEKEQN EIDRLIQQIS QLAQGVDRPF SAEAGTGGLE
PLGGLEPLNP NLSLSGAGPP VLSLDLKPWK CQELDFLVDP DNLFLEETPV EDIFMDLSTP
DPNGEWGSGD PEAEVPGGTL SPCNNLSPED HSFLEDLATY ETAFETGVST FPYEGFADEL
HQLQSQVQDS FHEDGSGGEP TF
