NPS4A_DANRE
ID NPS4A_DANRE Reviewed; 933 AA.
AC Q1ECW2; Q5I7E4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Neuronal PAS domain-containing protein 4A {ECO:0000305};
DE Short=Neuronal PAS4A {ECO:0000305};
GN Name=npas4a; ORFNames=zgc:136764 {ECO:0000303|Ref.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 487-682.
RA Flood W.D., Lardelli M.T., Koblar S.A.;
RT "Zebrafish Nxf (zNxf).";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=25538572; DOI=10.3389/fnana.2014.00148;
RA Klaric T., Lardelli M., Key B., Koblar S., Lewis M.;
RT "Activity-dependent expression of neuronal PAS domain-containing protein 4
RT (npas4a) in the developing zebrafish brain.";
RL Front. Neuroanat. 8:148-148(2014).
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. Plays a key role
CC in the structural and functional plasticity of neurons. Acts as an
CC early-response transcription factor in both excitatory and inhibitory
CC neurons, where it induces distinct but overlapping sets of late-
CC response genes in these two types of neurons, allowing the synapses
CC that form on inhibitory and excitatory neurons to be modified by
CC neuronal activity in a manner specific to their function within a
CC circuit, thereby facilitating appropriate circuit responses to sensory
CC experience. {ECO:0000250|UniProtKB:Q8BGD7}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. {ECO:0000250|UniProtKB:Q8BGD7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8BGD7,
CC ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:25538572}.
CC -!- INDUCTION: Expression is regulated by neuronal activity.
CC {ECO:0000269|PubMed:25538572}.
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DR EMBL; BC117648; AAI17649.1; -; mRNA.
DR EMBL; AY847288; AAW31762.1; -; mRNA.
DR RefSeq; NP_001038786.1; NM_001045321.1.
DR AlphaFoldDB; Q1ECW2; -.
DR SMR; Q1ECW2; -.
DR STRING; 7955.ENSDARP00000072616; -.
DR PaxDb; Q1ECW2; -.
DR Ensembl; ENSDART00000078154; ENSDARP00000072616; ENSDARG00000055752.
DR GeneID; 724016; -.
DR KEGG; dre:724016; -.
DR CTD; 724016; -.
DR ZFIN; ZDB-GENE-060616-396; npas4a.
DR eggNOG; ENOG502QRXX; Eukaryota.
DR GeneTree; ENSGT00530000064165; -.
DR HOGENOM; CLU_013890_0_0_1; -.
DR InParanoid; Q1ECW2; -.
DR OMA; YCDERIE; -.
DR OrthoDB; 219290at2759; -.
DR PhylomeDB; Q1ECW2; -.
DR TreeFam; TF319684; -.
DR PRO; PR:Q1ECW2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000055752; Expressed in brain and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0001568; P:blood vessel development; IGI:ZFIN.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISS:UniProtKB.
DR GO; GO:0030900; P:forebrain development; IMP:ZFIN.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; ISS:UniProtKB.
DR GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007614; P:short-term memory; ISS:UniProtKB.
DR GO; GO:0035176; P:social behavior; ISS:UniProtKB.
DR CDD; cd00130; PAS; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF08447; PAS_3; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55785; SSF55785; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 1.
PE 2: Evidence at transcript level;
KW Activator; Differentiation; DNA-binding; Neurogenesis; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..933
FT /note="Neuronal PAS domain-containing protein 4A"
FT /id="PRO_0000248225"
FT DOMAIN 1..53
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 74..148
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 220..290
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 295..334
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 361..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 504
FT /note="C -> Y (in Ref. 2; AAW31762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 933 AA; 100102 MW; 397FC07000549D64 CRC64;
MYRSTKGASK ARRDQINAEI RNLKDLLPIS DADKSRLSYL HIMSLACMYT RKSVFFSQDI
TTASSAEETT GFLSFYELNE LIQGMPGFLL LLTGEGKLLY LSDSVSDHLG HSMVDLVAQG
DSVYDIIDTA DHFIMRSNLV PPTSPDTDRL FRCRFNTSKS VRRQSAGNKL VLIRARCLSQ
TPSESSPGSY WTSNPVWVCF CAPLEPHTSR GGTASDREST SASALESSFF LPCFRSQHSR
DMRLHEAQES VSVYLGLNVE ILRSQSWYSF LHPQDLSHAS AQHCSLLREG GEGRAEMVVR
VETADHSWVW LYMVLQLETG ETPIVSNNYI ISETEAWSVR QQLSSEQTQL SLVLGSSTSQ
QESVSLQSPE TLSSPDQVFT PGSSGLSGQS FDFSTAACST GSTEEQGGSS SMEPAQVESG
PRSSLSSMEE ETFFQHEPSE PMASPSSASS PIPVTVATVS DLDFLTQNIL LPPAFQIDPP
LPVLPLPLPP VPTSQAQQTK EFVCTPPYTP QLGGSNFPFG EPHFSFDPTG ATSPPPLGQT
ATVTTTTAPS LSPSAPSNPQ SSPPPPTTTL SSLLPLTITS PTTEILFPVE PCSGSLYEKL
PPTPDSPGDG DCTVMTLPEV RGPLYVDVPH GPLPYPPEGL LTPEASPGKQ PSLPFFSSLR
DREKERTEIS LLAQHISTLA EGFYLDPLLA KLVPSTLSEH SQSPDSDGLD SIPLLGEFYP
LKSWKGLDLP IFQDDESLFE ESVLETLLQD LSSSPPLSPT PSSSSHSSPP SSPSTPECWC
PSLHFDGVSA VSAGHFCSVQ SAHCNNEAGR GAMMSPVNAG NMTDTKAAGE VPMETDVASS
PLFTGIPTSP PLQLTASPAS PILMPVSSPV SPPSPGLPCA QSLLEELAAL EPMFGAGASI
APGLGQQPEL YQLQSHVPQQ CFRKDGSGSD PPF
