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NPAS3_MOUSE
ID   NPAS3_MOUSE             Reviewed;         925 AA.
AC   Q9QZQ0; Q9EQP4;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 147.
DE   RecName: Full=Neuronal PAS domain-containing protein 3;
DE            Short=Neuronal PAS3;
DE   AltName: Full=Basic-helix-loop-helix-PAS protein MOP6;
DE   AltName: Full=Member of PAS protein 6;
GN   Name=Npas3; Synonyms=Mop6;
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 [MRNA].
RX   PubMed=10534623; DOI=10.1016/s0925-4773(99)00182-3;
RA   Brunskill E.W., Witte D.P., Shreiner A.B., Potter S.S.;
RT   "Characterization of Npas3, a novel basic helix-loop-helix PAS gene
RT   expressed in the developing mouse nervous system.";
RL   Mech. Dev. 88:237-241(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 141-280.
RA   Thomas R.S., Bradfield C.A.;
RT   "Cloning and chromosomal localization of MOP6.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15347806; DOI=10.1073/pnas.0405310101;
RA   Erbel-Sieler C., Dudley C., Zhou Y., Wu X., Estill S.J., Han T.,
RA   Diaz-Arrastia R., Brunskill E.W., Potter S.S., McKnight S.L.;
RT   "Behavioral and regulatory abnormalities in mice deficient in the NPAS1 and
RT   NPAS3 transcription factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13648-13653(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5] {ECO:0007744|PDB:5SY7}
RP   X-RAY CRYSTALLOGRAPHY (4.20 ANGSTROMS) OF 56-455 IN COMPLEXES WITH ARNT AND
RP   DNA, INTERACTION WITH ARNT, HETERODIMERIZATION, AND REGION.
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).
CC   -!- FUNCTION: May play a broad role in neurogenesis. May control regulatory
CC       pathways relevant to schizophrenia and to psychotic illness.
CC       {ECO:0000269|PubMed:15347806}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Interacts with ARNT; forms a heterodimer that binds core DNA
CC       sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of
CC       target gene promoters (PubMed:27782878). {ECO:0000269|PubMed:27782878}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC       ECO:0000269|PubMed:15347806}.
CC   -!- TISSUE SPECIFICITY: Detected exclusively in adult brain in inhibitory
CC       interneurons.
CC   -!- DEVELOPMENTAL STAGE: Expression detected between 9.5 and 11.5 dpc in
CC       the developing neural tube. Was also expressed throughout the
CC       neuroepithelium of the developing central nervous system between 10. 5
CC       and 12.5 dpc at 14.5 dpc, the expression became restricted to the
CC       neopallial layer of the cortex. At 12.5 dpc, expression was evident in
CC       nonneural tissues such as the developing dermis and mesenchyme
CC       surrounding the otic and nasal placodes. Expression was also detected
CC       in the developing cardiac valves, limb and developing kidney.
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DR   EMBL; AF173871; AAF14283.1; -; mRNA.
DR   EMBL; AF168769; AAG35181.1; -; mRNA.
DR   PDB; 5SY7; X-ray; 4.20 A; B=56-455.
DR   PDBsum; 5SY7; -.
DR   AlphaFoldDB; Q9QZQ0; -.
DR   SMR; Q9QZQ0; -.
DR   STRING; 10090.ENSMUSP00000098975; -.
DR   iPTMnet; Q9QZQ0; -.
DR   PhosphoSitePlus; Q9QZQ0; -.
DR   MaxQB; Q9QZQ0; -.
DR   PaxDb; Q9QZQ0; -.
DR   PRIDE; Q9QZQ0; -.
DR   ProteomicsDB; 295509; -.
DR   MGI; MGI:1351610; Npas3.
DR   eggNOG; KOG3558; Eukaryota.
DR   InParanoid; Q9QZQ0; -.
DR   PhylomeDB; Q9QZQ0; -.
DR   ChiTaRS; Npas3; mouse.
DR   PRO; PR:Q9QZQ0; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9QZQ0; protein.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0042711; P:maternal behavior; IGI:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0001964; P:startle response; IGI:MGI.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   PROSITE; PS50888; BHLH; 1.
DR   PROSITE; PS50112; PAS; 2.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..925
FT                   /note="Neuronal PAS domain-containing protein 3"
FT                   /id="PRO_0000127409"
FT   DOMAIN          58..111
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   DOMAIN          152..222
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          324..394
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          398..441
FT                   /note="PAC"
FT   REGION          60..71
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000269|PubMed:27782878"
FT   REGION          119..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..548
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..617
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..699
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        141
FT                   /note="R -> L (in Ref. 2; AAG35181)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156
FT                   /note="G -> E (in Ref. 2; AAG35181)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        166
FT                   /note="F -> L (in Ref. 2; AAG35181)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   925 AA;  100458 MW;  B6B07C9B6755B938 CRC64;
     MGRAGAAANG TPQNVQGITS YQQRITAQHP LPNQSECRKI YRYDGIYCES TYQNLQALRK
     EKSRDAARSR RGKENFEFYE LAKLLPLPAA ITSQLDKASI IRLTISYLKM RDFANQGDPP
     WNLRMEGPPP NTSVKGAQRR RSPSALAIEV FEAHLGSHIL QSLDGFVFAL NQEGKFLYIS
     ETVSIYLGLS QVELTGSSVF DYVHPGDHVE MAEQLGMKLP PGRGLLSQGT TEDAASSASS
     SSQSETPEPV ETTSPSLLTT DNTLERSFFI RMKSTLTKRG VHIKSSGYKV IHITGRLRLR
     VPLSHGRTVP SQIMGLVVVA HALPPPTINE VRIDCHMFVT RVNMDLNIIY CENRISDYMD
     LTPVDIVGKR CYHFIHAEDV EGIRHSHLDL LNKGQCVTKY YRWMQKNGGY IWIQSSATIA
     INAKNANEKN IIWVNYLLSN PEYKDTPMDI AQLPHLPEKA SESSETSDSE SDSKDTSGIT
     EDNENSKSDE KGNQSENSED PEPDRKKSGS ACDNDMNCND DGHSSSNPDS RDSDDSFEHS
     DFEHPKAAED GFGALGPMQI KVERYVESEA DLRLQPCESL TSDSAKDSDS ANEAGAQASS
     KHQKRKRRRK RQKGGSASRR RLSSASSPGL DAGLVEPPRL LSSPHSASVL KIKTEIAEPI
     NFDNESSIWN YPPNREISRN ESPYSMTKPP TSEHFPSPQG QGGSIGGGGA LHVAIPDSVL
     TPPGADGTAG RKTQFSGTAP VPSDPLSPPL SASPRDKHPG GGAGSGGGGP GASNSLLYTG
     DLEALQRLQA GNVVLPLVHR VTGTLAATST AAQRVYTTGT IRYAPAEVTL AMQGNLLPNA
     HAVNFVDVNS PGFGLDPKTP MEMLYHHVHR LNMSGPFGGA VSAASLTQMP GGNVFTTAEG
     LFSTLPFPVY SNGIHAAQTL ERKED
 
 
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