ID W5MTC3_LEPOC Unreviewed; 955 AA.
AC W5MTC3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Neuronal PAS domain protein 3 {ECO:0000313|Ensembl:ENSLOCP00000011632.1};
GN Name=NPAS3 {ECO:0000313|Ensembl:ENSLOCP00000011632.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000011632.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000011632.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01003861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01003862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01003863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015206013.1; XM_015350527.1.
DR AlphaFoldDB; W5MTC3; -.
DR STRING; 7918.ENSLOCP00000011632; -.
DR Ensembl; ENSLOCT00000011649.1; ENSLOCP00000011632.1; ENSLOCG00000009512.1.
DR GeneID; 102683864; -.
DR KEGG; loc:102683864; -.
DR CTD; 64067; -.
DR eggNOG; KOG3558; Eukaryota.
DR GeneTree; ENSGT00940000158051; -.
DR HOGENOM; CLU_009542_1_0_1; -.
DR InParanoid; W5MTC3; -.
DR OMA; PFRRTHY; -.
DR OrthoDB; 5396877at2759; -.
DR Proteomes; UP000018468; Linkage group LG7.
DR Bgee; ENSLOCG00000009512; Expressed in brain and 11 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd19732; bHLH-PAS_NPAS3_PASD6; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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 PANTHER; PTHR23043; HYPOXIA-INDUCIBLE FACTOR 1 ALPHA; 1.
DR PANTHER; PTHR23043:SF30; NEURONAL PAS DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 89..142
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT DOMAIN 185..255
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 372..427
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT REGION 17..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..649
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 103334 MW; 5182192F1097C827 CRC64;
MIRIFPDFSV QVTAAAAGGA GGVPGAPGVS RVPGTSNGSP QNVQGISSYQ QSDPYWERPA
NASSCSASRP KTLHLGGQQH TSSPWLQALR KEKSRDAARS RRGKENFEFY ELAKLLPLPG
AITSQLDKAS IIRLTISYLK MRDFANQGDP PWNLRIEGPP PNTSVKAIGA QRRRSPSVVA
TEIFEQHLGS HILQSLDGFV FALNKEGKFL YISETVSIYL GLSQVELTGS SVFDYVHPGD
HVEMAEQLGM KLPPGRGLLS QGTAEDGASS ASSSSQSETP EPVESTSPSL LAPDNTLERS
FFIRMKSTLT KRGVHIKSSG YKVIHITGRL RIRLSLTHGR TVPNQIMGMV VVAHALPPPT
INEVRIDCQM FVTRVNMDLN IVYCENRISD YMDLTPVDIV GKRCYHFIHA EDVEGIRHSH
LDLMNKGQCV TKYYRWIQKN GGYIWIQSSA TIAINAKNAN EKNIIWVNYV LSNPEYKDTP
MDIAQLPNLP EKASESSETS DSDSDSKENS EDNENSKSDG KGNQSENSED PESDSKKQPG
NPSDNEMNCN EDGNSSSNQE SQDSEDSFEP SDYESSKAAE EDGFGALDSM HIKVERYAEG
EAELRLPGRE SVTSDSAKDS DSAGEASTPS SSKHQKRKKR RKKQKGGSVT RRRLSSTSSP
SGLDPAIADQ PQLLSSPNSA SVLKIKTEIS EPINFDNDSS IWNYPPNREI SRNESPYSMT
KPPSSDHFPS PQASSSSLQV AIPDSVLTPP GAESSGSRKT QFGGGATSAS SAASLPPVSS
SDPLSPPLSA SPRDKQQGTP STSSSLLYAG DLEALQRLQA GNVVLPLVHR VTGTLAATST
AAQRVYTTGT IRYAPAEVTL AMQGNLLPNT HAVNFVDVNS SGFGIDPKTP MEMLYHHVHR
LNMSGPFGAA VSAASLTQMP AGNVFTTAEG LFSTLPFPVY SNGIHTTQTL ERKED
//
