ID A0A060XWV0_ONCMY Unreviewed; 355 AA.
AC A0A060XWV0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=BHLH domain-containing protein {ECO:0000259|PROSITE:PS50888};
GN ORFNames=GSONMT00012457001 {ECO:0000313|EMBL:CDQ83986.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ83986.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ83986.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ83986.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MAX.
CC {ECO:0000256|ARBA:ARBA00025872}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR001705}.
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DR EMBL; FR906303; CDQ83986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060XWV0; -.
DR STRING; 8022.A0A060XWV0; -.
DR PaxDb; 8022-A0A060XWV0; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd11457; bHLHzip_L-Myc; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR002418; Tscrpt_reg_Myc.
DR InterPro; IPR012682; Tscrpt_reg_Myc_N.
DR PANTHER; PTHR45851; MYC PROTO-ONCOGENE; 1.
DR PANTHER; PTHR45851:SF5; PROTEIN L-MYC-RELATED; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF01056; Myc_N; 2.
DR PIRSF; PIRSF001705; Myc_protein; 2.
DR PRINTS; PR00044; LEUZIPPRMYC.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR001705};
KW Nucleus {ECO:0000256|PIRNR:PIRNR001705};
KW Reference proteome {ECO:0000313|Proteomes:UP000193380}.
FT DOMAIN 270..322
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 158..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 355 AA; 40118 MW; E1C55A1BF82D4924 CRC64;
MEYDRYQHYF LDDLDKEEDF YKSTAPSEDI WKKFELLPTP PMSPTRTLDK FGWLSKVLGQ
DEEYEGPDTE ELFGNMSSII IQDCMWSSFS ASQHLEKVNE RLSAAAQARL SPPAPQNFAT
VSKVQCTLPT QPDATLPSTV AECVDPASVL TFPAISCRKP ASSGSESRSD SSDDDDDEID
VVTVESKQSR ARLLGSRKAV TVTVRADPCP QRFHMSVHQQ QHNYAAPSPE SDPEEEDEEP
QCKRFYSPAS ISPQGSSADS PQSSDAEDTD RRKNHNFLER KRRNDLRSRF LALRDEIPGL
VESAKTPKVA ILTQATEYLL QLHSREKHQA QERKRLKARQ QQLLQRLATL KRSLG
//
