ID A0A2U9CVE6_SCOMX Unreviewed; 415 AA.
AC A0A2U9CVE6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Putative N-myc proto-oncogene protein {ECO:0000313|EMBL:AWP20123.1};
GN ORFNames=SMAX5B_019681 {ECO:0000313|EMBL:AWP20123.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP20123.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP20123.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) 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; CP026262; AWP20123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CVE6; -.
DR STRING; 52904.ENSSMAP00000028428; -.
DR Proteomes; UP000246464; Chromosome 20.
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; cd11456; bHLHzip_N-Myc_like; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
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:SF2; N-MYC PROTO-ONCOGENE PROTEIN; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF01056; Myc_N; 1.
DR PIRSF; PIRSF001705; Myc_protein; 1.
DR PRINTS; PR00044; LEUZIPPRMYC.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR001705};
KW Nucleus {ECO:0000256|PIRNR:PIRNR001705};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 332..384
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 191..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 374..415
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 193..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..249
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 45795 MW; 15C5CF394C0FE163 CRC64;
MPAVTSKNSD LEFDSLQPCF YPDEDDFYFC GPDSAPPGED IWKKFELLPT PPLSPSRAAL
PGEPATADQE ADPLGFGLGD PLDWASELLL LPEDDIWGAS DDGDLFGSAL DTNPNSIIIQ
DCMWSGFSAR EKLERVVTEK LGKAISTAAA GGRSACVKAP EVVSSSSSSS MSECVDPAVV
FPFPVHKKNG SRVSCGAVNT PTAHGSASSD SEEEDDDEAE EEEDDDEEDD EEDEDEEDED
EDEEEEEIDV VTVEKRRSTI NKASPMATGT VTVSVHPKSQ DELILKRSSV HQQQHNYAAP
SPSVTCASGP RSKRSSSGDS SPRGSSDSED SERRRNHNIL ERQRRNDLRS SFLTLRDHVP
ELAHNEKAAK VLILKKATEY VSSLETEEMR LQQERDRLQA RRQQLMRRLE HARTR
//