GenomeNet

Database: UniProt
Entry: A0A2U9CVE6_SCOMX
LinkDB: A0A2U9CVE6_SCOMX
Original site: A0A2U9CVE6_SCOMX 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system