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Database: UniProt
Entry: Q9DFB9_ICTPU
LinkDB: Q9DFB9_ICTPU
Original site: Q9DFB9_ICTPU 
ID   Q9DFB9_ICTPU            Unreviewed;       390 AA.
AC   Q9DFB9;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Transcriptional regulator {ECO:0000256|PIRNR:PIRNR001705};
GN   Name=myc {ECO:0000313|EMBL:AAG14351.1,
GN   ECO:0000313|RefSeq:NP_001187019.1};
GN   Synonyms=myca {ECO:0000313|RefSeq:NP_001187019.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|EMBL:AAG14351.1};
RN   [1] {ECO:0000313|EMBL:AAG14351.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Barker K.S., Bengten E., Wilson M.R., Miller N.W., Warr G.W., Clem L.W.;
RT   "Catfish myc oncogene.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|RefSeq:NP_001187019.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA   Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA   Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA   Peatman E., Liu Z.;
RT   "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT   Seq analysis of a doubled haploid homozygote.";
RL   BMC Genomics 13:595-595(2012).
RN   [3] {ECO:0000313|RefSeq:NP_001187019.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Transcription factor that binds DNA in a non-specific manner,
CC       yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'.
CC       Activates the transcription of growth-related genes.
CC       {ECO:0000256|ARBA:ARBA00003607, ECO:0000256|PIRNR:PIRNR001705}.
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|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR001705}.
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DR   EMBL; AF283994; AAG14351.1; -; mRNA.
DR   RefSeq; NP_001187019.1; NM_001200090.1.
DR   STRING; 7998.ENSIPUP00000005992; -.
DR   GeneID; 100304504; -.
DR   KEGG; ipu:100304504; -.
DR   CTD; 30686; -.
DR   OrthoDB; 3039999at2759; -.
DR   Proteomes; UP000221080; Chromosome 23.
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; cd11458; bHLHzip_c-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; IPR003327; Myc-LZ.
DR   InterPro; IPR002418; Tscrpt_reg_Myc.
DR   InterPro; IPR012682; Tscrpt_reg_Myc_N.
DR   PANTHER; PTHR45851; MYC PROTO-ONCOGENE; 1.
DR   PANTHER; PTHR45851:SF1; MYC PROTO-ONCOGENE PROTEIN; 1.
DR   Pfam; PF00010; HLH; 1.
DR   Pfam; PF02344; Myc-LZ; 1.
DR   Pfam; PF01056; Myc_N; 1.
DR   PIRSF; PIRSF001705; Myc_protein; 1.
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   2: Evidence at transcript level;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR001705};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR001705}.
FT   DOMAIN          305..357
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   REGION          178..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..219
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  44696 MW;  2422D9A7DBD5D700 CRC64;
     MPMSSGLAWK NYDYDYDSVQ PYFYFDNDEE DFYKQLQQGQ APSEDIWKKF ELLPTPPLSP
     SRRPSTAEQL EIVSEFLGDD AVNQSFICDS DSSQTFLKSI IIQDCMWSGF SAVAKLEKVV
     SESSRRCTRR GKAYPRLPVV MQRDSSGVYL HDLSASECID PSMVFPYALT ESPKCAKLTA
     PADHAPPVDT PPNSGCSSDS DDEEEEDEED EEDDEEEIDV VTVEKRQRRS EAEVTESRQP
     SPLVLKRCHV STQQHNYAAQ PSTRHEHPVS KRPRLETSST GHGTIRHSKP RKCTSPRTSD
     SEDNDKRKTH NVLERQRRNE LKLSFFALRD EIPEVANNEK AAKVMILKKA AECIHSMQAD
     ERRLLSMKEQ LRRKSELLKH RLQQLRRSQL
//
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