ID   MYC2_OTOBE              Reviewed;         454 AA.
AC   Q64210;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=N-myc 2 proto-oncogene protein;
GN   Name=N-MYC2;
OS   Otospermophilus beecheyi (California ground squirrel) (Spermophilus
OS   beecheyi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Otospermophilus.
OX   NCBI_TaxID=34862;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RV53; TISSUE=Liver;
RX   PubMed=8649862;
RA   Quignon F., Renard C.A., Tiollais P., Buendia M.-A., Transy C.;
RT   "A functional N-myc2 retroposon in ground squirrels: implications for
RT   hepadnavirus-associated carcinogenesis.";
RL   Oncogene 12:2011-2017(1996).
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR   EMBL; X93018; CAA63600.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q64210; -.
DR   SMR; Q64210; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   Gene3D; 4.10.280.10; -; 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   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; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Nucleus; Proto-oncogene.
FT   CHAIN           1..454
FT                   /note="N-myc 2 proto-oncogene protein"
FT                   /id="PRO_0000127332"
FT   DOMAIN          371..423
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          133..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          423..444
FT                   /note="Leucine-zipper"
FT   COMPBIAS        256..270
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  49713 MW;  D533CAFF61E79C38 CRC64;
     MRSCTVSTMP RMICRNADLE FDWLQPCFYP DEDDFYFSGP NSTPPGEDIW KKFELLPTPP
     LSPSCAFLEL STEPSDWASE MMLTEADLWG NPDEEDVFGP GGLGSLTPNP VILRDCMWSG
     FSAREKLERA MSEKMQHGHE PAATGPATQV PGAGAASTAG RGHSGTAGAA LPAELAHPAA
     ECVDPAVVFL LPVSKRNPVP VRVAPARAPA RAPAVGAAVA RAAAPASAAV AAPPGLSSRP
     PNGGDHKVLS TSGEDALSDE VDEEEDEEEE IDVVTVEKSC KTGGTTFTLT VSPKNTALGL
     RREQSRELIL QRSVPIYQQH NYAAPSPYVE NEDAPPQKKI KREVSPHPLK SVIHPKGKSF
     SPRKSDSEDS VRRRNHNILE RQRRNDLRSS FTTLRDHVPE LVKNEKAAKV VILKKACEYV
     HYLQAKEHQL LMEKEKLQAR QQQLLKIIEL AWTF