ID   MYCB_XENLA              Reviewed;         420 AA.
AC   P15171;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Transcriptional regulator Myc-B;
DE   AltName: Full=c-Myc II;
GN   Name=myc-b; Synonyms=myc2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyte;
RX   PubMed=2686981; DOI=10.1002/j.1460-2075.1989.tb08593.x;
RA   Vriz S., Taylor M., Mechali M.;
RT   "Differential expression of two Xenopus c-myc proto-oncogenes during
RT   development.";
RL   EMBO J. 8:4091-4097(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Oocyte;
RX   PubMed=2057364; DOI=10.1093/nar/19.11.3081;
RA   Principaud E., Spohr G.;
RT   "Xenopus laevis c-myc I and II genes: molecular structure and developmental
RT   expression.";
RL   Nucleic Acids Res. 19:3081-3088(1991).
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:0000250|UniProtKB:P01106}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Binds DNA as a heterodimer with MAX (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DEVELOPMENTAL STAGE: C-MYC I is active in oocytes, while C-MYC II is
CC       active in both oocytes and post-gastrula embryos.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000250|UniProtKB:P01106}.
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DR   EMBL; X14807; CAA32912.1; -; mRNA.
DR   EMBL; X56870; CAA40194.1; -; mRNA.
DR   EMBL; X56872; CAA40196.1; -; Genomic_DNA.
DR   PIR; S12484; S12484.
DR   RefSeq; NP_001084122.1; NM_001090653.1.
DR   AlphaFoldDB; P15171; -.
DR   SMR; P15171; -.
DR   DNASU; 399315; -.
DR   GeneID; 399315; -.
DR   KEGG; xla:399315; -.
DR   CTD; 399315; -.
DR   Xenbase; XB-GENE-6256575; myc.L.
DR   OrthoDB; 877891at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 399315; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
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; IPR003327; Myc-LZ.
DR   InterPro; IPR002418; Tscrpt_reg_Myc.
DR   InterPro; IPR012682; Tscrpt_reg_Myc_N.
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; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..420
FT                   /note="Transcriptional regulator Myc-B"
FT                   /id="PRO_0000127320"
FT   DOMAIN          336..388
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          141..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..416
FT                   /note="Leucine-zipper"
FT   MOTIF           78..86
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P01106"
FT   COMPBIAS        141..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..245
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        185
FT                   /note="C -> W (in Ref. 2; CAA40194)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        324
FT                   /note="C -> Y (in Ref. 2; CAA40194)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        365..367
FT                   /note="RWR -> EVA (in Ref. 2; CAA40194)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   420 AA;  47861 MW;  B2FCB353B6AA3EAF CRC64;
     MPLNANFPSK NYDYDYDLQP CFFFLEEENF YHQQSRLQPP APSEDIWKKF ELLPTPPLSP
     SRRSSQSSLF PSTADQLEMV TEFLGGDMVN QSFICEADDE ALLKSIVIQD CMWSGFSAAA
     KLEKVVSEKL ASYQASRKES ALSTSQCQSQ PPQSPLKSPS CDGSLNLGGT NRSSHEFLQD
     PSSDCVDPSV VFPYPLNDSI SNASSPCQDL MLETPPISSN SSSSESEDEQ EDDDDDEDCD
     EEEEIDVVTV EKRQTASRRM ESGSHSQSSR PHHSPLVLKR CHVPIHQHNY AASPSTKVDY
     VSSKRAKLES NVRVLKQISN NRKCASPRSS DSEENDKRRT HNVLERQRRN ELKLSFFALR
     DQVPRWRNNE KAPKVVILKK ATEYAISMQE DERRLIRETE QLKYRKEQLK QRLQQLRNSV