ID   MCL1B_XENLA             Reviewed;         344 AA.
AC   P35805;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Protein L-Myc-1-B;
DE   AltName: Full=Protein L-Myc 2;
DE            Short=xL-Myc2;
GN   Name=mycl1-b; Synonyms=lmyc-b, lmyc2;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Oocyte;
RX   PubMed=8455622; DOI=10.1128/mcb.13.4.2456-2468.1993;
RA   Schreiber-Agus N., Torres R., Horner J., Lau A., Jamrich M., DePinho R.A.;
RT   "Comparative analysis of the expression and oncogenic activities of Xenopus
RT   c-, N-, and L-myc homologs.";
RL   Mol. Cell. Biol. 13:2456-2468(1993).
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Binds DNA as a heterodimer with MAX.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: High levels in oocytes, modest levels in kidney and
CC       low levels in spleen. {ECO:0000269|PubMed:8455622}.
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DR   EMBL; L11363; AAB59952.1; -; mRNA.
DR   AlphaFoldDB; P35805; -.
DR   SMR; P35805; -.
DR   Proteomes; UP000186698; Genome assembly.
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; 2.
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   DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..344
FT                   /note="Protein L-Myc-1-B"
FT                   /id="PRO_0000127338"
FT   DOMAIN          261..313
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          104..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..341
FT                   /note="Leucine-zipper"
FT   COMPBIAS        104..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  38540 MW;  445884BF445A33C3 CRC64;
     MDFSSCNNHY FYDVDMKEDF YRCIAPSEDI WKKFELVPGF PLSSGGCPGG GGTDWAAEMM
     DLGWESPVKL TGLSSVVLLR DCMWSGFSTR ERLEKVIHER LSTGSPRVTN TQKPVADNET
     SEPGVDSIEQ NATPLVVPTP IPEKVPNSSG SESTSDSEED EIDVVTVEKR KSYGGRQPVT
     ITVRADPTAT KLFHISIHQQ QHNYAARLPP EPNTMSPQHN FHSTVKEEPG EVTSPPELQP
     CSPQMPDSPL ASGSSDSEDL AKRKNHNYLE RKRRNDLRSR FLALREEVPS LSRSTKTPKV
     VVLSKATEFL KGLVIQEQQL TAEKLKLWSR HQQLLRRISQ LKGR