MCL1A_XENLA
ID MCL1A_XENLA Reviewed; 344 AA.
AC Q05404; Q5U4W8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein L-Myc-1-A;
DE AltName: Full=Protein L-Myc 1;
DE Short=xL-Myc1;
GN Name=mycl1-a; Synonyms=lmyc-a, lmyc1, mycl1;
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=Blastula;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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; L11362; AAA49994.1; -; mRNA.
DR EMBL; BC084925; AAH84925.1; -; mRNA.
DR PIR; A48101; A48101.
DR RefSeq; NP_001081340.1; NM_001087871.1.
DR AlphaFoldDB; Q05404; -.
DR SMR; Q05404; -.
DR DNASU; 397783; -.
DR GeneID; 397783; -.
DR KEGG; xla:397783; -.
DR CTD; 397783; -.
DR Xenbase; XB-GENE-6252588; mycl.L.
DR OrthoDB; 877891at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 397783; Expressed in blastula and 17 other tissues.
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-A"
FT /id="PRO_0000127337"
FT DOMAIN 261..313
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 100..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..341
FT /note="Leucine-zipper"
FT COMPBIAS 235..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 133
FT /note="N -> T (in Ref. 1; AAA49994)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="K -> R (in Ref. 1; AAA49994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38389 MW; 90B38BABB874C785 CRC64;
MDVGSCNNHY FYDVDMKEDF YRCIAPSEDI WKKFELVPGF PLSPGGCPGG GGTDWGAELM
DLGWESPMKL TGLSSVVLLR DCMWSGFSTR ERLEKVIHER LTTASPRATN PQKPVADHEN
SEPGVNSIEQ NANPLVVPTP VPEKVPNSSG SESTSDSEDD EIDVVTIEKR KSYGGRQPVT
ITVRADPTAT KLFHISIHQQ QHNYAARLPP EPNSMSPQPN FHSPIKEEPG EVTSPPALQQ
CSSPMPGSPL ASGSSDSEDI VKKKNHNYLE RKRRNDLRSR FLALREEVPS LTRSTKTPKV
VVLSKATEFL KGLVIQEQQL TAEKFKLWSR HQQLLRRISH LKGR
