ID   MCL1A_DANRE             Reviewed;         372 AA.
AC   Q9PSI9; Q6NW51;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Protein L-Myc-1a;
DE   AltName: Full=Protein L-Myc 1;
DE            Short=zL-Myc;
GN   Name=mycl1a {ECO:0000312|EMBL:AAH67723.1}; Synonyms=lmyc1, mycl1;
GN   ORFNames=zgc:85967;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000312|EMBL:AAH67723.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH67723.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 36-113, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo {ECO:0000269|PubMed:8474440};
RX   PubMed=8474440; DOI=10.1128/mcb.13.5.2765-2775.1993;
RA   Schreiber-Agus N., Horner J., Torres R., Chiu F.-C., DePinho R.A.;
RT   "Zebra fish myc family and max genes: differential expression and oncogenic
RT   activity throughout vertebrate evolution.";
RL   Mol. Cell. Biol. 13:2765-2775(1993).
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 {ECO:0000250|UniProtKB:P12524,
CC       ECO:0000255|PROSITE-ProRule:PRU00981}.
CC   -!- TISSUE SPECIFICITY: Uterus. {ECO:0000269|PubMed:8474440}.
CC   -!- DEVELOPMENTAL STAGE: Most abundant during early rapid cleavage,
CC       blastulation, and gastrulation. Reduced levels from time of
CC       establishment of the body plan (around 12 hours) and thereafter.
CC       {ECO:0000269|PubMed:8474440}.
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DR   EMBL; BC067723; AAH67723.1; -; mRNA.
DR   PIR; E48059; E48059.
DR   RefSeq; NP_998102.1; NM_212937.1.
DR   AlphaFoldDB; Q9PSI9; -.
DR   SMR; Q9PSI9; -.
DR   STRING; 7955.ENSDARP00000011307; -.
DR   PaxDb; Q9PSI9; -.
DR   Ensembl; ENSDART00000013961; ENSDARP00000011307; ENSDARG00000006003.
DR   GeneID; 405873; -.
DR   KEGG; dre:405873; -.
DR   CTD; 405873; -.
DR   ZFIN; ZDB-GENE-040426-2439; mycla.
DR   eggNOG; ENOG502QWSU; Eukaryota.
DR   GeneTree; ENSGT00940000158613; -.
DR   HOGENOM; CLU_052560_0_0_1; -.
DR   InParanoid; Q9PSI9; -.
DR   OMA; TEQRRNF; -.
DR   OrthoDB; 877891at2759; -.
DR   PhylomeDB; Q9PSI9; -.
DR   TreeFam; TF106001; -.
DR   PRO; PR:Q9PSI9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 13.
DR   Bgee; ENSDARG00000006003; Expressed in cleaving embryo and 43 other tissues.
DR   ExpressionAtlas; Q9PSI9; baseline and differential.
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; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0032502; P:developmental process; IEA:UniProt.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..372
FT                   /note="Protein L-Myc-1a"
FT                   /id="PRO_0000127336"
FT   DOMAIN          289..341
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          172..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..369
FT                   /note="Leucine-zipper"
FT   COMPBIAS        268..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        64
FT                   /note="I -> R (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69..76
FT                   /note="LGWAPPKV -> WVGAAEG (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   372 AA;  41380 MW;  A21893144C7C3198 CRC64;
     MPGVNTQTLY GWDMEHYFYD EMDTEEDFFK STAPSEDIWK KFELLPTPPM SPSRTLDGDW
     LFPIPGDRLG WAPPKVLTCD EEYEGLHKFD PLDIFGNLGS IVIKDCMWSG LSTSHRLEKV
     AHGERAPVAA LIQNSTAQKA ARAASGTPVT GSQAAQCVSP AAVLELPVPH KKVAAGSSGS
     ECRSDSSDDD EDDDEIDVVT VDNRPKRGRP PSRRTPVTIT VSADPFGPCP KRFHVSLHRQ
     QHNYAAPSPD TDPEDDFEIE PVSKRPRLES SSAPSSPLSS PATSDSEDST EQRRNFLERK
     RRDDLRSRFQ ALREEIPGLS GSSKTSKVAI LTQATDYLLQ LHSSQRRQAQ EKRKLKAKQQ
     QLLRRISALQ NS