MYCA_DANRE
ID MYCA_DANRE Reviewed; 408 AA.
AC P52160; Q7T2P1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Transcriptional regulator Myc-A;
DE Short=c-Myc-A;
DE Short=zc-Myc;
GN Name=myca; Synonyms=cmyc, myc;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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 -!- TISSUE SPECIFICITY: High levels are seen in the kidney, gills and
CC uterus. {ECO:0000269|PubMed:8474440}.
CC -!- DEVELOPMENTAL STAGE: Found in low abundance in the two-cell through
CC early somite stages (<1.5 through 12 hours) and increases during later
CC stages of growth and organ development. {ECO:0000269|PubMed:8474440}.
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; L11710; AAA02482.1; -; mRNA.
DR EMBL; BC053281; AAH53281.1; -; mRNA.
DR PIR; A48059; A48059.
DR RefSeq; NP_571487.2; NM_131412.1.
DR AlphaFoldDB; P52160; -.
DR SMR; P52160; -.
DR STRING; 7955.ENSDARP00000100455; -.
DR PaxDb; P52160; -.
DR GeneID; 30686; -.
DR KEGG; dre:30686; -.
DR CTD; 30686; -.
DR ZFIN; ZDB-GENE-990415-162; myca.
DR eggNOG; KOG2483; Eukaryota.
DR InParanoid; P52160; -.
DR OrthoDB; 877891at2759; -.
DR PhylomeDB; P52160; -.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR Reactome; R-DRE-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
DR SignaLink; P52160; -.
DR PRO; PR:P52160; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
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 GO; GO:0060218; P:hematopoietic stem cell differentiation; IGI:ZFIN.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:1901342; P:regulation of vasculature development; IGI:ZFIN.
DR GO; GO:0001944; P:vasculature development; IMP:ZFIN.
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; Glycoprotein; Nucleus; Proto-oncogene;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..408
FT /note="Transcriptional regulator Myc-A"
FT /id="PRO_0000127314"
FT DOMAIN 324..376
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 188..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..404
FT /note="Leucine-zipper"
FT MOTIF 76..84
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT COMPBIAS 205..234
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CONFLICT 194
FT /note="D -> H (in Ref. 1; AAA02482)"
FT /evidence="ECO:0000305"
FT CONFLICT 215..217
FT /note="Missing (in Ref. 1; AAA02482)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="S -> SS (in Ref. 1; AAA02482)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="Q -> R (in Ref. 1; AAA02482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 46710 MW; 3CC14D97DBAD38B6 CRC64;
MPVSASLACK NYDYDYDSIQ PYFYFDNDDE DFYHHQQGQT QPSAPSEDIW KKFELLPTPP
LSPSRRQSLS TAEQLEMVSE FLGDDVVSQS FICDDADYSQ SFIKSIIIQD CMWSGFSAAA
KLEKVVSERL ASLHAERKEL MSDSNSNRLN ASYLQDLSTS ASECIDPSVV FPYPLTECGK
AGKVASPQPM LVLDTPPNSS SSSGSDSEDE EEEDEEEEEE EEEEEEEEEE EEIDVVTVEK
RQKRHETDAS ESRYPSPLVL KRCHVSTHQH NYAAHPSTRH DQPAVKRLRL EASNNHSINS
SSSNRHVKQR KCASPRTSDS EDNDKRRTHN VLERQRRNEL KLSFFALRDE IPEVANNEKA
AKVVILKKAT ECIHSMQLDE QRLLSIKEQL RRKSEQLKHR LQQLRSSH
