MYC_CARAU
ID MYC_CARAU Reviewed; 399 AA.
AC P49709;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Transcriptional regulator Myc;
DE Short=c-Myc;
GN Name=myc;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zhang H., Zhang H., Okamoto N., Ikeda Y.;
RT "Cloning and sequencing of a c-myc gene from goldfish Carassius autatus.";
RL Submitted (JUN-1994) 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.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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; D31729; BAA06527.1; -; Genomic_DNA.
DR AlphaFoldDB; P49709; -.
DR SMR; P49709; -.
DR PRIDE; P49709; -.
DR Ensembl; ENSCART00000123522; ENSCARP00000110425; ENSCARG00000056880.
DR Proteomes; UP000515129; Genome assembly.
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 GO; GO:0032502; P:developmental process; IEA:UniProt.
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 3: Inferred from homology;
KW Activator; DNA-binding; Glycoprotein; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..399
FT /note="Transcriptional regulator Myc"
FT /id="PRO_0000127315"
FT DOMAIN 315..367
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 177..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..395
FT /note="Leucine-zipper"
FT MOTIF 76..84
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT COMPBIAS 177..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..249
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"
SQ SEQUENCE 399 AA; 45756 MW; FC4B2CEC361F1D42 CRC64;
MPVSASLAYK NYDYDYDSIQ PYFYFDNDDE DFYHHQQGQP QPPAPSEDIW KKFELLPTPP
LSPSRRQSLS TAEQLEMVSE FLGDDVVNQS FICDADYSQS FIKSIIIQDC MWSGFSAAAK
LEKAVSERLA SLHAARKELI SDSSSNRLSA SYLQDLSTSA SECIDPSVVF PYPLTESSKS
NKVAPSQPML VLDTPPNSSS SSGSDSEDEE EEEEEEEEEE EEEEEEEEEE EIDVVTVEKR
QKRNEADVSD SRYPSPLVLK RCHVSTHQHN YAAHPSTRHD QPAVKRLRLE TSSSNRHGKQ
RKCTSPRTSD SEDNDKRRTH NVLERQRRNE LKLSFFALRD EIPEVANNEK AAKVVILKKA
TECIHSMQLD EQRLLSIKEQ LRRKSEQLKH RLQQLRSSH