MYC1_XENLA
ID MYC1_XENLA Reviewed; 419 AA.
AC P06171; Q8AVZ1; Q91794;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Transcriptional regulator Myc-A;
DE AltName: Full=c-Myc I;
GN Name=myc-a; Synonyms=myc, myc1;
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].
RX PubMed=3540613; DOI=10.1128/mcb.6.12.4499-4508.1986;
RA King M.W., Roberts J.M., Eisenman R.N.;
RT "Expression of the c-myc proto-oncogene during development of Xenopus
RT laevis.";
RL Mol. Cell. Biol. 6:4499-4508(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=2686981; DOI=10.1002/j.1460-2075.1989.tb08593.x;
RA Vriz S., Taylor M., Mechali M.;
RT "Differential expression of two Xenopus c-myc proto-oncogenes during
RT development.";
RL EMBO J. 8:4091-4097(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1945855; DOI=10.1093/nar/19.20.5777;
RA King M.W.;
RT "Developmentally regulated alternative splicing in the Xenopus laevis c-Myc
RT gene creates an intron-1 containing c-Myc RNA present only in post-
RT midblastula embryos.";
RL Nucleic Acids Res. 19:5777-5783(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-83.
RC TISSUE=Liver;
RX PubMed=2057364; DOI=10.1093/nar/19.11.3081;
RA Principaud E., Spohr G.;
RT "Xenopus laevis c-myc I and II genes: molecular structure and developmental
RT expression.";
RL Nucleic Acids Res. 19:3081-3088(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 90-419.
RC TISSUE=Oocyte;
RX PubMed=3549280; DOI=10.1002/j.1460-2075.1986.tb04683.x;
RA Taylor M.V., Gusse M., Evan G.I., Dathan N., Mechali M.;
RT "Xenopus myc proto-oncogene during development: expression as a stable
RT maternal mRNA uncoupled from cell division.";
RL EMBO J. 5:3563-3570(1986).
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 -!- DEVELOPMENTAL STAGE: C-MYC I is active in oocytes, while C-MYC II is
CC active in both oocytes and post-gastrula embryos.
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; M14455; AAA49905.1; -; mRNA.
DR EMBL; X14806; CAA32911.1; -; mRNA.
DR EMBL; X53717; CAA37753.1; -; Genomic_DNA.
DR EMBL; BC041189; AAH41189.2; -; mRNA.
DR EMBL; X56871; CAA40195.1; -; Genomic_DNA.
DR EMBL; M26285; AAA49906.1; -; mRNA.
DR PIR; A25392; TVXLMC.
DR AlphaFoldDB; P06171; -.
DR SMR; P06171; -.
DR PRIDE; P06171; -.
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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
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; 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; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..419
FT /note="Transcriptional regulator Myc-A"
FT /id="PRO_0000127319"
FT DOMAIN 335..387
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 141..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..415
FT /note="Leucine-zipper"
FT MOTIF 78..86
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P01106"
FT COMPBIAS 206..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 90
FT /note="N -> R (in Ref. 6; AAA49906)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="P -> R (in Ref. 2; CAA32911 and 6; AAA49906)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="E -> G (in Ref. 3; CAA37753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 47361 MW; 61AC1DCBA35246DB CRC64;
MPLNANFPSK NYDYDYDLQP CFFFLEEENF YHQQSRLQPP APSEDIWKKF ELLPTPPLSP
SRRSSQSSLF PSTADQLEMV TEFLGGDMVN QSFICEADDE ALLKSIVIQD CMWSGFSAAA
KLEKVVSEKL ASYQASRKES ALSSSSPCQS QPPPSPLKSP SCHGSLSLGG THRSSHGFLQ
DPSSDCVDPS VVFPYPLNDS ISNASSPCQD LILETPPISS NSSSSESEEE PEDEDEDCDE
EEEIDVVTVE KRQSASKRVE SSSHSQPSRP HYSPLVLKRC HVPIHQHNYA ASPSTKVDYV
SSKRAKLESN IRVLKQISNN RKCASPRSSD SEENDKRKTH NVLERQRRNE LKLSFFALRD
QVPEVASNEK APKVVILKKA TEYAISLQED ERRLIRETEQ LKYRKEQLKQ RLQQLRNFV
