ID K9KFV4_HORSE Unreviewed; 175 AA.
AC K9KFV4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Myc proto-oncogene protein {ECO:0000256|ARBA:ARBA00013423};
DE AltName: Full=Proto-oncogene c-Myc {ECO:0000256|ARBA:ARBA00033247};
DE AltName: Full=Transcription factor p64 {ECO:0000256|ARBA:ARBA00030496};
DE Flags: Fragment;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|EMBL:AEQ00382.1};
RN [1] {ECO:0000313|EMBL:AEQ00382.1}
RP NUCLEOTIDE SEQUENCE.
RA Waegele B., Farthmann B., Nyakatura G., Heubner D., Mewes H.-W.,
RA Steinbach F.;
RT "Analysis of a normalised equine cDNA library using deep sequencing.";
RL Submitted (MAY-2011) 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. Binds to the VEGFA
CC promoter, promoting VEGFA production and subsequent sprouting
CC angiogenesis. Regulator of somatic reprogramming, controls self-renewal
CC of embryonic stem cells. Functions with TAF6L to activate target gene
CC expression through RNA polymerase II pause release (By similarity).
CC Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which
CC in turn regulate splicing of pyruvate kinase PKM by binding
CC repressively to sequences flanking PKM exon 9, inhibiting exon 9
CC inclusion and resulting in exon 10 inclusion and production of the PKM
CC M2 isoform. {ECO:0000256|ARBA:ARBA00029417}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
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DR EMBL; JL637837; AEQ00382.1; -; mRNA.
DR AlphaFoldDB; K9KFV4; -.
DR HOGENOM; CLU_052560_0_0_1; -.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; 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 CDD; cd11458; bHLHzip_c-Myc; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 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 PANTHER; PTHR45851; MYC PROTO-ONCOGENE; 1.
DR PANTHER; PTHR45851:SF1; MYC PROTO-ONCOGENE PROTEIN; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF02344; Myc-LZ; 1.
DR Pfam; PF01056; Myc_N; 1.
DR PRINTS; PR00044; LEUZIPPRMYC.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 2: Evidence at transcript level;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}.
FT DOMAIN 92..144
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEQ00382.1"
SQ SEQUENCE 175 AA; 20080 MW; 2D565342475DEC73 CRC64;
DVVSVEKRQP PAKRSESGSP SAGGHSKPPH SPLVLKRCHV STHQHNYAAP PSTRKDYPAA
KRAKLDSGRV LKQISNNRKC TSPRSSDTEE NDKRRTHNVL ERQRRNELKR SFFALRDQIP
ELENNEKAPK VVILKKATVF ILSVQAEEQK LVSEKDLLRK RREHLQLKLE QLRNC
//
