ID B5THP1_SACKO Unreviewed; 372 AA.
AC B5THP1;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 22-FEB-2023, entry version 63.
DE SubName: Full=Myc protein {ECO:0000313|EMBL:ACH73249.1};
GN Name=myc {ECO:0000313|EMBL:ACH73249.1};
OS Saccoglossus kowalevskii (Acorn worm).
OC Eukaryota; Metazoa; Hemichordata; Enteropneusta; Harrimaniidae;
OC Saccoglossus.
OX NCBI_TaxID=10224 {ECO:0000313|EMBL:ACH73249.1};
RN [1] {ECO:0000313|EMBL:ACH73249.1}
RP NUCLEOTIDE SEQUENCE.
RA Freeman R.M.Jr., Wu M., Cordonnier-Pratt M.-M., Pratt L.H., Gruber C.E.,
RA Smith M., Lander E.S., Stange-Thomann N., Lowe C.J., Gehart J.,
RA Kirschner M.;
RT "cDNA Sequences for Transcription Factors and Signaling Proteins of the
RT Hemichordate Saccoglossus kowalevskii: Efficacy of the Expressed Sequence
RT Tag (EST) Approach for Evolutionary and Developmental Studies of a New
RT Organism.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. {ECO:0000256|PIRNR:PIRNR001705}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR001705}.
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DR EMBL; EU939767; ACH73249.1; -; mRNA.
DR RefSeq; NP_001158444.1; NM_001164972.1.
DR AlphaFoldDB; B5THP1; -.
DR EnsemblMetazoa; NM_001164972.1; NP_001158444.1; GeneID_100303478.
DR GeneID; 100303478; -.
DR KEGG; sko:100303478; -.
DR CTD; 4609; -.
DR OrthoDB; 3039999at2759; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd11400; bHLHzip_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; IPR002418; Tscrpt_reg_Myc.
DR InterPro; IPR012682; Tscrpt_reg_Myc_N.
DR PANTHER; PTHR45851:SF3; MYC PROTEIN; 1.
DR PANTHER; PTHR45851; MYC PROTO-ONCOGENE; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF01056; Myc_N; 2.
DR PIRSF; PIRSF001705; Myc_protein; 2.
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 DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR001705};
KW Nucleus {ECO:0000256|PIRNR:PIRNR001705}.
FT DOMAIN 283..335
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 186..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 41577 MW; ED1DEFABE46AFF82 CRC64;
MPEMEPEQRI QSILDYDKYQ PYFLGHDENE EFYGATHTPS PSEDIWKKFE LLPTPPRSPG
RPAPIPLLSV VAEALQQVSE TLDDDNHTQT FVFPDLSNLK SNLIQDCMWS GGNNGTPEET
TKGETTLPAA IAACLTPPPL DYAVAECVDP TAVFPYPLND PKDQLSGPSQ SDSEEEIDVV
TVAEKLQQPP KRKVTAPATP ASNTATTTTN TTSSITLKRV RPSHNHHNHH SYSTPAKKTK
QELSMAELKA LMQQSNGGRR TPGNSRPGSR SSSRPSSDSE DNDKRATHNV LERKRRNDLK
TSFLTLRDNV PELENQERAP KVVILRKATD HIQQITADEL LLVKDKEGLK KRNVILLDKL
NRLKNDLNFM LY
//