ID   TWST1_MICMU             Reviewed;         199 AA.
AC   Q8MID5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Twist-related protein 1;
GN   Name=TWIST1; Synonyms=TWIST;
OS   Microcebus murinus (Gray mouse lemur) (Lemur murinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Cheirogaleidae; Microcebus.
OX   NCBI_TaxID=30608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RX   PubMed=12523351; DOI=10.1007/s00427-002-0263-y;
RA   Gachot-Neveu H., Stoetzel C., Quillet R., Dollfus H., Perrin-Schmitt F.;
RT   "Natural Twist protein variants in a panel of eleven non-human primates:
RT   possible implications of Twist gene-tree for primate species tree.";
RL   Dev. Genes Evol. 212:496-503(2002).
CC   -!- FUNCTION: Acts as a transcriptional regulator. Inhibits myogenesis by
CC       sequestrating E proteins, inhibiting trans-activation by MEF2, and
CC       inhibiting DNA-binding by MYOD1 through physical interaction. This
CC       interaction probably involves the basic domains of both proteins. Also
CC       represses expression of pro-inflammatory cytokines such as TNFA and
CC       IL1B. Regulates cranial suture patterning and fusion. Activates
CC       transcription as a heterodimer with E proteins. Regulates gene
CC       expression differentially, depending on dimer composition. Homodimers
CC       induce expression of FGFR2 and POSTN while heterodimers repress FGFR2
CC       and POSTN expression and induce THBS1 expression. Heterodimerization is
CC       also required for osteoblast differentiation. Represses the activity of
CC       the circadian transcriptional activator: NPAS2-ARNTL/BMAL1 heterodimer
CC       (By similarity). {ECO:0000250|UniProtKB:P26687}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Homodimer or heterodimer with E proteins such as TCF3. ID1
CC       binds preferentially to TCF3 but does not interact efficiently with
CC       TWIST1 so ID1 levels control the amount of TCF3 available to dimerize
CC       with TWIST and thus determine the type of dimer formed (By similarity).
CC       {ECO:0000250|UniProtKB:P26687}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR   EMBL; AJ488167; CAD32481.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8MID5; -.
DR   SMR; Q8MID5; -.
DR   PRIDE; Q8MID5; -.
DR   Proteomes; UP000694394; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR015789; Twist-related.
DR   PANTHER; PTHR23349:SF64; PTHR23349:SF64; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   3: Inferred from homology;
KW   Activator; Biological rhythms; Developmental protein; Differentiation;
KW   DNA-binding; Myogenesis; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..199
FT                   /note="Twist-related protein 1"
FT                   /id="PRO_0000284945"
FT   DOMAIN          105..156
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..188
FT                   /note="Sufficient for transactivation activity"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   199 AA;  20783 MW;  B94C27989D15EDB5 CRC64;
     MMQDVSSSPV SPADDSLSNS EEEPDRQQPP SGKRGGRKRR SSRRSAGGGA GPGGAAGGGV
     GGGDEPGSPA QGKRGKKSAG CGGGAGGGGS SSGGGSPQSY EELQTQRVMA NVRERQRTQS
     LNEAFAALRK IIPTLPSDKL SKIQTLKLAA RYIDFLYQVL QSDELDSKMA SCSYVAHERL
     SYAFSVWRME GAWSMSASH