ID   TWIST_DROVI             Reviewed;         519 AA.
AC   Q9TX44; Q8I187;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Protein twist;
GN   Name=twi {ECO:0000312|EMBL:AAO01084.1};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8068548; DOI=10.1016/0925-4773(94)90036-1;
RA   Pan D., Valentine S.A., Courey A.J.;
RT   "The bipartite D. melanogaster twist promoter is reorganized in D.
RT   virilis.";
RL   Mech. Dev. 46:41-53(1994).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAO01084.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-296.
RX   PubMed=12537575; DOI=10.1186/gb-2002-3-12-research0086;
RA   Bergman C.M., Pfeiffer B.D., Rincon-Limas D.E., Hoskins R.A., Gnirke A.,
RA   Mungall C.J., Wang A.M., Kronmiller B., Pacleb J.M., Park S., Stapleton M.,
RA   Wan K.H., George R.A., de Jong P.J., Botas J., Rubin G.M., Celniker S.E.;
RT   "Assessing the impact of comparative genomic sequence data on the
RT   functional annotation of the Drosophila genome.";
RL   Genome Biol. 3:RESEARCH0086.1-RESEARCH0086.20(2002).
CC   -!- FUNCTION: Involved in the establishment and dorsoventral patterning of
CC       germ layers in the embryo. {ECO:0000250|UniProtKB:P10627}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Homodimer (By similarity). {ECO:0000250|UniProtKB:P10627}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR   EMBL; AY190956; AAO01084.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9TX44; -.
DR   SMR; Q9TX44; -.
DR   STRING; 7244.FBpp0235993; -.
DR   eggNOG; KOG4447; Eukaryota.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblMetazoa.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:EnsemblMetazoa.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0031032; P:actomyosin structure organization; IEA:EnsemblMetazoa.
DR   GO; GO:0007369; P:gastrulation; ISS:UniProtKB.
DR   GO; GO:0007443; P:Malpighian tubule morphogenesis; ISS:UniProtKB.
DR   GO; GO:0007498; P:mesoderm development; ISS:UniProtKB.
DR   GO; GO:0001710; P:mesodermal cell fate commitment; ISS:UniProtKB.
DR   GO; GO:0055001; P:muscle cell development; IEA:EnsemblMetazoa.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblMetazoa.
DR   GO; GO:0016202; P:regulation of striated muscle tissue development; ISS:UniProtKB.
DR   GO; GO:0007435; P:salivary gland morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0007370; P:ventral furrow formation; ISS:UniProtKB.
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:SF50; PTHR23349:SF50; 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   Developmental protein; Differentiation; DNA-binding; Nucleus;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..519
FT                   /note="Protein twist"
FT                   /id="PRO_0000127479"
FT   DOMAIN          390..441
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          53..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        60..62
FT                   /note="QQH -> HQQ (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67..69
FT                   /note="QQH -> HQQ (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154..156
FT                   /note="ATA -> TTS (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196..201
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        288
FT                   /note="Q -> QQQ (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   519 AA;  58484 MW;  3DB4756CE40ED1B0 CRC64;
     MSARSVSPKV LLDISYKPTL PNIMELQHNV IKLIQVEQHA YMQLMEQPTA HYMQQQQQQQ
     QHQQQQQQHQ QQQQQQYAPL PSLAPNAADY AAYGITELED TDYNIPSNEV LSTSSNHSAQ
     SSLELNNNQH NFEQQQQQQQ QQQQQQTATP AGVATAAQTP HGYMLNEHGK RSRSSSDYDC
     QTDALSMQPE HKKLLQQQQQ QQQQQQQQQQ QQLYVDYLPT TVDEVAAAQT QAQAPTQQSA
     CLSPHSHSHS HFDFAADEEL QDHKAHIFKY GGYPQTIAQQ QQQQQQQQLH FQSSYRTGQN
     YEAYDPANSL NGSTYSSSDR DDMEYARQTA LSSVGGYAKE DELEDMSPTC LGDDSSLLDA
     GDAAGKAFRK PRRRLKRKPS KTEETDEFSN QRVMANVRER QRTQSLNDAF KALQQIIPTL
     PSDKLSKIQT LKLATRYIDF LCRMLSSSDI SLLKALEAQS SPVSPGYGNA STLLSAANGA
     EADLKCLRKA NGAPIIPPEK LSYLFGVWRM EGDAQHQKA