ID   HTF4_PAPHA              Reviewed;         160 AA.
AC   Q28772;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Transcription factor 12;
DE            Short=TCF-12;
DE   AltName: Full=DNA-binding protein HTF4;
DE   AltName: Full=E-box-binding protein;
DE   AltName: Full=Transcription factor HTF-4;
DE   Flags: Fragment;
GN   Name=TCF12; Synonyms=HTF4;
OS   Papio hamadryas (Hamadryas baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lymphoid tissue;
RX   PubMed=9032251; DOI=10.1128/mcb.17.3.1244;
RA   di Rocco G., Pennuto M., Illi B., Canu N., Filocamo G., Trani E.,
RA   Rinaldi A.M., Possenti R., Mandolesi G., Sirinian M.I., Jucker R., Levi A.,
RA   Nasi S.;
RT   "Interplay of the E box, the cyclic AMP response element, and HTF4/HEB in
RT   transcriptional regulation of the neurospecific, neurotrophin-inducible vgf
RT   gene.";
RL   Mol. Cell. Biol. 17:1244-1253(1997).
CC   -!- FUNCTION: Transcriptional regulator. Involved in the initiation of
CC       neuronal differentiation. Activates transcription by binding to the E
CC       box (5'-CANNTG-3').
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Forms homo- or heterooligomers with myogenin, E12 and ITF2
CC       proteins. Interacts with PTF1A. Interacts with RUNX1T1. Interacts with
CC       NEUROD2 (By similarity). Interacts with BHLHA9.
CC       {ECO:0000250|UniProtKB:Q61286, ECO:0000250|UniProtKB:Q99081}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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DR   EMBL; X97234; CAA65873.1; -; mRNA.
DR   AlphaFoldDB; Q28772; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; DNA-binding; Isopeptide bond;
KW   Neurogenesis; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           <1..160
FT                   /note="Transcription factor 12"
FT                   /id="PRO_0000127231"
FT   DOMAIN          55..108
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          110..133
FT                   /note="Class A specific domain"
FT   REGION          132..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99081"
FT   MOD_RES         36
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99081"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99081"
FT   CROSSLNK        29
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q99081"
FT   CROSSLNK        87
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q99081"
FT   CROSSLNK        131
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q99081"
FT   NON_TER         1
SQ   SEQUENCE   160 AA;  18302 MW;  4B7D037A19AFA395 CRC64;
     NKEKDENLHE PPSSDDMKSD DESSQKDIKV SSRGRTSTNE DEDLNPEQKI EREKERRMAN
     NARERLRVRD INEAFKELGR MCQLHLKSEK PQTKLLILHQ AVAVILSLEQ QVRERNLNPK
     AACLKRREEE KVSVVSAEPP TTLPGTHPGL SETTNPMGHM