HTF4_MESAU
ID HTF4_MESAU Reviewed; 437 AA.
AC Q60420;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Transcription factor 12;
DE Short=TCF-12;
DE AltName: Full=Beta-cell E-box transcriptional activator 1;
DE Short=BETA1;
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;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Insulinoma;
RX PubMed=7929299; DOI=10.1016/s0021-9258(18)47336-x;
RA Peyton M., Moss L.G., Tsai M.-J.;
RT "Two distinct class A helix-loop-helix transcription factors, E2A and
RT BETA1, form separate DNA binding complexes on the insulin gene E box.";
RL J. Biol. Chem. 269:25936-25941(1994).
CC -!- FUNCTION: Transcriptional regulator. Involved in the initiation of
CC neuronal differentiation. Activates transcription by binding to the E
CC box (5'-CANNTG-3'). Participates in the control of inducible RP4 gene
CC expression in salivary cells (By similarity). Binds to the RIPE3
CC element of the insulin II promoter. {ECO:0000250}.
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 NEUROD2. Interacts with PTF1A. Interacts with
CC RUNX1T1 (By similarity). Interacts with BHLHA9.
CC {ECO:0000250|UniProtKB:Q61286, ECO:0000250|UniProtKB:Q99081}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA65702.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U12585; AAA65702.1; ALT_FRAME; mRNA.
DR PIR; A55021; A55021.
DR AlphaFoldDB; Q60420; -.
DR Proteomes; UP000189706; Unplaced.
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; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN <1..437
FT /note="Transcription factor 12"
FT /id="PRO_0000127229"
FT DOMAIN 332..385
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..410
FT /note="Class A specific domain"
FT REGION 405..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT CROSSLNK 364
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT CROSSLNK 408
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 437 AA; 47426 MW; DB108DABEBD6A003 CRC64;
EFHDRLSYPP HSVSPTDIST SLPPMSSFHR GSTSSSPYVA ASHTPPINGS DSILGARGNA
AGSSQTGDAL GKALASIYSP DHTSSSFPSN PSTPVGSPSP LTGTSQWPRA GGQAPSSPSY
ENSLHSLKNR VEQQLHEHLQ DAMSFLKDVC EQSRMEDRLD RLDDAIHVLR NHAVGPSTSL
PTSHSDIHSL LGPSHNAPIG NLNSNYGGSS LVTNSRSASM VGTHREDSVN LNGNHSVLSS
TVAASNTDLN HKTPENYRGG LQNQSGNVVP TEIKTENKEK DENLHEPPSS DDMKSDDESS
QKDIKVSSRG RTSSTNEDED LNPEQKIERE KERRMANNAR ERLRVRDINE AFKELGRMCQ
LHLKSEKPQT KLLILHQAVA VILSLEQQVR ERNLNPKAAC LKRREEEKVS AASAEPPTTL
PGTHPGLSET TNPMGHL
