HTF4_RAT
ID HTF4_RAT Reviewed; 707 AA.
AC P51514;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
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=Salivary-specific cAMP response element-binding protein alpha;
DE Short=SCBP-alpha;
DE AltName: Full=Transcription factor HTF-4;
GN Name=Tcf12;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Salivary gland;
RX PubMed=7683670; DOI=10.1016/s0021-9258(18)82192-5;
RA Lin H.H., Li W.-Y., Ann D.K.;
RT "The helix-loop-helix proteins (salivary-specific cAMP response element-
RT binding proteins) can modulate cAMP-inducible RP4 gene expression in
RT salivary cells.";
RL J. Biol. Chem. 268:10214-10220(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 80-707.
RX PubMed=8422988; DOI=10.1101/gad.7.1.55;
RA Klein E.S., Simmons D.M., Swanson L.W., Rosenfeld M.G.;
RT "Tissue-specific RNA splicing generates an ankyrin-like domain that affects
RT the dimerization and DNA-binding properties of a bHLH protein.";
RL Genes Dev. 7:55-71(1993).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND SER-79, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcriptional regulator. Involved in the initiation of
CC neuronal differentiation. Activates transcription by binding to the E
CC box (5'-CANNTG-3') (By similarity). {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 PTF1. 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.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=Alpha; Synonyms=Beta;
CC IsoId=P51514-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P51514-2; Sequence=VSP_002107;
CC Name=Gamma; Synonyms=Alpha;
CC IsoId=P51514-3; Sequence=VSP_002106;
CC -!- TISSUE SPECIFICITY: Isoform gamma is highly expressed in lung, kidney,
CC spleen, and is expressed at reduced levels in heart, muscle, liver,
CC pituitary, brain and the trigeminal ganglion. The expression of isoform
CC alpha predominates over isoform gamma in the pituitary and the brain.
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DR EMBL; L09656; AAA42115.1; -; mRNA.
DR EMBL; S53913; AAB25128.2; -; mRNA.
DR EMBL; S53920; AAB25129.2; ALT_SEQ; mRNA.
DR EMBL; S53922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S53921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A46691; A46691.
DR RefSeq; NP_037308.1; NM_013176.2. [P51514-1]
DR RefSeq; XP_006243408.1; XM_006243346.2. [P51514-2]
DR RefSeq; XP_006243411.1; XM_006243349.2. [P51514-3]
DR AlphaFoldDB; P51514; -.
DR BMRB; P51514; -.
DR CORUM; P51514; -.
DR STRING; 10116.ENSRNOP00000023634; -.
DR iPTMnet; P51514; -.
DR PhosphoSitePlus; P51514; -.
DR jPOST; P51514; -.
DR PaxDb; P51514; -.
DR Ensembl; ENSRNOT00000081185; ENSRNOP00000074384; ENSRNOG00000057754. [P51514-1]
DR GeneID; 25720; -.
DR KEGG; rno:25720; -.
DR UCSC; RGD:3829; rat. [P51514-1]
DR CTD; 6938; -.
DR RGD; 3829; Tcf12.
DR eggNOG; KOG3910; Eukaryota.
DR GeneTree; ENSGT00940000155047; -.
DR HOGENOM; CLU_021099_2_0_1; -.
DR InParanoid; P51514; -.
DR OMA; XKTSERG; -.
DR OrthoDB; 571132at2759; -.
DR PhylomeDB; P51514; -.
DR Reactome; R-RNO-525793; Myogenesis.
DR Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR PRO; PR:P51514; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000057754; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; P51514; baseline and differential.
DR Genevisible; P51514; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0043425; F:bHLH transcription factor binding; ISO:RGD.
DR GO; GO:0035497; F:cAMP response element binding; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0071837; F:HMG box domain binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0046332; F:SMAD binding; ISO:RGD.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA-binding; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..707
FT /note="Transcription factor 12"
FT /id="PRO_0000127232"
FT DOMAIN 602..655
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 25..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..140
FT /note="Leucine-zipper"
FT REGION 140..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..680
FT /note="Class A specific domain"
FT REGION 675..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61286"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT MOD_RES 582
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT CROSSLNK 544
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT CROSSLNK 575
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT CROSSLNK 634
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT CROSSLNK 678
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99081"
FT VAR_SEQ 398..422
FT /note="Missing (in isoform Gamma)"
FT /evidence="ECO:0000305"
FT /id="VSP_002106"
FT VAR_SEQ 422
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_002107"
FT CONFLICT 80
FT /note="P -> A (in Ref. 2; AAB25128/AAB25129)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="S -> C (in Ref. 2; AAB25128/AAB25129)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="F -> S (in Ref. 2; AAB25128/AAB25129)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="T -> N (in Ref. 2; AAB25128/AAB25129)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 75896 MW; CC4AC60294601E2B CRC64;
MNPQQQRMAA IGTDKELSDL LDFSAMFSPP VNSGKTRPTT LGSSQFSGSG MDERGGTTSW
GTSGQPSPSY DSSRGFTDSP HYSDHLNDSR LGTHEGLSPT PFMNSNLIGK TSERGSFSLY
SRDSGLSGCQ SSLLRQDLGL GSPAQLSSSG KPGTPYYSFS ATSSRRRPLH DSVALDPLQA
KKVRKVPPGL PSSVYAPSPN SDDFNRESPS YPSPKPPTSM FASTFFMQDG THSSSDLWSS
SNGMSQPGFG GILGTSTSHM SQSSSYGSLH SHDRLSYPPH SVSPTDINTS LPPMSSFHRG
STSSSPYVAA SHTPPINGSD SILGTRGNAA GSSQTGDALG KALASIYSPD HTSSSFPSNP
STPVGSPSPL TAGTSQWPRA GGQAPSSPSY ENSLHSLKNR VEQQLHEHLQ DAMSFLKDVC
EQSRMEDRLD RLDDAIHVLR NHAVGPSTSL PTSHSDIHSL LGPSHNAPIG NLNSNYGGSS
LVTNSRSASM VGTHREDSVS LNGNHSVLSS TVAASNTELN HKTPESFRGG VQNQSGSVVP
TEIKTENKEK DENLHEPPSS DDMKSDDESS QKDIKVSSRG RTSSTNEDED LNPEQKIERE
KERRMANNAR ERLRVRDINE AFKELGRMCQ LHLKSEKPQT KLLILHQAVA VILSLEQQVR
ERNLNPKAAC LKRREEEKVS AASAEPPTTL PGTHPGLSET TNPMGHL
