KLF9_MOUSE
ID KLF9_MOUSE Reviewed; 244 AA.
AC O35739;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Krueppel-like factor 9;
DE AltName: Full=Basic transcription element-binding protein 1;
DE Short=BTE-binding protein 1;
DE AltName: Full=GC-box-binding protein 1;
DE AltName: Full=Transcription factor BTEB1;
GN Name=Klf9; Synonyms=Bteb, Bteb-1, Bteb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9858544; DOI=10.1128/mcb.19.1.194;
RA Imhof A., Schuierer M., Werner O., Moser M., Roth C., Bauer R.,
RA Buettner R.;
RT "Transcriptional regulation of the AP-2alpha promoter by BTEB-1 and AP-
RT 2rep, a novel wt-1/egr-related zinc finger repressor.";
RL Mol. Cell. Biol. 19:194-204(1999).
CC -!- FUNCTION: Transcription factor that binds to GC box promoter elements.
CC Selectively activates mRNA synthesis from genes containing tandem
CC repeats of GC boxes but represses genes with a single GC box. Acts as
CC an epidermal circadian transcription factor regulating keratinocyte
CC proliferation. {ECO:0000250|UniProtKB:Q13886}.
CC -!- SUBUNIT: Interacts with ZZEF1. {ECO:0000250|UniProtKB:Q13886}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13886}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y14296; CAA74671.1; -; mRNA.
DR CCDS; CCDS29706.1; -.
DR AlphaFoldDB; O35739; -.
DR SMR; O35739; -.
DR IntAct; O35739; 2.
DR STRING; 10090.ENSMUSP00000045639; -.
DR iPTMnet; O35739; -.
DR PhosphoSitePlus; O35739; -.
DR PaxDb; O35739; -.
DR PeptideAtlas; O35739; -.
DR PRIDE; O35739; -.
DR ProteomicsDB; 264769; -.
DR MGI; MGI:1333856; Klf9.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; O35739; -.
DR PhylomeDB; O35739; -.
DR ChiTaRS; Klf9; mouse.
DR PRO; PR:O35739; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35739; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISS:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0071387; P:cellular response to cortisol stimulus; ISS:UniProtKB.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISO:MGI.
DR GO; GO:0007566; P:embryo implantation; IDA:MGI.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 2: Evidence at transcript level;
KW Biological rhythms; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..244
FT /note="Krueppel-like factor 9"
FT /id="PRO_0000047155"
FT ZN_FING 143..167
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 173..197
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 203..225
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 26..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13886"
SQ SEQUENCE 244 AA; 27170 MW; BBDF607FFA218D5A CRC64;
MSAAAYMDFV AAQCLVSISN RAAVPEHGGA PEAERLRLPE REVTKEHGDP GDTWKDYCTL
VTIAKSLLDL NKYRPIQTPS VCSDSLESPD EDIGSDSDVT TESGSSPSHS PEERQDSGSA
PSPLSLLHSG VASKGKHASE KRHKCPYSGC GKVYGKSSHL KAHYRVHTGE RPFPCTWPDC
LKKFSRSDEL TRHYRTHTGE KQFRCPLCEK RFMRSDHLTK HARRHTVFHP SMIKRSKKAL
ACPL
