KLF9_RAT
ID KLF9_RAT Reviewed; 244 AA.
AC Q01713;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 140.
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, Bteb1;
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 TISSUE=Liver;
RX PubMed=1356762; DOI=10.1002/j.1460-2075.1992.tb05451.x;
RA Imataka H., Sogawa K., Yasumoto K., Kikuchi Y., Sasano K., Kobayashi A.,
RA Hayami M., Fujii-Kuriyama Y.;
RT "Two regulatory proteins that bind to the basic transcription element
RT (BTE), a GC box sequence in the promoter region of the rat P-4501A1 gene.";
RL EMBO J. 11:3663-3671(1992).
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}.
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DR EMBL; D12769; BAA02236.1; -; mRNA.
DR PIR; JS0748; JS0748.
DR PIR; S25288; S25288.
DR RefSeq; NP_476559.1; NM_057211.1.
DR AlphaFoldDB; Q01713; -.
DR SMR; Q01713; -.
DR STRING; 10116.ENSRNOP00000019367; -.
DR iPTMnet; Q01713; -.
DR PhosphoSitePlus; Q01713; -.
DR PaxDb; Q01713; -.
DR PRIDE; Q01713; -.
DR GeneID; 117560; -.
DR KEGG; rno:117560; -.
DR UCSC; RGD:70934; rat.
DR CTD; 687; -.
DR RGD; 70934; Klf9.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q01713; -.
DR OrthoDB; 1308225at2759; -.
DR PhylomeDB; Q01713; -.
DR PRO; PR:Q01713; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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: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; ISO:RGD.
DR GO; GO:0071387; P:cellular response to cortisol stimulus; ISS:UniProtKB.
DR GO; GO:1901653; P:cellular response to peptide; IEP:RGD.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISO:RGD.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0007566; P:embryo implantation; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; ISO:RGD.
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; ISO:RGD.
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_0000047157"
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 24..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; 27155 MW; FBD1D13FEAFA37E0 CRC64;
MSAAAYMDFV AAQCLVSISN RAAVPEHGGA PDAERLRLPE REVTKEHGDP GDTWKDYCTL
VTIAKSLLDL NKYRPIQTPS VCSDSLESPD EDIGSDSDVT TESGSSPSHS PEERQDSGSA
PSPLSLLHSG VASKGKHASE KRHKCPYSGC GKVYGKSSHL KAHYRVHTGE RPFPCTWPDC
LKKFSRSDEL TRHYRTHTGE KQFRCPLCEK RFMRSDHLTK HARRHTDFHP SMIKRSKKAL
ASPL
