KLF10_MOUSE
ID KLF10_MOUSE Reviewed; 479 AA.
AC O89091;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Krueppel-like factor 10;
DE AltName: Full=GDNF-inducible factor;
DE AltName: Full=Transcription factor GIF;
DE Short=mGIF;
DE AltName: Full=Transforming growth factor-beta-inducible early growth response protein 1;
DE Short=TGFB-inducible early growth response protein 1;
DE Short=TIEG-1;
GN Name=Klf10; Synonyms=Gdnfif, Tieg, Tieg1;
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], AND INDUCTION.
RX PubMed=9348334; DOI=10.1523/jneurosci.17-22-08657.1997;
RA Yajima S., Lammers C.H., Lee S.H., Hara Y., Mizuno K., Mouradian M.M.;
RT "Cloning and characterization of murine glial cell-derived neurotrophic
RT factor inducible transcription factor (MGIF).";
RL J. Neurosci. 17:8657-8666(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9745041; DOI=10.1007/s003359900878;
RA Fautsch M.P., Vrabel A., Rickard D., Subramaniam M., Spelsberg T.C.,
RA Wieben E.D.;
RT "Characterization of the mouse TGFbeta-inducible early gene (TIEG):
RT conservation of exon and transcriptional regulatory sequences with evidence
RT of additional transcripts.";
RL Mamm. Genome 9:838-842(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND PHOSPHORYLATION.
RX PubMed=20070857; DOI=10.1111/j.1365-2443.2009.01371.x;
RA Hirota T., Kon N., Itagaki T., Hoshina N., Okano T., Fukada Y.;
RT "Transcriptional repressor TIEG1 regulates Bmal1 gene through GC box and
RT controls circadian clockwork.";
RL Genes Cells 15:111-121(2010).
RN [5]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20385766; DOI=10.1128/mcb.01141-09;
RA Guillaumond F., Grechez-Cassiau A., Subramaniam M., Brangolo S.,
RA Peteri-Brunback B., Staels B., Fievet C., Spelsberg T.C., Delaunay F.,
RA Teboul M.;
RT "Kruppel-like factor KLF10 is a link between the circadian clock and
RT metabolism in liver.";
RL Mol. Cell. Biol. 30:3059-3070(2010).
CC -!- FUNCTION: Transcriptional repressor which binds to the consensus
CC sequence 5'-GGTGTG-3'. May play a role in the cell cycle regulation (By
CC similarity). Plays a role in the regulation of the circadian clock;
CC binds to the GC box sequence in the promoter of the core clock
CC component ARTNL/BMAL1 and represses its transcriptional activity.
CC Regulates the circadian expression of genes involved in lipogenesis,
CC gluconeogenesis, and glycolysis in the liver. Represses the expression
CC of PCK2, a rate-limiting step enzyme of gluconeogenesis.
CC {ECO:0000250|UniProtKB:Q13118, ECO:0000269|PubMed:20070857,
CC ECO:0000269|PubMed:20385766}.
CC -!- INTERACTION:
CC O89091; Q8C863: Itch; NbExp=4; IntAct=EBI-10949150, EBI-851782;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20070857}.
CC -!- INDUCTION: By TGF-beta and GDNF. Expressed in a circadian manner in the
CC liver with a high at ZT14-18 and a low at ZT2 (at protein level).
CC Expressed in a circadian manner in the bone, kidney and skeletal
CC muscle. Up-regulated in response to glucose.
CC {ECO:0000269|PubMed:20070857, ECO:0000269|PubMed:20385766,
CC ECO:0000269|PubMed:9348334}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent
CC proteasomal degradation. {ECO:0000250|UniProtKB:Q13118}.
CC -!- DISRUPTION PHENOTYPE: Male mice display postprandial and fasting
CC hyperglycemia while female mice are normoglycemic but display higher
CC plasma triglycerides. {ECO:0000269|PubMed:20385766}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF064088; AAC16734.1; -; mRNA.
DR EMBL; AF049880; AAC77797.1; -; Genomic_DNA.
DR EMBL; AF049879; AAC77796.1; -; mRNA.
DR EMBL; BC003316; AAH03316.1; -; mRNA.
DR CCDS; CCDS27438.1; -.
DR RefSeq; NP_038720.1; NM_013692.3.
DR AlphaFoldDB; O89091; -.
DR SMR; O89091; -.
DR BioGRID; 204195; 3.
DR IntAct; O89091; 1.
DR STRING; 10090.ENSMUSP00000073690; -.
DR ChEMBL; CHEMBL4523155; -.
DR iPTMnet; O89091; -.
DR PhosphoSitePlus; O89091; -.
DR PaxDb; O89091; -.
DR PeptideAtlas; O89091; -.
DR PRIDE; O89091; -.
DR ProteomicsDB; 263617; -.
DR Antibodypedia; 26326; 324 antibodies from 34 providers.
DR DNASU; 21847; -.
DR Ensembl; ENSMUST00000074043; ENSMUSP00000073690; ENSMUSG00000037465.
DR GeneID; 21847; -.
DR KEGG; mmu:21847; -.
DR UCSC; uc007vnr.2; mouse.
DR CTD; 7071; -.
DR MGI; MGI:1101353; Klf10.
DR VEuPathDB; HostDB:ENSMUSG00000037465; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159405; -.
DR HOGENOM; CLU_046370_1_0_1; -.
DR InParanoid; O89091; -.
DR OMA; CQPMVFM; -.
DR OrthoDB; 582598at2759; -.
DR PhylomeDB; O89091; -.
DR TreeFam; TF315506; -.
DR BioGRID-ORCS; 21847; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Klf10; mouse.
DR PRO; PR:O89091; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O89091; protein.
DR Bgee; ENSMUSG00000037465; Expressed in spermatocyte and 243 other tissues.
DR ExpressionAtlas; O89091; baseline and differential.
DR Genevisible; O89091; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO: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; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
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; IMP:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IDA:MGI.
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 1: Evidence at protein level;
KW Biological rhythms; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..479
FT /note="Krueppel-like factor 10"
FT /id="PRO_0000047178"
FT ZN_FING 368..392
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 398..422
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 428..450
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 94..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13118"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13118"
SQ SEQUENCE 479 AA; 51756 MW; 99A5969665962963 CRC64;
MLNFGASLQQ ASEGKMELIS EKPREGMHPW DKAEQSDFEA VEALMSMSCD WKSHFKKYLE
NRPVTPVSDT SEDDSLLPGT PDLQTVPAFC LTPPYSPSDF EPSQGSNLTA SAPSTGHFKS
FSDAAKPPGA TPFKEEEKNP LAAPPLPKAQ ATSVIRHTAD AQLCNHQSCP VKAASILNYQ
DNSFRRRTHG NVEATRKNIP CAAVSPNRSK PEPSTVSDGD EKAGAALYDF AVPSSETVIC
RSQPAPSSPV QKSVLVSSPT VSTGGVPPLP VICQMVPLPA NNSLVSTVVP STPPSQPPAV
CSPVLFMGTQ VPEGTVVFVV PQPVVQSPRP PVVSPSGTRL SPIAPAPGFS PSAARVTPQI
DSSRVRSHIC SHPGCGKTYF KSSHLKAHVR THTGEKPFSC SWKGCERRFA RSDELSRHRR
THTGEKKFAC PMCDRRFMRS DHLTKHARRH LSAKKLPNWQ MEVSKLNDIA LPPTPASAQ
