KLF10_RAT
ID KLF10_RAT Reviewed; 480 AA.
AC O08876; Q4QRA4;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Krueppel-like factor 10;
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;
DE AltName: Full=Zinc finger transcription factor homolog CPG20;
GN Name=Klf10; Synonyms=Cpg20, Tieg, Tieg1;
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=Wistar;
RX PubMed=9699150; DOI=10.1007/bf02737120;
RA Hevroni D., Rattner A., Bundman M., Lederfein D., Gabarah A., Mangelus M.,
RA Silverman M.A., Kedar H., Naor C., Kornuc M., Hanoch T., Seger R.,
RA Theill L.E., Nedivi E., Richter-Levin G., Citri Y.;
RT "Hippocampal plasticity involves extensive gene induction and multiple
RT cellular mechanisms.";
RL J. Mol. Neurosci. 10:75-98(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
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).
CC -!- FUNCTION: Transcriptional repressor which binds to the consensus
CC sequence 5'-GGTGTG-3'. Regulates the circadian expression of genes
CC involved in lipogenesis, gluconeogenesis, and glycolysis in the liver.
CC Represses the expression of PCK2, a rate-limiting step enzyme of
CC gluconeogenesis. 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 {ECO:0000250|UniProtKB:O89091, ECO:0000250|UniProtKB:Q13118,
CC ECO:0000269|PubMed:20070857}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20070857}.
CC -!- INDUCTION: Up-regulated in response to glucose.
CC {ECO:0000269|PubMed:20070857}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent
CC proteasomal degradation. {ECO:0000250|UniProtKB:Q13118}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; U78875; AAC99475.1; -; mRNA.
DR EMBL; BC097309; AAH97309.1; -; mRNA.
DR RefSeq; NP_112397.1; NM_031135.2.
DR AlphaFoldDB; O08876; -.
DR SMR; O08876; -.
DR STRING; 10116.ENSRNOP00000008350; -.
DR PaxDb; O08876; -.
DR Ensembl; ENSRNOT00000008350; ENSRNOP00000008350; ENSRNOG00000006118.
DR GeneID; 81813; -.
DR KEGG; rno:81813; -.
DR UCSC; RGD:621652; rat.
DR CTD; 7071; -.
DR RGD; 621652; Klf10.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159405; -.
DR HOGENOM; CLU_046370_1_0_1; -.
DR InParanoid; O08876; -.
DR OMA; CQPMVFM; -.
DR OrthoDB; 582598at2759; -.
DR PhylomeDB; O08876; -.
DR TreeFam; TF315506; -.
DR PRO; PR:O08876; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000006118; Expressed in lung and 20 other tissues.
DR ExpressionAtlas; O08876; baseline and differential.
DR Genevisible; O08876; RN.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; 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; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0030282; P:bone mineralization; ISO:RGD.
DR GO; GO:1901653; P:cellular response to peptide; IEP:RGD.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP: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; ISO:RGD.
DR GO; GO:0035019; P:somatic stem cell population maintenance; 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; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..480
FT /note="Krueppel-like factor 10"
FT /id="PRO_0000047179"
FT ZN_FING 369..393
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 399..423
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 429..451
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
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 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13118"
SQ SEQUENCE 480 AA; 51829 MW; EE6880C27F255029 CRC64;
MLNFGASLQQ ASEGKMELIS EKSKEGAHPW DKAEQSDFEA VEALMSMSCD WKSHFKKYLE
NRPVTPVSDT SEEDSLLPGT PDLQTVPAFC LTPPYSPSDF EPSQGSNLTA PAPPTGHFRS
LSDAAKPPSI APFKEEEKSP LAAPPLPKAQ ATSVIRHTAD AQLCNHQSCP VKAASILNYQ
DNSFRRRTHI NVEATRKNIP CAAVSPNRPK PEPSTAANGA EKAGTAPYDF AVPSSETVIC
RSSQPAPTSP VQKSVLMSSP TVSTGGVPPL PVICQMVPLP ANNSLVTTVV PSSPPSQPPA
VCSPVLFMGT QVPKGTVMFV VPQPVVQSPK PPVVSPNGTR LSPIAPAPGF SPSAARVTPQ
IDSSRVRSHI CSHPGCGKTY FKSSHLKAHV RTHTGEKPFS CSWKGCERRF ARSDELSRHR
RTHTGEKKFA CPMCDRRFMR SDHLTKHARR HLSAKKLPNW QMEVSKLNDI ALPPATASAQ
