KLF11_MOUSE
ID KLF11_MOUSE Reviewed; 502 AA.
AC Q8K1S5; Q8BHJ1; Q8BI37; Q8BI70;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Krueppel-like factor 11;
DE AltName: Full=TGFB-inducible early growth response protein 2b;
DE AltName: Full=Transforming growth factor-beta-inducible early growth response protein 3 {ECO:0000303|PubMed:14697507};
DE Short=TGFB-inducible early growth response protein 3 {ECO:0000303|PubMed:14697507};
DE Short=TIEG-3 {ECO:0000303|PubMed:14697507};
GN Name=Klf11 {ECO:0000312|MGI:MGI:2653368};
GN Synonyms=Tieg2b {ECO:0000312|EMBL:CAD30835.1}, Tieg3;
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] {ECO:0000305, ECO:0000312|EMBL:CAD30835.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RC STRAIN=NMRI {ECO:0000312|EMBL:CAD30835.1};
RX PubMed=14697507; DOI=10.1016/j.gene.2003.09.045;
RA Wang Z., Peters B., Klussmann S., Bender H., Herb A., Krieglstein K.;
RT "Gene structure and evolution of Tieg3, a new member of the Tieg family of
RT proteins.";
RL Gene 325:25-34(2004).
RN [2] {ECO:0000312|EMBL:BAC40717.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29509.1}, and
RC NOD {ECO:0000312|EMBL:BAC40717.1};
RC TISSUE=Bone {ECO:0000312|EMBL:BAC29509.1},
RC Embryonic stem cell {ECO:0000312|EMBL:BAC38647.1},
RC Head {ECO:0000312|EMBL:BAE36256.1},
RC Hypothalamus {ECO:0000312|EMBL:BAC29984.1},
RC Liver {ECO:0000312|EMBL:BAC34099.1}, Lung {ECO:0000312|EMBL:BAC39307.1},
RC Oviduct {ECO:0000312|EMBL:BAC35678.1}, and
RC Thymus {ECO:0000312|EMBL:BAC40717.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|EMBL:AAH60642.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH60642.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH60642.1};
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] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=15607700; DOI=10.1016/j.bcmd.2004.08.027;
RA Song C.Z., Gavriilidis G., Asano H., Stamatoyannopoulos G.;
RT "Functional study of transcription factor KLF11 by targeted gene
RT inactivation.";
RL Blood Cells Mol. Dis. 34:53-59(2005).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=18189266; DOI=10.1002/jcb.21669;
RA Gohla G., Krieglstein K., Spittau B.;
RT "Tieg3/Klf11 induces apoptosis in OLI-neu cells and enhances the TGF-beta
RT signaling pathway by transcriptional repression of Smad7.";
RL J. Cell. Biochem. 104:850-861(2008).
RN [6]
RP INDUCTION.
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: Transcription factor. Activates the epsilon- and gamma-globin
CC gene promoters and, to a much lower degree, the beta-globin gene and
CC represses promoters containing SP1-like binding sites inhibiting cell
CC growth (By similarity). Represses transcription of SMAD7 which enhances
CC TGF-beta signaling. Induces apoptosis. {ECO:0000250|UniProtKB:O14901,
CC ECO:0000269|PubMed:14697507, ECO:0000269|PubMed:18189266}.
CC -!- SUBUNIT: Interacts with SIN3A. {ECO:0000250|UniProtKB:O14901}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O14901}.
CC -!- INDUCTION: By TGF-beta. Expressed in a circadian manner in the kidney
CC and epididymal fat tissue. {ECO:0000269|PubMed:14697507,
CC ECO:0000269|PubMed:20385766}.
CC -!- DISRUPTION PHENOTYPE: Mice breed normally and are fertile.
CC Hematopoiesis at all stages of development is normal and there is no
CC effect on globin gene expression or longevity.
CC {ECO:0000269|PubMed:15607700}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC34099.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ459773; CAD30835.1; -; mRNA.
DR EMBL; AK036618; BAC29509.1; -; mRNA.
DR EMBL; AK038397; BAC29984.1; -; mRNA.
DR EMBL; AK050156; BAC34099.1; ALT_FRAME; mRNA.
DR EMBL; AK054170; BAC35678.1; -; mRNA.
DR EMBL; AK082838; BAC38647.1; -; mRNA.
DR EMBL; AK084913; BAC39307.1; -; mRNA.
DR EMBL; AK089044; BAC40717.1; -; mRNA.
DR EMBL; AK161233; BAE36256.1; -; mRNA.
DR EMBL; BC060642; AAH60642.1; -; mRNA.
DR CCDS; CCDS25842.1; -.
DR RefSeq; NP_848134.1; NM_178357.3.
DR AlphaFoldDB; Q8K1S5; -.
DR SMR; Q8K1S5; -.
DR BioGRID; 228800; 1.
DR STRING; 10090.ENSMUSP00000020982; -.
DR iPTMnet; Q8K1S5; -.
DR PhosphoSitePlus; Q8K1S5; -.
DR PaxDb; Q8K1S5; -.
DR PRIDE; Q8K1S5; -.
DR Antibodypedia; 12498; 367 antibodies from 32 providers.
DR DNASU; 194655; -.
DR Ensembl; ENSMUST00000020982; ENSMUSP00000020982; ENSMUSG00000020653.
DR GeneID; 194655; -.
DR KEGG; mmu:194655; -.
DR UCSC; uc007neo.2; mouse.
DR CTD; 8462; -.
DR MGI; MGI:2653368; Klf11.
DR VEuPathDB; HostDB:ENSMUSG00000020653; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000155982; -.
DR HOGENOM; CLU_046370_0_0_1; -.
DR InParanoid; Q8K1S5; -.
DR OMA; SCQPNVM; -.
DR OrthoDB; 582598at2759; -.
DR PhylomeDB; Q8K1S5; -.
DR TreeFam; TF315506; -.
DR BioGRID-ORCS; 194655; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Klf11; mouse.
DR PRO; PR:Q8K1S5; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8K1S5; protein.
DR Bgee; ENSMUSG00000020653; Expressed in animal zygote and 200 other tissues.
DR ExpressionAtlas; Q8K1S5; baseline and differential.
DR Genevisible; Q8K1S5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
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:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; ISO: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 2: Evidence at transcript level;
KW Activator; Apoptosis; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..502
FT /note="Krueppel-like factor 11"
FT /id="PRO_0000047189"
FT ZN_FING 384..408
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..438
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 444..466
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 133..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 262..263
FT /note="IT -> TA (in Ref. 1; CAD30835 and 2; BAC40717)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="S -> P (in Ref. 1; CAD30835)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="A -> V (in Ref. 1; CAD30835 and 2; BAC40717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 54054 MW; 158CD440B487F735 CRC64;
MHSPGSTGPG DGRAADIMDI CESILERKRH DSERSTCSVL EQTDIEAVEA LVCMSSWGQR
SQMRPLTPVS DSGDVTTAVL MDTAAPDLPK DFHSFSTLCI TPPQSPELTE PSTGTPVPSQ
VVNSKGCMVT ALPPSPAGGP RTLSKREPLE PASGSSCRAV MTSVIRHTGE SPAPTRFPTG
PTQEQRASDS GEGQERLLDH LEALQDTRLA NGLLVTNLVS CQPCLHKSGG SFPTDKGQQT
GWPAAVQTCL PKNPESDLSR KITPLISVPV SSPPVLCQMI PVAGQNGLFS AFLKPPTQLP
AGTIKPILPQ AASMSQPVFM GPPVPQGTVM LVLPQNTFPQ PAACPSSVMA IGNTKLLPLA
PAPVFLASSQ NCAPQVDFSR RRNYVCNFPG CRKTYFKSSH LKAHLRTHTG EKPFTCSWDG
CDKKFARSDE LSRHRRTHTG EKKFVCPVCD RRFMRSDHLT KHARRHMTTK KIPGWQAEVG
KLNRITLAES PGSILEPLPA SG
