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   27-MAR-2024, entry version 156.
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 NOD
RC   {ECO:0000312|EMBL:BAC40717.1};
RC   TISSUE=Bone {ECO:0000312|EMBL:BAC29509.1}, Embryonic stem cell
RC   {ECO:0000312|EMBL:BAC38647.1}, Head {ECO:0000312|EMBL:BAE36256.1},
RC   Hypothalamus {ECO:0000312|EMBL:BAC29984.1}, Liver
RC   {ECO:0000312|EMBL:BAC34099.1}, Lung {ECO:0000312|EMBL:BAC39307.1},
RC   Oviduct {ECO:0000312|EMBL:BAC35678.1}, and Thymus
RC   {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; 10090-ENSMUSP00000020982; -.
DR   ProteomicsDB; 264766; -.
DR   Antibodypedia; 12498; 416 antibodies from 32 providers.
DR   DNASU; 194655; -.
DR   Ensembl; ENSMUST00000020982.7; ENSMUSP00000020982.6; ENSMUSG00000020653.13.
DR   GeneID; 194655; -.
DR   KEGG; mmu:194655; -.
DR   UCSC; uc007neo.2; mouse.
DR   AGR; MGI:2653368; -.
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; ENEEPHC; -.
DR   OrthoDB; 2916922at2759; -.
DR   PhylomeDB; Q8K1S5; -.
DR   TreeFam; TF315506; -.
DR   BioGRID-ORCS; 194655; 0 hits in 79 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 203 other cell types or tissues.
DR   ExpressionAtlas; Q8K1S5; baseline and differential.
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:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd21584; KLF11_N; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23235:SF65; KRUEPPEL-LIKE FACTOR 11; 1.
DR   PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
DR   Genevisible; Q8K1S5; MM.
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
//