ID   KLF5_MOUSE              Reviewed;         446 AA.
AC   Q9Z0Z7; Q9JMI2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Krueppel-like factor 5;
DE   AltName: Full=Basic transcription element-binding protein 2;
DE            Short=BTE-binding protein 2;
DE   AltName: Full=Intestinal-enriched krueppel-like factor;
DE   AltName: Full=Transcription factor BTEB2;
GN   Name=Klf5; Synonyms=Bteb2, Iklf;
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].
RC   STRAIN=C57BL/6J; TISSUE=Intestine;
RX   PubMed=9973612; DOI=10.1093/nar/27.5.1263;
RA   Conkright M.D., Wani M.A., Anderson K.P., Lingrel J.B.;
RT   "A gene encoding an intestinal-enriched member of the Kruppel-like factor
RT   family expressed in intestinal epithelial cells.";
RL   Nucleic Acids Res. 27:1263-1270(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10767086;
RX   DOI=10.1002/(sici)1097-0177(200004)217:4<421::aid-dvdy9>3.0.co;2-1;
RA   Ohnishi S., Laub F., Matsumoto N., Asaka M., Ramirez F., Yoshida T.,
RA   Terada M.;
RT   "Developmental expression of the mouse gene coding for the Kruppel-like
RT   transcription factor KLF5.";
RL   Dev. Dyn. 217:421-429(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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).
CC   -!- FUNCTION: Transcription factor that binds to GC box promoter elements.
CC       Activates the transcription of these genes.
CC   -!- SUBUNIT: Interacts with WWP1. Interacts with ANP32B; this interaction
CC       induces promoter region-specific histone incorporation and inhibition
CC       of histone acetylation by ANP32B. {ECO:0000250|UniProtKB:Q13887}.
CC   -!- INTERACTION:
CC       Q9Z0Z7; Q969H0: FBXW7; Xeno; NbExp=2; IntAct=EBI-647919, EBI-359574;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Highest expression in digestive track.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000250|UniProtKB:Q13887}.
CC   -!- PTM: Ubiquitinated (By similarity). Polyubiquitination involves WWP1
CC       and leads to proteasomal degradation of this protein. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF079852; AAD17696.1; -; mRNA.
DR   EMBL; AB025099; BAA92284.3; -; mRNA.
DR   EMBL; BC012958; AAH12958.1; -; mRNA.
DR   CCDS; CCDS27311.1; -.
DR   RefSeq; NP_033899.2; NM_009769.4.
DR   AlphaFoldDB; Q9Z0Z7; -.
DR   SMR; Q9Z0Z7; -.
DR   BioGRID; 198396; 12.
DR   CORUM; Q9Z0Z7; -.
DR   DIP; DIP-49582N; -.
DR   IntAct; Q9Z0Z7; 6.
DR   MINT; Q9Z0Z7; -.
DR   STRING; 10090.ENSMUSP00000005279; -.
DR   GlyGen; Q9Z0Z7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Z0Z7; -.
DR   PhosphoSitePlus; Q9Z0Z7; -.
DR   MaxQB; Q9Z0Z7; -.
DR   PaxDb; 10090-ENSMUSP00000005279; -.
DR   PeptideAtlas; Q9Z0Z7; -.
DR   ProteomicsDB; 263649; -.
DR   Antibodypedia; 24429; 461 antibodies from 35 providers.
DR   DNASU; 12224; -.
DR   Ensembl; ENSMUST00000005279.8; ENSMUSP00000005279.7; ENSMUSG00000005148.9.
DR   GeneID; 12224; -.
DR   KEGG; mmu:12224; -.
DR   UCSC; uc007uvf.1; mouse.
DR   AGR; MGI:1338056; -.
DR   CTD; 688; -.
DR   MGI; MGI:1338056; Klf5.
DR   VEuPathDB; HostDB:ENSMUSG00000005148; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000156711; -.
DR   HOGENOM; CLU_002678_33_3_1; -.
DR   InParanoid; Q9Z0Z7; -.
DR   OMA; QEMPSQF; -.
DR   OrthoDB; 3168417at2759; -.
DR   PhylomeDB; Q9Z0Z7; -.
DR   TreeFam; TF350556; -.
DR   BioGRID-ORCS; 12224; 8 hits in 79 CRISPR screens.
DR   ChiTaRS; Klf5; mouse.
DR   PRO; PR:Q9Z0Z7; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q9Z0Z7; Protein.
DR   Bgee; ENSMUSG00000005148; Expressed in left colon and 263 other cell types or tissues.
DR   ExpressionAtlas; Q9Z0Z7; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043426; F:MRF binding; IPI:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR   GO; GO:0099156; P:cell-cell signaling via exosome; ISO:MGI.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
DR   GO; GO:0060576; P:intestinal epithelial cell development; IMP:MGI.
DR   GO; GO:0030033; P:microvillus assembly; IMP:MGI.
DR   GO; GO:0014908; P:myotube differentiation involved in skeletal muscle regeneration; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:MGI.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:MGI.
DR   GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0061586; P:positive regulation of transcription by transcription factor localization; IDA:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0032534; P:regulation of microvillus assembly; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0014901; P:satellite cell activation involved in skeletal muscle regeneration; IMP:MGI.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR   GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IMP:MGI.
DR   GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:MGI.
DR   CDD; cd21579; KLF5_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:SF82; KRUEPPEL-LIKE FACTOR 5; 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; Q9Z0Z7; MM.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..446
FT                   /note="Krueppel-like factor 5"
FT                   /id="PRO_0000047170"
FT   ZN_FING         362..386
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         392..416
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         422..444
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          50..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..317
FT                   /note="Interaction with WWP1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           107..115
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:Q13887"
FT   CROSSLNK        31
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13887"
FT   CROSSLNK        52
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13887"
FT   CROSSLNK        83
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13887"
FT   CROSSLNK        99
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13887"
FT   CONFLICT        23
FT                   /note="D -> A (in Ref. 2; AAD17696)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   446 AA;  49754 MW;  D8D1DBB952448AC5 CRC64;
     MPTRVLTMSA RLGPLPQPPA AQDEPVFAQL KPVLGAANPA RDAALFSGDD LKHAHHHPPA
     PPPAAGPRLP SEELVQTRCE MEKYLTPQLP PVPIISEHKK YRRDSASVVD QFFTDTEGIP
     YSINMNVFLP DITHLRTGLY KSQRPCVTQI KTEPVTIFSH QSESTAPPPP PAPTQALPEF
     TSIFSSHQTT APPQEVNNIF IKQELPIPDL HLSVPSQQGH LYQLLNTPDL DMPSSTNQTA
     VMDTLNVSMA GLNPHPSAVP QTSMKQFQGM PPCTYTMPSQ FLPQQATYFP PSPPSSEPGS
     PDRQAEMLQN LTPPPSYAAT IASKLAIHNP NLPATLPVNS PTLPPVRYNR RSNPDLEKRR
     IHFCDYNGCT KVYTKSSHLK AHLRTHTGEK PYKCTWEGCD WRFARSDELT RHYRKHTGAK
     PFQCMVCQRS FSRSDHLALH MKRHQN
//