KLF5_MOUSE
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 03-AUG-2022, entry version 186.
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; 11.
DR CORUM; Q9Z0Z7; -.
DR DIP; DIP-49582N; -.
DR IntAct; Q9Z0Z7; 6.
DR MINT; Q9Z0Z7; -.
DR STRING; 10090.ENSMUSP00000005279; -.
DR iPTMnet; Q9Z0Z7; -.
DR PhosphoSitePlus; Q9Z0Z7; -.
DR MaxQB; Q9Z0Z7; -.
DR PaxDb; Q9Z0Z7; -.
DR PeptideAtlas; Q9Z0Z7; -.
DR PRIDE; Q9Z0Z7; -.
DR ProteomicsDB; 263649; -.
DR Antibodypedia; 24429; 373 antibodies from 35 providers.
DR DNASU; 12224; -.
DR Ensembl; ENSMUST00000005279; ENSMUSP00000005279; ENSMUSG00000005148.
DR GeneID; 12224; -.
DR KEGG; mmu:12224; -.
DR UCSC; uc007uvf.1; mouse.
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; 382638at2759; -.
DR PhylomeDB; Q9Z0Z7; -.
DR TreeFam; TF350556; -.
DR BioGRID-ORCS; 12224; 8 hits in 74 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 260 other tissues.
DR ExpressionAtlas; Q9Z0Z7; baseline and differential.
DR Genevisible; Q9Z0Z7; MM.
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: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: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:0045893; P:positive regulation of transcription, DNA-templated; IMP: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 InterPro; IPR030401; KLF5.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23235:SF82; PTHR23235:SF82; 1.
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 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
