ID   KLF7_MOUSE              Reviewed;         301 AA.
AC   Q99JB0; Q99P62;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Krueppel-like factor 7;
GN   Name=Klf7;
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], AND DEVELOPMENTAL STAGE.
RC   STRAIN=CD-1;
RX   PubMed=11245580; DOI=10.1242/dev.128.7.1147;
RA   Lei L., Ma L., Nef S., Thai T., Parada L.F.;
RT   "mKlf7, a potential transcriptional regulator of TrkA nerve growth factor
RT   receptor expression in sensory and sympathetic neurons.";
RL   Development 128:1147-1158(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=Swiss Webster / NIH;
RX   PubMed=11336497; DOI=10.1006/dbio.2001.0243;
RA   Laub F.B., Aldabe R., Friedrich V. Jr., Ohnishi S., Yoshida T., Ramirez F.;
RT   "Developmental expression of mouse Kruppel-like transcription factor KLF7
RT   suggests a potential role in neurogenesis.";
RL   Dev. Biol. 233:305-318(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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]
RP   INTERACTION WITH FBXO38.
RX   PubMed=14729953; DOI=10.1128/mcb.24.3.1058-1069.2004;
RA   Smaldone S., Laub F., Else C., Dragomir C., Ramirez F.;
RT   "Identification of MoKA, a novel F-box protein that modulates Krueppel-like
RT   transcription factor 7 activity.";
RL   Mol. Cell. Biol. 24:1058-1069(2004).
RN   [5]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=15964824; DOI=10.1128/mcb.25.13.5699-5711.2005;
RA   Laub F., Lei L., Sumiyoshi H., Kajimura D., Dragomir C., Smaldone S.,
RA   Puche A.C., Petros T.J., Mason C., Parada L.F., Ramirez F.;
RT   "Transcription factor KLF7 is important for neuronal morphogenesis in
RT   selected regions of the nervous system.";
RL   Mol. Cell. Biol. 25:5699-5711(2005).
RN   [6]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=28916725; DOI=10.1074/jbc.m117.793117;
RA   Klein R.H., Hu W., Kashgari G., Lin Z., Nguyen T., Doan M., Andersen B.;
RT   "Characterization of enhancers and the role of the transcription factor
RT   KLF7 in regulating corneal epithelial differentiation.";
RL   J. Biol. Chem. 292:18937-18950(2017).
CC   -!- FUNCTION: Transcriptional factor (PubMed:11245580). Plays a critical
CC       role in neuronal morphogenesis (PubMed:11336497, PubMed:15964824).
CC       Represses the corneal epithelium differentiation (By similarity). Acts
CC       also as a metabolic regulator, by modulating insulin sensitivity in
CC       pancreatic beta cells and skeletal muscle cells. Inhibits
CC       transcriptional inducers of adipogenesis and has a repressive role in
CC       the expression of several adipokines, including leptin (By similarity).
CC       {ECO:0000250|UniProtKB:O75840, ECO:0000269|PubMed:11245580,
CC       ECO:0000269|PubMed:11336497, ECO:0000269|PubMed:15964824}.
CC   -!- SUBUNIT: Interacts with FBXO38. {ECO:0000269|PubMed:14729953}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75840}.
CC   -!- TISSUE SPECIFICITY: Widely expressed (PubMed:11336497). Detected in the
CC       cornea epithelium (at protein level) (PubMed:28916725).
CC       {ECO:0000269|PubMed:11336497, ECO:0000269|PubMed:28916725}.
CC   -!- DEVELOPMENTAL STAGE: Expression starts at 8.5 dpc in the trigeminal
CC       ganglion, the VII-VIII neural crest complex, and the subventricular
CC       neuroepithelium of both forebrain and hindbrain regions. At 11.5 dpc,
CC       expression is detected in the neural crest-derived sensory nervous
CC       system and, at 15.5 dpc, in the brain, spinal cord, retinal
CC       neuroepithelium and the inferior XI/X complex (PubMed:11336497,
CC       PubMed:11245580). In postnatal and adult animals, expression is
CC       confined to the cerebellum and dorsal root ganglia (PubMed:11336497).
CC       Expressed in the cornea epithelium at both 18.5 dpc and early postnatal
CC       (P5) but not at P50, when the corneal epithelium is fully
CC       differentiated (PubMed:28916725). {ECO:0000269|PubMed:11245580,
CC       ECO:0000269|PubMed:11336497, ECO:0000269|PubMed:28916725}.
CC   -!- DOMAIN: The acidic N-terminal part may favor interaction with the basic
CC       domain of transcription factors. {ECO:0000250|UniProtKB:O75840}.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors. In KLF7, the motif is
CC       inactive. {ECO:0000250|UniProtKB:O75840}.
CC   -!- DISRUPTION PHENOTYPE: Deficient mice die within the first 3 days of
CC       life, showing little or no milk in the stomachs, hypopnea, cyanosis,
CC       olfactory bulb hypoplasia, axon outgrowth defects in the olfactory and
CC       optic nerves, defects of axon growth in the brain and reduced dendritic
CC       branching in the hippocampus. {ECO:0000269|PubMed:28916725}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF338369; AAK31139.1; -; mRNA.
DR   EMBL; AF327568; AAK08964.1; -; mRNA.
DR   EMBL; BC004700; AAH04700.1; -; mRNA.
DR   EMBL; BC019604; AAH19604.1; -; mRNA.
DR   EMBL; BC040794; AAH40794.1; -; mRNA.
DR   CCDS; CCDS15003.1; -.
DR   RefSeq; NP_291041.2; NM_033563.2.
DR   RefSeq; XP_006496417.1; XM_006496354.3.
DR   AlphaFoldDB; Q99JB0; -.
DR   SMR; Q99JB0; -.
DR   STRING; 10090.ENSMUSP00000109720; -.
DR   iPTMnet; Q99JB0; -.
DR   PhosphoSitePlus; Q99JB0; -.
DR   MaxQB; Q99JB0; -.
DR   PaxDb; 10090-ENSMUSP00000109720; -.
DR   ProteomicsDB; 263621; -.
DR   Antibodypedia; 34186; 302 antibodies from 28 providers.
DR   DNASU; 93691; -.
DR   Ensembl; ENSMUST00000114086.8; ENSMUSP00000109720.3; ENSMUSG00000025959.14.
DR   GeneID; 93691; -.
DR   KEGG; mmu:93691; -.
DR   UCSC; uc007bgo.2; mouse.
DR   AGR; MGI:1935151; -.
DR   CTD; 8609; -.
DR   MGI; MGI:1935151; Klf7.
DR   VEuPathDB; HostDB:ENSMUSG00000025959; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000155235; -.
DR   HOGENOM; CLU_002678_33_4_1; -.
DR   InParanoid; Q99JB0; -.
DR   OMA; DCFLHAA; -.
DR   OrthoDB; 3168417at2759; -.
DR   PhylomeDB; Q99JB0; -.
DR   TreeFam; TF350556; -.
DR   BioGRID-ORCS; 93691; 4 hits in 80 CRISPR screens.
DR   ChiTaRS; Klf7; mouse.
DR   PRO; PR:Q99JB0; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q99JB0; Protein.
DR   Bgee; ENSMUSG00000025959; Expressed in rostral migratory stream and 264 other cell types or tissues.
DR   ExpressionAtlas; Q99JB0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; IDA:MGI.
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; ISO:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR   GO; GO:1904178; P:negative regulation of adipose tissue development; ISS:UniProtKB.
DR   GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045604; P:regulation of epidermal cell differentiation; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd21585; KLF7_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:SF77; KRUEPPEL-LIKE FACTOR 7; 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; Q99JB0; MM.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..301
FT                   /note="Krueppel-like factor 7"
FT                   /id="PRO_0000047175"
FT   ZN_FING         218..242
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         248..272
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         278..300
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   MOTIF           93..101
FT                   /note="9aaTAD; inactive"
FT                   /evidence="ECO:0000250|UniProtKB:O75840"
FT   MOTIF           214..219
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        175
FT                   /note="S -> P (in Ref. 2; AAK08964)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   301 AA;  33337 MW;  3AEB7135A9F6E6E7 CRC64;
     MDVLASYSIF QELQLVHDTG YFSALPSLEE TWQQTCLELE RYLQTEPRRI SETFGEDLDC
     FLHASPPPCI EESFRRLDPL LLPVEATICE KSSAVDILLS RDKLLSETCL SLQPTSSSLD
     SYTAVNQAQL NAVTSLTPPS SPELSRHLVK TSQTLSAVDG TVTLKLVAKK ASLSSVKVGG
     VAAAAAVTPA GAVKSGQSDS EQGGGGADTC PENKKRVHRC QFNGCRKVYT KSSHLKAHQR
     THTGEKPYKC SWEGCEWRFA RSDELTRHYR KHTGAKPFKC NHCDRCFSRS DHLALHMKRH
     I
//