KLF2_MOUSE
ID KLF2_MOUSE Reviewed; 354 AA.
AC Q60843; B2RS60;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Krueppel-like factor 2;
DE AltName: Full=Lung krueppel-like factor;
GN Name=Klf2; Synonyms=Lklf;
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/6 X CBA; TISSUE=Lung;
RX PubMed=7565748; DOI=10.1128/mcb.15.11.5957;
RA Anderson K.P., Kern C.B., Crable S.C., Lingrel J.B.;
RT "Isolation of a gene encoding a functional zinc finger protein homologous
RT to erythroid Kruppel-like factor: identification of a new multigene
RT family.";
RL Mol. Cell. Biol. 15:5957-5965(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP INTERACTION WITH WWP1.
RX PubMed=11375995; DOI=10.1074/jbc.m103670200;
RA Conkright M.D., Wani M.A., Lingrel J.B.;
RT "Lung Krueppel-like factor contains an autoinhibitory domain that regulates
RT its transcriptional activation by binding WWP1, an E3 ubiquitin ligase.";
RL J. Biol. Chem. 276:29299-29306(2001).
RN [4]
RP INTERACTION WITH WWP1, MUTAGENESIS OF LYS-121 AND LYS-146, AND
RP UBIQUITINATION.
RX PubMed=15003522; DOI=10.1016/j.bbrc.2004.02.033;
RA Zhang X., Srinivasan S.V., Lingrel J.B.;
RT "WWP1-dependent ubiquitination and degradation of the lung Kruppel-like
RT factor, KLF2.";
RL Biochem. Biophys. Res. Commun. 316:139-148(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-171; THR-243 AND SER-246, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcription factor that binds to the CACCC box in the
CC promoter of target genes such as HBB/beta globin or NOV and activates
CC their transcription. Might be involved in transcriptional regulation by
CC modulating the binding of the RARA nuclear receptor to RARE DNA
CC elements (By similarity). {ECO:0000250|UniProtKB:Q9Y5W3}.
CC -!- SUBUNIT: Interacts with WWP1. {ECO:0000269|PubMed:11375995,
CC ECO:0000269|PubMed:15003522}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominant expression in the lungs and spleen.
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:Q9Y5W3}.
CC -!- PTM: Ubiquitinated. Polyubiquitination involves WWP1 and leads to
CC proteasomal degradation of this protein. {ECO:0000269|PubMed:15003522}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U25096; AAA86728.1; -; mRNA.
DR EMBL; BC138737; AAI38738.1; -; mRNA.
DR EMBL; BC138738; AAI38739.1; -; mRNA.
DR CCDS; CCDS22412.1; -.
DR RefSeq; NP_032478.2; NM_008452.2.
DR AlphaFoldDB; Q60843; -.
DR SMR; Q60843; -.
DR BioGRID; 200964; 2.
DR STRING; 10090.ENSMUSP00000064823; -.
DR iPTMnet; Q60843; -.
DR PhosphoSitePlus; Q60843; -.
DR jPOST; Q60843; -.
DR MaxQB; Q60843; -.
DR PaxDb; Q60843; -.
DR PRIDE; Q60843; -.
DR ProteomicsDB; 263619; -.
DR Antibodypedia; 27348; 459 antibodies from 32 providers.
DR DNASU; 16598; -.
DR Ensembl; ENSMUST00000067912; ENSMUSP00000064823; ENSMUSG00000055148.
DR GeneID; 16598; -.
DR KEGG; mmu:16598; -.
DR UCSC; uc009mfq.2; mouse.
DR CTD; 10365; -.
DR MGI; MGI:1342772; Klf2.
DR VEuPathDB; HostDB:ENSMUSG00000055148; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163163; -.
DR HOGENOM; CLU_002678_33_1_1; -.
DR InParanoid; Q60843; -.
DR OMA; LHERWKC; -.
DR OrthoDB; 1273088at2759; -.
DR TreeFam; TF350556; -.
DR BioGRID-ORCS; 16598; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Klf2; mouse.
DR PRO; PR:Q60843; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q60843; protein.
DR Bgee; ENSMUSG00000055148; Expressed in granulocyte and 212 other tissues.
DR Genevisible; Q60843; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; ISS:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS: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:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0071409; P:cellular response to cycloheximide; IEA:Ensembl.
DR GO; GO:0071498; P:cellular response to fluid shear stress; ISO:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0071499; P:cellular response to laminar fluid shear stress; ISO:MGI.
DR GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0097533; P:cellular stress response to acid chemical; ISO:MGI.
DR GO; GO:0034101; P:erythrocyte homeostasis; IMP:MGI.
DR GO; GO:0043249; P:erythrocyte maturation; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
DR GO; GO:0048386; P:positive regulation of retinoic acid receptor signaling pathway; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060509; P:type I pneumocyte differentiation; IMP:MGI.
DR GO; GO:0042311; P:vasodilation; 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 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..354
FT /note="Krueppel-like factor 2"
FT /id="PRO_0000047163"
FT ZN_FING 271..295
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 301..325
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 331..353
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 52..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..267
FT /note="Interaction with WWP1"
FT REGION 145..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 42..50
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5W3"
FT COMPBIAS 58..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 243
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 121
FT /note="K->R: Greatly impairs polyubiquitination. Abolishes
FT polyubiquitination; when associated with R-146."
FT /evidence="ECO:0000269|PubMed:15003522"
FT MUTAGEN 146
FT /note="K->R: Abolishes polyubiquitination; when associated
FT with R-121."
FT /evidence="ECO:0000269|PubMed:15003522"
FT CONFLICT 88
FT /note="A -> D (in Ref. 1; AAA86728)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 37657 MW; 31A99C00DFC5B810 CRC64;
MALSEPILPS FATFASPCER GLQERWPRNE PEAGGTDEDL NNVLDFILSM GLDGLGAENP
PEPPPQPPPP AFYYPEPGAP PPYSIPAASL GTELLRPDLD PPQGPALHGR FLLAPPGRLV
KAEPPEVDGG GYGCAPGLAH GPRGLKLEGA PGATGACMRG PAGRPPPPPD TPPLSPDGPL
RIPASGPRNP FPPPFGPGPS FGGPGPALHY GPPAPGAFGL FEDAAAAAAA LGLAPPATRG
LLTPPSSPLE LLEAKPKRGR RSWPRKRAAT HTCSYTNCGK TYTKSSHLKA HLRTHTGEKP
YHCNWEGCGW KFARSDELTR HYRKHTGHRP FQCHLCDRAF SRSDHLALHM KRHM
