KLF3_MOUSE
ID KLF3_MOUSE Reviewed; 344 AA.
AC Q60980;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Krueppel-like factor 3;
DE AltName: Full=Basic krueppel-like factor;
DE AltName: Full=CACCC-box-binding protein BKLF;
DE AltName: Full=TEF-2;
GN Name=Klf3; Synonyms=Bklf;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=DBA; TISSUE=Leukemia;
RX PubMed=8657145; DOI=10.1128/mcb.16.4.1695;
RA Crossley M., Whitelaw E., Perkins A., Williams G., Fujiwara Y., Orkin S.H.;
RT "Isolation and characterization of the cDNA encoding BKLF/TEF-2, a major
RT CACCC-box-binding protein in erythroid cells and selected other cells.";
RL Mol. Cell. Biol. 16:1695-1705(1996).
RN [2]
RP SUMOYLATION AT LYS-10 AND LYS-197, FUNCTION, AND MUTAGENESIS OF LYS-10;
RP GLU-12; LYS-197 AND GLU-199.
RX PubMed=15684403; DOI=10.1128/mcb.25.4.1549-1559.2005;
RA Perdomo J., Verger A., Turner J., Crossley M.;
RT "Role for SUMO modification in facilitating transcriptional repression by
RT BKLF.";
RL Mol. Cell. Biol. 25:1549-1559(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; SER-100; SER-107;
RP SER-110; SER-215 AND SER-223, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, 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).
RN [4]
RP STRUCTURE BY NMR OF 314-344 OF WILD TYPE AND MUTANT FORMS, SUBUNIT,
RP DNA-BINDING, AND MUTAGENESIS OF HIS-341.
RX PubMed=12736264; DOI=10.1074/jbc.m211146200;
RA Simpson R.J.Y., Cram E.D., Czolij R., Matthews J.M., Crossley M.,
RA Mackay J.P.;
RT "CCHX zinc finger derivatives retain the ability to bind Zn(II) and mediate
RT protein-DNA interactions.";
RL J. Biol. Chem. 278:28011-28018(2003).
CC -!- FUNCTION: Binds to the CACCC box of erythroid cell-expressed genes. May
CC play a role in hematopoiesis. {ECO:0000269|PubMed:15684403,
CC ECO:0000269|PubMed:8657145}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12736264}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In 8.5 day embryos, expressed in midbrain, anterior
CC hindbrain and ventral forebrain. In 9 day embryos, expressed throughout
CC ventral anterior half of embryo including midbrain-hindbrain junction,
CC ventral midbrain, diencephalon and forebrain. At 10.5 days,
CC distribution is more widespread with expression also found in
CC developing limb buds. Widely expressed in the adult.
CC {ECO:0000269|PubMed:8657145}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors. In KLF3, the motif is
CC inactive. {ECO:0000250|UniProtKB:P57682}.
CC -!- PTM: Sumoylated with SUMO1. Sumoylation is enhanced by PIAS1,
CC PIAS2alpha and PIAS2beta, and PIAS4, but not by Pc2. Enhances
CC transcriptional repression, but has no effect on DNA binding.
CC Sumoylation on Lys-197 is the major site.
CC {ECO:0000269|PubMed:15684403}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U36340; AAA93256.1; -; mRNA.
DR CCDS; CCDS19301.1; -.
DR PIR; JC6100; JC6100.
DR RefSeq; NP_032479.1; NM_008453.5.
DR RefSeq; XP_006503814.1; XM_006503751.3.
DR PDB; 1P7A; NMR; -; A=314-344.
DR PDB; 1U85; NMR; -; A=314-344.
DR PDB; 1U86; NMR; -; A=314-344.
DR PDBsum; 1P7A; -.
DR PDBsum; 1U85; -.
DR PDBsum; 1U86; -.
DR AlphaFoldDB; Q60980; -.
DR SMR; Q60980; -.
DR BioGRID; 200965; 3.
DR STRING; 10090.ENSMUSP00000129363; -.
DR iPTMnet; Q60980; -.
DR PhosphoSitePlus; Q60980; -.
DR jPOST; Q60980; -.
DR MaxQB; Q60980; -.
DR PaxDb; Q60980; -.
DR PRIDE; Q60980; -.
DR ProteomicsDB; 269223; -.
DR Antibodypedia; 10444; 185 antibodies from 29 providers.
DR DNASU; 16599; -.
DR Ensembl; ENSMUST00000165536; ENSMUSP00000129363; ENSMUSG00000029178.
DR Ensembl; ENSMUST00000166409; ENSMUSP00000128429; ENSMUSG00000029178.
DR GeneID; 16599; -.
DR KEGG; mmu:16599; -.
DR UCSC; uc008xmr.1; mouse.
DR CTD; 51274; -.
DR MGI; MGI:1342773; Klf3.
DR VEuPathDB; HostDB:ENSMUSG00000029178; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157456; -.
DR HOGENOM; CLU_002678_33_0_1; -.
DR InParanoid; Q60980; -.
DR OMA; QEAMEPV; -.
DR OrthoDB; 1014205at2759; -.
DR PhylomeDB; Q60980; -.
DR TreeFam; TF350556; -.
DR BioGRID-ORCS; 16599; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Klf3; mouse.
DR EvolutionaryTrace; Q60980; -.
DR PRO; PR:Q60980; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q60980; protein.
DR Bgee; ENSMUSG00000029178; Expressed in tail skin and 257 other tissues.
DR ExpressionAtlas; Q60980; baseline and differential.
DR Genevisible; Q60980; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISS:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IC:NTNU_SB.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 3D-structure; Activator; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..344
FT /note="Krueppel-like factor 3"
FT /id="PRO_0000047166"
FT ZN_FING 259..283
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 289..313
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 319..341
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..74
FT /note="Repressor domain"
FT REGION 66..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 60..68
FT /note="9aaTAD; inactive"
FT /evidence="ECO:0000250|UniProtKB:P57682"
FT MOTIF 61..65
FT /note="CTBP-binding motif"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57682"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57682"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15684403"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P57682"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P57682"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P57682"
FT MUTAGEN 10
FT /note="K->A: Reduced sumoylation levels. No effect on DNA-
FT binding and slight reduction of transcriptional repression.
FT Abolishes sumoylation. No effect on DNA-binding but great
FT reduction in transcriptional repression; when associated
FT with A-197."
FT /evidence="ECO:0000269|PubMed:15684403"
FT MUTAGEN 12
FT /note="E->A: Slight reduction of transcriptional
FT repression. Great reduction of transcriptional repression;
FT when associated with A-199."
FT /evidence="ECO:0000269|PubMed:15684403"
FT MUTAGEN 197
FT /note="K->A: Reduced sumoylation levels. No effect on DNA-
FT binding and slight reduction of transcriptional repression.
FT Abolishes sumoylation. No effect on DNA-binding but great
FT reduction of transcriptional repression; when associated
FT with A-10."
FT /evidence="ECO:0000269|PubMed:15684403"
FT MUTAGEN 199
FT /note="E->A: Slight reduction of transcriptional
FT repression. Great reduction of transcriptional repression;
FT when associated with A-199."
FT /evidence="ECO:0000269|PubMed:15684403"
FT MUTAGEN 341
FT /note="H->A,D,E,N,Q,R: Little change in DNA-binding
FT ability."
FT /evidence="ECO:0000269|PubMed:12736264"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:1P7A"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:1P7A"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:1P7A"
FT HELIX 331..338
FT /evidence="ECO:0007829|PDB:1P7A"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:1P7A"
SQ SEQUENCE 344 AA; 38561 MW; 2BB7E3B63A7C1D88 CRC64;
MLMFDPVPVK QEAMDPVSVS FPSNYIESMK PNKYGVIYST PLPDKFFQTP EGLTHGIQVE
PVDLTVNKRG SPPAAGGSPS SLKFPSHRRA SPGLSMPSSS PPIKKYSPPS PGVQPFGVPL
SMPPVMAAAL SRHGIRSPGI LPVIQPVVVQ PVPFMYTSHL QQPLMVSLSE EMDNSNSGMP
VPVIESYEKP LLQKKIKIEP GIEPQRTDYY PEEMSPPLMN PVSPPQALLQ ENHPSVIVQP
GKRPLPVESP DTQRKRRIHR CDYDGCNKVY TKSSHLKAHR RTHTGEKPYK CTWEGCTWKF
ARSDELTRHF RKHTGIKPFQ CPDCDRSFSR SDHLALHRKR HMLV
