ZFP69_MOUSE
ID ZFP69_MOUSE Reviewed; 587 AA.
AC A2A761;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Zinc finger protein 69 {ECO:0000305};
DE AltName: Full=Zinc finger protein 642;
GN Name=Zfp69 {ECO:0000312|MGI:MGI:107794}; Synonyms=Znf642;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP POLYMORPHISM, AND FUNCTION.
RX PubMed=19578398; DOI=10.1371/journal.pgen.1000541;
RA Scherneck S., Nestler M., Vogel H., Blueher M., Block M.D.,
RA Berriel Diaz M., Herzig S., Schulz N., Teichert M., Tischer S.,
RA Al-Hasani H., Kluge R., Schuermann A., Joost H.G.;
RT "Positional cloning of zinc finger domain transcription factor Zfp69, a
RT candidate gene for obesity-associated diabetes contributed by mouse locus
RT Nidd/SJL.";
RL PLoS Genet. 5:E1000541-E1000541(2009).
RN [3]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=26232096; DOI=10.1007/s00125-015-3703-8;
RA Chung B., Stadion M., Schulz N., Jain D., Scherneck S., Joost H.G.,
RA Schuermann A.;
RT "The diabetes gene Zfp69 modulates hepatic insulin sensitivity in mice.";
RL Diabetologia 58:2403-2413(2015).
CC -!- FUNCTION: Putative transcription factor that appears to regulate lipid
CC metabolism. {ECO:0000269|PubMed:19578398, ECO:0000269|PubMed:26232096}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26232096}.
CC -!- POLYMORPHISM: New Zealand obese (NZO) mice carry a loss-of-function
CC mutation due to the integration of the retrotransposon IAPLTR1 in
CC intron 3 which generates a truncated mRNA lacking both the KRAB and the
CC C2H2 domains. This strain is less diabetes prone (NZO).
CC {ECO:0000269|PubMed:19578398}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL606904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18597.2; -.
DR RefSeq; NP_001005788.2; NM_001005788.3.
DR AlphaFoldDB; A2A761; -.
DR SMR; A2A761; -.
DR STRING; 10090.ENSMUSP00000101887; -.
DR iPTMnet; A2A761; -.
DR PhosphoSitePlus; A2A761; -.
DR MaxQB; A2A761; -.
DR PaxDb; A2A761; -.
DR PeptideAtlas; A2A761; -.
DR PRIDE; A2A761; -.
DR ProteomicsDB; 344659; -.
DR Antibodypedia; 32097; 41 antibodies from 16 providers.
DR DNASU; 381549; -.
DR Ensembl; ENSMUST00000106280; ENSMUSP00000101887; ENSMUSG00000064141.
DR Ensembl; ENSMUST00000106281; ENSMUSP00000101888; ENSMUSG00000064141.
DR GeneID; 381549; -.
DR KEGG; mmu:381549; -.
DR UCSC; uc008unv.2; mouse.
DR CTD; 339559; -.
DR MGI; MGI:107794; Zfp69.
DR VEuPathDB; HostDB:ENSMUSG00000064141; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162278; -.
DR HOGENOM; CLU_002678_0_13_1; -.
DR InParanoid; A2A761; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; A2A761; -.
DR TreeFam; TF337055; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 381549; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Zfp69; mouse.
DR PRO; PR:A2A761; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2A761; protein.
DR Bgee; ENSMUSG00000064141; Expressed in tertiary ovarian follicle and 133 other tissues.
DR ExpressionAtlas; A2A761; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 3: Inferred from homology;
KW DNA-binding; Lipid metabolism; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..587
FT /note="Zinc finger protein 69"
FT /id="PRO_0000444716"
FT DOMAIN 76..147
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 271..293
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 299..321
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 327..349
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 355..377
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..405
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 411..433
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 439..461
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 467..489
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..517
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 42..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 65725 MW; 762F13B25B00426D CRC64;
MPQQLLITPA TEATWVKLKE VSLWEDVTKM FGGEALLSHD ANGTQQESLA DGTTPGTPAA
GSHDGATPGT TATGSHDEAT PGTPAAGSHD GETPGIPAAG SHDGETPGTP TAGSHDGVTP
GTTAAGSQES LTFKDIAVDL SQEEWGQLAP AYQDLYREVM LENYRNLVSV AGYQLSKPTV
ISQLEKGEGP CMAESQGPED PILDVKNKLE TKESTAEDDI SVKLDHGITR GRLIEDDIVC
SPLKKASSYS DTLESHRATC GKGTRRAIWT HKKKRQEGNK LENPESSNVI LEQKHRKHKP
ARKRNKYKLD SIDHPVSCMR ARRYPCNVCE KMFKQPIHLV EHMRTHTGEK PFRCKECGRA
FSQSASLNTH QRIHTGEKPF ACEECGKAFR HRSSLNQHHR THTGEKPFTC DKCQKAFSQN
ISLVQHLRTH SGEKPFSCSE CGKPFRQIRH LSEHVRIHTG EKPYKCTSCC KTFSHRAYLT
HHQRIHTGER PYKCKECGKA FRQRIHLSNH RTVHTGVKAY ECNRCGKAYR HDSSFKKHQR
HHTGEKPYEC TECGKSFSYN SSLSRHQKIH RRNTFRDDPG HENKRQL
