ZFP1_MOUSE
ID ZFP1_MOUSE Reviewed; 402 AA.
AC P08042; P16074; Q7TNS0;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 25-MAY-2022, entry version 182.
DE RecName: Full=Zinc finger protein 1;
DE Short=Zfp-1;
DE AltName: Full=Protein mKR1;
GN Name=Zfp1; Synonyms=Fnp-1, Zfp-1;
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] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=2574853; DOI=10.1093/nar/17.24.10427;
RA Chowdhury K., Dietrich S., Balling R., Guenet J.-L., Gruss P.;
RT "Structure, expression and chromosomal localization of Zfp-1, a murine zinc
RT finger protein gene.";
RL Nucleic Acids Res. 17:10427-10438(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 63-402.
RX PubMed=3815523; DOI=10.1016/0092-8674(87)90074-2;
RA Chowdhury K., Deutsch U., Gruss P.;
RT "A multigene family encoding several 'finger' structures is present and
RT differentially active in mammalian genomes.";
RL Cell 48:771-778(1987).
RN [4]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=20624068; DOI=10.1089/dna.2010.1040;
RA Albertsen M., Teperek M., Elholm G., Fuechtbauer E.M., Lykke-Hartmann K.;
RT "Localization and differential expression of the Krueppel-associated box
RT zinc finger proteins 1 and 54 in early mouse development.";
RL DNA Cell Biol. 29:589-601(2010).
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20624068}. Note=Shows
CC widespread expression throughout the nucleus, but appears to be
CC excluded from nucleoli. {ECO:0000269|PubMed:20624068}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P08042-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P08042-2; Sequence=VSP_012683;
CC -!- DEVELOPMENTAL STAGE: Expressed at peak level in day 12 embryos
CC (PubMed:2574853). Isoform 1: Maternally contributed and highly
CC expressed at the zygotic stage, with rapidly decreasing expression at
CC the two cell stage remaining consistently low through to morula stage
CC (PubMed:20624068). {ECO:0000269|PubMed:20624068,
CC ECO:0000269|PubMed:2574853}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37639.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA34510.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X16493; CAA34510.1; ALT_FRAME; mRNA.
DR EMBL; BC055796; AAH55796.1; -; mRNA.
DR EMBL; BC062970; AAH62970.1; -; mRNA.
DR EMBL; M15708; AAA37639.1; ALT_FRAME; Genomic_DNA.
DR CCDS; CCDS85614.1; -. [P08042-2]
DR PIR; S15917; S15917.
DR RefSeq; NP_001032754.1; NM_001037665.2.
DR RefSeq; NP_035872.2; NM_011742.2.
DR AlphaFoldDB; P08042; -.
DR SMR; P08042; -.
DR BioGRID; 204630; 1.
DR STRING; 10090.ENSMUSP00000076964; -.
DR iPTMnet; P08042; -.
DR PhosphoSitePlus; P08042; -.
DR EPD; P08042; -.
DR PaxDb; P08042; -.
DR PeptideAtlas; P08042; -.
DR PRIDE; P08042; -.
DR ProteomicsDB; 302128; -. [P08042-1]
DR ProteomicsDB; 302129; -. [P08042-2]
DR DNASU; 22640; -.
DR GeneID; 22640; -.
DR KEGG; mmu:22640; -.
DR CTD; 162239; -.
DR MGI; MGI:99154; Zfp1.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; P08042; -.
DR OrthoDB; 1318335at2759; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 22640; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Zfp1; mouse.
DR PRO; PR:P08042; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P08042; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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: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; 6.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..402
FT /note="Zinc finger protein 1"
FT /id="PRO_0000047280"
FT DOMAIN 7..83
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 182..204
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 210..232
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 238..260
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 266..288
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 294..316
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 322..344
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 350..372
FT /note="C2H2-type 7; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 378..400
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..165
FT /note="Required for correct nuclear localization and
FT exclusion from the nucleoli"
FT /evidence="ECO:0000269|PubMed:20624068"
FT REGION 169..402
FT /note="Does not affect nuclear localization pattern"
FT /evidence="ECO:0000269|PubMed:20624068"
FT CROSSLNK 73
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6P2D0"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6P2D0"
FT CROSSLNK 143
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6P2D0"
FT VAR_SEQ 1..17
FT /note="MGSQGSVSFTDVTVDFT -> MMGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2574853"
FT /id="VSP_012683"
FT CONFLICT 372
FT /note="R -> H (in Ref. 1; CAA34510/AAA37639)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 46511 MW; 5FA205A7A37E3D09 CRC64;
MGSQGSVSFT DVTVDFTQEE WEQLDPSQRI LYMDVMLENY SNLLSVEVWK ADGQVERDPR
DLQRQVGSLT TIKNQPPTEE RGSRFGKTLT LNTDFVSLRQ VPYKYDLYEK TLKYNSDLLS
SRNCVRKKGD GCGGFGEPLL YLKQEKPHAG LEYSEYNGNG RALSHKDAIF KHRKIKSLVQ
PFVCNYCDKT FSFKSLLVSH KRIHTGEKPY ECDVCQKTFS HKANLIKHQR IHTGEKPFEC
PECGKAFTHQ SNLIVHQRAH MEKKPYGCSE CGKTFAQKFE LTTHQRIHTG ERPYECNECA
KTFFKKSNLI IHQKIHTGEK RYECSECGKS FIQNSQLIIH RRTHTGEKPY ECTECGKTFS
QRSTLRLHLR IRTGEKPYEC AECGKAFSRK SRLSVHQRVH MA
