ZN445_MOUSE
ID ZN445_MOUSE Reviewed; 986 AA.
AC Q8R2V3; A4FTX7; Q8K216;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Zinc finger protein 445;
GN Name=Znf445; Synonyms=Zfp445;
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/6J;
RA Zhou G., Wang J., Zhang Y.;
RT "Cloning of mouse zinc finger protein 445.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30602440; DOI=10.1101/gad.320069.118;
RA Takahashi N., Coluccio A., Thorball C.W., Planet E., Shi H., Offner S.,
RA Turelli P., Imbeault M., Ferguson-Smith A.C., Trono D.;
RT "ZNF445 is a primary regulator of genomic imprinting.";
RL Genes Dev. 33:49-54(2019).
CC -!- FUNCTION: Transcription regulator required to maintain maternal and
CC paternal gene imprinting, a process by which gene expression is
CC restricted in a parent of origin-specific manner by epigenetic
CC modification of genomic DNA and chromatin, including DNA methylation.
CC Acts by controlling DNA methylation during the earliest multicellular
CC stages of development at multiple imprinting control regions (ICRs)
CC (PubMed:30602440). Acts together with ZFP57, but ZFP57 plays the
CC predominant role in imprinting maintenance. In contrast, ZNF445 seems
CC to be the major factor in human early embryonic imprinting maintenance
CC (PubMed:30602440). {ECO:0000269|PubMed:30602440}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30602440}. Note=Binds
CC various differentially methylated regions (DMR).
CC {ECO:0000269|PubMed:30602440}.
CC -!- DISRUPTION PHENOTYPE: About one-third of zygotic mutants survived to
CC adulthood. They do not exhibit any loss of methylation imprints at ICRs
CC in the brain and liver at 12.5 dpc (PubMed:30602440). Double zygotic
CC mutations of ZFP57 and ZNF445 are embryonically lethal and embryos show
CC no gross morphological abnormalities but significant reduction in size
CC and weight at 11.5 dpc, a phenotype more pronounced than in ZFP57
CC mutant mice with a more severe loss of impinting (PubMed:30602440).
CC {ECO:0000269|PubMed:30602440}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34572.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY341877; AAQ24161.1; -; mRNA.
DR EMBL; BC027167; AAH27167.1; -; mRNA.
DR EMBL; BC034572; AAH34572.1; ALT_INIT; mRNA.
DR EMBL; BC099896; AAH99896.1; -; mRNA.
DR CCDS; CCDS23648.1; -.
DR RefSeq; NP_775540.4; NM_173364.5.
DR RefSeq; XP_006512186.1; XM_006512123.2.
DR AlphaFoldDB; Q8R2V3; -.
DR STRING; 10090.ENSMUSP00000055738; -.
DR iPTMnet; Q8R2V3; -.
DR PhosphoSitePlus; Q8R2V3; -.
DR MaxQB; Q8R2V3; -.
DR PaxDb; Q8R2V3; -.
DR PRIDE; Q8R2V3; -.
DR ProteomicsDB; 275289; -.
DR Antibodypedia; 29430; 48 antibodies from 13 providers.
DR DNASU; 235682; -.
DR Ensembl; ENSMUST00000056467; ENSMUSP00000055738; ENSMUSG00000047036.
DR Ensembl; ENSMUST00000216063; ENSMUSP00000151198; ENSMUSG00000047036.
DR GeneID; 235682; -.
DR KEGG; mmu:235682; -.
DR UCSC; uc009sfe.2; mouse.
DR CTD; 235682; -.
DR MGI; MGI:2143340; Zfp445.
DR VEuPathDB; HostDB:ENSMUSG00000047036; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00900000141186; -.
DR HOGENOM; CLU_002678_23_0_1; -.
DR InParanoid; Q8R2V3; -.
DR OMA; CHKCNIC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8R2V3; -.
DR TreeFam; TF350827; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 235682; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp445; mouse.
DR PRO; PR:Q8R2V3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R2V3; protein.
DR Bgee; ENSMUSG00000047036; Expressed in secondary palatal shelf and 260 other tissues.
DR ExpressionAtlas; Q8R2V3; baseline and differential.
DR Genevisible; Q8R2V3; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:UniProtKB.
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:0010216; P:maintenance of DNA methylation; IGI:UniProtKB.
DR GO; GO:2000653; P:regulation of genetic imprinting; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..986
FT /note="Zinc finger protein 445"
FT /id="PRO_0000047595"
FT DOMAIN 52..134
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 219..289
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 470..492
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 498..520
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 553..575
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 581..604
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 662..686
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 718..740
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 746..768
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 796..818
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 824..846
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 933..955
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 961..983
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 433..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 302
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P59923"
FT CROSSLNK 360
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P59923"
FT CROSSLNK 385
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P59923"
FT CROSSLNK 524
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P59923"
FT CROSSLNK 609
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P59923"
FT CROSSLNK 691
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P59923"
FT CROSSLNK 929
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P59923"
FT CONFLICT 495
FT /note="V -> L (in Ref. 2; AAH34572)"
FT /evidence="ECO:0000305"
FT CONFLICT 709
FT /note="R -> Q (in Ref. 2; AAH34572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 986 AA; 114774 MW; 26F5684634C32DFE CRC64;
MPPGRWHAAR SAQVSREQGC LRMVKEEEED GYISMQTARP QTLNRPGQEL FRQLFRQLRY
HESSGPLETL SRLQELCRWW MRPDVLSKAQ MLELLVLEQF LSILPGELRT WVQLHCPESG
AEVVALLEEL QRDLDGTPLK DPCLTQNPDV HWIGTSALQP AQIWSPASHL KNSSALEDHL
ETSHGIGICD VLAEQTDSPA VSVPDYFQLE EGIEYQEALT FQDVEVTFSQ EEWGCLNSAQ
RNLYRDVILE NYGNVVSVVG SSPKPALISW LEARKPWGVN ICTVQLKRDA DAAPEGGKLQ
IKPNKFILKQ KPSEYIEACV KTSVSPETSV SEETGLKESF KQKSRLQTSC GDSIQMKEMK
EGADISQRTG RESEVLRNND ILELKHVKCV SVSRKRLSFK HGYDRNFRKS SHHYNNKYGE
GLRGTGEGFG VYQNTGLKEN GKDRYGETSR KSWHAHPEHR QPSYSEEGLF QCRVCGKAFK
WRSNRIRHEK IHTGVKPYQC SLCEKAFQRL SSYRLHQKTH SKQKRGSSKY KNALTCSLDV
SHHLTDRDER KHLHCNQCGK NFSCKSYAIE HQRIHTQEKP YKCTRCRKTF RWKSNFSRHM
KLHHKEVYKQ EKRQEDFKQS YRQSQVISTV EKTFPCQNCG KTFTQKKSLI EHQRIHTGEK
PYQCSGCGET FTYRSSYIIH MKRTQHAIKI KPEHGCLTFS QGAVFPIPRG SHNTEGSNKC
KYCGKAFHNR SFLLIHERVH TREKPYQCRE CEKAFRWSSN LYRHQRKHFL HKRYKYRESK
ETSNLQSKIL IDQKPFWCQE CGKTFTRKRS LLDHKGIHSG ERRFKCNLCE KSFDRNYRLV
NHQRIHTTEQ PQWRDKDFVG IHARSVDQRK HSNTLQSEYG LHSDKPGLSY CQDVRLNIQE
LSGKLRKECD NPSDESSKSI AFQNVPTKKK ACHKCSTCGK TFKKHSHLIS HKRCHTKERP
FKCIVCGKTF RWSSNLTRHM KNHVRN
