ZNF8_MOUSE
ID ZNF8_MOUSE Reviewed; 572 AA.
AC Q8BGV5; Q52KP6; Q8BJ50;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Zinc finger protein 8 {ECO:0000303|PubMed:12370310};
DE AltName: Full=Zinc finger protein 128 {ECO:0000312|MGI:MGI:2389445};
GN Name=Znf8 {ECO:0000303|PubMed:12370310};
GN Synonyms=Zfp128 {ECO:0000312|MGI:MGI:2389445};
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] {ECO:0000312|EMBL:AAN40973.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SMAD1; SMAD2; SMAD3;
RP SMAD4 AND SMAD5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=CD-1 {ECO:0000312|EMBL:AAN40973.1};
RX PubMed=12370310; DOI=10.1128/mcb.22.21.7633-7644.2002;
RA Jiao K., Zhou Y., Hogan B.L.M.;
RT "Identification of mZnf8, a mouse Kruppel-like transcriptional repressor,
RT as a novel nuclear interaction partner of Smad1.";
RL Mol. Cell. Biol. 22:7633-7644(2002).
RN [2] {ECO:0000312|EMBL:BAC29237.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [4] {ECO:0000312|EMBL:AAH88998.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH88998.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH88998.1};
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).
CC -!- FUNCTION: Transcriptional repressor. May modulate BMP and TGF-beta
CC signal transduction, through its interaction with SMAD proteins.
CC {ECO:0000269|PubMed:12370310}.
CC -!- SUBUNIT: Interacts with SMAD1 (via MH1 and MH2 domains). Interacts with
CC SMAD5. Interacts weakly with SMAD2, SMAD3 and SMAD4.
CC {ECO:0000269|PubMed:12370310}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12370310}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in testis, where it localizes to
CC seminiferous tubules. Weakly expressed in heart, brain, lung, liver and
CC kidney. {ECO:0000269|PubMed:12370310}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in embryos. Detected from
CC stage 7 dpc onwards, reaching peak levels at stage 11 dpc and declining
CC by stages 15 dpc and 17 dpc. {ECO:0000269|PubMed:12370310}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27668.1; Type=Frameshift; Evidence={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; AF480861; AAN40973.1; -; mRNA.
DR EMBL; AK032046; BAC27668.1; ALT_FRAME; mRNA.
DR EMBL; AK035906; BAC29237.1; -; mRNA.
DR EMBL; AC107704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC088998; AAH88998.1; -; mRNA.
DR EMBL; BC094248; AAH94248.1; -; mRNA.
DR CCDS; CCDS20815.1; -.
DR RefSeq; NP_722497.1; NM_153802.4.
DR AlphaFoldDB; Q8BGV5; -.
DR SMR; Q8BGV5; -.
DR STRING; 10090.ENSMUSP00000115378; -.
DR iPTMnet; Q8BGV5; -.
DR PhosphoSitePlus; Q8BGV5; -.
DR EPD; Q8BGV5; -.
DR MaxQB; Q8BGV5; -.
DR PaxDb; Q8BGV5; -.
DR PRIDE; Q8BGV5; -.
DR ProteomicsDB; 275100; -.
DR Antibodypedia; 74823; 92 antibodies from 15 providers.
DR DNASU; 243833; -.
DR Ensembl; ENSMUST00000144578; ENSMUSP00000115378; ENSMUSG00000060397.
DR GeneID; 243833; -.
DR KEGG; mmu:243833; -.
DR UCSC; uc009fek.2; mouse.
DR UCSC; uc012ezc.1; mouse.
DR CTD; 243833; -.
DR MGI; MGI:2389445; Zfp128.
DR VEuPathDB; HostDB:ENSMUSG00000060397; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162352; -.
DR HOGENOM; CLU_002678_0_3_1; -.
DR InParanoid; Q8BGV5; -.
DR OMA; ECQSQGL; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8BGV5; -.
DR TreeFam; TF337898; -.
DR BioGRID-ORCS; 243833; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q8BGV5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BGV5; protein.
DR Bgee; ENSMUSG00000060397; Expressed in otolith organ and 206 other tissues.
DR Genevisible; Q8BJ50; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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:0030509; P:BMP signaling pathway; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA: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; 7.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
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; 7.
PE 1: Evidence at protein level;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..572
FT /note="Zinc finger protein 8"
FT /id="PRO_0000436533"
FT DOMAIN 25..96
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 254..276
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 282..304
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 310..332
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 338..360
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 366..388
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 394..416
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 464..486
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 140..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17098"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17098"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P17098"
FT CONFLICT 346
FT /note="A -> S (in Ref. 4; AAH94248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 64737 MW; 6BC546057EAE5A04 CRC64;
MDHQDKAATV AMASRPQATQ LQEPVTFRDV AVDFTQEEWG QLDPTQRTLY RDVMLETFGH
LLSVGPDLPK PAVISQLEQG AELWVADRGG TGACHPGWIL EPEDHTLLKD QGLPKMEPSP
ITEKDGFAKA VPCRSMIGID QESDGQRQAL KKDQSNLNDP KEIPLQSQSH KSLGLVEACV
LGLNTYLLPD ISGREYGCTY DSQVKNSEHN PSLVRQRTDS PATQSFDDNG SQKAFDQIMP
ITELTKSQVQ DKPYKCTDCG KSFNHNAHLT VHKRIHTGER PYMCKECGKA FSQNSSLVQH
ERIHTGDKPY KCDECGKSFC HSTHLTVHRR IHTGEKPYEC QDCGRAFNQN SSLGRHKRTH
TGEKPYTCSV CGKSFSRTTC LFLHLRTHTE ERPYECNHCG KGFRHSSSLA QHQRKHAGEK
PYECRQRLIF EQAPALIKYE WTEPLGCDSP LSQGERTQRS DRPFKCNQCG KCFTQSSHLI
RHQLTHSREE EPLRGRSRRQ EQPCRRGSRL IQNTNSNSRE LPVAQPKAGQ ASRTLALFDL
REIMQEQNPV HVIGVEEPSV GNSMLFDTRE SR
