IKZF4_MOUSE
ID IKZF4_MOUSE Reviewed; 586 AA.
AC Q8C208; B9EJ21; Q3TCZ7; Q9Z2Z2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Zinc finger protein Eos;
DE AltName: Full=Ikaros family zinc finger protein 4;
GN Name=Ikzf4; Synonyms=Zfpn1a4;
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), FUNCTION, INTERACTION WITH IKZF1,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=ICR;
RX PubMed=10218586; DOI=10.1016/s0014-5793(99)00265-3;
RA Honma Y., Kiyosawa H., Mori T., Oguri A., Nikaido T., Kanazawa K., Tojo M.,
RA Takeda J., Tanno Y., Yokoya S., Kawabata I., Ikeda H., Wanaka A.;
RT "Eos: a novel member of the Ikaros gene family expressed predominantly in
RT the developing nervous system.";
RL FEBS Lett. 447:76-80(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=NOD; TISSUE=Dendritic cell;
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]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC 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 [5]
RP INTERACTION WITH CTBP2.
RX PubMed=12444977; DOI=10.1046/j.1432-1033.2002.03313.x;
RA Perdomo J., Crossley M.;
RT "The Ikaros family protein Eos associates with C-terminal-binding protein
RT corepressors.";
RL Eur. J. Biochem. 269:5885-5892(2002).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH SPI1 AND MITF.
RX PubMed=17403896; DOI=10.1128/mcb.01839-06;
RA Hu R., Sharma S.M., Bronisz A., Srinivasan R., Sankar U., Ostrowski M.C.;
RT "Eos, MITF, and PU.1 recruit corepressors to osteoclast-specific genes in
RT committed myeloid progenitors.";
RL Mol. Cell. Biol. 27:4018-4027(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH FOXP3 AND CTBP1.
RX PubMed=19696312; DOI=10.1126/science.1176077;
RA Pan F., Yu H., Dang E.V., Barbi J., Pan X., Grosso J.F., Jinasena D.,
RA Sharma S.M., McCadden E.M., Getnet D., Drake C.G., Liu J.O.,
RA Ostrowski M.C., Pardoll D.M.;
RT "Eos mediates Foxp3-dependent gene silencing in CD4+ regulatory T cells.";
RL Science 325:1142-1146(2009).
CC -!- FUNCTION: DNA-binding protein that binds to the 5'GGGAATRCC-3' Ikaros-
CC binding sequence. Interacts with SPI1 and MITF to repress transcription
CC of the CTSK and ACP5 promoters via recruitment of corepressors SIN3A
CC and CTBP2. May be involved in the development of central and peripheral
CC nervous systems. Essential for the inhibitory function of regulatory T-
CC cells (Treg). Mediates FOXP3-mediated gene silencing in regulatory T-
CC cells (Treg) via recruitment of corepressor CTBP1 (PubMed:19696312).
CC {ECO:0000269|PubMed:10218586, ECO:0000269|PubMed:17403896,
CC ECO:0000269|PubMed:19696312}.
CC -!- SUBUNIT: Self-associates. Interacts with other family members; IKZF1,
CC IKZF2, IKZF3 AND IKZF5 (By similarity). Interacts with CTBP2, SPI1 and
CC MITF. Interacts with FOXP3 and CTBP1. {ECO:0000250|UniProtKB:Q9H2S9,
CC ECO:0000269|PubMed:10218586, ECO:0000269|PubMed:12444977,
CC ECO:0000269|PubMed:17403896, ECO:0000269|PubMed:19696312}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8C208-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C208-2; Sequence=VSP_027690;
CC Name=3;
CC IsoId=Q8C208-3; Sequence=VSP_027689;
CC Name=4;
CC IsoId=Q8C208-4; Sequence=VSP_027691;
CC -!- TISSUE SPECIFICITY: Expressed mainly in the brain. Up-regulated in long
CC term cultured astrocytes. Down-regulated during osteoclast
CC differentiation. {ECO:0000269|PubMed:10218586,
CC ECO:0000269|PubMed:17403896}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the brain at 15 dpc and 18
CC dpc. Expression gradually decreased as postnatal development proceeded.
CC No expression detected in the liver, kidney, lung, thymus or spleen
CC during all developmental stages. {ECO:0000269|PubMed:10218586}.
CC -!- DOMAIN: The N-terminal zinc fingers are involved in sequence-specific
CC DNA binding.
CC -!- DOMAIN: C-terminal zinc fingers mediate homodimerization.
CC -!- MISCELLANEOUS: Eos is a Greek word for rising sun.
CC -!- SIMILARITY: Belongs to the Ikaros C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA36213.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB017615; BAA36213.1; ALT_FRAME; mRNA.
DR EMBL; AK089522; BAC40912.1; -; mRNA.
DR EMBL; AK170453; BAE41808.1; -; mRNA.
DR EMBL; AC117232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC141286; AAI41287.1; -; mRNA.
DR CCDS; CCDS24284.2; -. [Q8C208-1]
DR RefSeq; NP_035902.2; NM_011772.2. [Q8C208-1]
DR RefSeq; XP_006513677.1; XM_006513614.2.
DR RefSeq; XP_006513678.1; XM_006513615.2.
DR RefSeq; XP_011241744.1; XM_011243442.2. [Q8C208-2]
DR AlphaFoldDB; Q8C208; -.
DR SMR; Q8C208; -.
DR BioGRID; 204703; 1.
DR STRING; 10090.ENSMUSP00000114404; -.
DR iPTMnet; Q8C208; -.
DR PhosphoSitePlus; Q8C208; -.
DR EPD; Q8C208; -.
DR jPOST; Q8C208; -.
DR MaxQB; Q8C208; -.
DR PaxDb; Q8C208; -.
DR PRIDE; Q8C208; -.
DR ProteomicsDB; 267226; -. [Q8C208-1]
DR ProteomicsDB; 267227; -. [Q8C208-2]
DR ProteomicsDB; 267228; -. [Q8C208-3]
DR ProteomicsDB; 267229; -. [Q8C208-4]
DR Antibodypedia; 27854; 185 antibodies from 30 providers.
DR DNASU; 22781; -.
DR Ensembl; ENSMUST00000133342; ENSMUSP00000114404; ENSMUSG00000002578. [Q8C208-1]
DR Ensembl; ENSMUST00000221150; ENSMUSP00000152617; ENSMUSG00000002578. [Q8C208-4]
DR Ensembl; ENSMUST00000222067; ENSMUSP00000152234; ENSMUSG00000002578. [Q8C208-2]
DR GeneID; 22781; -.
DR KEGG; mmu:22781; -.
DR UCSC; uc007hnp.1; mouse. [Q8C208-1]
DR UCSC; uc011xqg.1; mouse. [Q8C208-3]
DR CTD; 64375; -.
DR MGI; MGI:1343139; Ikzf4.
DR VEuPathDB; HostDB:ENSMUSG00000002578; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158308; -.
DR HOGENOM; CLU_025502_0_0_1; -.
DR InParanoid; Q8C208; -.
DR OMA; NSTPICN; -.
DR OrthoDB; 385551at2759; -.
DR PhylomeDB; Q8C208; -.
DR TreeFam; TF331189; -.
DR BioGRID-ORCS; 22781; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Ikzf4; mouse.
DR PRO; PR:Q8C208; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8C208; protein.
DR Bgee; ENSMUSG00000002578; Expressed in rostral migratory stream and 181 other tissues.
DR ExpressionAtlas; Q8C208; baseline and differential.
DR Genevisible; Q8C208; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IPI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
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; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..586
FT /note="Zinc finger protein Eos"
FT /id="PRO_0000299469"
FT ZN_FING 159..181
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 187..209
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 215..237
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 248..271
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 531..553
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 559..583
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..586
FT /note="Interaction with FOXP3"
FT /evidence="ECO:0000269|PubMed:19696312"
FT REGION 413..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 423..433
FT /note="CTBP-binding motif PEDLG"
FT COMPBIAS 78..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKS7"
FT MOD_RES 335
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKS7"
FT CROSSLNK 100
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2S9"
FT CROSSLNK 501
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H2S9"
FT VAR_SEQ 1..61
FT /note="MHTPPALPRRFQGGGRVRTPGSHRQGKDNLERELSGGCAPDFLPQAQDSNHF
FT IMESLFCES -> MFIPVG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027689"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10218586,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_027690"
FT VAR_SEQ 572..586
FT /note="YEFSSHIVRGEHKVG -> TRRLVPRLLGPVMINGREKGDVSFLSANFQYNQ
FT KNCPRMNYTYVPVNHSTLVPARMGRTQLGVTSTALSILSSRHRAGEAVFSGGCRHSGYS
FT DNRGFVRPCRRRHSSIAGGSLSL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027691"
FT CONFLICT 70..71
FT /note="EF -> DS (in Ref. 1; BAA36213)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="E -> V (in Ref. 2; BAE41808)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="G -> S (in Ref. 2; BAE41808)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="P -> T (in Ref. 2; BAC40912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 64155 MW; BC39FF5BBE7F914C CRC64;
MHTPPALPRR FQGGGRVRTP GSHRQGKDNL ERELSGGCAP DFLPQAQDSN HFIMESLFCE
SSGDSSLEKE FLGAPVGPSV STPNSQHSSP SRSLSANSIK VEMYSDEESS RLLGPDERLL
DKDDSVIVED SLSEPLGYCD GSGPEPHSPG GIRLPNGKLK CDVCGMVCIG PNVLMVHKRS
HTGERPFHCN QCGASFTQKG NLLRHIKLHS GEKPFKCPFC NYACRRRDAL TGHLRTHSVS
SPTVGKPYKC NYCGRSYKQQ STLEEHKERC HNYLQSLSTD AQALTGQPGD EIRDLEMVPD
SMLHPSTERP TFIDRLANSL TKRKRSTPQK FVGEKQMRFS LSDLPYDVNA SGGYEKDVEL
VAHHGLEPGF GGSLAFVGTE HLRPLRLPPT NCISELTPVI SSVYTQMQPI PSRLELPGSR
EAGEGPEDLG DGGPLLYRAR GSLTDPGASP SNGCQDSTDT ESNHEDRIGG VVSLPQGPPP
QPPPTIVVGR HSPAYAKEDP KPQEGLLRGT PGPSKEVLRV VGESGEPVKA FKCEHCRILF
LDHVMFTIHM GCHGFRDPFE CNICGYHSQD RYEFSSHIVR GEHKVG
