ZN366_MOUSE
ID ZN366_MOUSE Reviewed; 746 AA.
AC Q6NS86;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Zinc finger protein 366 {ECO:0000312|MGI:MGI:2178429};
DE AltName: Full=Dendritic cell-specific transcript protein {ECO:0000303|PubMed:16522745};
DE Short=DC-SCRIPT {ECO:0000303|PubMed:16522745};
GN Name=Znf366 {ECO:0000250|UniProtKB:Q8N895};
GN Synonyms=Zfp366 {ECO:0000312|MGI:MGI:2178429};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {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 [2] {ECO:0000312|EMBL:AAH70399.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH70399.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH70399.1};
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).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16522745; DOI=10.1189/jlb.1005588;
RA Triantis V., Moulin V., Looman M.W., Hartgers F.C., Janssen R.A.,
RA Adema G.J.;
RT "Molecular characterization of the murine homologue of the DC-derived
RT protein DC-SCRIPT.";
RL J. Leukoc. Biol. 79:1083-1091(2006).
CC -!- FUNCTION: Has transcriptional repression activity. Acts as corepressor
CC of ESR1; the function seems to involve CTBP1 and histone deacetylases.
CC {ECO:0000250|UniProtKB:Q8N895}.
CC -!- SUBUNIT: Interacts with ESR1 and NRIP1. Interacts (via PXDLS motif)
CC with CTBP1. {ECO:0000250|UniProtKB:Q8N895}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16522745}.
CC -!- TISSUE SPECIFICITY: Expressed in immature and mature dendritic cells
CC (DCs). {ECO:0000269|PubMed:16522745}.
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DR EMBL; AC128670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC070399; AAH70399.1; -; mRNA.
DR CCDS; CCDS26720.1; -.
DR RefSeq; NP_001004149.1; NM_001004149.1.
DR AlphaFoldDB; Q6NS86; -.
DR SMR; Q6NS86; -.
DR STRING; 10090.ENSMUSP00000060040; -.
DR PhosphoSitePlus; Q6NS86; -.
DR MaxQB; Q6NS86; -.
DR PaxDb; Q6NS86; -.
DR PeptideAtlas; Q6NS86; -.
DR PRIDE; Q6NS86; -.
DR ProteomicsDB; 275009; -.
DR Antibodypedia; 12194; 145 antibodies from 28 providers.
DR DNASU; 238803; -.
DR Ensembl; ENSMUST00000056558; ENSMUSP00000060040; ENSMUSG00000050919.
DR GeneID; 238803; -.
DR KEGG; mmu:238803; -.
DR UCSC; uc007rpl.1; mouse.
DR CTD; 238803; -.
DR MGI; MGI:2178429; Zfp366.
DR VEuPathDB; HostDB:ENSMUSG00000050919; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000155498; -.
DR HOGENOM; CLU_019459_2_1_1; -.
DR InParanoid; Q6NS86; -.
DR OMA; KRWQCPM; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6NS86; -.
DR TreeFam; TF331510; -.
DR BioGRID-ORCS; 238803; 5 hits in 70 CRISPR screens.
DR ChiTaRS; Zfp366; mouse.
DR PRO; PR:Q6NS86; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q6NS86; protein.
DR Bgee; ENSMUSG00000050919; Expressed in lung and 50 other tissues.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..746
FT /note="Zinc finger protein 366"
FT /id="PRO_0000439856"
FT ZN_FING 250..272
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 278..300
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 306..328
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 334..356
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..384
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 390..412
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 418..440
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 446..468
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 474..496
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 502..524
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 530..553
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..746
FT /note="Interaction with NRIP1"
FT /evidence="ECO:0000250|UniProtKB:Q8N895"
FT REGION 587..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 587..591
FT /note="PXDLS"
FT /evidence="ECO:0000250|UniProtKB:Q8N895"
FT COMPBIAS 595..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..626
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 84826 MW; 428CD35E52054AEA CRC64;
MQKAMKMVKD EDGPLNAAAK SIPSFPHCLQ PEASRGKAPQ RHPFPEALRG PFSQFRYEPS
PGDLDGFPEV FEGGGSRKRK SMPTKVPYTH PAEEASIAQE SKSLGPPNLT LLFPQPQRPK
CDSQMIDLCN VGLQFYRTLE HLGGKPVKQE PVKPSAMWPQ PTPPAFLPAP YPYYPKVHPG
LMFPFFVPSS SPFPFSRHTF LPKQPPEPVL PRKVEPLESE ETKQKVERVD VNVQIDDSYY
VDVGGAQKRW QCPTCEKSYT SKYNLVTHIL GHSGIKPHAC SRCGKLFKQL SHLHTHMLTH
QGTRPHKCQV CHKAFTQTSH LKRHMMQHSE VKPHNCRVCS RGFAYPSELK AHEAKHASGR
ENICVECGLD FPTLAQLKRH LTTHRGPIQY NCSECDKTFQ YPSQLQNHMM KHKDIRPYIC
SECGMEFVQP HHLKQHSLTH KGVKEHKCGI CGREFTLLAN MKRHVLIHTN IRAYQCHLCY
KSFVQKQTLK AHMIVHSDVK PFKCKLCGKE FNRMHNLMGH LHLHSDSKPF KCLYCPSKFT
LKGNLTRHMK VKHGVMERGL HSQGLGRGRL VLVQSAGVLR NLEQEEPFDL SQKRSANGPM
FQSDVDSTQD CLCQEEEEEA GEEDNCYEVE PYSPSLAPES QQLCAPEDLS TKQEQTLQDP
GEGCRDQDAP EEQQEDRSED HEGSDIDCEG KDIDCAIREE RLSSRLLQSG GQGPSFSDYL
YFKHRDEGLK ELLERKMEKQ AVLLGI
