ZN382_MOUSE
ID ZN382_MOUSE Reviewed; 579 AA.
AC B2RXC5; Q3UYY9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Zinc finger protein 382;
DE AltName: Full=KRAB/zinc finger suppressor protein 1;
DE Short=KS1;
DE AltName: Full=Multiple zinc finger and krueppel-associated box protein KS1;
GN Name=Znf382; Synonyms=Zfp382;
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-578.
RC STRAIN=C57BL/6J; TISSUE=Forelimb;
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 [4]
RP INTERACTION WITH TRIM28.
RX PubMed=11154279; DOI=10.1128/mcb.21.3.928-939.2001;
RA Gebelein B., Urrutia R.;
RT "Sequence-specific transcriptional repression by KS1, a multiple-zinc-
RT finger-Kruppel-associated box protein.";
RL Mol. Cell. Biol. 21:928-939(2001).
CC -!- FUNCTION: Functions as a sequence-specific transcriptional repressor.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TRIM28; enhances the transcriptional repressor
CC activity. {ECO:0000269|PubMed:11154279}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-37 is the initiator.
CC {ECO:0000305}.
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DR EMBL; CH466593; EDL24044.1; -; Genomic_DNA.
DR EMBL; BC151163; AAI51164.1; -; mRNA.
DR EMBL; AK134263; BAE22072.1; -; mRNA.
DR CCDS; CCDS39877.1; -.
DR RefSeq; NP_001074476.1; NM_001081007.1.
DR AlphaFoldDB; B2RXC5; -.
DR SMR; B2RXC5; -.
DR BioGRID; 231361; 27.
DR STRING; 10090.ENSMUSP00000096196; -.
DR PhosphoSitePlus; B2RXC5; -.
DR MaxQB; B2RXC5; -.
DR PaxDb; B2RXC5; -.
DR PRIDE; B2RXC5; -.
DR ProteomicsDB; 275010; -.
DR Antibodypedia; 16319; 30 antibodies from 15 providers.
DR Ensembl; ENSMUST00000098596; ENSMUSP00000096196; ENSMUSG00000074220.
DR GeneID; 233060; -.
DR KEGG; mmu:233060; -.
DR UCSC; uc009gdf.1; mouse.
DR CTD; 233060; -.
DR MGI; MGI:3588204; Zfp382.
DR VEuPathDB; HostDB:ENSMUSG00000074220; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162338; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; B2RXC5; -.
DR OMA; GFHITKP; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; B2RXC5; -.
DR TreeFam; TF337898; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 233060; 2 hits in 73 CRISPR screens.
DR PRO; PR:B2RXC5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; B2RXC5; protein.
DR Bgee; ENSMUSG00000074220; Expressed in spermatocyte and 63 other tissues.
DR ExpressionAtlas; B2RXC5; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
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:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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; 9.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..579
FT /note="Zinc finger protein 382"
FT /id="PRO_0000361567"
FT DOMAIN 42..113
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 241..263
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 325..347
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 353..375
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 381..403
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 409..431
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 437..459
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 465..487
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 493..515
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 521..543
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 549..571
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 12..135
FT /note="Mediates interaction with TRIM28"
FT /evidence="ECO:0000250"
FT REGION 40..81
FT /note="Represses transcription"
FT /evidence="ECO:0000250"
FT REGION 105..240
FT /note="Represses transcription"
FT /evidence="ECO:0000250"
FT REGION 325..579
FT /note="Required for transcriptional repression activity;
FT probably mediates sequence-specific DNA-binding"
FT /evidence="ECO:0000250"
FT CONFLICT 576
FT /note="M -> T (in Ref. 3; BAE22072)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 66547 MW; 9FF4EAAFA05A3FF7 CRC64;
MGRPGRKPRG RARPGLFPFP KEELRQGGSS PANLNAMSKG PVSFKDVTVD FTQEEWQRLD
PAQKALYRDV MLENYCHFIS VGFHITKPDM IRKLEQGEEL WTERIFPSQS YLEEEEVLVK
FSDYQDKPPK SIVIIKHKKL IKERSSVYGE ALGKNRVVSK TLFEYKSDGK VLKNISEFIS
RDINPAMGKL GGSKEWEGSI LTSKQEKTHP ASILHKQIGR ALSSEWDLAQ HQKTQIPEQR
FEYNKCDSSF LMTGVEFPHG RAHRGGGNFN YSKDDITLFE KSDLGIHPHD LMEKKCSSYN
KYGELLCRKS VFVMHPSSQM DERPFQCPYC GNSFRRKSYL IEHERIHTGE KPYICCQCGR
AFRQKTALTL HEKTHTEGKP YLCVDCGKSF RQKATLTRHH KAHTGEKAYE CTQCGSAFGK
KSYLIDHQRT HTGEKPYQCT ECGKAFIQKT TLTVHQRTHT GEKPYICSEC GKSFCQKTTL
TLHQRIHTGE KPYICSDCGK SFRQKAILTV HYRIHTGEKS NGCPQCGKAF SRKSNLIRHQ
KIHTGEKPYE CQECGKFFSC KSNLITHQKT HKTETMRFQ
