ID ZN382_RAT Reviewed; 549 AA. AC A0JPL0; Q62977; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 121. 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 Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY RP EGF, AND TISSUE SPECIFICITY. RC STRAIN=Wistar; TISSUE=Pancreas; RX PubMed=9835615; DOI=10.1172/jci1919; RA Gebelein B., Fernandez-Zapico M., Imoto M., Urrutia R.; RT "KRAB-independent suppression of neoplastic cell growth by the novel zinc RT finger transcription factor KS1."; RL J. Clin. Invest. 102:1911-1919(1998). 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 FUNCTION, MUTAGENESIS OF 16-ASP-VAL-17, INTERACTION WITH TRIM28, AND RP SUBCELLULAR LOCATION. 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:0000269|PubMed:11154279, ECO:0000269|PubMed:9835615}. CC -!- SUBUNIT: Interacts with TRIM28; enhances the transcriptional repressor CC activity. {ECO:0000269|PubMed:11154279}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11154279, CC ECO:0000269|PubMed:9835615}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in CC lung, kidney and testis. {ECO:0000269|PubMed:9835615}. CC -!- INDUCTION: Up-regulated by EGF; delayed early response target for EGF CC (at protein level). {ECO:0000269|PubMed:9835615}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD05020.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; 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; U56732; AAD05020.1; ALT_SEQ; mRNA. DR EMBL; BC127483; AAI27484.1; -; mRNA. DR RefSeq; NP_653350.1; NM_144749.1. DR AlphaFoldDB; A0JPL0; -. DR SMR; A0JPL0; -. DR STRING; 10116.ENSRNOP00000028187; -. DR PhosphoSitePlus; A0JPL0; -. DR PaxDb; 10116-ENSRNOP00000028187; -. DR GeneID; 246264; -. DR KEGG; rno:246264; -. DR UCSC; RGD:708385; rat. DR AGR; RGD:708385; -. DR CTD; 233060; -. DR RGD; 708385; Zfp382. DR VEuPathDB; HostDB:ENSRNOG00000020777; -. DR eggNOG; KOG1721; Eukaryota. DR HOGENOM; CLU_002678_44_5_1; -. DR InParanoid; A0JPL0; -. DR OrthoDB; 5252528at2759; -. DR PhylomeDB; A0JPL0; -. DR TreeFam; TF337898; -. DR Reactome; R-RNO-212436; Generic Transcription Pathway. DR PRO; PR:A0JPL0; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000020777; Expressed in frontal cortex and 19 other cell types or tissues. DR ExpressionAtlas; A0JPL0; baseline and differential. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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; IDA:NTNU_SB. 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; IDA:NTNU_SB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:RGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0001558; P:regulation of cell growth; NAS:RGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd07765; KRAB_A-box; 1. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 10. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24381:SF390; B-CELL CLL_LYMPHOMA 6 MEMBER B PROTEIN; 1. DR PANTHER; PTHR24381; ZINC FINGER PROTEIN; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 9. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 10. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10. 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..549 FT /note="Zinc finger protein 382" FT /id="PRO_0000361568" FT DOMAIN 12..83 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 211..233 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 295..317 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 323..345 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 351..373 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 379..401 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 407..429 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 435..457 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 463..485 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 491..513 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 519..541 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..105 FT /note="Mediates interaction with TRIM28" FT /evidence="ECO:0000269|PubMed:11154279" FT REGION 10..51 FT /note="Represses transcription" FT REGION 75..210 FT /note="Represses transcription" FT REGION 295..549 FT /note="Required for transcriptional repression activity; FT probably mediates sequence-specific DNA-binding" FT MUTAGEN 16..17 FT /note="DV->AA: Loss of transcriptional repressor activity. FT Loss of interaction with TRIM28." FT /evidence="ECO:0000269|PubMed:11154279" SQ SEQUENCE 549 AA; 63563 MW; 72B9DA5087E9C177 CRC64; MNCHSVPLQG PVSFKDVTVD FTQEEWQRLD PAQKALYRDV MLENYCHFIS VGFHITKPDM IRKLEQGEEL WTERMFPSQS YLEDEEVLVK FRDYQDKPPT SIVIINHKKL IKERNNVYEK TLGNNHIISK TLFEYKSDGK VLKNISDFIS RDINPVMGTL GDSSEWEESV LTSEQEKTHP VPTLYKQIGR NLSSSLELAQ HQKTQIPEQR FECDECDSSF LMTEVAFPHD RAHRGVRDFN CSKDEIAFFE KSDLGIHPHN LMEKKCSTYN KYGKLLCRKS VFVMHPRSQV DERPFQCPYC GNSFRRKSYL IEHQRIHTGE KPYICSQCGK AFRQKTALTL HEKTHTDGKP YLCVDCGKSF RQKATLTRHH KTHTGEKAYE CTQCGSAFGK KSYLIDHQRT HTGEKPYQCA ECGKAFIQKT TLTVHQRTHT GEKPYMCSEC GKSFCQKTTL TLHQRIHTGE KPYVCSDCGK SFRQKAILTV HYRIHTGEKS NGCPQCGKAF SRKSNLIRHQ KTHTGEKPYE CHECGKFFSC KSNLVAHQKT HKAETVRFQ //