ZN382_RAT
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 03-AUG-2022, entry version 114.
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};
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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 PaxDb; A0JPL0; -.
DR GeneID; 246264; -.
DR KEGG; rno:246264; -.
DR UCSC; RGD:708385; rat.
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; 1318335at2759; -.
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 tissues.
DR ExpressionAtlas; A0JPL0; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:RGD.
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 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; 10.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
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
