ZN746_BOVIN
ID ZN746_BOVIN Reviewed; 630 AA.
AC Q3B7M4; E1BEU3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Zinc finger protein 746 {ECO:0000305};
GN Name=ZNF746 {ECO:0000250|UniProtKB:Q6NUN9};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription repressor that specifically binds to the 5'-
CC TATTTT[T/G]-3' consensus sequence on promoters and repress
CC transcription of PGC-1-alpha (PPARGC1A), thereby playing a role in
CC regulation of neuron death. {ECO:0000250|UniProtKB:Q6NUN9}.
CC -!- SUBUNIT: Interacts (via C2H2-type zinc fingers) with PRKN (By
CC similarity). Interacts with TRIM28 (By similarity).
CC {ECO:0000250|UniProtKB:Q3U133, ECO:0000250|UniProtKB:Q6NUN9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Mainly localizes to the cytoplasm; probably translocates to the
CC nucleus to repress selected genes. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by PRKN. 'Lys-48'-linked polyubiquitination by PRKN
CC leads to degradation by the proteasome and may play a key role in
CC regulation of neuron death (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AAFC03042442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03042444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03054460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC107543; AAI07544.1; -; mRNA.
DR RefSeq; NP_001030418.1; NM_001035341.1.
DR AlphaFoldDB; Q3B7M4; -.
DR SMR; Q3B7M4; -.
DR STRING; 9913.ENSBTAP00000018668; -.
DR PaxDb; Q3B7M4; -.
DR PRIDE; Q3B7M4; -.
DR Ensembl; ENSBTAT00000018668; ENSBTAP00000018668; ENSBTAG00000031106.
DR GeneID; 521998; -.
DR KEGG; bta:521998; -.
DR CTD; 155061; -.
DR VEuPathDB; HostDB:ENSBTAG00000031106; -.
DR VGNC; VGNC:37339; ZNF746.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161747; -.
DR InParanoid; Q3B7M4; -.
DR OMA; RPERDMS; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000031106; Expressed in retina and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IBA:GO_Central.
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:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0051291; P:protein heterooligomerization; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
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; 3.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..630
FT /note="Zinc finger protein 746"
FT /id="PRO_0000253727"
FT DOMAIN 96..167
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 454..476
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 496..518
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 524..546
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 552..575
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 155..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 16..92
FT /evidence="ECO:0000255"
FT COMPBIAS 583..601
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NUN9"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6NUN9"
SQ SEQUENCE 630 AA; 67972 MW; 170541E82C6E8057 CRC64;
MAEAAAAPIS PWTMAATIQA MERKIESQAA RLLSLEGRTG MAEKKLADCE KTAVEFGNQL
EGKWAVLGTL LQEYGLLQRR LENVENLLRN RNFWILRLPP GSKGEAPKEW GKLDEWQKEL
YKHVMRGNYE TLVSLDYAIS KPEVLSQIEQ GKEPCSWRRA GPKVPDVPVD PSPGSGPPVP
APDLLMQIKQ EGELQLQEQQ ALGVEAWAAG QPDIGEEPWG LSQLDSGAGD VSTDAASGVH
ANFSTTIPPT SWQADLPPHH PSSACSDGTL KLSTAASTEA DVKIVIKTEV QEEEVVATPV
HPTDLEAHGT LFGPGQATRF FPSPVQEGAW ESQGSSFPSQ DPVLGLREPA RPERDLGDPT
PTVPQDETSP GDWLFGGVRW GWNFRCKPPA GLNPRTGPEG LPFSSSDNGE AVLDPGQAPR
PFNDPCKYPG RTKGFGHKPG LKKHPAAPPG GRPFTCATCG KSFQLQVSLS AHQRSCGGQP
DGVPGAAGSA RDGSGLRCGE CGRCFTRPAH LIRHRMLHTG ERPFPCTECE KRFTERSKLI
DHYRTHTGVR PFTCTVCGKS FIRKDHLRKH QRNHAAGAKP ARGQPLPPLP AVPPDPFKSP
AAKGPLAPTD LVTDWTCGLS VLGPTDGGDL
