ZN746_MOUSE
ID ZN746_MOUSE Reviewed; 652 AA.
AC Q3U133; E9QPR1;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Zinc finger protein 746;
GN Name=Znf746; Synonyms=Zfp746;
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 MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
RP TISSUE SPECIFICITY, AND INTERACTION WITH PRKN.
RX PubMed=21376232; DOI=10.1016/j.cell.2011.02.010;
RA Shin J.H., Ko H.S., Kang H., Lee Y., Lee Y.I., Pletinkova O.,
RA Troconso J.C., Dawson V.L., Dawson T.M.;
RT "PARIS (ZNF746) repression of PGC-1alpha contributes to neurodegeneration
RT in Parkinson's disease.";
RL Cell 144:689-702(2011).
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
CC (PubMed:21376232). Interacts with TRIM28 (By similarity).
CC {ECO:0000250|UniProtKB:Q6NUN9, ECO:0000269|PubMed:21376232}.
CC -!- INTERACTION:
CC Q3U133; Q9WVS6: Prkn; NbExp=2; IntAct=EBI-3862590, EBI-973635;
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 -!- TISSUE SPECIFICITY: Widely expressed. In brain, it is heterogeneously
CC distributed throughout the brain and localizes to neurons, including
CC substantia nigra pars compacta dopamine-containing neurons. Weakly
CC expressed in cerebellum and midbrain (at protein level).
CC {ECO:0000269|PubMed:21376232}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE33667.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK156312; BAE33667.1; ALT_INIT; mRNA.
DR EMBL; AC166290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS51762.1; -.
DR RefSeq; NP_001156947.1; NM_001163475.1.
DR AlphaFoldDB; Q3U133; -.
DR BioGRID; 213305; 15.
DR IntAct; Q3U133; 1.
DR STRING; 10090.ENSMUSP00000072868; -.
DR iPTMnet; Q3U133; -.
DR PhosphoSitePlus; Q3U133; -.
DR MaxQB; Q3U133; -.
DR PaxDb; Q3U133; -.
DR PeptideAtlas; Q3U133; -.
DR PRIDE; Q3U133; -.
DR ProteomicsDB; 275298; -.
DR ABCD; Q3U133; 1 sequenced antibody.
DR Antibodypedia; 46329; 66 antibodies from 21 providers.
DR Ensembl; ENSMUST00000073124; ENSMUSP00000072868; ENSMUSG00000057691.
DR GeneID; 69228; -.
DR KEGG; mmu:69228; -.
DR UCSC; uc009btv.2; mouse.
DR CTD; 69228; -.
DR MGI; MGI:1916478; Zfp746.
DR VEuPathDB; HostDB:ENSMUSG00000057691; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161747; -.
DR HOGENOM; CLU_002678_76_3_1; -.
DR InParanoid; Q3U133; -.
DR OMA; RPERDMS; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q3U133; -.
DR TreeFam; TF337777; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 69228; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp746; mouse.
DR PRO; PR:Q3U133; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3U133; protein.
DR Bgee; ENSMUSG00000057691; Expressed in otic placode and 246 other tissues.
DR ExpressionAtlas; Q3U133; baseline and differential.
DR Genevisible; Q3U133; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; IGI:ParkinsonsUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
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 1: Evidence at protein 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..652
FT /note="Zinc finger protein 746"
FT /id="PRO_0000253729"
FT DOMAIN 96..167
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 454..479
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 517..539
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 545..567
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 573..595
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 155..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 16..92
FT /evidence="ECO:0000255"
FT COMPBIAS 480..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..621
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"
FT CONFLICT 490
FT /note="T -> A (in Ref. 1; BAE33667)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 652 AA; 69821 MW; 680CFF21F30CEDE0 CRC64;
MAEAAAAPIS PWTMAATIQA MERKIESQAA RLLSLEGRTG MAEKKLADCE KTAVEFSNQL
EGKWAVLGTL LQEYGLLQRR LENVENLLRN RNFWILRLPP GSKGEVPKEW GKLEDWQKEL
YKHVMRGNYE TLVSLDYAIS KPEVLSQIEQ GKEPCTWRRT GPKVPEVPVD PSPGSGAPVP
APDLLMQIKQ EGELQLQEQQ ALGVEAWAAG QPDIGEEPWG LSQLDSGAGD ISTDATSGVH
SNFSTTIPPT SWQADLPPHH PSSACSDGTL KLNTAASTEA DVKIVIKTEV QEEEVVATPV
HPTDLEAHGT LFAPGQATRF FPSPVQEGAW ESQGSSFPSQ DPVLGLREPT RPERDIGELS
PAIAQEEAPA GDWLFGGVRW GWNFRCKPPV GLNPRTVPEG LPFSSPDNGE AILDPSQAPR
PFNDPCKYPG RTKGFGHKPG LKKHPAAPPG GRPFTCATCG KSFQLQVSLS AHQRSCGLSD
GAATGAASTT TGGGGGGSGG GGGSSGGGSS ARDSSALRCG ECGRCFTRPA HLIRHRMLHT
GERPFPCTEC EKRFTERSKL IDHYRTHTGV RPFTCTVCGK SFIRKDHLRK HQRNHPAVAK
APAHGQPLPP LPAPPDPFKS PAAKGPMAST DLVTDWTCGL SVLGPSDGGG DL
