ZN653_MOUSE
ID ZN653_MOUSE Reviewed; 615 AA.
AC Q6YND2; Q8BHT8; Q8CI02;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Zinc finger protein 653;
DE AltName: Full=67 kDa zinc finger protein;
DE AltName: Full=Zinc finger protein Zip67;
GN Name=Znf653; Synonyms=Zfp653, Zip67;
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 [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=12920234; DOI=10.1210/me.2003-0158;
RA Borud B., Mellgren G., Lund J., Bakke M.;
RT "Cloning and characterization of a novel zinc finger protein that modulates
RT the transcriptional activity of nuclear receptors.";
RL Mol. Endocrinol. 17:2303-2319(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 59-615 (ISOFORM 1).
RC STRAIN=NOD; TISSUE=Thymus;
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).
CC -!- FUNCTION: Transcriptional repressor. May repress NR5A1, PPARG, NR1H3,
CC NR4A2, ESR1 and NR3C1 transcriptional activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NR5A1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6YND2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6YND2-2; Sequence=VSP_021015;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and spleen. Moderately
CC expressed in lung, adrenal gland, uterus, and ovary. Very low
CC expression in pancreas, heart, skeletal muscle, adipose tissue, kidney,
CC and liver. {ECO:0000269|PubMed:12920234}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AY072705; AAL66764.1; -; mRNA.
DR EMBL; AK089104; BAC40752.1; -; mRNA.
DR EMBL; BC038037; AAH38037.1; -; mRNA.
DR CCDS; CCDS22919.1; -. [Q6YND2-1]
DR CCDS; CCDS80968.1; -. [Q6YND2-2]
DR RefSeq; NP_796292.1; NM_177318.3. [Q6YND2-1]
DR AlphaFoldDB; Q6YND2; -.
DR SMR; Q6YND2; -.
DR STRING; 10090.ENSMUSP00000137064; -.
DR iPTMnet; Q6YND2; -.
DR PhosphoSitePlus; Q6YND2; -.
DR EPD; Q6YND2; -.
DR MaxQB; Q6YND2; -.
DR PaxDb; Q6YND2; -.
DR PRIDE; Q6YND2; -.
DR ProteomicsDB; 275028; -. [Q6YND2-1]
DR ProteomicsDB; 275029; -. [Q6YND2-2]
DR Antibodypedia; 25888; 23 antibodies from 9 providers.
DR DNASU; 319601; -.
DR Ensembl; ENSMUST00000043922; ENSMUSP00000045895; ENSMUSG00000038895. [Q6YND2-1]
DR Ensembl; ENSMUST00000179605; ENSMUSP00000137064; ENSMUSG00000038895. [Q6YND2-2]
DR GeneID; 319601; -.
DR KEGG; mmu:319601; -.
DR UCSC; uc009onp.1; mouse. [Q6YND2-1]
DR UCSC; uc012gpl.1; mouse. [Q6YND2-2]
DR CTD; 319601; -.
DR MGI; MGI:2442362; Zfp653.
DR VEuPathDB; HostDB:ENSMUSG00000038895; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160257; -.
DR HOGENOM; CLU_037389_0_0_1; -.
DR InParanoid; Q6YND2; -.
DR OMA; GAPLCPN; -.
DR PhylomeDB; Q6YND2; -.
DR TreeFam; TF332664; -.
DR BioGRID-ORCS; 319601; 3 hits in 58 CRISPR screens.
DR ChiTaRS; Zfp653; mouse.
DR PRO; PR:Q6YND2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6YND2; protein.
DR Bgee; ENSMUSG00000038895; Expressed in primary oocyte and 175 other tissues.
DR Genevisible; Q6YND2; MM.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0050682; F:AF-2 domain binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:1900116; P:extracellular negative regulation of signal transduction; ISS:UniProtKB.
DR GO; GO:1903507; P:negative regulation of nucleic acid-templated transcription; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..615
FT /note="Zinc finger protein 653"
FT /id="PRO_0000253345"
FT ZN_FING 467..492
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 498..522
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 528..550
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 556..578
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 586..609
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 388
FT /note="K -> KDTTPCHPV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12920234"
FT /id="VSP_021015"
FT CONFLICT 41
FT /note="D -> V (in Ref. 1; AAL66764)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="V -> A (in Ref. 1; AAL66764)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="G -> D (in Ref. 1; AAL66764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 615 AA; 67517 MW; C89971AD817AB43D CRC64;
MAERAPEPGA EAEAGAGGEA AAEEGAAGRK ARGRPRLTES DRARRRLESR KKYDVRRVYL
GEAHGPWVDL RRRSGWSDAK LAAYLISLER GQRSGRHGKP WEQVPKKPKR KKRRRRNVNC
LKNVVIWYED HKHRCPYEPH LAELDPTFGL YTTAVWQCEA GHRYFQDLHS PLKPLSDSEP
DSDKVGSGLV AGSSDSSSSG SSSDSEEPPE TQPAKASAAA AALTPASPTG SSGLITQEGV
HIPFDVHHVE SLAEQGTPLC QNPAGSGPEA LETVVCVPVP MQVGTGPGTL FENMPQEALG
EVVASCPVSG MVPGSQVIII AGPGYDALTA EGIRLNVAAG GGTPSSSLGE EVPCAMMEGV
AAYTQTEPEG TQHSTMDTTS IASIETKKEK EDLYMLKEEK EDSVAPELAE LAATVPENAE
AEAEVDGEEL DSSEMSAIIY EIPKEPEKRR RSKRSRVMDA DGLLEMFHCP YEGCSQVYVA
LSSFQNHVNL VHRKGKTKVC PHPGCGKKFY LSNHLRRHMI IHSGVREFTC ETCGKSFKRK
NHLEVHRRTH TGETPLQCEI CGYQCRQRAS LNWHMKKHTA EVQYNFTCDR CGKRFEKLDS
VKFHTLKSHP DHKPT
