ZFP64_MOUSE
ID ZFP64_MOUSE Reviewed; 643 AA.
AC Q99KE8; P97365; Q9CWR3;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Zinc finger protein 64 {ECO:0000305};
DE Short=Zfp-64;
GN Name=Zfp64 {ECO:0000312|MGI:MGI:107342};
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 3), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Fetal eye;
RX PubMed=9034307; DOI=10.1016/s0378-1119(96)00607-5;
RA Mack H.G., Beck F., Bowtell D.D.;
RT "A search for a mammalian homologue of the Drosophila photoreceptor
RT development gene glass yields Zfp64, a zinc finger encoding gene which maps
RT to the distal end of mouse chromosome 2.";
RL Gene 185:11-17(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor;
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 [4]
RP INTERACTION WITH NOTCH1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP FUNCTION.
RX PubMed=18430783; DOI=10.1242/jcs.023119;
RA Sakamoto K., Tamamura Y., Katsube K., Yamaguchi A.;
RT "Zfp64 participates in Notch signaling and regulates differentiation in
RT mesenchymal cells.";
RL J. Cell Sci. 121:1613-1623(2008).
CC -!- FUNCTION: May be involved in the regulation of mesenchymal cell
CC differentiation through transactivation of NOTCH1 target genes.
CC {ECO:0000269|PubMed:18430783}.
CC -!- SUBUNIT: Interacts with NOTCH1. {ECO:0000269|PubMed:18430783}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18430783}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99KE8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99KE8-2; Sequence=VSP_007288, VSP_007289;
CC Name=3;
CC IsoId=Q99KE8-3; Sequence=VSP_007287, VSP_007290, VSP_007291;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:9034307). Expressed in the
CC brain, spleen, liver, and heart (PubMed:18430783).
CC {ECO:0000269|PubMed:18430783, ECO:0000269|PubMed:9034307}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 10.5 dpc.
CC {ECO:0000269|PubMed:9034307}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U49046; AAC53039.1; -; mRNA.
DR EMBL; AK010444; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC004695; AAH04695.1; -; mRNA.
DR CCDS; CCDS89588.1; -. [Q99KE8-1]
DR AlphaFoldDB; Q99KE8; -.
DR SMR; Q99KE8; -.
DR STRING; 10090.ENSMUSP00000085285; -.
DR iPTMnet; Q99KE8; -.
DR PhosphoSitePlus; Q99KE8; -.
DR MaxQB; Q99KE8; -.
DR PRIDE; Q99KE8; -.
DR ProteomicsDB; 275360; -. [Q99KE8-1]
DR ProteomicsDB; 275361; -. [Q99KE8-2]
DR ProteomicsDB; 275362; -. [Q99KE8-3]
DR Antibodypedia; 13873; 209 antibodies from 26 providers.
DR Ensembl; ENSMUST00000109161; ENSMUSP00000104789; ENSMUSG00000027551. [Q99KE8-2]
DR UCSC; uc008obl.1; mouse. [Q99KE8-2]
DR MGI; MGI:107342; Zfp64.
DR VEuPathDB; HostDB:ENSMUSG00000027551; -.
DR GeneTree; ENSGT00940000156405; -.
DR HOGENOM; CLU_1022925_0_0_1; -.
DR InParanoid; Q99KE8; -.
DR PhylomeDB; Q99KE8; -.
DR ChiTaRS; Zfp64; mouse.
DR PRO; PR:Q99KE8; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99KE8; protein.
DR Bgee; ENSMUSG00000027551; Expressed in ectoplacental cone and 207 other tissues.
DR ExpressionAtlas; Q99KE8; baseline and differential.
DR Genevisible; Q99KE8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043076; C:megasporocyte nucleus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048762; P:mesenchymal cell differentiation; ISS:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..643
FT /note="Zinc finger protein 64"
FT /id="PRO_0000047309"
FT ZN_FING 173..195
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 201..223
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 229..251
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 297..322
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..463
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 465..487
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 493..515
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 578..600
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 538..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 495
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 511
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 523
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 526
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 544
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 234..388
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9034307"
FT /id="VSP_007287"
FT VAR_SEQ 254..272
FT /note="SVLENDVQKPAGLPAEESD -> WRCDCLGSTKPWVPSLVTT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007288"
FT VAR_SEQ 273..643
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007289"
FT VAR_SEQ 464..628
FT /note="TFKCLHCAFQGRDRADLLEHSRLHQADHPEKCPECSYSCSNPAALRVHSRVH
FT CTDRPFKCDFCSFDTKRPSSLAKHIDKVHREGAKTENRAPPGKDGPGESGPHHVPNVST
FT QRAFGCDKCGASFVRDDSLRCHRKQHSDWGENKNSNLVTFPSEGIATGQLGPLV -> S
FT GNNFKCPHCDFLGDSKSTLRKHSRLHQSEHPEKCPECSYSCSSKAALRVHERIHCTERP
FT FKCSYCSFDTKQPSNLSKHMKKFHADMLKNEAPEKKESGRQSSRQVARLDAKKTFHCDI
FT CDASFMREDSLRSHKRQHSEYHSKNSDVTVVQLHLEPSKQPLRPSP (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:9034307"
FT /id="VSP_007290"
FT VAR_SEQ 629..643
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9034307"
FT /id="VSP_007291"
FT CONFLICT 23
FT /note="L -> V (in Ref. 1; AAC53039)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="T -> A (in Ref. 1; AAC53039)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="I -> R (in Ref. 1; AAC53039)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="D -> N (in Ref. 1; AAC53039)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="A -> G (in Ref. 1; AAC53039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 71765 MW; A04D3E5DD96EBD2D CRC64;
MNASVEGDTF SGSMQIPGGT TVLVELAPDI HICGLCKQHF SNLDAFVAHK QSGCQLTTTP
VTAPSTVQFV AEETEPATQT TTTTISSETQ TITVSAPEFV FEHGYQTYLP TESTDNQTAT
VISLPTKSRT KKPTAPPAQK RLGCCYPGCQ FKTAYGMKDM ERHLKIHTGD KPHKCEVCGK
CFSRKDKLKT HMRCHTGVKP YKCKTCDYAA ADSSSLNKHL RIHSDERPFK CQICPYASRN
SSQLTVHLRS HTASVLENDV QKPAGLPAEE SDAQQAPAVT LSLEAKERTA TLGERTFNCR
YPGCHFKTVH GMKDLDRHLR IHTGDKPHKC EFCDKCFSRK DNLTMHMRCH TSVKPHKCHL
CDYAAVDSSS LKKHLRIHSD ERPYKCQLCP YASRNSSQLT VHLRSHTGDT PFQCWLCSAK
FKISSDLKRH MIVHSGEKPF KCEFCDVRCT MKANLKSHIR IKHTFKCLHC AFQGRDRADL
LEHSRLHQAD HPEKCPECSY SCSNPAALRV HSRVHCTDRP FKCDFCSFDT KRPSSLAKHI
DKVHREGAKT ENRAPPGKDG PGESGPHHVP NVSTQRAFGC DKCGASFVRD DSLRCHRKQH
SDWGENKNSN LVTFPSEGIA TGQLGPLVSV GQLESTLEPS HDL
