ID ZFR_MOUSE Reviewed; 1074 AA.
AC O88532; Q3TY30; Q8BS85; Q8CGG5; Q91VZ0; Q9CT34;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 24-JAN-2024, entry version 155.
DE RecName: Full=Zinc finger RNA-binding protein;
GN Name=Zfr;
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], DNA-BINDING, RNA-BINDING, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Spermatocyte;
RX PubMed=10072773; DOI=10.1016/s0378-1119(98)00615-5;
RA Meagher M.J., Schumacher J.M., Lee K., Holdcraft R.W., Edelhoff S.,
RA Disteche C., Braun R.E.;
RT "Identification of ZFR, an ancient and highly conserved murine chromosome-
RT associated zinc finger protein.";
RL Gene 228:197-211(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-357, AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 632-1074.
RC STRAIN=129, C57BL/6J, and FVB/N; TISSUE=Eye, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 458-1074.
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Eye;
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 [4]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11283266; DOI=10.1128/mcb.21.8.2880-2890.2001;
RA Meagher M.J., Braun R.E.;
RT "Requirement for the murine zinc finger protein ZFR in perigastrulation
RT growth and survival.";
RL Mol. Cell. Biol. 21:2880-2890(2001).
RN [5]
RP FUNCTION, INTERACTION WITH STAU2, AND SUBCELLULAR LOCATION.
RX PubMed=16277607; DOI=10.1111/j.1471-4159.2005.03523.x;
RA Elvira G., Massie B., DesGroseillers L.;
RT "The zinc-finger protein ZFR is critical for Staufen 2 isoform specific
RT nucleocytoplasmic shuttling in neurons.";
RL J. Neurochem. 96:105-117(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-509 AND LYS-516, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Involved in postimplantation and gastrulation stages of
CC development. Binds to DNA and RNA. Involved in the nucleocytoplasmic
CC shuttling of STAU2 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:16277607}.
CC -!- SUBUNIT: Found in a cytoplasmic mRNP complex with STAU2. Does not
CC interact with STAU1 (By similarity). Interacts with STAU2.
CC {ECO:0000250, ECO:0000269|PubMed:16277607}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasmic granule
CC {ECO:0000250}. Chromosome {ECO:0000250}. Note=Associated with
CC chromosome foci in meiotic cells. Localizes in somatodendritic
CC compartment of primary hippocampal neurons (By similarity). Colocalizes
CC with STAU2 in several cytosolic RNA granules (By similarity).
CC Associated with chromosomes. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in Sertoli cells, spermatocytes, primary
CC and growing oocytes and granulosa cells (at protein level). Expressed
CC in testis, ovary and brain. {ECO:0000269|PubMed:10072773,
CC ECO:0000269|PubMed:11283266}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos at 5.5, 6.5 and 7 dpc (at
CC protein level). Expressed in the trophoectoderm cells and inner cell
CC mass of blastocysts (at protein level). {ECO:0000269|PubMed:11283266}.
CC -!- MISCELLANEOUS: Knockout mice form mesoderm but are delayed in their
CC development and fail to form normal anterior embryonic structures. They
CC show both an increase in programmed cell death and a decrease in
CC mitotic index, especially in the region of the distal tip of the
CC embryonic ectoderm. They also show a reduction in apical vacuoles in
CC the columnar visceral endoderm cells in the extraembryonic region.
CC Knockout mice die by 8 to 9 days of gestation.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC25762.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH06962.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH38599.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH38599.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH58570.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH58570.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC28897.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF071059; AAC25762.1; ALT_INIT; mRNA.
DR EMBL; BC006962; AAH06962.1; ALT_INIT; mRNA.
DR EMBL; BC038599; AAH38599.1; ALT_SEQ; mRNA.
DR EMBL; BC058570; AAH58570.1; ALT_SEQ; mRNA.
DR EMBL; AK011329; BAB27548.1; -; mRNA.
DR EMBL; AK034963; BAC28897.1; ALT_INIT; mRNA.
DR EMBL; AK158938; BAE34733.1; -; mRNA.
DR CCDS; CCDS37044.2; -.
DR PIR; T14343; T14343.
DR RefSeq; NP_035897.2; NM_011767.2.
DR AlphaFoldDB; O88532; -.
DR SMR; O88532; -.
DR BioGRID; 204689; 19.
DR IntAct; O88532; 9.
DR MINT; O88532; -.
DR STRING; 10090.ENSMUSP00000118911; -.
DR GlyGen; O88532; 13 sites, 1 O-linked glycan (13 sites).
DR iPTMnet; O88532; -.
DR PhosphoSitePlus; O88532; -.
DR SwissPalm; O88532; -.
DR EPD; O88532; -.
DR jPOST; O88532; -.
DR MaxQB; O88532; -.
DR PaxDb; 10090-ENSMUSP00000118911; -.
DR PeptideAtlas; O88532; -.
DR ProteomicsDB; 302056; -.
DR Pumba; O88532; -.
DR Antibodypedia; 9796; 89 antibodies from 17 providers.
DR DNASU; 22763; -.
DR Ensembl; ENSMUST00000122941.8; ENSMUSP00000118911.2; ENSMUSG00000022201.17.
DR GeneID; 22763; -.
DR KEGG; mmu:22763; -.
DR UCSC; uc007vhk.3; mouse.
DR AGR; MGI:1341890; -.
DR CTD; 51663; -.
DR MGI; MGI:1341890; Zfr.
DR VEuPathDB; HostDB:ENSMUSG00000022201; -.
DR eggNOG; KOG3792; Eukaryota.
DR GeneTree; ENSGT00940000155290; -.
DR HOGENOM; CLU_012026_1_0_1; -.
DR InParanoid; O88532; -.
DR OMA; QYSSVLW; -.
DR OrthoDB; 4565640at2759; -.
DR PhylomeDB; O88532; -.
DR TreeFam; TF320194; -.
DR BioGRID-ORCS; 22763; 9 hits in 77 CRISPR screens.
DR ChiTaRS; Zfr; mouse.
DR PRO; PR:O88532; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O88532; Protein.
DR Bgee; ENSMUSG00000022201; Expressed in dorsomedial nucleus of hypothalamus and 279 other cell types or tissues.
DR ExpressionAtlas; O88532; baseline and differential.
DR Genevisible; O88532; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 1.10.1410.40; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR InterPro; IPR006561; DZF_dom.
DR InterPro; IPR049402; DZF_dom_C.
DR InterPro; IPR049401; DZF_dom_N.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45762; ZINC FINGER RNA-BINDING PROTEIN; 1.
DR PANTHER; PTHR45762:SF3; ZINC FINGER RNA-BINDING PROTEIN; 1.
DR Pfam; PF20965; DZF_C; 1.
DR Pfam; PF07528; DZF_N; 1.
DR Pfam; PF12874; zf-met; 3.
DR SMART; SM00572; DZF; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SMART; SM00451; ZnF_U1; 3.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR PROSITE; PS51703; DZF; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Cytoplasm; Developmental protein; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..1074
FT /note="Zinc finger RNA-binding protein"
FT /id="PRO_0000312720"
FT DOMAIN 703..1073
FT /note="DZF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01040"
FT REGION 120..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 509
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 516
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96KR1"
FT CROSSLNK 541
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96KR1"
FT CROSSLNK 623
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96KR1"
FT CONFLICT 355
FT /note="H -> K (in Ref. 2; AAH58570/AAH38599)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="T -> S (in Ref. 3; BAC28897)"
FT /evidence="ECO:0000305"
FT CONFLICT 877
FT /note="M -> I (in Ref. 3; BAB27548)"
FT /evidence="ECO:0000305"
FT CONFLICT 1016
FT /note="F -> K (in Ref. 1; AAC25762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1074 AA; 116859 MW; F0CE7B9F84A79A07 CRC64;
MIPICPVVSF TYVPSRLGED AKMATGNYFG FTHSGAAAAA AAAQYSQQPA SGVAYSHPTT
VASYTVHQAP VAAHTVTAAY APAAATVAVA RPAPVAVAAA ATAAAYGGYP TAHTATDYGY
TQRQQEAPPP PPPATTQNYQ DSYSYVRSTA PAVAYDSKQY YQQPTATAAA VAAAAQPQPS
VAETYYQTAP KAGYSQGATQ YTQAQQARQV TAIKPATPSP ATTTFSIYPV SSTVQPVAAA
ATVVPSYTQS ATYSTTAVTY SGTSYSGYEA AVYSAASSYY QQQQQQQKQA AAAAAAAAAT
AAWTGTTFTK KTPFQNKQLK PKQPPKPPQI HYCDVCKISC AGPQTYKEHL EGQKHKKKEA
ALKASQNTSS SNNSTRGTQN QLRCELCDVS CTGADAYAAH IRGAKHQKVV KLHTKLGKPI
PSTEPNVVSQ ATSSTAASAS KPTASPSSIG ASNCTLNTSS IATSSVKGLS TTGNSSLNST
SNTKVSAIPT NMAAKKTSTP KINFVGGNKL QSTGNKTEDL KGIDCVKNTP AASAVQIPEV
KQDAGSEPVT PASLAALQSD VQPVGHDYVE EVRNDEGKVI RFHCKLCECS FNDPNAKEMH
LKGRRHRLQY KKKVNPDLQV EVKPSIRARK IQEEKMRKQM QKEEYWRRRE EEERWRMEIR
RYEEDMYWRR MEEEQHHWDD RRRMPDGGYP HGPPGPLGLL GVRPGMPPQP QGPAPLRRPD
SSDDRYVMTK HATIYPTEEE LQAVQKIVSI TERALKLVSD SLSEHEKSKN KEGDDKKEGG
KDRALKGVLR VGVLAKGLLL RGDRNVNLVL LCSEKPSKSL LSRIAENLPK QLAVISPEKY
DIKCAVSEAA IILNSCVEPK MQVTITLTSP IIREENMREG DVTSGMVKDP PDVLDRQKCL
DALAALRHAK WFQARANGLQ SCVIIIRILR DLCQRVPTWS DFPSWAMELL VEKAISSASS
PQSPGDALRR VFECISSGII LKGSPGLLDP CEKDPFDTLA TMTDQQREDI TSSAQFALRL
LAFRQIHKVL GMDPLPQMNQ RFNIHNNRKR RRDSDGVDGF EAEGKKDKKD YDNF
//
