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ZFR_MOUSE
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   03-AUG-2022, entry version 147.
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; 18.
DR   IntAct; O88532; 9.
DR   MINT; O88532; -.
DR   STRING; 10090.ENSMUSP00000118911; -.
DR   iPTMnet; O88532; -.
DR   PhosphoSitePlus; O88532; -.
DR   EPD; O88532; -.
DR   jPOST; O88532; -.
DR   MaxQB; O88532; -.
DR   PaxDb; O88532; -.
DR   PeptideAtlas; O88532; -.
DR   PRIDE; O88532; -.
DR   ProteomicsDB; 302056; -.
DR   Antibodypedia; 9796; 80 antibodies from 17 providers.
DR   DNASU; 22763; -.
DR   Ensembl; ENSMUST00000122941; ENSMUSP00000118911; ENSMUSG00000022201.
DR   GeneID; 22763; -.
DR   KEGG; mmu:22763; -.
DR   UCSC; uc007vhk.3; mouse.
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; QCSQQPA; -.
DR   OrthoDB; 612611at2759; -.
DR   PhylomeDB; O88532; -.
DR   TreeFam; TF320194; -.
DR   BioGRID-ORCS; 22763; 9 hits in 72 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 275 other 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; 3.30.460.10; -; 1.
DR   InterPro; IPR006561; DZF_dom.
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   Pfam; PF07528; DZF; 1.
DR   SMART; SM00572; DZF; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SMART; SM00451; ZnF_U1; 3.
DR   SUPFAM; SSF57667; SSF57667; 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
 
 
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