ID ZPR1_MOUSE Reviewed; 459 AA. AC Q62384; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 151. DE RecName: Full=Zinc finger protein ZPR1; DE AltName: Full=Zinc finger protein 259; GN Name=Zpr1; Synonyms=Zfp259, Znf259; 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], FUNCTION, INTERACTION WITH EGFR, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=8650580; DOI=10.1126/science.272.5269.1797; RA Galcheva-Gargova Z., Konstantinov K.N., Wu I.-H., Klier F.G., Barrett T., RA Davis R.J.; RT "Binding of zinc finger protein ZPR1 to the epidermal growth factor RT receptor."; RL Science 272:1797-1802(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EEF1A1 AND EGFR, AND RP SUBCELLULAR LOCATION. RX PubMed=9852145; DOI=10.1083/jcb.143.6.1471; RA Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J.; RT "Interaction of ZPR1 with translation elongation factor-1alpha in RT proliferating cells."; RL J. Cell Biol. 143:1471-1484(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary 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 [4] RP SUBCELLULAR LOCATION. RX PubMed=9763455; DOI=10.1091/mbc.9.10.2963; RA Galcheva-Gargova Z., Gangwani L., Konstantinov K.N., Mikrut M., RA Theroux S.J., Enoch T., Davis R.J.; RT "The cytoplasmic zinc finger protein ZPR1 accumulates in the nucleolus of RT proliferating cells."; RL Mol. Biol. Cell 9:2963-2971(1998). RN [5] RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION. RX PubMed=15767679; DOI=10.1128/mcb.25.7.2744-2756.2005; RA Gangwani L., Flavell R.A., Davis R.J.; RT "ZPR1 is essential for survival and is required for localization of the RT survival motor neurons (SMN) protein to Cajal bodies."; RL Mol. Cell. Biol. 25:2744-2756(2005). RN [6] RP INDUCTION, AND TISSUE SPECIFICITY. RX PubMed=16465397; RA Nogusa Y., Yanaka N., Sumiyoshi N., Takeda K., Kato N.; RT "Expression of zinc finger protein ZPR1 mRNA in brain is up-regulated in RT mice fed a high-fat diet."; RL Int. J. Mol. Med. 17:491-496(2006). RN [7] RP FUNCTION, INVOLVEMENT IN NEURODEGENERATION, AND TISSUE SPECIFICITY. RX PubMed=16648254; DOI=10.1073/pnas.0602057103; RA Doran B., Gherbesi N., Hendricks G., Flavell R.A., Davis R.J., Gangwani L.; RT "Deficiency of the zinc finger protein ZPR1 causes neurodegeneration."; RL Proc. Natl. Acad. Sci. U.S.A. 103:7471-7475(2006). RN [8] RP INTERACTION WITH EEF1A1. RX PubMed=19966453; DOI=10.1271/bbb.90745; RA Yanaka N., Kaseda Y., Tanaka A., Nogusa Y., Sumiyoshi N., Kato N.; RT "Generation of a zinc finger protein ZPR1 mutant that constitutively RT interacted with translation elongation factor 1alpha."; RL Biosci. Biotechnol. Biochem. 73:2809-2811(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, 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 [10] RP FUNCTION, INTERACTION WITH SMN1, INVOLVEMENT IN NEURODEGENERATION, AND RP SUBCELLULAR LOCATION. RX PubMed=22422766; DOI=10.1093/hmg/dds102; RA Ahmad S., Wang Y., Shaik G.M., Burghes A.H., Gangwani L.; RT "The zinc finger protein ZPR1 is a potential modifier of spinal muscular RT atrophy."; RL Hum. Mol. Genet. 21:2745-2758(2012). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 47-440, AND INTERACTION WITH EF1A. RX PubMed=17704259; DOI=10.1073/pnas.0704915104; RA Mishra A.K., Gangwani L., Davis R.J., Lambright D.G.; RT "Structural insights into the interaction of the evolutionarily conserved RT ZPR1 domain tandem with eukaryotic EF1A, receptors, and SMN complexes."; RL Proc. Natl. Acad. Sci. U.S.A. 104:13930-13935(2007). CC -!- FUNCTION: Acts as a signaling molecule that communicates proliferative CC growth signals from the cytoplasm to the nucleus. It is involved in the CC positive regulation of cell cycle progression (By similarity). Plays a CC role for the localization and accumulation of the survival motor neuron CC protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. CC Induces neuron differentiation and stimulates axonal growth and CC formation of growth cone in spinal cord motor neurons. Plays a role in CC the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced CC neuronal cell death. {ECO:0000250|UniProtKB:O75312, CC ECO:0000269|PubMed:15767679, ECO:0000269|PubMed:16648254, CC ECO:0000269|PubMed:22422766, ECO:0000269|PubMed:8650580}. CC -!- SUBUNIT: Component of an import snRNP complex composed of KPNB1, SNUPN, CC SMN1 and ZNF259. Interacts (via C-terminal region) with SMN1 (via C- CC terminal region); the interaction occurs after treatment with serum (By CC similarity). Interacts with elongation factor 1-alpha EEF1A1; the CC interaction occurs in a epidermal growth factor (EGF)-dependent manner. CC Interacts (via zinc fingers) with EGFR (via C-terminal cytoplasmic CC kinase domain); the interaction is negatively regulated in response to CC epidermal growth factor (EGF) stimulation and EGFR kinase activity. May CC also bind to the PDGFR receptor. {ECO:0000250, CC ECO:0000269|PubMed:17704259, ECO:0000269|PubMed:19966453, CC ECO:0000269|PubMed:22422766, ECO:0000269|PubMed:8650580, CC ECO:0000269|PubMed:9852145}. CC -!- INTERACTION: CC Q62384; P02994: TEF2; Xeno; NbExp=2; IntAct=EBI-11566629, EBI-6314; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Nucleus, nucleolus. CC Cytoplasm, perinuclear region {ECO:0000250}. Nucleus, gem. Nucleus, CC Cajal body. Cell projection, axon. Cell projection, growth cone. CC Note=Localized predominantly in the cytoplasm in serum-starved cells CC growth arrested in G0 of the mitotic cell cycle. Localized both in the CC nucleus and cytoplasm at the G1 phase of the mitotic cell cycle. CC Accumulates in the subnuclear bodies during progression into the S CC phase of the mitotic cell cycle. Diffusely localized throughout the CC cell during mitosis. Colocalized with NPAT and SMN1 in nuclear bodies CC including gems (Gemini of coiled bodies) and Cajal bodies in a cell CC cycle-dependent manner. Colocalized with EGFR in the cytoplasm of CC quiescent cells. Translocates from the cytoplasm to the nucleus in a CC epidermal growth factor (EGF)-dependent manner (By similarity). CC Translocates together with EEF1A1 from the cytoplasm to the nucleolus CC after treatment with mitogens. Colocalized with SMN1 in Gemini of CC coiled bodies (gems), Cajal bodies, axon and growth cones of neurons. CC {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in brain. Expressed in the spinal cord CC motor neurons (at protein level). Expressed in spleen, liver, muscle, CC kidney and testis. Expressed in the frontal cortex, cornus ammonis, CC dentate gyrus of the hippocampus and in Purkinje cells of the CC cerebellum. {ECO:0000269|PubMed:16465397, ECO:0000269|PubMed:16648254, CC ECO:0000269|PubMed:8650580}. CC -!- INDUCTION: Up-regulated by high fat diet. CC {ECO:0000269|PubMed:16465397}. CC -!- DISEASE: Note=May contribute to the severity of spinal muscular atrophy CC by increasing spinal motor neurons degeneration. CC {ECO:0000269|PubMed:16648254}. CC -!- DISRUPTION PHENOTYPE: Die during early embryonic development. Embryos CC show growth delay, failed to form normal trophectoderm and to expand CC the inner cell mass. {ECO:0000269|PubMed:15767679}. CC -!- SIMILARITY: Belongs to the ZPR1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U41287; AAC52662.1; -; mRNA. DR EMBL; BC021397; AAH21397.1; -; mRNA. DR CCDS; CCDS23144.1; -. DR RefSeq; NP_035882.1; NM_011752.2. DR PDB; 2QKD; X-ray; 2.00 A; A=47-440. DR PDBsum; 2QKD; -. DR AlphaFoldDB; Q62384; -. DR SMR; Q62384; -. DR BioGRID; 204651; 11. DR DIP; DIP-46465N; -. DR IntAct; Q62384; 4. DR STRING; 10090.ENSMUSP00000117725; -. DR iPTMnet; Q62384; -. DR PhosphoSitePlus; Q62384; -. DR SwissPalm; Q62384; -. DR EPD; Q62384; -. DR MaxQB; Q62384; -. DR PaxDb; 10090-ENSMUSP00000117725; -. DR PeptideAtlas; Q62384; -. DR ProteomicsDB; 275242; -. DR Pumba; Q62384; -. DR Antibodypedia; 18410; 307 antibodies from 28 providers. DR DNASU; 22687; -. DR Ensembl; ENSMUST00000156440.8; ENSMUSP00000117725.2; ENSMUSG00000032078.18. DR GeneID; 22687; -. DR KEGG; mmu:22687; -. DR UCSC; uc009phh.1; mouse. DR AGR; MGI:1330262; -. DR CTD; 8882; -. DR MGI; MGI:1330262; Zpr1. DR VEuPathDB; HostDB:ENSMUSG00000032078; -. DR eggNOG; KOG2703; Eukaryota. DR GeneTree; ENSGT00390000005306; -. DR HOGENOM; CLU_024138_5_0_1; -. DR InParanoid; Q62384; -. DR OMA; PVQSQKG; -. DR OrthoDB; 1113465at2759; -. DR PhylomeDB; Q62384; -. DR TreeFam; TF313084; -. DR BioGRID-ORCS; 22687; 30 hits in 82 CRISPR screens. DR ChiTaRS; Zpr1; mouse. DR EvolutionaryTrace; Q62384; -. DR PRO; PR:Q62384; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q62384; Protein. DR Bgee; ENSMUSG00000032078; Expressed in ectoplacental cone and 266 other cell types or tissues. DR ExpressionAtlas; Q62384; baseline and differential. DR GO; GO:0030424; C:axon; IDA:UniProtKB. DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0097504; C:Gemini of coiled bodies; IDA:UniProtKB. DR GO; GO:0030426; C:growth cone; IDA:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0044183; F:protein folding chaperone; ISS:UniProtKB. DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB. DR GO; GO:0031369; F:translation initiation factor binding; IPI:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:MGI. DR GO; GO:1902742; P:apoptotic process involved in development; IMP:UniProtKB. DR GO; GO:0061564; P:axon development; IMP:UniProtKB. DR GO; GO:0030576; P:Cajal body organization; IMP:UniProtKB. DR GO; GO:0008283; P:cell population proliferation; IBA:GO_Central. DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB. DR GO; GO:0042023; P:DNA endoreduplication; IMP:UniProtKB. DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB. DR GO; GO:0001833; P:inner cell mass cell proliferation; IMP:UniProtKB. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IMP:UniProtKB. DR GO; GO:0045787; P:positive regulation of cell cycle; ISO:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:0045927; P:positive regulation of growth; IMP:UniProtKB. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB. DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB. DR GO; GO:1990261; P:pre-mRNA catabolic process; ISS:UniProtKB. DR GO; GO:0006457; P:protein folding; ISS:UniProtKB. DR GO; GO:0031641; P:regulation of myelination; IMP:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR GO; GO:0021510; P:spinal cord development; IMP:UniProtKB. DR GO; GO:0001834; P:trophectodermal cell proliferation; IMP:UniProtKB. DR Gene3D; 2.60.120.1040; ZPR1, A/B domain; 2. DR Gene3D; 2.20.25.420; ZPR1, zinc finger domain; 2. DR InterPro; IPR004457; Znf_ZPR1. DR InterPro; IPR040141; ZPR1. DR InterPro; IPR042451; ZPR1_A/B_dom. DR InterPro; IPR042452; ZPR1_Znf1/2. DR NCBIfam; TIGR00310; ZPR1_znf; 2. DR PANTHER; PTHR10876; ZINC FINGER PROTEIN ZPR1; 1. DR PANTHER; PTHR10876:SF0; ZINC FINGER PROTEIN ZPR1; 1. DR Pfam; PF03367; zf-ZPR1; 2. DR SMART; SM00709; Zpr1; 2. DR Genevisible; Q62384; MM. PE 1: Evidence at protein level; KW 3D-structure; Cell projection; Cytoplasm; Developmental protein; KW Differentiation; Metal-binding; mRNA processing; mRNA splicing; Nucleus; KW Reference proteome; Repeat; Zinc; Zinc-finger. FT CHAIN 1..459 FT /note="Zinc finger protein ZPR1" FT /id="PRO_0000119037" FT ZN_FING 51..83 FT /note="C4-type 1" FT ZN_FING 259..291 FT /note="C4-type 2" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 439..459 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:2QKD" FT TURN 52..54 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 55..67 FT /evidence="ECO:0007829|PDB:2QKD" FT TURN 68..70 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 71..79 FT /evidence="ECO:0007829|PDB:2QKD" FT TURN 81..83 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 86..96 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 98..107 FT /evidence="ECO:0007829|PDB:2QKD" FT HELIX 110..113 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 116..119 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:2QKD" FT HELIX 128..130 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:2QKD" FT HELIX 146..158 FT /evidence="ECO:0007829|PDB:2QKD" FT HELIX 161..167 FT /evidence="ECO:0007829|PDB:2QKD" FT HELIX 169..184 FT /evidence="ECO:0007829|PDB:2QKD" FT HELIX 185..187 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 192..198 FT /evidence="ECO:0007829|PDB:2QKD" FT TURN 208..211 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 217..222 FT /evidence="ECO:0007829|PDB:2QKD" FT HELIX 226..231 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 252..257 FT /evidence="ECO:0007829|PDB:2QKD" FT TURN 260..262 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 268..273 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 281..287 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 294..300 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 302..304 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 308..315 FT /evidence="ECO:0007829|PDB:2QKD" FT HELIX 318..322 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 324..327 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 332..335 FT /evidence="ECO:0007829|PDB:2QKD" FT HELIX 336..338 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 340..342 FT /evidence="ECO:0007829|PDB:2QKD" FT TURN 344..347 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 349..353 FT /evidence="ECO:0007829|PDB:2QKD" FT HELIX 354..366 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:2QKD" FT HELIX 378..380 FT /evidence="ECO:0007829|PDB:2QKD" FT HELIX 382..395 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 401..407 FT /evidence="ECO:0007829|PDB:2QKD" FT TURN 417..420 FT /evidence="ECO:0007829|PDB:2QKD" FT STRAND 426..431 FT /evidence="ECO:0007829|PDB:2QKD" FT TURN 437..439 FT /evidence="ECO:0007829|PDB:2QKD" SQ SEQUENCE 459 AA; 50715 MW; 771D38C7B806044F CRC64; MSASGAVQPG HPGAAVGPSP AAAASPATGP LFRPLSAEDE EQQPTEIESL CMNCYRNGTT RLLLTKIPFF REIIVSSFSC EHCGWNNTEI QSAGRIQDQG VRYTLTVRSQ EDMNREVVKT DSATTRIPEL DFEIPAFSQK GALTTVEGLI SRAISGLEQD QPTRRAVEGA IAERIDEFIG KLKDLKQMAS PFTLVIDDPS GNSFVENPHA PQKDNALVIT YYDRTPQQAE MLGLQAEAPE EKAEEEDLRN EVLQFNTNCP ECNAPAQTNM KLVQIPHFKE VIIMATNCEN CGHRTNEVKS GGAVEPLGTR ITLHITDPSD MTRDLLKSET CSVEIPELEF ELGMAVLGGK FTTLEGLLKD IRELVTKNPF TLGDSSNPDQ SEKLQEFSQK LGQIIEGKMK AHFIMNDPAG NSYLQNVYAP EDDPEMKVER YKRTFDQNEE LGLNDMKTEG YEAGLAPQR //