ZPR1_MOUSE
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 03-AUG-2022, entry version 143.
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}.
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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 EPD; Q62384; -.
DR MaxQB; Q62384; -.
DR PaxDb; Q62384; -.
DR PeptideAtlas; Q62384; -.
DR PRIDE; Q62384; -.
DR ProteomicsDB; 275242; -.
DR Antibodypedia; 18410; 273 antibodies from 28 providers.
DR DNASU; 22687; -.
DR Ensembl; ENSMUST00000156440; ENSMUSP00000117725; ENSMUSG00000032078.
DR GeneID; 22687; -.
DR KEGG; mmu:22687; -.
DR UCSC; uc009phh.1; mouse.
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; 453044at2759; -.
DR PhylomeDB; Q62384; -.
DR TreeFam; TF313084; -.
DR BioGRID-ORCS; 22687; 29 hits in 76 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 263 other tissues.
DR ExpressionAtlas; Q62384; baseline and differential.
DR Genevisible; Q62384; MM.
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: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: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:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:1990261; P:pre-mRNA catabolic process; 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; 2.20.25.420; -; 2.
DR Gene3D; 2.60.120.1040; -; 2.
DR InterPro; IPR004457; Znf_ZPR1.
DR InterPro; IPR040141; ZPR1.
DR InterPro; IPR042451; ZPR1_A/B_dom.
DR InterPro; IPR042452; ZPR1_Znf1/2.
DR PANTHER; PTHR10876; PTHR10876; 1.
DR Pfam; PF03367; zf-ZPR1; 2.
DR SMART; SM00709; Zpr1; 2.
DR TIGRFAMs; TIGR00310; ZPR1_znf; 2.
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
