CPEB3_MOUSE
ID CPEB3_MOUSE Reviewed; 716 AA.
AC Q7TN99; A1A562; Q3TT89; Q3UHR6; Q8CHC2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 3;
DE Short=CPE-BP3;
DE Short=CPE-binding protein 3;
DE Short=mCPEB-3;
GN Name=Cpeb3; Synonyms=Kiaa0940;
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] (ISOFORMS 1; 2; 3 AND 4), INDUCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12871996; DOI=10.1073/pnas.1133424100;
RA Theis M., Si K., Kandel E.R.;
RT "Two previously undescribed members of the mouse CPEB family of genes and
RT their inducible expression in the principal cell layers of the
RT hippocampus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9602-9607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC STRAIN=C57BL/6J;
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=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17024188; DOI=10.1038/sj.emboj.7601322;
RA Huang Y.S., Kan M.C., Lin C.L., Richter J.D.;
RT "CPEB3 and CPEB4 in neurons: analysis of RNA-binding specificity and
RT translational control of AMPA receptor GluR2 mRNA.";
RL EMBO J. 25:4865-4876(2006).
RN [6]
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20003455; DOI=10.1186/1471-2199-10-109;
RA Wang X.P., Cooper N.G.;
RT "Characterization of the transcripts and protein isoforms for cytoplasmic
RT polyadenylation element binding protein-3 (CPEB3) in the mouse retina.";
RL BMC Mol. Biol. 10:109-109(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-197, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Kidney;
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 INTERACTION WITH STAT5B.
RX PubMed=20639532; DOI=10.1093/nar/gkq634;
RA Peng S.C., Lai Y.T., Huang H.Y., Huang H.D., Huang Y.S.;
RT "A novel role of CPEB3 in regulating EGFR gene transcription via
RT association with Stat5b in neurons.";
RL Nucleic Acids Res. 38:7446-7457(2010).
RN [9]
RP FUNCTION, INTERACTION WITH NEURL1, SUBCELLULAR LOCATION, AND
RP UBIQUITINATION.
RX PubMed=22153079; DOI=10.1016/j.cell.2011.09.056;
RA Pavlopoulos E., Trifilieff P., Chevaleyre V., Fioriti L., Zairis S.,
RA Pagano A., Malleret G., Kandel E.R.;
RT "Neuralized1 activates CPEB3: a function for nonproteolytic ubiquitin in
RT synaptic plasticity and memory storage.";
RL Cell 147:1369-1383(2011).
RN [10]
RP FUNCTION, INTERACTION WITH CAPN2, SUBCELLULAR LOCATION, AND PROTEOLYTIC
RP CLEAVAGE.
RX PubMed=22711986; DOI=10.1128/mcb.00296-12;
RA Wang C.F., Huang Y.S.;
RT "Calpain 2 activated through N-methyl-D-aspartic acid receptor signaling
RT cleaves CPEB3 and abrogates CPEB3-repressed translation in neurons.";
RL Mol. Cell. Biol. 32:3321-3332(2012).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=22730302; DOI=10.1093/nar/gks598;
RA Chao H.W., Lai Y.T., Lu Y.L., Lin C.L., Mai W., Huang Y.S.;
RT "NMDAR signaling facilitates the IPO5-mediated nuclear import of CPEB3.";
RL Nucleic Acids Res. 40:8484-8498(2012).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24155305; DOI=10.1523/jneurosci.3043-13.2013;
RA Chao H.W., Tsai L.Y., Lu Y.L., Lin P.Y., Huang W.H., Chou H.J., Lu W.H.,
RA Lin H.C., Lee P.T., Huang Y.S.;
RT "Deletion of CPEB3 enhances hippocampus-dependent memory via increasing
RT expressions of PSD95 and NMDA receptors.";
RL J. Neurosci. 33:17008-17022(2013).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-309, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [14]
RP FUNCTION, INTERACTION WITH UBC9, AND SUMOYLATION.
RX PubMed=26074071; DOI=10.1016/j.celrep.2015.04.061;
RA Drisaldi B., Colnaghi L., Fioriti L., Rao N., Myers C., Snyder A.M.,
RA Metzger D.J., Tarasoff J., Konstantinov E., Fraser P.E., Manley J.L.,
RA Kandel E.R.;
RT "SUMOylation is an inhibitory constraint that regulates the prion-like
RT aggregation and activity of CPEB3.";
RL Cell Rep. 11:1694-1702(2015).
RN [15]
RP FUNCTION, SUBUNIT, AND INDUCTION.
RX PubMed=26074072; DOI=10.1016/j.celrep.2015.04.060;
RA Stephan J.S., Fioriti L., Lamba N., Colnaghi L., Karl K., Derkatch I.L.,
RA Kandel E.R.;
RT "The CPEB3 protein is a functional prion that interacts with the actin
RT cytoskeleton.";
RL Cell Rep. 11:1772-1785(2015).
RN [16]
RP FUNCTION, SUBUNIT, INDUCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=26074003; DOI=10.1016/j.neuron.2015.05.021;
RA Fioriti L., Myers C., Huang Y.Y., Li X., Stephan J.S., Trifilieff P.,
RA Colnaghi L., Kosmidis S., Drisaldi B., Pavlopoulos E., Kandel E.R.;
RT "The persistence of hippocampal-based memory requires protein synthesis
RT mediated by the prion-like protein CPEB3.";
RL Neuron 86:1433-1448(2015).
RN [17]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26915043; DOI=10.1371/journal.pone.0148491;
RA Fong S.W., Lin H.C., Wu M.F., Chen C.C., Huang Y.S.;
RT "CPEB3 deficiency elevates TRPV1 expression in dorsal root ganglia neurons
RT to potentiate thermosensation.";
RL PLoS ONE 11:E0148491-E0148491(2016).
RN [18]
RP PHOSPHORYLATION AT SER-291; SER-419 AND SER-420, AND MUTAGENESIS OF SER-419
RP AND SER-420.
RX PubMed=26915047; DOI=10.1371/journal.pone.0150000;
RA Kaczmarczyk L., Labrie-Dion E., Sehgal K., Sylvester M., Skubal M.,
RA Josten M., Steinhaeuser C., De Koninck P., Theis M.;
RT "New phosphospecific antibody reveals isoform-specific phosphorylation of
RT CPEB3 protein.";
RL PLoS ONE 11:E0150000-E0150000(2016).
CC -!- FUNCTION: Sequence-specific RNA-binding protein which acts as a
CC translational repressor in the basal unstimulated state but, following
CC neuronal stimulation, acts as a translational activator
CC (PubMed:17024188, PubMed:26074072). In contrast to CPEB1, does not bind
CC to the cytoplasmic polyadenylation element (CPE), a uridine-rich
CC sequence element within the mRNA 3'-UTR, but binds to a U-rich loop
CC within a stem-loop structure (PubMed:17024188). Required for the
CC consolidation and maintenance of hippocampal-based long term memory
CC (PubMed:26074003). In the basal state, binds to the mRNA 3'-UTR of the
CC glutamate receptors GRIA1 and GRIA2 and negatively regulates their
CC translation (PubMed:17024188, PubMed:22153079). Also represses the
CC translation of DLG4, GRIN1 GRIN2A and GRIN2B (PubMed:24155305). When
CC activated, acts as a translational activator of GRIA1 and GRIA2
CC (PubMed:22153079, PubMed:26074003). In the basal state, suppresses
CC SUMO2 translation but activates it following neuronal stimulation
CC (PubMed:26074071). Binds to the 3'-UTR of TRPV1 mRNA and represses
CC TRPV1 translation which is required to maintain normal thermoception
CC (PubMed:26915043). Binds actin mRNA, leading to actin translational
CC repression in the basal state and to translational activation following
CC neuronal stimulation (PubMed:26074072). Negatively regulates target
CC mRNA levels by binding to TOB1 which recruits CNOT7/CAF1 to a ternary
CC complex and this leads to target mRNA deadenylation and decay (By
CC similarity). In addition to its role in translation, binds to and
CC inhibits the transcriptional activation activity of STAT5B without
CC affecting its dimerization or DNA-binding activity. This, in turn,
CC represses transcription of the STAT5B target gene EGFR which has been
CC shown to play a role in enhancing learning and memory performance (By
CC similarity). In contrast to CPEB1, CPEB2 and CPEB4, not required for
CC cell cycle progression (By similarity). {ECO:0000250|UniProtKB:Q8NE35,
CC ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:22153079,
CC ECO:0000269|PubMed:22711986, ECO:0000269|PubMed:24155305,
CC ECO:0000269|PubMed:26074003, ECO:0000269|PubMed:26074071,
CC ECO:0000269|PubMed:26074072, ECO:0000269|PubMed:26915043}.
CC -!- SUBUNIT: Following synaptic activity, aggregates to form amyloid-like
CC oligomers (PubMed:26074003, PubMed:26074072). Aggregation requires an
CC intact actin cytoskeleton (PubMed:26074072). Interacts with STAT5B;
CC this inhibits STAT5B-mediated transcriptional activation
CC (PubMed:20639532). Interacts with E3 ubiquitin-protein ligase NEURL1;
CC this leads to monoubiquitination and activation of CPEB3
CC (PubMed:22153079). Interacts with CAPN2; this leads to cleavage of
CC CPEB3 (PubMed:22711986). Interacts (via C-terminal RNA-binding region)
CC with TOB1; TOB1 also binds CNOT7/CAF1 and recruits it to CPEB3 to form
CC a ternary complex (By similarity). Interacts with SUMO-conjugating
CC enzyme UBC9 (PubMed:26074071). Interacts with IPO5; the interaction is
CC enhanced in a RAN-regulated manner following neuronal stimulation and
CC mediates CPEB3 nuclear import (By similarity). Interacts with exportin
CC XPO1/CRM1 (By similarity). {ECO:0000250|UniProtKB:Q8NE35,
CC ECO:0000269|PubMed:20639532, ECO:0000269|PubMed:22153079,
CC ECO:0000269|PubMed:22711986, ECO:0000269|PubMed:26074003,
CC ECO:0000269|PubMed:26074071, ECO:0000269|PubMed:26074072}.
CC -!- INTERACTION:
CC Q7TN99; Q923S6: Neurl1; NbExp=9; IntAct=EBI-5376779, EBI-5376802;
CC Q7TN99; P62991: Ubc; NbExp=2; IntAct=EBI-5376779, EBI-413074;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22711986}. Nucleus
CC {ECO:0000269|PubMed:22711986}. Synapse {ECO:0000269|PubMed:17024188}.
CC Cell projection, dendrite {ECO:0000269|PubMed:17024188,
CC ECO:0000269|PubMed:22153079, ECO:0000269|PubMed:22711986}. Postsynaptic
CC density {ECO:0000269|PubMed:17024188}. Note=Predominantly cytoplasmic
CC in unstimulated neurons but translocates to the nucleus following
CC neuronal stimulation (PubMed:22711986). Nuclear import is mediated by
CC importin IPO5 (PubMed:22730302). {ECO:0000269|PubMed:22711986,
CC ECO:0000269|PubMed:22730302}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=mCPEB-3a;
CC IsoId=Q7TN99-1; Sequence=Displayed;
CC Name=2; Synonyms=mCPEB-3b;
CC IsoId=Q7TN99-2; Sequence=VSP_022037;
CC Name=3; Synonyms=mCPEB-3c;
CC IsoId=Q7TN99-3; Sequence=VSP_022036;
CC Name=4; Synonyms=mCPEB-3d;
CC IsoId=Q7TN99-4; Sequence=VSP_022036, VSP_022037;
CC Name=5;
CC IsoId=Q7TN99-5; Sequence=VSP_022036, VSP_022038, VSP_022039;
CC Name=6;
CC IsoId=Q7TN99-6; Sequence=VSP_058565, VSP_022036;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain (at protein level)
CC (PubMed:17024188). In brain, expressed in the hippocampus, granule
CC cells and interneurons of the cerebellum, and mitral cells of the
CC olfactory bulb (at protein level) (PubMed:17024188). Detected in the
CC spinal cord and in peripheral dorsal root ganglia (at protein level)
CC (PubMed:26915043). In the retina, strongly expressed in the retinal
CC ganglion layer and, to a lesser extent, in the inner margin of the
CC inner nuclear layer with expression also detected in the inner and
CC outer plexiform layers (at protein level) (PubMed:20003455). Highly
CC expressed in brain and heart, less in liver, kidney, embryo, skeletal
CC muscle, lung and ovary (PubMed:12871996). Weakly expressed in granular
CC cells of dentate gyrus and the pyramidal cells of CA3 and CA1 of the
CC hippocampus (PubMed:12871996). {ECO:0000269|PubMed:12871996,
CC ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:20003455,
CC ECO:0000269|PubMed:26915043}.
CC -!- DEVELOPMENTAL STAGE: In the retina, expression increases throughout
CC postnatal development and remains high in the adult (at protein level).
CC {ECO:0000269|PubMed:20003455}.
CC -!- INDUCTION: Up-regulated following synaptic activity (at protein level)
CC (PubMed:26074003, PubMed:26074072). Up-regulated in granular cells of
CC the dentate gyrus and the pyramidal cells of CA1 and CA3 after kainate-
CC induced seizures (PubMed:12871996). {ECO:0000269|PubMed:12871996,
CC ECO:0000269|PubMed:26074003, ECO:0000269|PubMed:26074072}.
CC -!- DOMAIN: The N-terminal Gln-rich region is required for the formation of
CC amyloid-like oligomers and for the stability of long-term potentiation
CC and spatial memory. {ECO:0000269|PubMed:26074003}.
CC -!- PTM: Activated by NEURL1-mediated monoubiquitination, resulting in the
CC growth of new dendritic spines and increased levels of GRIA1 and GRIA2.
CC NEURL1-mediated monoubiquitination facilitates synaptic plasticity and
CC hippocampal-dependent memory storage. {ECO:0000269|PubMed:22153079}.
CC -!- PTM: Under basal unstimulated conditions when CPEB3 is mainly
CC unaggregated, sumoylated and acts as a translational repressor.
CC Following neuronal stimulation, becomes desumoylated and aggregated
CC which is required for the translation of mRNA targets and for dendritic
CC filopodia formation. {ECO:0000269|PubMed:26074071}.
CC -!- PTM: Following neuronal stimulation, cleaved by CAPN2 which abolishes
CC its translational repressor activity, leading to translation of CPEB3
CC target mRNAs. {ECO:0000269|PubMed:22711986}.
CC -!- PTM: Phosphorylation is enhanced by neuronal stimulation.
CC {ECO:0000269|PubMed:26915047}.
CC -!- DISRUPTION PHENOTYPE: Enhanced thermal sensitivity and increased levels
CC of Trpv1 in lumbar sciatic nerves and spinal cord (PubMed:26915043).
CC Elevated short-term fear response, enhanced long-term spatial memory,
CC dendritic spine enlargement and elevated levels of Dlg4/Psd95, Gria1
CC and NMDA receptor subunits Grin1, Grin2a and Grin2b (PubMed:26074071).
CC Conditional knockout in the adult forebrain results in viable mice with
CC no gross neurological defects which display normal locomotor,
CC exploratory and anxiety behaviors but have impaired long-term memory,
CC impaired long-term synaptic plasticity and increased levels of Gria1
CC and Gria2 (PubMed:26074003). {ECO:0000269|PubMed:26074003,
CC ECO:0000269|PubMed:26074071, ECO:0000269|PubMed:26915043}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41458.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY313774; AAQ20843.1; -; mRNA.
DR EMBL; AK147243; BAE27791.1; -; mRNA.
DR EMBL; AK161513; BAE36436.1; -; mRNA.
DR EMBL; AB093274; BAC41458.1; ALT_INIT; mRNA.
DR EMBL; BC128377; AAI28378.1; -; mRNA.
DR CCDS; CCDS29775.1; -. [Q7TN99-1]
DR CCDS; CCDS70946.1; -. [Q7TN99-4]
DR CCDS; CCDS70947.1; -. [Q7TN99-3]
DR RefSeq; NP_001277755.1; NM_001290826.1.
DR RefSeq; NP_001277756.1; NM_001290827.1.
DR RefSeq; NP_001277757.1; NM_001290828.1. [Q7TN99-3]
DR RefSeq; NP_001277758.1; NM_001290829.1.
DR RefSeq; NP_938042.2; NM_198300.3.
DR RefSeq; XP_006526892.1; XM_006526829.3.
DR RefSeq; XP_006526893.1; XM_006526830.3.
DR RefSeq; XP_006526894.1; XM_006526831.3.
DR RefSeq; XP_006526895.1; XM_006526832.3.
DR RefSeq; XP_006526896.1; XM_006526833.3.
DR RefSeq; XP_006526897.1; XM_006526834.2.
DR RefSeq; XP_006526902.1; XM_006526839.3.
DR RefSeq; XP_011245510.1; XM_011247208.1. [Q7TN99-3]
DR AlphaFoldDB; Q7TN99; -.
DR BMRB; Q7TN99; -.
DR SMR; Q7TN99; -.
DR BioGRID; 229024; 2.
DR IntAct; Q7TN99; 3.
DR MINT; Q7TN99; -.
DR STRING; 10090.ENSMUSP00000118723; -.
DR iPTMnet; Q7TN99; -.
DR PhosphoSitePlus; Q7TN99; -.
DR MaxQB; Q7TN99; -.
DR PaxDb; Q7TN99; -.
DR PeptideAtlas; Q7TN99; -.
DR PRIDE; Q7TN99; -.
DR ProteomicsDB; 278012; -. [Q7TN99-1]
DR ProteomicsDB; 278013; -. [Q7TN99-2]
DR ProteomicsDB; 278014; -. [Q7TN99-3]
DR ProteomicsDB; 278015; -. [Q7TN99-4]
DR ProteomicsDB; 278016; -. [Q7TN99-5]
DR ProteomicsDB; 278017; -. [Q7TN99-6]
DR Antibodypedia; 30391; 121 antibodies from 19 providers.
DR DNASU; 208922; -.
DR Ensembl; ENSMUST00000126188; ENSMUSP00000120416; ENSMUSG00000039652. [Q7TN99-3]
DR Ensembl; ENSMUST00000126781; ENSMUSP00000122442; ENSMUSG00000039652. [Q7TN99-5]
DR GeneID; 208922; -.
DR KEGG; mmu:208922; -.
DR UCSC; uc008hhz.2; mouse. [Q7TN99-1]
DR UCSC; uc008hia.2; mouse. [Q7TN99-3]
DR UCSC; uc008hic.2; mouse. [Q7TN99-5]
DR CTD; 22849; -.
DR MGI; MGI:2443075; Cpeb3.
DR VEuPathDB; HostDB:ENSMUSG00000039652; -.
DR eggNOG; KOG0129; Eukaryota.
DR GeneTree; ENSGT00940000158949; -.
DR InParanoid; Q7TN99; -.
DR OrthoDB; 1075356at2759; -.
DR PhylomeDB; Q7TN99; -.
DR TreeFam; TF317658; -.
DR BioGRID-ORCS; 208922; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Cpeb3; mouse.
DR PRO; PR:Q7TN99; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q7TN99; protein.
DR Bgee; ENSMUSG00000039652; Expressed in secondary oocyte and 60 other tissues.
DR ExpressionAtlas; Q7TN99; baseline and differential.
DR Genevisible; Q7TN99; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; IDA:UniProtKB.
DR GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0035613; F:RNA stem-loop binding; IDA:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, RNA binding; IDA:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
DR GO; GO:0007616; P:long-term memory; IMP:UniProtKB.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IBA:GO_Central.
DR GO; GO:1900248; P:negative regulation of cytoplasmic translational elongation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IDA:UniProtKB.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; IDA:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
DR GO; GO:0060998; P:regulation of dendritic spine development; IMP:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0050955; P:thermoception; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IMP:MGI.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 4.10.640.40; -; 1.
DR InterPro; IPR032296; CEBP_ZZ.
DR InterPro; IPR038446; CEBP_ZZ_sf.
DR InterPro; IPR034819; CPEB.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR12566; PTHR12566; 1.
DR Pfam; PF16366; CEBP_ZZ; 1.
DR Pfam; PF16367; RRM_7; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Amyloid; Cell projection; Cytoplasm;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; RNA-binding; Synapse; Translation regulation; Ubl conjugation.
FT CHAIN 1..716
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 3"
FT /id="PRO_0000269262"
FT DOMAIN 459..550
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 567..649
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..103
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..185
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 459..460
FT /note="Cleavage; by CAPN2"
FT /evidence="ECO:0000269|PubMed:22711986"
FT SITE 462
FT /note="Required for RNA-binding activity"
FT /evidence="ECO:0000250|UniProtKB:Q8NE35"
FT SITE 506
FT /note="Required for RNA-binding activity"
FT /evidence="ECO:0000250|UniProtKB:Q8NE35"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26915047"
FT MOD_RES 309
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26915047"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26915047"
FT VAR_SEQ 1..216
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:20003455"
FT /id="VSP_058565"
FT VAR_SEQ 367..389
FT /note="Missing (in isoform 3, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:12871996,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:20003455"
FT /id="VSP_022036"
FT VAR_SEQ 409..416
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12871996"
FT /id="VSP_022037"
FT VAR_SEQ 581..584
FT /note="VELA -> GEWK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022038"
FT VAR_SEQ 585..716
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022039"
FT MUTAGEN 419
FT /note="S->A: Abolishes phosphorylation by PKA."
FT /evidence="ECO:0000269|PubMed:26915047"
FT MUTAGEN 420
FT /note="S->A: Reduces phosphorylation by PKA."
FT /evidence="ECO:0000269|PubMed:26915047"
FT CONFLICT 372
FT /note="N -> P (in Ref. 2; BAE27791 and 3; BAC41458)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 78335 MW; 1FA1D8125FD69819 CRC64;
MQDDLLMDKS KTQPQSQQQQ RQQQQQQQQL QPEPGAAEAP STPLSSEIPK PEDSSAVPAL
SPASAPPAPN GPDKMQMESP LLPGLSFHQP PQQPPPPQEP TAPGASLSPS FGSTWSTGTT
NAVEDSFFQG ITPVNGTMLF QNFPHHVNPV FGGTFSPQIG LAQTQHHQQP PPPAPQPPQP
AQPPQAQPSQ QRRSPASPSQ APYAQRSAAA YGHQPIMTSK PSSSSAVAAA AAAAAASSAS
SSWNTHQSVN AAWSAPSNPW GGLQAGRDPR RAVGVGVGVG VGVPSPLNPI SPLKKPFSSN
VIAPPKFPRA APLTSKSWME DNAFRTDNGN NLLPFQDRSR PYDTFNLHSL ENSLMDMIRT
DHEPLKGKHY PNSGPPMSFA DIMWRNHFAG RMGINFHHPG TDNIMALNTR SYGRRRGRSS
LFPFEDAFLD DSHGDQALSS GLSSPTRCQN GERVERYSRK VFVGGLPPDI DEDEITASFR
RFGPLVVDWP HKAESKSYFP PKGYAFLLFQ EESSVQALID ACLEEDGKLY LCVSSPTIKD
KPVQIRPWNL SDSDFVMDGS QPLDPRKTIF VGGVPRPLRA VELAMIMDRL YGGVCYAGID
TDPELKYPKG AGRVAFSNQQ SYIAAISARF VQLQHNDIDK RVEVKPYVLD DQMCDECQGT
RCGGKFAPFF CANVTCLQYY CEYCWASIHS RAGREFHKPL VKEGGDRPRH VPFRWS
