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Cytoplasmic polyadenylation element-binding protein 3 (CPE-BP3) (CPE-binding protein 3) (mCPEB-3)

 CPEB3_MOUSE             Reviewed;         716 AA.
Q7TN99; A1A562; Q3TT89; Q3UHR6; Q8CHC2;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
25-OCT-2017, entry version 114.
RecName: Full=Cytoplasmic polyadenylation element-binding protein 3;
Short=CPE-BP3;
Short=CPE-binding protein 3;
Short=mCPEB-3;
Name=Cpeb3; Synonyms=Kiaa0940;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), INDUCTION, AND
TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=12871996; DOI=10.1073/pnas.1133424100;
Theis M., Si K., Kandel E.R.;
"Two previously undescribed members of the mouse CPEB family of genes
and their inducible expression in the principal cell layers of the
hippocampus.";
Proc. Natl. Acad. Sci. U.S.A. 100:9602-9607(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17024188; DOI=10.1038/sj.emboj.7601322;
Huang Y.S., Kan M.C., Lin C.L., Richter J.D.;
"CPEB3 and CPEB4 in neurons: analysis of RNA-binding specificity and
translational control of AMPA receptor GluR2 mRNA.";
EMBO J. 25:4865-4876(2006).
[6]
ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=20003455; DOI=10.1186/1471-2199-10-109;
Wang X.P., Cooper N.G.;
"Characterization of the transcripts and protein isoforms for
cytoplasmic polyadenylation element binding protein-3 (CPEB3) in the
mouse retina.";
BMC Mol. Biol. 10:109-109(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-197, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, and Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
INTERACTION WITH STAT5B.
PubMed=20639532; DOI=10.1093/nar/gkq634;
Peng S.C., Lai Y.T., Huang H.Y., Huang H.D., Huang Y.S.;
"A novel role of CPEB3 in regulating EGFR gene transcription via
association with Stat5b in neurons.";
Nucleic Acids Res. 38:7446-7457(2010).
[9]
FUNCTION, INTERACTION WITH NEURL1, SUBCELLULAR LOCATION, AND
UBIQUITINATION.
PubMed=22153079; DOI=10.1016/j.cell.2011.09.056;
Pavlopoulos E., Trifilieff P., Chevaleyre V., Fioriti L., Zairis S.,
Pagano A., Malleret G., Kandel E.R.;
"Neuralized1 activates CPEB3: a function for nonproteolytic ubiquitin
in synaptic plasticity and memory storage.";
Cell 147:1369-1383(2011).
[10]
FUNCTION, INTERACTION WITH CAPN2, SUBCELLULAR LOCATION, AND
PROTEOLYTIC CLEAVAGE.
PubMed=22711986; DOI=10.1128/MCB.00296-12;
Wang C.F., Huang Y.S.;
"Calpain 2 activated through N-methyl-D-aspartic acid receptor
signaling cleaves CPEB3 and abrogates CPEB3-repressed translation in
neurons.";
Mol. Cell. Biol. 32:3321-3332(2012).
[11]
SUBCELLULAR LOCATION.
PubMed=22730302; DOI=10.1093/nar/gks598;
Chao H.W., Lai Y.T., Lu Y.L., Lin C.L., Mai W., Huang Y.S.;
"NMDAR signaling facilitates the IPO5-mediated nuclear import of
CPEB3.";
Nucleic Acids Res. 40:8484-8498(2012).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24155305; DOI=10.1523/JNEUROSCI.3043-13.2013;
Chao H.W., Tsai L.Y., Lu Y.L., Lin P.Y., Huang W.H., Chou H.J.,
Lu W.H., Lin H.C., Lee P.T., Huang Y.S.;
"Deletion of CPEB3 enhances hippocampus-dependent memory via
increasing expressions of PSD95 and NMDA receptors.";
J. Neurosci. 33:17008-17022(2013).
[13]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-309, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[14]
FUNCTION, INTERACTION WITH UBC9, AND SUMOYLATION.
PubMed=26074071; DOI=10.1016/j.celrep.2015.04.061;
Drisaldi B., Colnaghi L., Fioriti L., Rao N., Myers C., Snyder A.M.,
Metzger D.J., Tarasoff J., Konstantinov E., Fraser P.E., Manley J.L.,
Kandel E.R.;
"SUMOylation is an inhibitory constraint that regulates the prion-like
aggregation and activity of CPEB3.";
Cell Rep. 11:1694-1702(2015).
[15]
FUNCTION, SUBUNIT, AND INDUCTION.
PubMed=26074072; DOI=10.1016/j.celrep.2015.04.060;
Stephan J.S., Fioriti L., Lamba N., Colnaghi L., Karl K.,
Derkatch I.L., Kandel E.R.;
"The CPEB3 protein is a functional prion that interacts with the actin
cytoskeleton.";
Cell Rep. 11:1772-1785(2015).
[16]
FUNCTION, SUBUNIT, INDUCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
PubMed=26074003; DOI=10.1016/j.neuron.2015.05.021;
Fioriti L., Myers C., Huang Y.Y., Li X., Stephan J.S., Trifilieff P.,
Colnaghi L., Kosmidis S., Drisaldi B., Pavlopoulos E., Kandel E.R.;
"The persistence of hippocampal-based memory requires protein
synthesis mediated by the prion-like protein CPEB3.";
Neuron 86:1433-1448(2015).
[17]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=26915043; DOI=10.1371/journal.pone.0148491;
Fong S.W., Lin H.C., Wu M.F., Chen C.C., Huang Y.S.;
"CPEB3 deficiency elevates TRPV1 expression in dorsal root ganglia
neurons to potentiate thermosensation.";
PLoS ONE 11:E0148491-E0148491(2016).
[18]
PHOSPHORYLATION AT SER-291; SER-419 AND SER-420, AND MUTAGENESIS OF
SER-419 AND SER-420.
PubMed=26915047; DOI=10.1371/journal.pone.0150000;
Kaczmarczyk L., Labrie-Dion E., Sehgal K., Sylvester M., Skubal M.,
Josten M., Steinhaeuser C., De Koninck P., Theis M.;
"New phosphospecific antibody reveals isoform-specific phosphorylation
of CPEB3 protein.";
PLoS ONE 11:E0150000-E0150000(2016).
-!- FUNCTION: Sequence-specific RNA-binding protein which acts as a
translational repressor in the basal unstimulated state but,
following neuronal stimulation, acts as a translational activator
(PubMed:17024188, PubMed:26074072). In contrast to CPEB1, does not
bind to the cytoplasmic polyadenylation element (CPE), a uridine-
rich sequence element within the mRNA 3'-UTR, but binds to a U-
rich loop within a stem-loop structure (PubMed:17024188). Required
for the consolidation and maintenance of hippocampal-based long
term memory (PubMed:26074003). In the basal state, binds to the
mRNA 3'-UTR of the glutamate receptors GRIA1 and GRIA2 and
negatively regulates their translation (PubMed:17024188,
PubMed:22153079). Also represses the translation of DLG4, GRIN1
GRIN2A and GRIN2B (PubMed:24155305). When activated, acts as a
translational activator of GRIA1 and GRIA2 (PubMed:22153079,
PubMed:26074003). In the basal state, suppresses SUMO2 translation
but activates it following neuronal stimulation (PubMed:26074071).
Binds to the 3'-UTR of TRPV1 mRNA and represses TRPV1 translation
which is required to maintain normal thermoception
(PubMed:26915043). Binds actin mRNA, leading to actin
translational repression in the basal state and to translational
activation following neuronal stimulation (PubMed:26074072).
Negatively regulates target mRNA levels by binding to TOB1 which
recruits CNOT7/CAF1 to a ternary complex and this leads to target
mRNA deadenylation and decay (By similarity). In addition to its
role in translation, binds to and inhibits the transcriptional
activation activity of STAT5B without affecting its dimerization
or DNA-binding activity. This, in turn, represses transcription of
the STAT5B target gene EGFR which has been shown to play a role in
enhancing learning and memory performance (By similarity). In
contrast to CPEB1, CPEB2 and CPEB4, not required for cell cycle
progression (By similarity). {ECO:0000250|UniProtKB:Q8NE35,
ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:22153079,
ECO:0000269|PubMed:22711986, ECO:0000269|PubMed:24155305,
ECO:0000269|PubMed:26074003, ECO:0000269|PubMed:26074071,
ECO:0000269|PubMed:26074072, ECO:0000269|PubMed:26915043}.
-!- SUBUNIT: Following synaptic activity, aggregates to form amyloid-
like oligomers (PubMed:26074003, PubMed:26074072). Aggregation
requires an intact actin cytoskeleton (PubMed:26074072). Interacts
with STAT5B; this inhibits STAT5B-mediated transcriptional
activation (PubMed:20639532). Interacts with E3 ubiquitin-protein
ligase NEURL1; this leads to monoubiquitination and activation of
CPEB3 (PubMed:22153079). Interacts with CAPN2; this leads to
cleavage of CPEB3 (PubMed:22711986). Interacts (via C-terminal
RNA-binding region) with TOB1; TOB1 also binds CNOT7/CAF1 and
recruits it to CPEB3 to form a ternary complex (By similarity).
Interacts with SUMO-conjugating enzyme UBC9 (PubMed:26074071).
Interacts with IPO5; the interaction is enhanced in a RAN-
regulated manner following neuronal stimulation and mediates CPEB3
nuclear import (By similarity). Interacts with exportin XPO1/CRM1
(By similarity). {ECO:0000250|UniProtKB:Q8NE35,
ECO:0000269|PubMed:20639532, ECO:0000269|PubMed:22153079,
ECO:0000269|PubMed:22711986, ECO:0000269|PubMed:26074003,
ECO:0000269|PubMed:26074071, ECO:0000269|PubMed:26074072}.
-!- INTERACTION:
Q923S6:Neurl1; NbExp=9; IntAct=EBI-5376779, EBI-5376802;
P62991:Ubc; NbExp=2; IntAct=EBI-5376779, EBI-413074;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22711986}.
Nucleus {ECO:0000269|PubMed:22711986}. Cell junction, synapse
{ECO:0000269|PubMed:17024188}. Cell projection, dendrite
{ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:22153079,
ECO:0000269|PubMed:22711986}. Cell junction, synapse, postsynaptic
cell membrane, postsynaptic density {ECO:0000269|PubMed:17024188}.
Note=Predominantly cytoplasmic in unstimulated neurons but
translocates to the nucleus following neuronal stimulation
(PubMed:22711986). Nuclear import is mediated by importin IPO5
(PubMed:22730302). {ECO:0000269|PubMed:22711986,
ECO:0000269|PubMed:22730302}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=mCPEB-3a;
IsoId=Q7TN99-1; Sequence=Displayed;
Name=2; Synonyms=mCPEB-3b;
IsoId=Q7TN99-2; Sequence=VSP_022037;
Name=3; Synonyms=mCPEB-3c;
IsoId=Q7TN99-3; Sequence=VSP_022036;
Name=4; Synonyms=mCPEB-3d;
IsoId=Q7TN99-4; Sequence=VSP_022036, VSP_022037;
Name=5;
IsoId=Q7TN99-5; Sequence=VSP_022036, VSP_022038, VSP_022039;
Name=6;
IsoId=Q7TN99-6; Sequence=VSP_058565, VSP_022036;
-!- TISSUE SPECIFICITY: Highly expressed in brain (at protein level)
(PubMed:17024188). In brain, expressed in the hippocampus, granule
cells and interneurons of the cerebellum, and mitral cells of the
olfactory bulb (at protein level) (PubMed:17024188). Detected in
the spinal cord and in peripheral dorsal root ganglia (at protein
level) (PubMed:26915043). In the retina, strongly expressed in the
retinal ganglion layer and, to a lesser extent, in the inner
margin of the inner nuclear layer with expression also detected in
the inner and outer plexiform layers (at protein level)
(PubMed:20003455). Highly expressed in brain and heart, less in
liver, kidney, embryo, skeletal muscle, lung and ovary
(PubMed:12871996). Weakly expressed in granular cells of dentate
gyrus and the pyramidal cells of CA3 and CA1 of the hippocampus
(PubMed:12871996). {ECO:0000269|PubMed:12871996,
ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:20003455,
ECO:0000269|PubMed:26915043}.
-!- DEVELOPMENTAL STAGE: In the retina, expression increases
throughout postnatal development and remains high in the adult (at
protein level). {ECO:0000269|PubMed:20003455}.
-!- INDUCTION: Up-regulated following synaptic activity (at protein
level) (PubMed:26074003, PubMed:26074072). Up-regulated in
granular cells of the dentate gyrus and the pyramidal cells of CA1
and CA3 after kainate-induced seizures (PubMed:12871996).
{ECO:0000269|PubMed:12871996, ECO:0000269|PubMed:26074003,
ECO:0000269|PubMed:26074072}.
-!- DOMAIN: The N-terminal Gln-rich region is required for the
formation of amyloid-like oligomers and for the stability of long-
term potentiation and spatial memory.
{ECO:0000269|PubMed:26074003}.
-!- PTM: Activated by NEURL1-mediated monoubiquitination, resulting in
the growth of new dendritic spines and increased levels of GRIA1
and GRIA2. NEURL1-mediated monoubiquitination facilitates synaptic
plasticity and hippocampal-dependent memory storage.
{ECO:0000269|PubMed:22153079}.
-!- PTM: Under basal unstimulated conditions when CPEB3 is mainly
unaggregated, sumoylated and acts as a translational repressor.
Following neuronal stimulation, becomes desumoylated and
aggregated which is required for the translation of mRNA targets
and for dendritic filopodia formation.
{ECO:0000269|PubMed:26074071}.
-!- PTM: Following neuronal stimulation, cleaved by CAPN2 which
abolishes its translational repressor activity, leading to
translation of CPEB3 target mRNAs. {ECO:0000269|PubMed:22711986}.
-!- PTM: Phosphorylation is enhanced by neuronal stimulation.
{ECO:0000269|PubMed:26915047}.
-!- DISRUPTION PHENOTYPE: Enhanced thermal sensitivity and increased
levels of Trpv1 in lumbar sciatic nerves and spinal cord
(PubMed:26915043). Elevated short-term fear response, enhanced
long-term spatial memory, dendritic spine enlargement and elevated
levels of Dlg4/Psd95, Gria1 and NMDA receptor subunits Grin1,
Grin2a and Grin2b (PubMed:26074071). Conditional knockout in the
adult forebrain results in viable mice with no gross neurological
defects which display normal locomotor, exploratory and anxiety
behaviors but have impaired long-term memory, impaired long-term
synaptic plasticity and increased levels of Gria1 and Gria2
(PubMed:26074003). {ECO:0000269|PubMed:26074003,
ECO:0000269|PubMed:26074071, ECO:0000269|PubMed:26915043}.
-!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC41458.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY313774; AAQ20843.1; -; mRNA.
EMBL; AK147243; BAE27791.1; -; mRNA.
EMBL; AK161513; BAE36436.1; -; mRNA.
EMBL; AB093274; BAC41458.1; ALT_INIT; mRNA.
EMBL; BC128377; AAI28378.1; -; mRNA.
CCDS; CCDS29775.1; -. [Q7TN99-1]
CCDS; CCDS70946.1; -. [Q7TN99-4]
CCDS; CCDS70947.1; -. [Q7TN99-3]
RefSeq; NP_001277755.1; NM_001290826.1.
RefSeq; NP_001277756.1; NM_001290827.1.
RefSeq; NP_001277757.1; NM_001290828.1. [Q7TN99-3]
RefSeq; NP_001277758.1; NM_001290829.1.
RefSeq; NP_938042.2; NM_198300.3.
RefSeq; XP_006526892.1; XM_006526829.3.
RefSeq; XP_006526893.1; XM_006526830.3.
RefSeq; XP_006526894.1; XM_006526831.3.
RefSeq; XP_006526895.1; XM_006526832.3.
RefSeq; XP_006526896.1; XM_006526833.3.
RefSeq; XP_006526897.1; XM_006526834.2.
RefSeq; XP_006526902.1; XM_006526839.3.
RefSeq; XP_011245510.1; XM_011247208.1. [Q7TN99-3]
UniGene; Mm.391176; -.
ProteinModelPortal; Q7TN99; -.
SMR; Q7TN99; -.
BioGrid; 229024; 1.
IntAct; Q7TN99; 2.
STRING; 10090.ENSMUSP00000078690; -.
iPTMnet; Q7TN99; -.
PhosphoSitePlus; Q7TN99; -.
PaxDb; Q7TN99; -.
PeptideAtlas; Q7TN99; -.
PRIDE; Q7TN99; -.
Ensembl; ENSMUST00000126188; ENSMUSP00000120416; ENSMUSG00000039652. [Q7TN99-3]
Ensembl; ENSMUST00000126781; ENSMUSP00000122442; ENSMUSG00000039652. [Q7TN99-5]
Ensembl; ENSMUST00000213231; ENSMUSP00000151042; ENSMUSG00000111861. [Q7TN99-3]
Ensembl; ENSMUST00000214706; ENSMUSP00000150033; ENSMUSG00000111861. [Q7TN99-5]
GeneID; 208922; -.
KEGG; mmu:208922; -.
UCSC; uc008hhz.2; mouse. [Q7TN99-1]
UCSC; uc008hia.2; mouse. [Q7TN99-3]
UCSC; uc008hic.2; mouse. [Q7TN99-5]
CTD; 22849; -.
MGI; MGI:2443075; Cpeb3.
eggNOG; KOG0129; Eukaryota.
eggNOG; ENOG410Y1XZ; LUCA.
GeneTree; ENSGT00390000012886; -.
HOGENOM; HOG000290660; -.
HOVERGEN; HBG058010; -.
InParanoid; Q7TN99; -.
KO; K02602; -.
PhylomeDB; Q7TN99; -.
TreeFam; TF317658; -.
ChiTaRS; Cpeb3; mouse.
PRO; PR:Q7TN99; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000039652; -.
ExpressionAtlas; Q7TN99; baseline and differential.
Genevisible; Q7TN99; MM.
GO; GO:0097440; C:apical dendrite; IDA:UniProtKB.
GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:MGI.
GO; GO:0035613; F:RNA stem-loop binding; IDA:UniProtKB.
GO; GO:0008135; F:translation factor activity, RNA binding; IDA:UniProtKB.
GO; GO:0000900; F:translation repressor activity, nucleic acid binding; IDA:UniProtKB.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
GO; GO:0007616; P:long-term memory; IMP:UniProtKB.
GO; GO:1900248; P:negative regulation of cytoplasmic translational elongation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0060999; P:positive regulation of dendritic spine development; IDA:UniProtKB.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:UniProtKB.
GO; GO:1900365; P:positive regulation of mRNA polyadenylation; IDA:UniProtKB.
GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
GO; GO:0060998; P:regulation of dendritic spine development; IMP:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
GO; GO:0050955; P:thermoception; IMP:UniProtKB.
InterPro; IPR032296; CEBP_ZZ.
InterPro; IPR034819; CPEB.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR12566; PTHR12566; 1.
Pfam; PF16366; CEBP_ZZ; 1.
Pfam; PF16367; RRM_7; 1.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
Activator; Alternative splicing; Amyloid; Cell junction;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Membrane; Methylation; Nucleus; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Repeat; Repressor;
RNA-binding; Synapse; Translation regulation; Ubl conjugation.
CHAIN 1 716 Cytoplasmic polyadenylation element-
binding protein 3.
/FTId=PRO_0000269262.
DOMAIN 459 550 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 567 649 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 13 31 Gln-rich.
COMPBIAS 32 202 Pro-rich.
COMPBIAS 226 236 Poly-Ala.
SITE 459 460 Cleavage; by CAPN2.
{ECO:0000269|PubMed:22711986}.
SITE 462 462 Required for RNA-binding activity.
{ECO:0000250|UniProtKB:Q8NE35}.
SITE 506 506 Required for RNA-binding activity.
{ECO:0000250|UniProtKB:Q8NE35}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 197 197 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000269|PubMed:26915047}.
MOD_RES 309 309 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000269|PubMed:26915047}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000269|PubMed:26915047}.
VAR_SEQ 1 216 Missing (in isoform 6).
{ECO:0000303|PubMed:20003455}.
/FTId=VSP_058565.
VAR_SEQ 367 389 Missing (in isoform 3, isoform 4, isoform
5 and isoform 6).
{ECO:0000303|PubMed:12871996,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:20003455}.
/FTId=VSP_022036.
VAR_SEQ 409 416 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:12871996}.
/FTId=VSP_022037.
VAR_SEQ 581 584 VELA -> GEWK (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_022038.
VAR_SEQ 585 716 Missing (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_022039.
MUTAGEN 419 419 S->A: Abolishes phosphorylation by PKA.
{ECO:0000269|PubMed:26915047}.
MUTAGEN 420 420 S->A: Reduces phosphorylation by PKA.
{ECO:0000269|PubMed:26915047}.
CONFLICT 372 372 N -> P (in Ref. 2; BAE27791 and 3;
BAC41458). {ECO:0000305}.
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


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