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

 CPEB3_XENTR             Reviewed;         632 AA.
Q28CH2;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 1.
16-JAN-2019, entry version 67.
RecName: Full=Cytoplasmic polyadenylation element-binding protein 3;
Short=CPE-BP3;
Short=CPE-binding protein 3;
Short=CPEB-3;
Name=cpeb3; ORFNames=TGas021m22.1;
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Silurana.
NCBI_TaxID=8364;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Gastrula;
Sanger Xenopus tropicalis EST/cDNA project;
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=18472403; DOI=10.1016/j.mod.2008.03.001;
Kyuno J., Masse K., Jones E.A.;
"A functional screen for genes involved in Xenopus pronephros
development.";
Mech. Dev. 125:571-586(2008).
-!- 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
(By similarity). 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 (By
similarity). Required for the consolidation and maintenance of
hippocampal-based long term memory (By similarity). Inhibits
differentiation of intermediate mesoderm from an early stage to
inhibit pronephric differentiation but induce neural
differentiation (PubMed:18472403). {ECO:0000250|UniProtKB:Q7TN99,
ECO:0000269|PubMed:18472403}.
-!- SUBUNIT: Following synaptic activity, forms amyloid-like oligomers
(By similarity). Aggregation requires an intact actin cytoskeleton
(By similarity). {ECO:0000250|UniProtKB:Q7TN99}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7TN99}.
Nucleus {ECO:0000250|UniProtKB:Q7TN99}. Cell junction, synapse
{ECO:0000250|UniProtKB:Q7TN99}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q7TN99}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000250|UniProtKB:Q7TN99}. Note=Predominantly cytoplasmic in
unstimulated neurons but translocates to the nucleus following
neuronal stimulation. {ECO:0000250|UniProtKB:Q7TN99}.
-!- TISSUE SPECIFICITY: In embryos, expressed in the central nervous
system, and intermediate and distal pronephric tubule segments of
the embryonic kidney. {ECO:0000269|PubMed:18472403}.
-!- 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:0000250|UniProtKB:Q7TN99}.
-!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
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EMBL; CR926390; CAJ82507.1; -; mRNA.
RefSeq; NP_001015925.1; NM_001015925.2.
UniGene; Str.27689; -.
ProteinModelPortal; Q28CH2; -.
SMR; Q28CH2; -.
STRING; 8364.ENSXETP00000026614; -.
PaxDb; Q28CH2; -.
GeneID; 548679; -.
KEGG; xtr:548679; -.
CTD; 22849; -.
Xenbase; XB-GENE-5716009; cpeb3.
eggNOG; KOG0129; Eukaryota.
eggNOG; ENOG410Y1XZ; LUCA.
HOGENOM; HOG000290660; -.
HOVERGEN; HBG058010; -.
InParanoid; Q28CH2; -.
KO; K02602; -.
OrthoDB; 1075356at2759; -.
Proteomes; UP000008143; Unassembled WGS sequence.
GO; GO:0097440; C:apical dendrite; ISS:UniProtKB.
GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
GO; GO:0008135; F:translation factor activity, RNA binding; ISS:UniProtKB.
GO; GO:0000900; F:translation repressor activity, mRNA regulatory element binding; ISS:UniProtKB.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
GO; GO:2000766; P:negative regulation of cytoplasmic translation; IBA:GO_Central.
GO; GO:1900248; P:negative regulation of cytoplasmic translational elongation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:UniProtKB.
GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISS: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; ISS:UniProtKB.
GO; GO:0048793; P:pronephros development; IMP:UniProtKB.
GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
Gene3D; 3.30.40.130; -; 1.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR032296; CEBP_ZZ.
InterPro; IPR038446; CEBP_ZZ_sf.
InterPro; IPR034819; CPEB.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
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.
2: Evidence at transcript level;
Activator; Cell junction; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Developmental protein; Differentiation;
Membrane; Nucleus; Postsynaptic cell membrane; Reference proteome;
Repeat; Repressor; RNA-binding; Synapse.
CHAIN 1 632 Cytoplasmic polyadenylation element-
binding protein 3.
/FTId=PRO_0000269263.
DOMAIN 375 466 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 483 565 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 13 30 Gln-rich.
SEQUENCE 632 AA; 70211 MW; F15B94347560ED82 CRC64;
MQDDLLMDKS KAQQRQQPQQ PPSSQTQQQQ KEAASVAEPP SSRESSPPTH KDKMQMESPL
LPGLSFQQEP PTTPSLSPSF GSTWSTGGSN SAVDDSFFPG ITPVNGTMLF QNFPHHHHVN
PVFGGTFSPQ MGLAHQTQQQ QRRSPASPNN HTAYTQRNAY SHQPILTNKP SSSPNSSSPS
PSNWNNQQNA AWNTPSNPWG AMQPGRDPRR AVGVGVGVGV GVPSPLNPIS PLKKTFSSNV
IAPPKFSRAS PLTPKSWVED NAFRTDNGNT LLPLQDRNRP YDSFNLHTLE NSLMDMIRTD
HEPLKARMGL NFHHPGTDNI MALNTRSYGR RRGRSSLFPF EDGFLGDGHG DQSLSSGLSS
PTHCQNGERI ERYSRKVFVG GLPPDIDEDE ITASFRRFGP LVVDWPHKAE SKSYFPPKGY
AFLLFQEESS VQALIDACLE EDGKLYLCVS SPTIKDKPVQ IRPWNLSDSD FVMDGSQPLD
PRKTIFVGGV PRPLRAVELA MIMDRLYGGV CYAGIDTDPE LKYPKGAGRV AFSNQQSYIA
AISARFVQLQ HNDIDKRVEV KPYVLDDQMC DECQGTRCGG KFAPFFCANV TCLQYYCEYC
WASIHSRAGR EFHKPLVKEG GDRPRHVPFH WS


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