CPEB3_XENTR
ID CPEB3_XENTR Reviewed; 632 AA.
AC Q28CH2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 3;
DE Short=CPE-BP3;
DE Short=CPE-binding protein 3;
DE Short=CPEB-3;
GN Name=cpeb3; ORFNames=TGas021m22.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18472403; DOI=10.1016/j.mod.2008.03.001;
RA Kyuno J., Masse K., Jones E.A.;
RT "A functional screen for genes involved in Xenopus pronephros
RT development.";
RL Mech. Dev. 125:571-586(2008).
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 (By
CC similarity). Does not bind to the cytoplasmic polyadenylation element
CC (CPE), a uridine-rich sequence element within the mRNA 3'-UTR, but
CC binds to a U-rich loop within a stem-loop structure (By similarity).
CC Required for the consolidation and maintenance of hippocampal-based
CC long term memory (By similarity). Inhibits differentiation of
CC intermediate mesoderm from an early stage to inhibit pronephric
CC differentiation but induce neural differentiation (PubMed:18472403).
CC {ECO:0000250|UniProtKB:Q7TN99, ECO:0000269|PubMed:18472403}.
CC -!- SUBUNIT: Following synaptic activity, forms amyloid-like oligomers (By
CC similarity). Aggregation requires an intact actin cytoskeleton (By
CC similarity). {ECO:0000250|UniProtKB:Q7TN99}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7TN99}. Nucleus
CC {ECO:0000250|UniProtKB:Q7TN99}. Synapse {ECO:0000250|UniProtKB:Q7TN99}.
CC Cell projection, dendrite {ECO:0000250|UniProtKB:Q7TN99}. Postsynaptic
CC density {ECO:0000250|UniProtKB:Q7TN99}. Note=Predominantly cytoplasmic
CC in unstimulated neurons but translocates to the nucleus following
CC neuronal stimulation. {ECO:0000250|UniProtKB:Q7TN99}.
CC -!- TISSUE SPECIFICITY: In embryos, expressed in the central nervous
CC system, and intermediate and distal pronephric tubule segments of the
CC embryonic kidney. {ECO:0000269|PubMed:18472403}.
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:0000250|UniProtKB:Q7TN99}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
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DR EMBL; CR926390; CAJ82507.1; -; mRNA.
DR RefSeq; NP_001015925.1; NM_001015925.2.
DR AlphaFoldDB; Q28CH2; -.
DR BMRB; Q28CH2; -.
DR SMR; Q28CH2; -.
DR STRING; 8364.ENSXETP00000011081; -.
DR PaxDb; Q28CH2; -.
DR GeneID; 548679; -.
DR KEGG; xtr:548679; -.
DR CTD; 22849; -.
DR Xenbase; XB-GENE-5716009; cpeb3.
DR eggNOG; KOG0129; Eukaryota.
DR InParanoid; Q28CH2; -.
DR OrthoDB; 1075356at2759; -.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; ISS:UniProtKB.
DR GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, RNA binding; ISS:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISS: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; ISS:UniProtKB.
DR GO; GO:0048793; P:pronephros development; IMP:UniProtKB.
DR GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
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; 2.
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 2: Evidence at transcript level;
KW Activator; Cell projection; Cytoplasm; Developmental protein;
KW Differentiation; Nucleus; Reference proteome; Repeat; Repressor;
KW RNA-binding; Synapse.
FT CHAIN 1..632
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 3"
FT /id="PRO_0000269263"
FT DOMAIN 375..466
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 483..565
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ 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
