CPEB1_PONAB
ID CPEB1_PONAB Reviewed; 486 AA.
AC Q5R733;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 1;
DE Short=CPE-BP1;
DE Short=CPE-binding protein 1;
DE Short=CPEB-1;
GN Name=CPEB1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sequence-specific RNA-binding protein that regulates mRNA
CC cytoplasmic polyadenylation and translation initiation during oocyte
CC maturation, early development and at postsynapse sites of neurons.
CC Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich
CC sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-
CC UTR. In absence of phosphorylation and in association with TACC3 is
CC also involved as a repressor of translation of CPE-containing mRNA; a
CC repression that is relieved by phosphorylation or degradation. Involved
CC in the transport of CPE-containing mRNA to dendrites; those mRNAs may
CC be transported to dendrites in a translationally dormant form and
CC translationally activated at synapses. Its interaction with APLP1
CC promotes local CPE-containing mRNA polyadenylation and translation
CC activation. Induces the assembly of stress granules in the absence of
CC stress. Required for cell cycle progression, specifically for prophase
CC entry. {ECO:0000250|UniProtKB:P70166, ECO:0000250|UniProtKB:Q9BZB8}.
CC -!- SUBUNIT: Interacts with kinesin, dynein, APLP1, APLP2, TENT2/GLD2 and
CC APP. Both phosphorylated and non phosphorylated forms interact with
CC APLP1 (By similarity). Interacts with TENT4B; the interaction is
CC required for TENT4B-mediated translational control (By similarity).
CC {ECO:0000250|UniProtKB:P70166, ECO:0000250|UniProtKB:Q9BZB8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}. Cytoplasmic
CC granule {ECO:0000250}. Synapse {ECO:0000250}. Membrane {ECO:0000250}.
CC Postsynaptic density {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000250}. Note=Also found in stress granules. Recruited to stress
CC granules (SGs) upon arsenite treatment. In dendrites. Localizes in
CC synaptosomes at dendritic synapses of neurons. Strongly enriched in
CC postsynaptic density (PSD) fractions. Transported into dendrites in a
CC microtubule-dependent fashion and colocalizes in mRNA-containing
CC particles with TACC3, dynein and kinesin. Membrane-associated.
CC Colocalizes at excitatory synapses with members of the polyadenylation
CC and translation complex factors (CPSF, APLP1, TACC3, AURKA, SYP, etc.)
CC including CPE-containing RNAs (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The 2 RRM domains and the C-terminal region mediate interaction
CC with CPE-containing RNA. The interdomain linker (411-429) acts as a
CC hinge to fix the relative orientation of the 2 RRMs. The ZZ domain
CC (509-566) coordinates 2 Zn ions and is probably implicated in mediating
CC interactions with other proteins in addition to increasing the affinity
CC of the RRMs for the CPEs. A continuous hydrophobic interface is formed
CC between the 2 RRM. {ECO:0000250|UniProtKB:Q9BZB8}.
CC -!- PTM: Phosphorylated on serine/threonine residues by AURKA within
CC positions 91 and 122. Phosphorylation and dephosphorylation on Thr-97
CC regulates cytoplasmic polyadenylation and translation of CPE-containing
CC mRNAs. Phosphorylation on Thr-97 by AURKA and CAMK2A activates CPEB1.
CC Phosphorylation on Thr-97 may be promoted by APLP1. Phosphorylation
CC increases binding to RNA (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
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DR EMBL; CR860287; CAH92427.1; -; mRNA.
DR RefSeq; NP_001126432.1; NM_001132960.1.
DR AlphaFoldDB; Q5R733; -.
DR BMRB; Q5R733; -.
DR SMR; Q5R733; -.
DR STRING; 9601.ENSPPYP00000007800; -.
DR GeneID; 100173415; -.
DR KEGG; pon:100173415; -.
DR CTD; 64506; -.
DR eggNOG; KOG0129; Eukaryota.
DR InParanoid; Q5R733; -.
DR OrthoDB; 1075356at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; ISS:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISS:UniProtKB.
DR CDD; cd12723; RRM1_CPEB1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 4.10.640.40; -; 1.
DR InterPro; IPR032292; CEBP1_N.
DR InterPro; IPR032296; CEBP_ZZ.
DR InterPro; IPR038446; CEBP_ZZ_sf.
DR InterPro; IPR034819; CPEB.
DR InterPro; IPR034977; CPEB1_RRM1.
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; PF16368; CEBP1_N; 1.
DR Pfam; PF16366; CEBP_ZZ; 1.
DR Pfam; PF16367; RRM_7; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 2: Evidence at transcript level;
KW Activator; Cell projection; Cytoplasm; Membrane; Metal-binding;
KW mRNA processing; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Ribonucleoprotein; RNA-binding; Synapse; Translation regulation; Zinc.
FT CHAIN 1..486
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 1"
FT /id="PRO_0000269253"
FT DOMAIN 236..328
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 350..431
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 87..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..486
FT /note="Necessary for stress granule assembly and correct
FT localization in dcp1 bodies"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT COMPBIAS 99..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 473
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT SITE 331
FT /note="Important for the positionning of RRM1 relative to
FT RRM2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT MOD_RES 97
FT /note="Phosphothreonine; by AURKA and CAMK2A"
FT /evidence="ECO:0000250|UniProtKB:P70166"
SQ SEQUENCE 486 AA; 53662 MW; 334C244660F6126F CRC64;
MLFPTSAQES SRGLPDANDL CLGLQSLSLT GWDRPWSTQD SDSSAQSSTH SVLSMLHNPL
GNVLGKPPLS FLPLDPLGSD LVDKFPAPSV RGSRLDTRPI LDSRSSSPSD SDTSGFSSGS
DHLSDLISSL RISPPLPFLS LTGGGPRDPL KMGVGSRMDQ EQAALAAVTP SPTSASKRWP
GASVWPSWDL LEAPKDPFSI EREARLHRQA AAVNEATCTW SGQLPPRNYK NPIYSCKVFL
GGVPWDITEA GLVNTFRVFG SLSVEWPGKD GKHPRCPPKG YVYLVFELEK SVRSLLQACS
HDPLSPDGLS EYYFKMSSRR MRCKEVQVIP WVLADSNFVR SPSQRLNPSR TVFVGALHGM
LNAEALAAIL NDLFGGVVYA GIDTDKHKYP IGSGRVTFNN QRSYLKAVTA AFVEIKTTKF
TKKVQIDPYL EDSLCHICSS QPGPFFCRDQ VCFKYFCRSC WHWRHSMEGL RHHSPLMRNQ
KNRDSS
