CPEB1_RAT
ID CPEB1_RAT Reviewed; 561 AA.
AC P0C279;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 1;
DE Short=CPE-BP1;
DE Short=CPE-binding protein 1;
DE Short=CPEB;
DE Short=CPEB-1;
GN Name=Cpeb1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9856468; DOI=10.1016/s0896-6273(00)80630-3;
RA Wu L., Wells D., Tay J., Mendis D., Abbott M.-A., Barnitt A., Quinlan E.,
RA Heynen A., Fallon J.R., Richter J.D.;
RT "CPEB-mediated cytoplasmic polyadenylation and the regulation of
RT experience-dependent translation of alpha-CaMKII mRNA at synapses.";
RL Neuron 21:1129-1139(1998).
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 3'-UTR
CC of mRNAs. In absence of phosphorylation and in association with TACC3
CC is also involved as a repressor of translation of CPE-containing mRNA;
CC a repression that is relieved by phosphorylation or degradation.
CC Involved in the transport of CPE-containing mRNA to dendrites; those
CC mRNAs may be transported to dendrites in a translationally dormant form
CC and 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 {ECO:0000250}. Synapse {ECO:0000250}.
CC Cytoplasm, P-body {ECO:0000250}. Cytoplasmic granule {ECO:0000250}.
CC Membrane {ECO:0000250}. Postsynaptic density {ECO:0000250}.
CC Note=Localizes in synaptosomes at dendritic synapses of neurons.
CC Strongly enriched in postsynaptic density fractions. Transported into
CC dendrites in a microtubule-dependent fashion and colocalizes in mRNA-
CC containing particles with TACC3, dynein and kinesin (By similarity).
CC Membrane-associated (By similarity). Colocalizes at excitatory synapses
CC with members of the polyadenylation and translation complex factors
CC (CPSF, APLP1, TACC3, AURKA, SYP, etc.) including CPE-containing RNAs
CC (By similarity). In P-bodies and stress granules (By similarity).
CC Recruited to stress granules (SGs) upon arsenite treatment (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampus and cerebral cortex (at
CC protein level). Expressed in hippocampus (dentate gyrus and CA1-CA4
CC regions), cerebellum (Purkinje cells), cortex, visual cortex (layers 1
CC and 2), mesencephalon, diencephalon and brain stem.
CC {ECO:0000269|PubMed:9856468}.
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 165 and 196. Phosphorylation and dephosphorylation on Thr-171
CC regulates cytoplasmic polyadenylation and translation of CPE-containing
CC mRNAs. Phosphorylation on Thr-171 by AURKA and CAMK2A activates CPEB1.
CC Phosphorylation on Thr-171 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; AABR03000812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03000839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001099746.1; NM_001106276.1.
DR AlphaFoldDB; P0C279; -.
DR BMRB; P0C279; -.
DR SMR; P0C279; -.
DR STRING; 10116.ENSRNOP00000026009; -.
DR iPTMnet; P0C279; -.
DR PhosphoSitePlus; P0C279; -.
DR PaxDb; P0C279; -.
DR PRIDE; P0C279; -.
DR GeneID; 293056; -.
DR KEGG; rno:293056; -.
DR UCSC; RGD:1310421; rat.
DR CTD; 64506; -.
DR RGD; 1310421; Cpeb1.
DR VEuPathDB; HostDB:ENSRNOG00000019161; -.
DR eggNOG; KOG0129; Eukaryota.
DR InParanoid; P0C279; -.
DR OrthoDB; 1075356at2759; -.
DR PhylomeDB; P0C279; -.
DR TreeFam; TF317658; -.
DR PRO; PR:P0C279; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019161; Expressed in Ammon's horn and 13 other tissues.
DR ExpressionAtlas; P0C279; baseline and differential.
DR Genevisible; P0C279; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0072687; C:meiotic spindle; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
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:0003730; F:mRNA 3'-UTR binding; IDA:RGD.
DR GO; GO:0003729; F:mRNA binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0008135; F:translation factor activity, RNA binding; IBA:GO_Central.
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:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IMP:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
DR GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0006417; P:regulation of translation; ISO:RGD.
DR GO; GO:0007130; P:synaptonemal complex assembly; ISO:RGD.
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 SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Membrane; Metal-binding; mRNA processing;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Ribonucleoprotein;
KW RNA-binding; Synapse; Translation regulation; Zinc.
FT CHAIN 1..561
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 1"
FT /id="PRO_0000269254"
FT DOMAIN 310..407
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 429..510
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 158..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..561
FT /note="Necessary for stress granule assembly and correct
FT localization in dcp1 bodies"
FT /evidence="ECO:0000250"
FT COMPBIAS 173..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 514
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 526
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 531
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 536
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 539
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 544
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT BINDING 552
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT SITE 410
FT /note="Important for the positionning of RRM1 relative to
FT RRM2"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZB8"
FT MOD_RES 171
FT /note="Phosphothreonine; by AURKA and CAMK2A"
FT /evidence="ECO:0000250|UniProtKB:P70166"
SQ SEQUENCE 561 AA; 62062 MW; AF890EA7A263FC5A CRC64;
MAFSLEEESG RIKDCWDNQE VPALSTCSNA NIFRRINAIL DDSLDFSKVC TTPINRGIHD
QLPDFQDSEE AITSRMLFPT SAQESPRGLP DANGLCLGLQ SLSLTGWDRP WSTQDSDSSA
QSNTQSVLSM LQNPLGNVLG KTPLSFLSLD PLGSDLDKFP APSVRGSRLD TRPILDSRSS
SPSDSDTSGF SSGSDHLSDL ISSLRISPPL PFLSMTGNGP RDPLKMGVGS RMDQEQAALA
AVAPSPTSAP KRWPGTSVWP SWDLLGAPKD PFSIEREARL HRQAAAVNEA TCTWSGQLPP
RNYKNPIYSC KVFLGGVPWD ITEAGLVNTF RVFGSLSVEW PGKDGKHPRC PPKGNMPKGY
VYLVFELEKS VRALLQACSH DPLSPDGLSE YYFKMSSRRM RCKEVQVIPW VLADSNFVWS
PSQRLDPSRT VFVGALHGML NAEALAAILN DLFGGVVYAG IDTDKHKYPI GSGRVTFNNQ
RSYLKAVTAA FVEIKTTKFT KKVQIDPYLE DSLCLICSSQ PGPFFCRDQV CFKYFCRSCW
HWRHSMEGLR HHSPLMRNQK N
