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Cytoplasmic polyadenylation element-binding protein 1 (CPE-BP1) (CPE-binding protein 1) (CPEB) (CPEB-1)

 CPEB1_RAT               Reviewed;         561 AA.
P0C279;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 1.
22-NOV-2017, entry version 91.
RecName: Full=Cytoplasmic polyadenylation element-binding protein 1;
Short=CPE-BP1;
Short=CPE-binding protein 1;
Short=CPEB;
Short=CPEB-1;
Name=Cpeb1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9856468; DOI=10.1016/S0896-6273(00)80630-3;
Wu L., Wells D., Tay J., Mendis D., Abbott M.-A., Barnitt A.,
Quinlan E., Heynen A., Fallon J.R., Richter J.D.;
"CPEB-mediated cytoplasmic polyadenylation and the regulation of
experience-dependent translation of alpha-CaMKII mRNA at synapses.";
Neuron 21:1129-1139(1998).
-!- FUNCTION: Sequence-specific RNA-binding protein that regulates
mRNA cytoplasmic polyadenylation and translation initiation during
oocyte maturation, early development and at postsynapse sites of
neurons. Binds to the cytoplasmic polyadenylation element (CPE),
an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-
3') within the 3'-UTR of mRNAs. In absence of phosphorylation and
in association with TACC3 is also involved as a repressor of
translation of CPE-containing mRNA; a repression that is relieved
by phosphorylation or degradation. Involved in the transport of
CPE-containing mRNA to dendrites; those mRNAs may be transported
to dendrites in a translationally dormant form and translationally
activated at synapses. Its interaction with APLP1 promotes local
CPE-containing mRNA polyadenylation and translation activation.
Induces the assembly of stress granules in the absence of stress.
Required for cell cycle progression, specifically for prophase
entry. {ECO:0000250|UniProtKB:P70166,
ECO:0000250|UniProtKB:Q9BZB8}.
-!- SUBUNIT: Interacts with kinesin, dynein, APLP1, APLP2, PAPD4/GLD2
and APP. Both phosphorylated and non phosphorylated forms interact
with APLP1 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction,
synapse {ECO:0000250}. Cytoplasm, P-body {ECO:0000250}.
Cytoplasmic granule {ECO:0000250}. Membrane {ECO:0000250}. Cell
junction, synapse, postsynaptic cell membrane, postsynaptic
density {ECO:0000250}. Note=Localizes in synaptosomes at dendritic
synapses of neurons. Strongly enriched in postsynaptic density
fractions. Transported into dendrites in a microtubule-dependent
fashion and colocalizes in mRNA-containing particles with TACC3,
dynein and kinesin (By similarity). Membrane-associated (By
similarity). Colocalizes at excitatory synapses with members of
the polyadenylation and translation complex factors (CPSF, APLP1,
TACC3, AURKA, SYP, etc.) including CPE-containing RNAs (By
similarity). In P-bodies and stress granules (By similarity).
Recruited to stress granules (SGs) upon arsenite treatment (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in hippocampus and cerebral cortex
(at protein level). Expressed in hippocampus (dentate gyrus and
CA1-CA4 regions), cerebellum (Purkinje cells), cortex, visual
cortex (layers 1 and 2), mesencephalon, diencephalon and brain
stem. {ECO:0000269|PubMed:9856468}.
-!- DOMAIN: The 2 RRM domains and the C-terminal region mediate
interaction with CPE-containing RNA. The interdomain linker (411-
429) acts as a hinge to fix the relative orientation of the 2
RRMs. The ZZ domain (509-566) coordinates 2 Zn ions and is
probably implicated in mediating interactions with other proteins
in addition to increasing the affinity of the RRMs for the CPEs. A
continuous hydrophobic interface is formed between the 2 RRM.
{ECO:0000250|UniProtKB:Q9BZB8}.
-!- PTM: Phosphorylated on serine/threonine residues by AURKA within
positions 165 and 196. Phosphorylation and dephosphorylation on
Thr-171 regulates cytoplasmic polyadenylation and translation of
CPE-containing mRNAs. Phosphorylation on Thr-171 by AURKA and
CAMK2A activates CPEB1. Phosphorylation on Thr-171 may be promoted
by APLP1. Phosphorylation increases binding to RNA (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AABR03000812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03000839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001099746.1; NM_001106276.1.
UniGene; Rn.224485; -.
ProteinModelPortal; P0C279; -.
SMR; P0C279; -.
STRING; 10116.ENSRNOP00000026009; -.
iPTMnet; P0C279; -.
PhosphoSitePlus; P0C279; -.
PaxDb; P0C279; -.
PRIDE; P0C279; -.
Ensembl; ENSRNOT00000026009; ENSRNOP00000026009; ENSRNOG00000019161.
GeneID; 293056; -.
KEGG; rno:293056; -.
UCSC; RGD:1310421; rat.
CTD; 64506; -.
RGD; 1310421; Cpeb1.
eggNOG; ENOG410KDT8; Eukaryota.
eggNOG; ENOG410YBXF; LUCA.
GeneTree; ENSGT00390000012886; -.
HOGENOM; HOG000290661; -.
HOVERGEN; HBG079080; -.
InParanoid; P0C279; -.
KO; K02602; -.
PhylomeDB; P0C279; -.
TreeFam; TF317658; -.
PRO; PR:P0C279; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000019161; -.
ExpressionAtlas; P0C279; baseline and differential.
Genevisible; P0C279; RN.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005813; C:centrosome; IDA:RGD.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; IDA:RGD.
GO; GO:0072687; C:meiotic spindle; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:RGD.
GO; GO:0003729; F:mRNA binding; ISO:RGD.
GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; ISO:RGD.
GO; GO:0008135; F:translation factor activity, RNA binding; IBA:GO_Central.
GO; GO:0000900; F:translation repressor activity, nucleic acid binding; ISS:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; IMP:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:RGD.
GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISS:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IMP:RGD.
GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:RGD.
GO; GO:0006417; P:regulation of translation; ISO:RGD.
GO; GO:0007130; P:synaptonemal complex assembly; ISO:RGD.
CDD; cd12723; RRM1_CPEB1; 1.
InterPro; IPR032292; CEBP1_N.
InterPro; IPR032296; CEBP_ZZ.
InterPro; IPR034819; CPEB.
InterPro; IPR034977; CPEB1_RRM1.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR12566; PTHR12566; 1.
Pfam; PF16368; CEBP1_N; 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; Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Membrane; Metal-binding; mRNA processing; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Repeat; Repressor;
Ribonucleoprotein; RNA-binding; Synapse; Translation regulation; Zinc.
CHAIN 1 561 Cytoplasmic polyadenylation element-
binding protein 1.
/FTId=PRO_0000269254.
DOMAIN 310 407 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 429 510 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 329 561 Necessary for stress granule assembly and
correct localization in dcp1 bodies.
{ECO:0000250}.
METAL 514 514 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 517 517 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 526 526 Zinc 2. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 531 531 Zinc 2. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 536 536 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 539 539 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 544 544 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:Q9BZB8}.
METAL 552 552 Zinc 2; via pros nitrogen.
{ECO:0000250|UniProtKB:Q9BZB8}.
SITE 410 410 Important for the positionning of RRM1
relative to RRM2.
{ECO:0000250|UniProtKB:Q9BZB8}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BZB8}.
MOD_RES 171 171 Phosphothreonine; by AURKA and CAMK2A.
{ECO:0000250|UniProtKB:P70166}.
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


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