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Cytoplasmic polyadenylation element-binding protein 4 (CPE-BP4) (CPE-binding protein 4) (mCPEB-4)

 CPEB4_MOUSE             Reviewed;         729 AA.
Q7TN98; A6H6G0; Q69ZD7;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
25-OCT-2017, entry version 103.
RecName: Full=Cytoplasmic polyadenylation element-binding protein 4;
Short=CPE-BP4;
Short=CPE-binding protein 4;
Short=mCPEB-4;
Name=Cpeb4; Synonyms=Kiaa1673;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), ALTERNATIVE
SPLICING, INDUCTION, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=12871996; DOI=10.1073/pnas.1133424100;
Theis M., Si K., Kandel E.R.;
"Two previously undescribed members of the mouse CPEB family of genes
and their inducible expression in the principal cell layers of the
hippocampus.";
Proc. Natl. Acad. Sci. U.S.A. 100:9602-9607(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Brain;
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17024188; DOI=10.1038/sj.emboj.7601322;
Huang Y.S., Kan M.C., Lin C.L., Richter J.D.;
"CPEB3 and CPEB4 in neurons: analysis of RNA-binding specificity and
translational control of AMPA receptor GluR2 mRNA.";
EMBO J. 25:4865-4876(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-99, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
FUNCTION.
PubMed=22138752; DOI=10.1038/nm.2540;
Ortiz-Zapater E., Pineda D., Martinez-Bosch N., Fernandez-Miranda G.,
Iglesias M., Alameda F., Moreno M., Eliscovich C., Eyras E.,
Real F.X., Mendez R., Navarro P.;
"Key contribution of CPEB4-mediated translational control to cancer
progression.";
Nat. Med. 18:83-90(2011).
[8]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=24386439; DOI=10.1371/journal.pone.0084978;
Tsai L.Y., Chang Y.W., Lin P.Y., Chou H.J., Liu T.J., Lee P.T.,
Huang W.H., Tsou Y.L., Huang Y.S.;
"CPEB4 knockout mice exhibit normal hippocampus-related synaptic
plasticity and memory.";
PLoS ONE 8:E84978-E84978(2013).
[9]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=27381259; DOI=10.1038/srep29395;
Shin J., Salameh J.S., Richter J.D.;
"Impaired neurodevelopment by the low complexity domain of CPEB4
reveals a convergent pathway with neurodegeneration.";
Sci. Rep. 6:29395-29395(2016).
[10]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY ER
STRESS, AND DISRUPTION PHENOTYPE.
PubMed=28092655; DOI=10.1038/ncb3461;
Maillo C., Martin J., Sebastian D., Hernandez-Alvarez M.,
Garcia-Rocha M., Reina O., Zorzano A., Fernandez M., Mendez R.;
"Circadian- and UPR-dependent control of CPEB4 mediates a
translational response to counteract hepatic steatosis under ER
stress.";
Nat. Cell Biol. 19:94-105(2017).
-!- FUNCTION: Sequence-specific RNA-binding protein that binds to the
cytoplasmic polyadenylation element (CPE), an uridine-rich
sequence element (consensus sequence 5'-UUUUUAU-3') within the
mRNA 3'-UTR (PubMed:17024188). RNA binding results in a clear
conformational change analogous to the Venus fly trap mechanism
(By similarity). Regulates activation of unfolded protein response
(UPR) in the process of adaptation to ER stress in liver, by
maintaining translation of CPE-regulated mRNAs in conditions in
which global protein synthesis is inhibited (PubMed:28092655).
Required for cell cycle progression, specifically for cytokinesis
and chromosomal segregation (By similarity). Plays a role as an
oncogene promoting tumor growth and progression by positively
regulating translation of t-plasminogen activator/PLAT
(PubMed:22138752). Stimulates proliferation of melanocytes (By
similarity). In contrast to CPEB1 and CPEB3, does not play role in
synaptic plasticity, learning and memory (PubMed:24386439).
{ECO:0000250|UniProtKB:Q17RY0, ECO:0000269|PubMed:17024188,
ECO:0000269|PubMed:22138752, ECO:0000269|PubMed:24386439,
ECO:0000269|PubMed:28092655}.
-!- SUBUNIT: Interacts with TOB1. {ECO:0000250|UniProtKB:Q17RY0}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27381259}.
Cell projection, dendrite {ECO:0000269|PubMed:17024188,
ECO:0000269|PubMed:24386439}. Cell projection, dendritic spine
{ECO:0000269|PubMed:24386439}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000269|PubMed:17024188}. Cell projection, axon
{ECO:0000269|PubMed:27381259}. Cell projection, growth cone
{ECO:0000269|PubMed:27381259}. Endoplasmic reticulum
{ECO:0000269|PubMed:28092655}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:28092655}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=mCPEB-4a;
IsoId=Q7TN98-1; Sequence=Displayed;
Name=2; Synonyms=mCPEB-4b;
IsoId=Q7TN98-2; Sequence=VSP_022046;
Name=3; Synonyms=mCPEB-4c;
IsoId=Q7TN98-3; Sequence=VSP_022044;
Name=4; Synonyms=mCPEB-4d;
IsoId=Q7TN98-4; Sequence=VSP_022043;
Name=5;
IsoId=Q7TN98-5; Sequence=VSP_022045;
-!- TISSUE SPECIFICITY: Highly expressed in brain, including
hippocampus, amygdala, granule and Purkinje cells of the
cerebellum (at protein level) (PubMed:17024188, PubMed:24386439).
Expressed in spinal cord (at protein level) (PubMed:27381259).
Expressed in kidney, lung and heart (at protein level)
(PubMed:12871996, PubMed:27381259, PubMed:24386439). Expressed in
liver (at protein level) (PubMed:28092655, PubMed:12871996,
PubMed:27381259, PubMed:24386439). Expressed in spleen and testis
(at protein level) (PubMed:24386439, PubMed:12871996). Weakly
expressed in ovary and in granular cells of dentate gyrus and the
pyramidal cells of CA3 and CA1 of the hippocampus
(PubMed:12871996). {ECO:0000269|PubMed:12871996,
ECO:0000269|PubMed:17024188, ECO:0000269|PubMed:24386439,
ECO:0000269|PubMed:27381259, ECO:0000269|PubMed:28092655}.
-!- DEVELOPMENTAL STAGE: Highly expressed in developing brain, spinal
cord and attached dorsal root ganglia (DRG) (at protein level). At
embryonic day 18.5 expressed in gray matter of spinal cord,
diencephalons, hippocampus and parts of midbrain and hindbrain. At
postnatal day 20 expression persists in spinal cord and brain.
Expressed in embryonic heart. {ECO:0000269|PubMed:27381259}.
-!- INDUCTION: Up-regulated in granular cells of the dentate gyrus of
CA1 and CA3 after kainate-induced seizures (PubMed:12871996). Up-
regulated by high-fat-diet and aging-induced endoplasmic reticulum
stress (PubMed:28092655). Expression level fluctuation follows the
circadian clock amplitude (PubMed:28092655).
{ECO:0000269|PubMed:12871996, ECO:0000269|PubMed:28092655}.
-!- DOMAIN: The 2 RRM domains and the C-terminal region mediate
interaction with CPE-containing RNA. The interdomain linker (564-
579) 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.
Unlike in CPEB1, a continuous polar interface is formed between
the 2 RRMs. {ECO:0000250|UniProtKB:Q17RY0,
ECO:0000250|UniProtKB:Q9BZB8}.
-!- DISRUPTION PHENOTYPE: No visible phenotype at young age or under
unchallenged conditions (PubMed:24386439, PubMed:28092655). At 80
weeks or under high fat diet feeding conditions, mutant mice
develop hepatosteatosis with excessive liver weight and
accumulation of cytosolic lipid droplets sometimes accompanied by
fibrosis (PubMed:28092655). {ECO:0000269|PubMed:24386439,
ECO:0000269|PubMed:28092655}.
-!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY313775; AAQ20844.1; -; mRNA.
EMBL; AK173229; BAD32507.1; -; mRNA.
EMBL; BC115430; AAI15431.1; -; mRNA.
EMBL; BC115431; AAI15432.1; -; mRNA.
EMBL; BC145863; AAI45864.1; -; mRNA.
EMBL; BC145865; AAI45866.1; -; mRNA.
CCDS; CCDS24514.1; -. [Q7TN98-1]
RefSeq; NP_001277607.1; NM_001290678.1. [Q7TN98-5]
RefSeq; NP_080528.2; NM_026252.4. [Q7TN98-1]
UniGene; Mm.339792; -.
ProteinModelPortal; Q7TN98; -.
SMR; Q7TN98; -.
STRING; 10090.ENSMUSP00000020543; -.
iPTMnet; Q7TN98; -.
PhosphoSitePlus; Q7TN98; -.
PaxDb; Q7TN98; -.
PRIDE; Q7TN98; -.
Ensembl; ENSMUST00000020543; ENSMUSP00000020543; ENSMUSG00000020300. [Q7TN98-1]
GeneID; 67579; -.
KEGG; mmu:67579; -.
UCSC; uc007iir.2; mouse. [Q7TN98-2]
UCSC; uc007iis.2; mouse. [Q7TN98-5]
UCSC; uc007iit.2; mouse. [Q7TN98-1]
CTD; 80315; -.
MGI; MGI:1914829; Cpeb4.
eggNOG; KOG0129; Eukaryota.
eggNOG; ENOG410Y1XZ; LUCA.
GeneTree; ENSGT00390000012886; -.
HOGENOM; HOG000290660; -.
HOVERGEN; HBG058010; -.
InParanoid; Q7TN98; -.
KO; K02602; -.
OMA; TGFNNWS; -.
OrthoDB; EOG091G0AO9; -.
PhylomeDB; Q7TN98; -.
TreeFam; TF317658; -.
PRO; PR:Q7TN98; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020300; -.
ExpressionAtlas; Q7TN98; baseline and differential.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:MGI.
GO; GO:0008135; F:translation factor activity, RNA binding; IBA:GO_Central.
GO; GO:0000900; F:translation repressor activity, nucleic acid binding; IBA:GO_Central.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
GO; GO:0036294; P:cellular response to decreased oxygen levels; ISS:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
GO; GO:2000766; P:negative regulation of cytoplasmic translation; IBA:GO_Central.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0002931; P:response to ischemia; IDA:UniProtKB.
InterPro; IPR032296; CEBP_ZZ.
InterPro; IPR034819; CPEB.
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.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Endoplasmic reticulum; Membrane;
Metal-binding; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Repeat; RNA-binding; Synapse; Zinc.
CHAIN 1 729 Cytoplasmic polyadenylation element-
binding protein 4.
/FTId=PRO_0000269265.
DOMAIN 472 563 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 580 662 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 1 375 Low complexity region.
{ECO:0000303|PubMed:27381259}.
REGION 541 543 RNA-binding.
{ECO:0000250|UniProtKB:Q17RY0}.
COMPBIAS 232 246 His-rich.
COMPBIAS 302 310 Poly-Gly.
METAL 667 667 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 675 675 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 684 684 Zinc 2. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 689 689 Zinc 2. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 694 694 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 697 697 Zinc 1. {ECO:0000250|UniProtKB:Q9BZB8}.
METAL 702 702 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:Q9BZB8}.
METAL 710 710 Zinc 2; via pros nitrogen.
{ECO:0000250|UniProtKB:Q9BZB8}.
SITE 473 473 RNA-binding.
{ECO:0000250|UniProtKB:Q17RY0}.
SITE 561 561 Important for the positionning of RRM1
relative to RRM2.
{ECO:0000250|UniProtKB:Q17RY0}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000250|UniProtKB:Q17RY0}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000250|UniProtKB:Q17RY0}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000250|UniProtKB:Q17RY0}.
MOD_RES 326 326 Phosphothreonine.
{ECO:0000250|UniProtKB:Q17RY0}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000250|UniProtKB:Q17RY0}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000250|UniProtKB:Q17RY0}.
VAR_SEQ 402 427 Missing (in isoform 4).
{ECO:0000303|PubMed:12871996}.
/FTId=VSP_022043.
VAR_SEQ 402 419 Missing (in isoform 3).
{ECO:0000303|PubMed:12871996}.
/FTId=VSP_022044.
VAR_SEQ 404 428 Missing (in isoform 5).
{ECO:0000303|PubMed:15368895,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_022045.
VAR_SEQ 420 427 Missing (in isoform 2).
{ECO:0000303|PubMed:12871996}.
/FTId=VSP_022046.
SEQUENCE 729 AA; 80122 MW; 7CB042EDE4B7C0CA CRC64;
MGDYGFGVLV QSNTGNKSAF PVRFHPHLQP PHHHQNATPN PAAFINNNTA ANGSSAGSAW
LFPAPATHNI QDEILGSEKA KSQQQEQQDP LEKQQLSPSP GQEAGILPET EKAKAEENPG
DSSSENSNGK EKLRIESPVL TGFDYQEATG LGTSTQPLTS SASSLTGFSN WSAAIAPSSS
TIINEDASFF HQGGVPGASA NNGALLFQNF PHHVSPGFGG SFSPQIGPLS QHHPHHPHFQ
HHHSQHQQQR RSPASPHPPP FTHRSAAFNQ LPHLANNLNK PPSPWSSYQS PSPTPSSSWS
PGGGGYGGWG ASQGRDHRRG LNGGITPLNS ISPLKKNFAS NHIQLQKYAR PSSAFAPKSW
MEDSLNRADN IFPFPERPRT FDMHSLESSL IDIMRAENDS IKGRLNYSYP GSDSSLLINA
RTYGRRRGQS SLFPMEDGFL DDGRGDQPLH SGLGSPHCFT HQNGERVERY SRKVFVGGLP
PDIDEDEITA SFRRFGPLIV DWPHKAESKS YFPPKGYAFL LFQDESSVQA LIDACIEEDG
KLYLCVSSPT IKDKPVQIRP WNLSDSDFVM DGSQPLDPRK TIFVGGVPRP LRAVELAMIM
DRLYGGVCYA GIDTDPELKY PKGAGRVAFS NQQSYIAAIS ARFVQLQHGE IDKRVEVKPY
VLDDQLCDEC QGARCGGKFA PFFCANVTCL QYYCEYCWAA IHSRAGREFH KPLVKEGGDR
PRHISFRWN


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