CPEB2_MOUSE
ID CPEB2_MOUSE Reviewed; 521 AA.
AC Q812E0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 2;
DE Short=CPE-BP2;
DE Short=CPE-binding protein 2;
DE Short=mCPEB-2;
GN Name=Cpeb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], RNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12672660; DOI=10.1095/biolreprod.103.015677;
RA Kurihara Y., Tokuriki M., Myojin R., Hori T., Kuroiwa A., Matsuda Y.,
RA Sakurai T., Kimura M., Hecht N.B., Uesugi S.;
RT "CPEB2, a novel putative translational regulator in mouse haploid germ
RT cells.";
RL Biol. Reprod. 69:261-268(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY, AND ABSENCE OF INDUCTION.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12871996; DOI=10.1073/pnas.1133424100;
RA Theis M., Si K., Kandel E.R.;
RT "Two previously undescribed members of the mouse CPEB family of genes and
RT their inducible expression in the principal cell layers of the
RT hippocampus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9602-9607(2003).
RN [4]
RP INTERACTION WITH TENT2.
RX PubMed=17927953; DOI=10.1016/j.bbrc.2007.09.096;
RA Nakanishi T., Kumagai S., Kimura M., Watanabe H., Sakurai T., Kimura M.,
RA Kashiwabara S., Baba T.;
RT "Disruption of mouse poly(A) polymerase mGLD-2 does not alter
RT polyadenylation status in oocytes and somatic cells.";
RL Biochem. Biophys. Res. Commun. 364:14-19(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May play a role in translational regulation of stored mRNAs
CC in transcriptionally inactive haploid spermatids. Binds to poly(U) RNA
CC oligomers (PubMed:12672660). Required for cell cycle progression,
CC specifically for the transition from metaphase to anaphase (By
CC similarity). {ECO:0000250|UniProtKB:Q7Z5Q1,
CC ECO:0000269|PubMed:12672660}.
CC -!- SUBUNIT: Interacts with TENT2/GLD2. {ECO:0000269|PubMed:17927953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12672660}.
CC -!- TISSUE SPECIFICITY: Expressed in embryo, cerebellum, salivary gland,
CC thymus, heart, liver, lung, spleen, kidney, intestine, ovary and round
CC spermatids. Weakly expressed in granular cells of dentate gyrus and the
CC pyramidal cells of CA3 and CA1 of the hippocampus.
CC {ECO:0000269|PubMed:12672660, ECO:0000269|PubMed:12871996}.
CC -!- INDUCTION: Not induced by kainate. {ECO:0000269|PubMed:12871996}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
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DR EMBL; AB100307; BAC57076.1; -; mRNA.
DR EMBL; BC107349; AAI07350.1; -; mRNA.
DR EMBL; BC107350; AAI07351.1; -; mRNA.
DR AlphaFoldDB; Q812E0; -.
DR SMR; Q812E0; -.
DR STRING; 10090.ENSMUSP00000130921; -.
DR iPTMnet; Q812E0; -.
DR PhosphoSitePlus; Q812E0; -.
DR MaxQB; Q812E0; -.
DR PRIDE; Q812E0; -.
DR ProteomicsDB; 284156; -.
DR MGI; MGI:2442640; Cpeb2.
DR eggNOG; KOG0129; Eukaryota.
DR HOGENOM; CLU_014948_2_0_1; -.
DR InParanoid; Q812E0; -.
DR PhylomeDB; Q812E0; -.
DR ChiTaRS; Cpeb2; mouse.
DR PRO; PR:Q812E0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q812E0; protein.
DR Genevisible; Q812E0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; IDA:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005095; F:GTPase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IDA:UniProtKB.
DR GO; GO:0008187; F:poly-pyrimidine tract binding; IDA:MGI.
DR GO; GO:0043023; F:ribosomal large subunit binding; ISS:UniProtKB.
DR GO; GO:0043024; F:ribosomal small subunit binding; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, RNA binding; IBA:GO_Central.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IDA:UniProtKB.
DR GO; GO:1900248; P:negative regulation of cytoplasmic translational elongation; ISS:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0045900; P:negative regulation of translational elongation; IGI:MGI.
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; 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 Cytoplasm; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Translation regulation.
FT CHAIN 1..521
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 2"
FT /id="PRO_0000269260"
FT DOMAIN 264..355
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 372..454
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 521 AA; 58442 MW; 88B0D73942770A17 CRC64;
MNLPQQQPPA AAPQQPQSRR SPVSPQLQQQ HQAAAAAFLQ QRNSYNHHQP LLKQSPWSNH
QNSGWGTASM SWGAMHGRDH RRSGNMGIPG TMNQISPLKK PFSGNVIAPP KFTRSTPSLT
PKSWIEDNVF RTDNNSNTLL PLQVRSSLQL PAWGSDSLQD SWCTAAGTSR IDQDRSRMYD
SLNMHSLENS LIDIMRAEHD PLKGRLSYPH PGTDNLLMLN GRSSLFPIDD SLLDDGHSDQ
VGVLNSPTCY SAHQNGERIE RFSRKVFVGG LPPDIDEDEI TASFRRFGPL VVDWPHKAES
KSYFPPKGYA FLLFQEESSV QALIDACIEE DGKLYLCVSS PTIKDKPVQI RPWNLSDSDF
VMDGSQPLDP RKTIFVGGVP RPLRAVELAM IMDRLYGGVC YAGIDTDPEL KYPKGAGRVA
FSNQQSYIAA ISARFVQLQH GDIDKRVEVK PYVLDDQMCD ECQGARCGGK FAPFFCANVT
CLQYYCEFCW ANIHSRAGRE FHKPLVKEGA DRPRQIHFRW N
