CPEB4_DANRE
ID CPEB4_DANRE Reviewed; 635 AA.
AC Q7SXN4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 4;
DE Short=CPE-BP4;
DE Short=CPE-binding protein 4;
DE Short=CPEB-4;
GN Name=cpeb4; ORFNames=zgc:66166;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=SJD;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sequence-specific RNA-binding protein that binds to the
CC cytoplasmic polyadenylation element (CPE), an uridine-rich sequence
CC element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. RNA
CC binding results in a clear conformational change analogous to the Venus
CC fly trap mechanism. {ECO:0000250|UniProtKB:Q17RY0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7TN98}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:Q7TN98}. Cell projection,
CC dendritic spine {ECO:0000250|UniProtKB:Q7TN98}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q7TN98}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q7TN98}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q7TN98}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH55522.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC055522; AAH55522.1; ALT_INIT; mRNA.
DR RefSeq; NP_957275.1; NM_200981.1.
DR AlphaFoldDB; Q7SXN4; -.
DR BMRB; Q7SXN4; -.
DR SMR; Q7SXN4; -.
DR STRING; 7955.ENSDARP00000109818; -.
DR PaxDb; Q7SXN4; -.
DR GeneID; 393956; -.
DR KEGG; dre:393956; -.
DR CTD; 393956; -.
DR ZFIN; ZDB-GENE-040426-1557; cpeb4a.
DR eggNOG; KOG0129; Eukaryota.
DR InParanoid; Q7SXN4; -.
DR OrthoDB; 1075356at2759; -.
DR PRO; PR:Q7SXN4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
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:0036294; P:cellular response to decreased oxygen levels; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
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; 2.
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 2: Evidence at transcript level;
KW Cell projection; Cytoplasm; Endoplasmic reticulum; Reference proteome;
KW Repeat; RNA-binding; Synapse.
FT CHAIN 1..635
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 4"
FT /id="PRO_0000269266"
FT DOMAIN 378..469
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 486..568
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 70733 MW; 7D49E294200D94BF CRC64;
MQDDILESEM SKAPQLQQES QEGQDKQTLS PPGHQEPPGI ISELDNALPE ENQLEKGTME
NANGKETLRL ESPVLSGFDY QETTGIGTLA QSSSSSSSSL TGFSSWSTAM PPNPSTLIEE
VGFFNQAATT NNAPPPLLFQ SFSHHTSTGF GGNFSHQIGP LSQHHPSPHP HFQHPHNQHR
RSSASPHPPP FSHRSAAFNQ LPHLGNNLSK PPSPWGSYQS PSSTPSSTSW SPGGGYGGWG
SSQGREYRRG GVNPLNSISP LKKSFPNNQT QTQKYPRNNS GFNTKPWVED TINRNESIFP
FQERSRSFDG FSMHSLENSL IDIMRAEQDS LKGHSSLFPM EDERSYGEDE RSDQSLSGLG
SPHSFPHQNG ERIERYSRKV FVGGLPPDID EDEITASFRR FGHLFVDWPH KAESKSYFPP
KGYAFLLFQD ESSVQALIDA CMEEDGKLYL CVSSPTIKDK PVQIRPWNLN DSDFVMDGSQ
PLDPRKTIFV GGVPRPLRAV ELAMIMDRLY GGVCYAGIDT DPELKYPKGA GRVAFSNQQS
YIAAISARFV QLQHGEIDKR VEVKPYVLDD QLCDECQGTR CGGKFAPFFC ANVTCLQYYC
EYCWAAIHSR AGREFHKPLV KEGGDRPRHI SFRWN
