CPEB1_CARAU
ID CPEB1_CARAU Reviewed; 559 AA.
AC Q9DED5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 1;
DE Short=CPE-BP1;
DE Short=CPE-binding protein 1;
DE Short=CPEB-1;
GN Name=cpeb1; Synonyms=cpeb;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Katsu Y., Yamashita M., Ogawa K., Nagahama Y.;
RT "Goldfish cytoplasmic polyadenylation element binding protein (CPEB): its
RT interaction with CPE of cyclin B mRNA and phosphorylation by cdk and Eg2
RT protein kinases.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sequence-specific RNA-binding protein that regulates mRNA
CC cytoplasmic polyadenylation and translation initiation during oocyte
CC maturation and early development. Binds to the cytoplasmic
CC polyadenylation element (CPE), an uridine-rich sequence element
CC (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR (By
CC similarity). {ECO:0000250}.
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}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
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DR EMBL; AB044534; BAB19051.1; -; mRNA.
DR AlphaFoldDB; Q9DED5; -.
DR SMR; Q9DED5; -.
DR Proteomes; UP000515129; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0000900; F:mRNA regulatory element binding translation repressor activity; ISS:UniProtKB.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISS:UniProtKB.
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; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; mRNA processing; Reference proteome; Repeat;
KW RNA-binding; Translation regulation; Zinc.
FT CHAIN 1..559
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 1"
FT /id="PRO_0000269256"
FT DOMAIN 304..401
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 423..504
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 223..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 511
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 533
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 538
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 546
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 559 AA; 62123 MW; 05507CE5D1568144 CRC64;
MAFSLSENPR LLNCLDSDIP ALSTCSNADT FSRMNTMLGN SLDLSGVCTT PTAKCKRDPF
NGRPDSDLSA VRSRMLFLSG GQDSSRGLPD VSNWGLGLQS LSLSDWERPW SSHDSDPSAQ
TNTASLHGIL GTPSHLSNRL PSYSEPSIGA TDFLERFPGM ARLNSQSFLD SHSISPVDSE
TSGFSSGSDH LSDLLSSLRI SPSVPFLMSS MQRDPLKLAL GSRLDHSSSP LTPPPSATSS
GGLSHRWPGA SIWPNWDLMK TPESPFSIER EAWLHRQAAS INEATFTWSG QLPPRHYQNP
IYSCKVFLGG VPWDITEAGL INTFKCYGPL SVEWPGKDGK HPRCPPKGNM PKGYVYLVFE
SDKSVRALLQ DCTEDLLHPE GYSEYYFKMS SRRMRCKDAQ VIPWVISDSN YVSCPSQRLD
PRNTVFVGAL HGMLNAEALA SIMNDLFGGV VYAGIDTDKH KYPIGSGRVT FNNQRSYLKA
VSAAFVEIKT PKFTKKVQID PYLEDAICQS CSREPGPFFC RDKTCFKYYC RSCWHRQHSM
DILSNHRPLM RNQKKRDVN
