CPE1B_XENLA
ID CPE1B_XENLA Reviewed; 568 AA.
AC Q52KN7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 1-B;
DE Short=CPE-BP1-B;
DE Short=CPE-binding protein 1-B;
DE Short=CPEB-1-B;
GN Name=cpeb1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2005) 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. In the
CC absence of phosphorylation and in association with tacc3/maskin, also
CC acts as a repressor of translation of CPE-containing mRNA; a repression
CC that is relieved by phosphorylation or degradation. Requires zinc for
CC RNA binding. Involved in the cell cycle progression from S phase into M
CC phase (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a complex with cpeb1, tacc3/maskin and eif4e;
CC dissolution of this complex results in the binding of eif4e to eif4g
CC and the translational activation of CPE-containing mRNAs. Found in a
CC complex with cpeb1, cpsf1, the cytoplasmic poly(A) polymerase
CC papd4/gld2 and sympk. Found in a mRNP complex with cpeb1, a guanine
CC exchange factor xgef and mos mRNA. Interacts with cpsf1, papd4/gld2,
CC tacc3/maskin, microtubules, sympk and xgef. Component of a
CC ribonucleoprotein (RNP) complex, at least composed of cpeb1,
CC lsm14b/rap55b, ddx6/Xp54, ybx2/frgy2, pat1/P100, eif4enif1/4E-T and
CC eif4e1b. Interaction with ybx2/frgy2 is RNA-dependent. May interact
CC with aplp1. Interaction with cpsf1 increases during meiotic maturation
CC and is not mediated through RNA. Interaction with xgef is necessary for
CC its early activating phosphorylation status (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Membrane
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}.
CC Note=During mitosis localizes with tacc3/maskin and CPE-containing
CC mRNAs to both spindle poles. Membrane-associated. Colocalizes with
CC members of the polyadenylation and translation complex factors (cpsf,
CC aplp1, tacc3/maskin, aurka, etc.), including CPE-containing RNAs (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The 2 RRM domains and the C-terminal region mediate interaction
CC with CPE-containing RNA. {ECO:0000250}.
CC -!- PTM: Ser-174 phosphorylation by aurka in immature oocytes is essential
CC to trigger CPE-containing mRNA cytoplasmic polyadenylation and
CC translation activation and the subsequent signaling events that result
CC in meiotic progression. Ser-174 phosphorylation recruits the cleavage
CC and polyadenylation specificity factor (cpsf1) into an active
CC cytoplasmic polyadenylation complex. Ser-174 phosphorylation increases
CC its affinity for cpsf1 and papd4/gld2. Heavily phosphorylated by CDK1
CC on serines late during oocyte maturation. Ser-210 phosphorylation is
CC sufficient to target cpeb1 for degradation. Ser-174 phosphorylation
CC oscillates with the cell cycle (phosphorylated at M phase, but not at S
CC phase) and is necessary for S phase to M phase progression.
CC Phosphorylation at Ser-174 may be promoted by aplp1 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Requires a PEST box and the proteasome pathway for
CC destruction during oocyte maturation. Ser-210 phosphorylation triggers
CC its destruction, an event important to allow the transition from
CC metaphase I to metaphase II and cytokinesis in the early embryo (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
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DR EMBL; BC094261; AAH94261.1; -; mRNA.
DR RefSeq; NP_001089420.1; NM_001095951.1.
DR AlphaFoldDB; Q52KN7; -.
DR SMR; Q52KN7; -.
DR iPTMnet; Q52KN7; -.
DR MaxQB; Q52KN7; -.
DR DNASU; 734470; -.
DR GeneID; 734470; -.
DR KEGG; xla:734470; -.
DR CTD; 734470; -.
DR Xenbase; XB-GENE-6256188; cpeb1.S.
DR OMA; NCYGPLS; -.
DR OrthoDB; 1075356at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 734470; Expressed in egg cell and 16 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
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 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; 2.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; Cytoskeleton; Membrane; Metal-binding;
KW mRNA processing; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Ribonucleoprotein; RNA-binding; Translation regulation; Ubl conjugation;
KW Zinc.
FT CHAIN 1..568
FT /note="Cytoplasmic polyadenylation element-binding protein
FT 1-B"
FT /id="PRO_0000269258"
FT DOMAIN 313..410
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 432..513
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 172..175
FT /note="Necessary for interaction with microtubules and
FT localization at the mitotic apparatus"
FT /evidence="ECO:0000250"
FT REGION 181..208
FT /note="Necessary for degradation by the proteasome"
FT /evidence="ECO:0000250"
FT REGION 182..191
FT /note="Necessary for interaction with microtubules and
FT localization at the mitotic apparatus"
FT /evidence="ECO:0000250"
FT BINDING 517
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="1"
FT /evidence="ECO:0000250"
FT BINDING 529
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 534
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 138
FT /note="Phosphoserine; by cdk1"
FT /evidence="ECO:0000250"
FT MOD_RES 174
FT /note="Phosphoserine; by aurka"
FT /evidence="ECO:0000250"
FT MOD_RES 210
FT /note="Phosphoserine; by cdk1"
FT /evidence="ECO:0000250"
FT MOD_RES 248
FT /note="Phosphoserine; by cdk1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 568 AA; 62632 MW; 109829643720D8F2 CRC64;
MAFPLKDDLG RAKDCWGCSS DTPALSTCSN ADIFRRINAM LDNSLDFTGV CTTPNTKGKC
EHLQDYPDTE GAAASRMLFS TSHEPLPRGL PDTNDLCLGL QSLSLTGWDR PWSTQDSEAG
GQSSTPTAAQ SVFSMLNSPM GKPSPLGFLP LDPIGSDLVE KYPTHLLRSS RFDSRSILDS
RSSSPSDSDT SGFSSGSDHL SDLISSLRIS PPLPFLPLGS GISRDPLRLG VGSRLDQDHA
ALAAATASPL GITKRWPGTS VWPSWDLLDS ADDPFSIERE ARLHRQAAAV NEATCTWSGQ
LPPRNYKNPV YSCKVFLGGV PWDITETGLI NTFRVFGALS VEWPGKDGKH PRCPPKGNMP
KGYVYLVFES EKSVRALLQA CTQDLLSQDG LSEHYFKMSS RRMRCKEVQV IPWVLADSNF
VRSPSQRLDP SKTVFVGALH GMLNAEALAS IMNDLFGGVV YAGIDTDKHK YPIGSGRVTF
NNQRSYLKAV SAAFVEIKTA KFTKKVQIDP YLEDSVCQVC NAQPGPFFCR DQVCFKYFCR
SCWHWQHSME ILRHHRPLMR NQKSRDSS
