CPEB1_DANRE
ID CPEB1_DANRE Reviewed; 559 AA.
AC Q9YGX5; O93386;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cytoplasmic polyadenylation element-binding protein 1;
DE Short=CPE-BP1;
DE Short=CPE-binding protein 1;
DE Short=CPEB-1;
DE AltName: Full=Orb/CPEB-related RNA-binding protein;
DE AltName: Full=Protein Zorba;
DE AltName: Full=ZOR-1;
DE AltName: Full=Zebrafish orb-type a;
GN Name=cpeb1; Synonyms=zor1, zorba;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Blastula;
RX PubMed=9784598; DOI=10.1016/s0925-4773(98)00109-9;
RA Bally-Cuifu L., Schatz W.J., Ho R.K.;
RT "Characterization of the zebrafish Orb/CPEB-related RNA-binding protein and
RT localization of maternal components in the zebrafish oocyte.";
RL Mech. Dev. 77:31-47(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Suzuki H., Maegawa S., Murakawa M., Hoshijima K., Shimura Y., Yasuda K.,
RA Inoue K.;
RT "Identification of zebrafish maternal RNA-binding proteins, ZOR-1 and -2.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9784598}.
CC Note=Microtubule-associated.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes (at protein level). During
CC oocyte maturation becomes detectable at stage Ib, and remains
CC ubiquitously distributed within the oocyte cytoplasm until stage II. It
CC then follows a gradual accumulation to the future animal pole during
CC stage III, and remains localized to this pole at stage IV (at protein
CC level). Expressed in oocytes, blastomeres and pre-mid-blastula
CC transition embryos. Its expression during oogenesis is ubiquitous at
CC stages I and II, but gradually accumulated at the periphery of the
CC oocyte in the presumptive animal pole during stage III. Expression was
CC maintained in that region at stage IV, and then became delocalized at
CC stage V to cover a much broader area presumably encompassing the future
CC blastodisc. {ECO:0000269|PubMed:9784598}.
CC -!- SIMILARITY: Belongs to the RRM CPEB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC96114.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF076918; AAC96114.1; ALT_FRAME; mRNA.
DR EMBL; AB011680; BAA75637.1; -; mRNA.
DR EMBL; BC045467; AAH45467.1; -; mRNA.
DR RefSeq; NP_571502.2; NM_131427.2.
DR AlphaFoldDB; Q9YGX5; -.
DR SMR; Q9YGX5; -.
DR STRING; 7955.ENSDARP00000109570; -.
DR PaxDb; Q9YGX5; -.
DR DNASU; 30702; -.
DR Ensembl; ENSDART00000098904; ENSDARP00000089674; ENSDARG00000008454.
DR GeneID; 30702; -.
DR KEGG; dre:30702; -.
DR CTD; 30702; -.
DR ZFIN; ZDB-GENE-990927-1; cpeb1b.
DR eggNOG; KOG0129; Eukaryota.
DR GeneTree; ENSGT00940000155524; -.
DR HOGENOM; CLU_014948_1_1_1; -.
DR InParanoid; Q9YGX5; -.
DR OMA; NCYGPLS; -.
DR OrthoDB; 1075356at2759; -.
DR PhylomeDB; Q9YGX5; -.
DR TreeFam; TF317658; -.
DR PRO; PR:Q9YGX5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000008454; Expressed in mature ovarian follicle and 30 other tissues.
DR ExpressionAtlas; Q9YGX5; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0032991; C:protein-containing complex; IPI:ZFIN.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
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:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IPI:ZFIN.
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: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 1: Evidence at protein 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_0000269255"
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 222..243
FT /note="Disordered"
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"
FT CONFLICT 18
FT /note="D -> E (in Ref. 1; AAC96114)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="S -> I (in Ref. 1; AAC96114)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="W -> R (in Ref. 1; AAC96114)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="Y -> C (in Ref. 1; AAC96114)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 62255 MW; 36CF42E1AC70A377 CRC64;
MAFSLRENPR LLNCLDSDIP ALSTCSNADA FCRMNTMLGN SLDLSGVCTT PTAKCKRDPF
NDRPDSDLSA VRSRMLFPSG GQDSSRGLPD VNNWGLGLQS LSLSDWERPW SSHDTDPSVK
TNTASLQGIL GTPSQLTNKL SNYSDSSIGA TDFLEKFPGM ARLNSQSFLD SHSISPVDSE
TSGFSSGSDH LSDLLSSLRI SPSVPFLMSS MQRDPLKLAL DSRMDHSSSP LTPPPSASPS
GSLSHRWPGA SIWPSWDLMK TPESPFSIER EAWLHRQAAS INEATFTWSG QLPPRHYQNP
VYSCKVFLGG VPWDITEAGL INTFKCYGPL SVEWPGKDGK HPRCPPKGNM PKGYVYLVFE
SDKSVRALLQ DCTEDLLHPE GYSEYYFKMS SRRMRCKDAQ VIPWVISDSN YVSCPSQRLD
PRNTVFVGAL HGMLNAEALA SIMNDLFGGV VYAGIDTDKH KYPIGSGRVT FNNQRSYLKA
VSAAFVEIKT PKFTKKVQID PYLEDAICQS CSREPGPFFC RDKTCFKYYC RSCWHRQHSM
DILSNHRPLM RNQKKRDAN
