CEL1A_XENLA
ID CEL1A_XENLA Reviewed; 489 AA.
AC O57406;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=CUGBP Elav-like family member 1-A;
DE Short=CELF-1A;
DE AltName: Full=Bruno-like protein 2-A;
DE AltName: Full=CUG triplet repeat RNA-binding protein 1-A;
DE Short=CUG-BP1-A;
DE AltName: Full=CUG-BP- and ETR-3-like factor 1-A;
DE AltName: Full=Embryo deadenylation element-binding protein A;
DE Short=EDEN-BP-A;
DE AltName: Full=RNA-binding protein BRUNOL-2-A;
DE AltName: Full=p53/p55;
GN Name=cugbp1-a; Synonyms=celf1-a;
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 [MRNA], PROTEIN SEQUENCE OF 18-24; 167-176; 196-213 AND
RP 399-420, RNA-BINDING, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=9427761; DOI=10.1093/emboj/17.1.278;
RA Paillard L., Omilli F., Legagneux V., Bassez T., Maniey D., Osborne H.B.;
RT "EDEN and EDEN-BP, a cis element and an associated factor that mediate
RT sequence-specific mRNA deadenylation in Xenopus embryos.";
RL EMBO J. 17:278-287(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=9819376; DOI=10.1128/mcb.18.12.6879;
RA Audic Y., Omilli F., Osborne H.B.;
RT "Embryo deadenylation element-dependent deadenylation is enhanced by a cis
RT element containing AUU repeats.";
RL Mol. Cell. Biol. 18:6879-6884(1998).
RN [4]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=11707455; DOI=10.1074/jbc.m109362200;
RA Paillard L., Legagneux V., Maniey D., Osborne H.B.;
RT "c-Jun ARE targets mRNA deadenylation by an EDEN-BP (embryo deadenylation
RT element-binding protein)-dependent pathway.";
RL J. Biol. Chem. 277:3232-3235(2002).
RN [5]
RP RNA-BINDING.
RX PubMed=12409457; DOI=10.1093/nar/gkf586;
RA Bonnet-Corven S., Audic Y., Omilli F., Osborne H.B.;
RT "An analysis of the sequence requirements of EDEN-BP for specific RNA
RT binding.";
RL Nucleic Acids Res. 30:4667-4674(2002).
RN [6]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=12799066; DOI=10.1016/s0248-4900(03)00010-8;
RA Paillard L., Legagneux V., Beverley Osborne H.;
RT "A functional deadenylation assay identifies human CUG-BP as a
RT deadenylation factor.";
RL Biol. Cell 95:107-113(2003).
RN [7]
RP PHOSPHORYLATION.
RX PubMed=12746489; DOI=10.1242/jcs.00477;
RA Detivaud L., Pascreau G., Karaieskou A., Osborne H.B., Kubiak J.Z.;
RT "Regulation of EDEN-dependent deadenylation of Aurora A/Eg2-derived mRNA
RT via phosphorylation and dephosphorylation in Xenopus laevis egg extracts.";
RL J. Cell Sci. 116:2697-2705(2003).
RN [8]
RP FUNCTION, SUBUNIT, AND RNA-BINDING.
RX PubMed=16836486; DOI=10.1042/bc20060054;
RA Cosson B., Gautier-Courteille C., Maniey D., Aiet-Ahmed O., Lesimple M.,
RA Osborne H.B., Paillard L.;
RT "Oligomerization of EDEN-BP is required for specific mRNA deadenylation and
RT binding.";
RL Biol. Cell 98:653-665(2006).
RN [9]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=16938098; DOI=10.1042/bj20060490;
RA Marquis J., Paillard L., Audic Y., Cosson B., Danos O., Le Bec C.,
RA Osborne H.B.;
RT "CUG-BP1/CELF1 requires UGU-rich sequences for high-affinity binding.";
RL Biochem. J. 400:291-301(2006).
CC -!- FUNCTION: RNA-binding protein implicated in the regulation of several
CC post-transcriptional events. May be involved in pre-mRNA alternative
CC splicing, mRNA translation activation and stability (By similarity).
CC Mediates the rapid and sequence-specific cytoplasmic deadenylation of
CC EDEN-containing maternal mRNAs following fertilization. Binds to AU-
CC rich sequences (AREs) of jun mRNA. Binds to the embryonic deadenylation
CC element (EDEN) motif localized in the 3'-UTR of maternal mRNAs. Binds
CC to RNA containing several repeats of the consensus sequence 5'-UGU-3'.
CC EDEN-dependent deadenylation is enhanced by the presence of an
CC additional cis element composed of three AUU repeats. {ECO:0000250,
CC ECO:0000269|PubMed:11707455, ECO:0000269|PubMed:12799066,
CC ECO:0000269|PubMed:16836486, ECO:0000269|PubMed:16938098,
CC ECO:0000269|PubMed:9819376}.
CC -!- SUBUNIT: Oligomer. Oligomerization is required for RNA-binding and
CC EDEN-dependent deadenylation. {ECO:0000269|PubMed:16836486}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9427761}. Cytoplasm
CC {ECO:0000269|PubMed:9427761}.
CC -!- DEVELOPMENTAL STAGE: Expressed in egg and embryo (at protein level).
CC {ECO:0000269|PubMed:9427761}.
CC -!- DOMAIN: The 2 N-terminal RRMs and a part of the linker region (between
CC RRM2 and RRM3) are necessary for binding to EDEN of mos mRNA.
CC -!- PTM: Phosphorylated during oocyte maturation and dephosphorylated
CC following egg activation. Dephosphorylation is calcium dependent and
CC correlates with the increase in the activity of EDEN-dependent
CC deadenylation. {ECO:0000269|PubMed:12746489}.
CC -!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
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DR EMBL; AF003923; AAC41243.1; -; mRNA.
DR EMBL; BC108574; AAI08575.1; -; mRNA.
DR RefSeq; NP_001084196.1; NM_001090727.1.
DR AlphaFoldDB; O57406; -.
DR SMR; O57406; -.
DR PRIDE; O57406; -.
DR DNASU; 399360; -.
DR GeneID; 399360; -.
DR KEGG; xla:399360; -.
DR CTD; 399360; -.
DR Xenbase; XB-GENE-854043; celf1.L.
DR OrthoDB; 1209165at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 399360; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12631; RRM1_CELF1_2_Bruno; 1.
DR CDD; cd12634; RRM2_CELF1_2; 1.
DR CDD; cd12638; RRM3_CELF1_2; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR034196; CELF1/2_RRM1.
DR InterPro; IPR034198; CELF1/2_RRM2.
DR InterPro; IPR034199; CELF1/2_RRM3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Direct protein sequencing; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..489
FT /note="CUGBP Elav-like family member 1-A"
FT /id="PRO_0000295186"
FT DOMAIN 16..99
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 108..188
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 404..482
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 183..210
FT /note="Necessary for oligomerization and EDEN-dependent
FT deadenylation"
SQ SEQUENCE 489 AA; 52424 MW; E077504D3385DCC8 CRC64;
MNGTMDHPDH PDPDSIKMFV GQVPRSWSEK ELRELFEQYG AVYEINVLRD RSQNPPQSKG
CCFITFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE KNNAVEDRKL FIGMVSKNCN
ENDIRAMFSP FGQIEECRIL RGPDGMSRGC AFVTFTTRSM AQMAIKSMHQ AQTMEGCSSP
IVVKFADTQK DKEQKRMTQQ LQQQMQQLNA ASMWGNLTGL NSLAPQYLAL LQQTASSGNL
NSLSGLHPMG AEYGTGMTSG LNAIQLQNLA ALAAAASAAQ NTPSAGAALT SSSSPLSILT
SSGSSPSSNN SSINTMASLG ALQTLAGATA GLNVNSLAGM AAFNGGLGSS LSNGTGSTME
ALSQAYSGIQ QYAAAALPSL YNQSLLSQQG LGAAGSQKEG PEGANLFIYH LPQEFGDQDL
LQMFMPFGNV VSSKVFIDKQ TNLSKCFGFV SYDNPVSAQA AIQSMNGFQI GMKRLKVQLK
RSKNDSKPY
