CELF1_XENTR
ID CELF1_XENTR Reviewed; 490 AA.
AC Q28HE9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=CUGBP Elav-like family member 1;
DE Short=CELF-1;
DE AltName: Full=Bruno-like protein 2;
DE AltName: Full=CUG triplet repeat RNA-binding protein 1;
DE Short=CUG-BP1;
DE AltName: Full=CUG-BP- and ETR-3-like factor 1;
DE AltName: Full=RNA-binding protein BRUNOL-2;
GN Name=celf1; Synonyms=cugbp1; ORFNames=TEgg064f02.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Oligomer. Oligomerization is required for RNA-binding and
CC EDEN-dependent deadenylation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
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 {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
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DR EMBL; CR760913; CAJ82289.1; -; mRNA.
DR RefSeq; NP_001017152.1; NM_001017152.2.
DR AlphaFoldDB; Q28HE9; -.
DR BMRB; Q28HE9; -.
DR SMR; Q28HE9; -.
DR STRING; 8364.ENSXETP00000019816; -.
DR PaxDb; Q28HE9; -.
DR GeneID; 549906; -.
DR KEGG; xtr:549906; -.
DR CTD; 10658; -.
DR Xenbase; XB-GENE-854036; celf1.
DR eggNOG; KOG0144; Eukaryota.
DR HOGENOM; CLU_015367_0_2_1; -.
DR InParanoid; Q28HE9; -.
DR OrthoDB; 1209165at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006376; P:mRNA splice site selection; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
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; IPR002343; Hud_Sxl_RNA.
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 PRINTS; PR00961; HUDSXLRNA.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..490
FT /note="CUGBP Elav-like family member 1"
FT /id="PRO_0000295188"
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 405..483
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 283..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 52387 MW; 73AEEB55E18C5382 CRC64;
MNGTMDHPDH PDPDSIKMFV GQVPRSWSEK ELRELFEQYG AVYEINVLRD RSQNPPQSKG
CCFITFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE KNNAVEDRKL FVGMVSKKCN
ENDIRAMFSQ FGQIEESRIL RGPDGMSRGC AFVTFTTRSM AQMAIKAMHQ AQTMEGCSSP
IVVKFADTQK DKEQKRMTQQ LQQQMQQLNA ASMWGNLAGL SSLAPQYLAL LQQTASSGNL
NSLSGLHPMG GEYATGMTSG LNAMQLQNLA ALAAAASAAQ NTPSAGSALT TSSSPLSILT
SSGSSPSSNN NSAVNPMASL GALQTLAGAT AGLNVGSLAG MAALNGGLGS SLSNGTGSTM
EALSQAYSGI QQYAAAALPS LYNQSLLSQQ GLGAAGSQKE GPEGANLFIY HLPQEFGDQD
LLQMFMPFGN VVSAKVFIDK QTNLSKCFGF VSYDNPVSAQ AAIQSMNGFQ IGMKRLKVQL
KRSKNDSKPY