CELF1_PONAB
ID CELF1_PONAB Reviewed; 513 AA.
AC Q5R995;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding protein implicated in the regulation of several
CC post-transcriptional events. Involved in pre-mRNA alternative splicing,
CC mRNA translation and stability. Mediates exon inclusion and/or
CC exclusion in pre-mRNA that are subject to tissue-specific and
CC developmentally regulated alternative splicing. Specifically activates
CC exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling
CC at the juvenile to adult transition. Acts as both an activator and
CC repressor of a pair of coregulated exons: promotes inclusion of the
CC smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in
CC actinin pre-mRNAs. Activates SM exon 5 inclusion by antagonizing the
CC repressive effect of PTB. Promotes exclusion of exon 11 of the INSR
CC pre-mRNA. Inhibits, together with HNRNPH1, insulin receptor (IR) pre-
CC mRNA exon 11 inclusion in myoblast. Increases translation and controls
CC the choice of translation initiation codon of CEBPB mRNA. Increases
CC mRNA translation of CEBPB in aging liver. Increases translation of
CC CDKN1A mRNA by antagonizing the repressive effect of CALR3. Mediates
CC rapid cytoplasmic mRNA deadenylation. Recruits the deadenylase PARN to
CC the poly(A) tail of EDEN-containing mRNAs to promote their
CC deadenylation. Required for completion of spermatogenesis. Binds to
CC (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to
CC Bruno response elements (BREs). Binds to muscle-specific splicing
CC enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2
CC pre-mRNA. Binds to AU-rich sequences (AREs or EDEN-like) localized in
CC the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA. Binds to the 5'-
CC region of CDKN1A and CEBPB mRNAs. Binds with the 5'-region of CEBPB
CC mRNA in aging liver (By similarity). May be a specific regulator of
CC miRNA biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF2,
CC negatively regulates the processing to mature miRNA (By similarity).
CC {ECO:0000250|UniProtKB:P28659, ECO:0000250|UniProtKB:Q92879}.
CC -!- SUBUNIT: Associates with polysomes. Interacts with HNRNPH1; the
CC interaction in RNA-dependent. Interacts with PARN. Component of an EIF2
CC complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2,
CC HSP90B1 and HSPA5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=RNA-binding activity is detected in both nuclear and cytoplasmic
CC compartments. {ECO:0000250}.
CC -!- DOMAIN: RRM1 and RRM2 domains preferentially target UGU(U/G)-rich mRNA
CC elements. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
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DR EMBL; CR859496; CAH91665.1; -; mRNA.
DR RefSeq; NP_001125976.1; NM_001132504.1.
DR AlphaFoldDB; Q5R995; -.
DR BMRB; Q5R995; -.
DR SMR; Q5R995; -.
DR STRING; 9601.ENSPPYP00000003787; -.
DR GeneID; 100172914; -.
DR KEGG; pon:100172914; -.
DR CTD; 10658; -.
DR eggNOG; KOG0144; Eukaryota.
DR InParanoid; Q5R995; -.
DR Proteomes; UP000001595; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Activator; Cytoplasm; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..513
FT /note="CUGBP Elav-like family member 1"
FT /id="PRO_0000295182"
FT DOMAIN 43..126
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 135..215
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 428..506
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 304..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92879"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92879"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28659"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92879"
SQ SEQUENCE 513 AA; 55068 MW; C1AF7494210F9E7F CRC64;
MAAFKLDFLP EMMVDHCSLN SSPVSKKMNG TLDHPDQPDL DAIKMFVGQV PRTWSEKDLR
ELFEQYGAVY EINVLRDRSQ NPPQSKGCCF VTFYTRKAAL EAQNALHNMK VLPGMHHPIQ
MKPADSEKNN AVEDRKLFIG MISKKCTEND IRVMFSSFGQ IEECRILWGP DGLSRGCALV
TFTTRAMAQT AIKAMHQAQT MEGCSSPMVV KFADTQKDKE QKRMAQQLQQ QMQQISAASV
WGNLAGLNTL GPQYLALYLQ LLQQTASSGN LNTLSSLHPM GGLNAMQLQN LAALAAAASA
AQNTPSGTNA LTTSSSPLSV LTSSGSSPSS SSSNSVNPIA SLGALQTLAG ATAGLNVGSL
AGMAALNGGL GSSGLSNGTG STMEALTQAY SGIQQYAAAA LPTLYNQNLL TQQSIGAAGS
QKEGPEGANL FIYHLPQEFG DQDLLQMFMP FGNVVSAKVF IDKQTNLSKC FGFVSYDNPV
SAQAAIQSMN GFQIGMKRLK VQLKRSKNDS KPY
