CELF1_RAT
ID CELF1_RAT Reviewed; 487 AA.
AC Q4QQT3;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP ASSOCIATION WITH POLYSOMES.
RX PubMed=10536163; DOI=10.1093/nar/27.22.4517;
RA Timchenko N.A., Welm A.L., Lu X., Timchenko L.T.;
RT "CUG repeat binding protein (CUGBP1) interacts with the 5' region of
RT C/EBPbeta mRNA and regulates translation of C/EBPbeta isoforms.";
RL Nucleic Acids Res. 27:4517-4525(1999).
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: Interacts with HNRNPH1; the interaction in RNA-dependent.
CC Interacts with PARN. Component of an EIF2 complex at least composed of
CC CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5 (By
CC similarity). Associates with polysomes. {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; BC098012; AAH98012.1; -; mRNA.
DR RefSeq; NP_001020592.1; NM_001025421.1.
DR RefSeq; XP_006234584.1; XM_006234522.2.
DR RefSeq; XP_006234585.1; XM_006234523.2.
DR RefSeq; XP_006234586.1; XM_006234524.2.
DR RefSeq; XP_008760232.1; XM_008762010.2.
DR RefSeq; XP_017447388.1; XM_017591899.1.
DR AlphaFoldDB; Q4QQT3; -.
DR BMRB; Q4QQT3; -.
DR SMR; Q4QQT3; -.
DR BioGRID; 263230; 1.
DR IntAct; Q4QQT3; 20.
DR STRING; 10116.ENSRNOP00000014484; -.
DR iPTMnet; Q4QQT3; -.
DR PhosphoSitePlus; Q4QQT3; -.
DR jPOST; Q4QQT3; -.
DR PaxDb; Q4QQT3; -.
DR PeptideAtlas; Q4QQT3; -.
DR PRIDE; Q4QQT3; -.
DR GeneID; 362160; -.
DR KEGG; rno:362160; -.
DR UCSC; RGD:1307721; rat.
DR CTD; 10658; -.
DR RGD; 1307721; Celf1.
DR VEuPathDB; HostDB:ENSRNOG00000010379; -.
DR eggNOG; KOG0144; Eukaryota.
DR HOGENOM; CLU_015367_0_2_1; -.
DR InParanoid; Q4QQT3; -.
DR OMA; QWHKPRK; -.
DR OrthoDB; 1209165at2759; -.
DR PhylomeDB; Q4QQT3; -.
DR PRO; PR:Q4QQT3; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000010379; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; Q4QQT3; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0097356; C:perinucleolar compartment; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0042835; F:BRE binding; ISO:RGD.
DR GO; GO:0106222; F:lncRNA binding; ISO:RGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:ARUK-UCL.
DR GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR GO; GO:0036002; F:pre-mRNA binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0031369; F:translation initiation factor binding; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; ISO:RGD.
DR GO; GO:0061157; P:mRNA destabilization; IDA:ARUK-UCL.
DR GO; GO:0006376; P:mRNA splice site selection; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0017148; P:negative regulation of translation; ISO:RGD.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:ARUK-UCL.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0016441; P:post-transcriptional gene silencing; IMP:ARUK-UCL.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:ARUK-UCL.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; ISO:RGD.
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 Acetylation; Activator; Cytoplasm; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..487
FT /note="CUGBP Elav-like family member 1"
FT /id="PRO_0000295183"
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 402..480
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 277..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q92879"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92879"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92879"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28659"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92879"
SQ SEQUENCE 487 AA; 52205 MW; D39AD132660EBF40 CRC64;
MNGTLDHPDQ PDLDAIKMFV GQVPRTWSEK DLRELFEQYG AVYEINILRD RSQNPPQSKG
CCFVTFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE KNNAVEDRKL FIGMISKKCT
ENDIRVMFSS FGQIEECRIL RGPDGLSRGC AFVTFTTRTM AQTAIKAMHQ AQTMEGCSSP
MVVKFADTQK DKEQKRMAQQ LQQQMQQISA ASVWGNLAGL NTLGPQYLAL YLQLLQQTAN
SGNLNTLSSL HPMGGLNAMQ LQNLAALAAA ASAAQNTPSG TNALTTSSSP LSVLTSSAGS
SPSSSSSNSV NPIASLGALQ TLAGATAGLN VGSLAGMAAL NGGLGSSGLS NGTGSTMEAL
TQAYSGIQQY AAAALPTLYN QNLLTQQSIG AAGSQKEGPE GANLFIYHLP QEFGDQDLLQ
MFMPFGNVVS AKVFIDKQTN LSKCFGFVSY DNPVSAQAAI QSMNGFQIGM KRLKVQLKRS
KNDSKPY
