CELF2_PONAB
ID CELF2_PONAB Reviewed; 508 AA.
AC Q5R8Y8; Q5R427; Q5R4P3; Q5R6N8; Q5RAD1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=CUGBP Elav-like family member 2;
DE Short=CELF-2;
DE AltName: Full=Bruno-like protein 3;
DE AltName: Full=CUG triplet repeat RNA-binding protein 2;
DE Short=CUG-BP2;
DE AltName: Full=CUG-BP- and ETR-3-like factor 2;
DE AltName: Full=RNA-binding protein BRUNOL-3;
GN Name=CELF2; Synonyms=CUGBP2;
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] (ISOFORMS 1; 2; 3; 4 AND 5).
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 TNNT2 in embryonic, but not adult, skeletal muscle.
CC Activates TNNT2 exon 5 inclusion by antagonizing the repressive effect
CC of PTB. Acts as both an activator and repressor of a pair of
CC coregulated exons: promotes inclusion of the smooth muscle (SM) exon
CC but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs.
CC Promotes inclusion of exonS 21 and exclusion of exon 5 of the NMDA
CC receptor R1 pre-mRNA. Involved in the apoB RNA editing activity.
CC Increases COX2 mRNA stability and inhibits COX2 mRNA translation in
CC epithelial cells after radiation injury. Modulates the cellular
CC apoptosis program by regulating COX2-mediated prostaglandin E2 (PGE2)
CC expression. Binds to (CUG)n triplet repeats in the 3'-UTR of
CC transcripts such as DMPK. Binds to the muscle-specific splicing
CC enhancer (MSE) intronic sites flanking the TNNT2 alternative exon 5.
CC Binds preferentially to UG-rich sequences, in particular UG repeat and
CC UGUU motifs. Binds to apoB mRNA, specifically to AU-rich sequences
CC located immediatly upstream of the edited cytidine. Binds AU-rich
CC sequences in the 3'-UTR of COX2 mRNA. Binds to an intronic RNA element
CC responsible for the silencing of exon 21 splicing. Binds to (CUG)n
CC repeats (By similarity). May be a specific regulator of miRNA
CC biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF1,
CC negatively regulates the processing to mature miRNA (By similarity).
CC {ECO:0000250|UniProtKB:O95319, ECO:0000250|UniProtKB:Q9Z0H4}.
CC -!- SUBUNIT: Interacts with A1CF. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95319}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Z0H4}. Note=Accumulates in the cytoplasm after
CC ionizing radiation. Colocalizes with APOBEC1 and A1CF. RNA-binding
CC activity is detected in both nuclear and cytoplasmic compartments (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q5R8Y8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R8Y8-2; Sequence=VSP_026810;
CC Name=3;
CC IsoId=Q5R8Y8-3; Sequence=VSP_026809, VSP_026810;
CC Name=4;
CC IsoId=Q5R8Y8-4; Sequence=VSP_026809;
CC Name=5;
CC IsoId=Q5R8Y8-5; Sequence=VSP_026811, VSP_026812;
CC -!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH91772.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CR859087; CAH91279.1; -; mRNA.
DR EMBL; CR859609; CAH91772.1; ALT_FRAME; mRNA.
DR EMBL; CR860449; CAH92572.1; -; mRNA.
DR EMBL; CR861202; CAH93273.1; -; mRNA.
DR EMBL; CR861433; CAH93489.1; -; mRNA.
DR RefSeq; NP_001126925.1; NM_001133453.1.
DR RefSeq; NP_001153184.1; NM_001159712.1.
DR AlphaFoldDB; Q5R8Y8; -.
DR BMRB; Q5R8Y8; -.
DR SMR; Q5R8Y8; -.
DR GeneID; 100173942; -.
DR KEGG; pon:100173942; -.
DR CTD; 10659; -.
DR eggNOG; KOG0144; Eukaryota.
DR HOGENOM; CLU_015367_0_2_1; -.
DR InParanoid; Q5R8Y8; -.
DR OMA; PMGNGMN; -.
DR OrthoDB; 1209165at2759; -.
DR TreeFam; TF314924; -.
DR Proteomes; UP000001595; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; 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; 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 Alternative splicing; Cytoplasm; mRNA processing; Nucleus;
KW Reference proteome; Repeat; Repressor; RNA-binding.
FT CHAIN 1..508
FT /note="CUGBP Elav-like family member 2"
FT /id="PRO_0000295191"
FT DOMAIN 40..123
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 132..212
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 423..501
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..283
FT /note="Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1
FT exon 21 inclusion"
FT /evidence="ECO:0000250"
FT REGION 357..508
FT /note="Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1
FT exon 21 inclusion"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_026809"
FT VAR_SEQ 358
FT /note="A -> AVAQMLS (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_026810"
FT VAR_SEQ 359..360
FT /note="GM -> VA (in isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_026811"
FT VAR_SEQ 361..508
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_026812"
FT CONFLICT 70
FT /note="N -> D (in Ref. 1; CAH93489)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="T -> S (in Ref. 1; CAH93273)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="R -> W (in Ref. 1; CAH93489)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="F -> S (in Ref. 1; CAH91772)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="P -> S (in Ref. 1; CAH91279)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="L -> P (in Ref. 1; CAH92572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 54285 MW; C65F337D462717F2 CRC64;
MRCPKSAVTM RNEELLLSNG TANKMNGALD HSDQPDPDAI KMFVGQIPRS WSEKELKELF
EPYGAVYQIN VLRDRSQNPP QSKGCCFVTF YTRKAALEAQ NALHNIKTLP GMHHPIQMKP
ADSEKSNAVE DRKLFIGMVS KKCNENDIRV MFSPFGQIEE CRILRGPDGL SRGCAFVTFS
TRAMAQNAIK AMHQSQTMEG CSSPIVVKFA DTQKDKEQRR LQQQLAQQMQ QLNTATWGNL
TGLGGLTPQY LALLQQATSS SNLGAFSGIQ QMAGMNALQL QNLATLAAAA AAAQTSATST
NANPLSTTSS ALGALTSPVA ASTPNSTAGA AMNSLTSLGT LQGLAGATVG LNNINALAGM
AALNGGLGAT GLTNGTAGTM DALTQAYSGI QQYAAAALPT LYSQSLLQQQ SAAGSQKEGP
EGANLFIYHL PQEFGDQDIL QMFMPFGNVI SAKVFIDKQT NLSKCFGFVS YDNPVSAQAA
IQAMNGFQIG MKRLKVQLKR SKNDSKPY
