CELF2_XENLA
ID CELF2_XENLA Reviewed; 536 AA.
AC Q7ZXE2; P70055; Q90WV9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=ELAV-type RNA-binding protein 3;
DE Short=ETR-3;
DE AltName: Full=RNA-binding protein BRUNOL-3;
GN Name=celf2; Synonyms=brunol3, cugbp2, etr3;
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] (ISOFORM 1), RNA-BINDING, AND MUTAGENESIS OF
RP PHE-105 AND PHE-194.
RC TISSUE=Head;
RX PubMed=10893231; DOI=10.1074/jbc.m003083200;
RA Good P.J., Chen Q., Warner S.J., Herring D.C.;
RT "A family of human RNA-binding proteins related to the Drosophila Bruno
RT translational regulator.";
RL J. Biol. Chem. 275:28583-28592(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) 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 repression and stability (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95319}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q7T2T1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7ZXE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7ZXE2-2; Sequence=VSP_026822, VSP_026823;
CC -!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
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DR EMBL; AY052559; AAL14122.1; -; mRNA.
DR EMBL; U69547; AAB09041.1; -; mRNA.
DR EMBL; BC045035; AAH45035.1; -; mRNA.
DR RefSeq; NP_001079593.1; NM_001086124.1. [Q7ZXE2-1]
DR RefSeq; NP_001165444.1; NM_001171973.1. [Q7ZXE2-2]
DR RefSeq; XP_018106118.1; XM_018250629.1. [Q7ZXE2-2]
DR AlphaFoldDB; Q7ZXE2; -.
DR BMRB; Q7ZXE2; -.
DR SMR; Q7ZXE2; -.
DR MaxQB; Q7ZXE2; -.
DR DNASU; 379280; -.
DR GeneID; 100335150; -.
DR GeneID; 379280; -.
DR KEGG; xla:379280; -.
DR CTD; 100335150; -.
DR CTD; 379280; -.
DR Xenbase; XB-GENE-963644; celf2.L.
DR OrthoDB; 1209165at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 379280; Expressed in brain and 13 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 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 Alternative splicing; Cytoplasm; mRNA processing; Nucleus;
KW Reference proteome; Repeat; Repressor; RNA-binding.
FT CHAIN 1..536
FT /note="CUGBP Elav-like family member 2"
FT /id="PRO_0000295195"
FT DOMAIN 58..141
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 150..230
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 451..529
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT VAR_SEQ 381..387
FT /note="IAQMLSG -> S (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_026822"
FT VAR_SEQ 446
FT /note="E -> EGLLFISAQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_026823"
FT MUTAGEN 105
FT /note="F->L: Does not reduce RNA-binding. Reduces strongly
FT RNA-binding; when associated with L-194."
FT /evidence="ECO:0000269|PubMed:10893231"
FT MUTAGEN 194
FT /note="F->L: Reduces slightly RNA-binding. Reduces strongly
FT RNA-binding; when associated with L-105."
FT /evidence="ECO:0000269|PubMed:10893231"
SQ SEQUENCE 536 AA; 57429 MW; EE8BEA229957577D CRC64;
MFERTSKPAF VENICVESMR CPKSAVTMRN EELLFSNGTT NKMNGALDHS DQPDPDAIKM
FVGQIPRSWS EKELKDLFEP YGAVYQINVL RDRSQNPPQS KGCCFVTFYT RKAALEAQNA
LHNIKTLPGM HHPIQMKPAD SEKSNAVEDR KLFIGMVSKK CNENDIRVMF SPFGQIEECR
ILRGPDGLSR GCAFVTFSTR AMAQNAIKAM HQSQTMEGCS SPIVVKFADT QKDKEQRRLQ
QQLAQQMQQL NTATWGNLTG LGGLTPQYLA LLQQATTPSN LGAFSGIQQM AGMNALQLQN
LATLAAAAAA AQTSATTTNV NPLSTTASAL GALTSPVAAS TANSSAGAAM NSLTSLGTLQ
GLAGATVGLN NINALAGTVN IAQMLSGMAA LNGGLGATGL TNGTAGTMDA LTQAYSGIQQ
YAAAALPTLY SQSLLQQQSA AGSQKEGPEG ANLFIYHLPQ EFGDQDILQM FMPFGNVISA
KVFIDKQTNL SKCFGFVSYD NPVSAQAAIQ AMNGFQIGMK RLKVQLKRSK NDSKPY
