CELF4_MOUSE
ID CELF4_MOUSE Reviewed; 486 AA.
AC Q7TSY6; Q80Y76; Q811Z7; Q8BKM2; Q8BLM9; Q8BXA2; Q99PE0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=CUGBP Elav-like family member 4;
DE Short=CELF-4;
DE AltName: Full=Bruno-like protein 4;
DE AltName: Full=CUG-BP- and ETR-3-like factor 4;
DE AltName: Full=RNA-binding protein BRUNOL-4;
GN Name=Celf4; Synonyms=Brul4, Brunol4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=12438720; DOI=10.1159/000066619;
RA Meins M., Schlickum S., Wilhelm C., Missbach J., Yadav S., Glaeser B.,
RA Grzmil M., Burfeind P., Laccone F.;
RT "Identification and characterization of murine Brunol4, a new member of the
RT elav/bruno family.";
RL Cytogenet. Genome Res. 97:254-260(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 7).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Head, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 7).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 188-486 (ISOFORMS 2/3/4/5).
RC STRAIN=C57BL/6J;
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 [6]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=11158314; DOI=10.1128/mcb.21.4.1285-1296.2001;
RA Ladd A.N., Charlet-B N., Cooper T.A.;
RT "The CELF family of RNA binding proteins is implicated in cell-specific and
RT developmentally regulated alternative splicing.";
RL Mol. Cell. Biol. 21:1285-1296(2001).
CC -!- FUNCTION: RNA-binding protein implicated in the regulation of pre-mRNA
CC alternative splicing. Mediates exon inclusion and/or exclusion in pre-
CC mRNA that are subject to tissue-specific and developmentally regulated
CC alternative splicing. Specifically activates exon 5 inclusion of
CC cardiac isoforms of TNNT2 during heart remodeling at the juvenile to
CC adult transition. Promotes exclusion of both the smooth muscle (SM) and
CC non-muscle (NM) exons in actinin pre-mRNAs. Activates the splicing of
CC MAPT/Tau exon 10. Binds to muscle-specific splicing enhancer (MSE)
CC intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q7TSY6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TSY6-2; Sequence=VSP_026835, VSP_026838;
CC Name=3;
CC IsoId=Q7TSY6-3; Sequence=VSP_026838;
CC Name=4;
CC IsoId=Q7TSY6-4; Sequence=VSP_026837, VSP_026838, VSP_026839;
CC Name=5;
CC IsoId=Q7TSY6-5; Sequence=VSP_026835, VSP_026838, VSP_026840;
CC Name=6;
CC IsoId=Q7TSY6-6; Sequence=VSP_026834, VSP_026840;
CC Name=7;
CC IsoId=Q7TSY6-7; Sequence=VSP_026833, VSP_026836;
CC -!- TISSUE SPECIFICITY: Expressed strongly in skeletal muscle, heart and
CC adipose tissue (at protein level). Expressed in the brain and
CC cerebellum. {ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:12438720}.
CC -!- DEVELOPMENTAL STAGE: Expressed in muscle and brain at 14 dpc (at
CC protein level). Expressed in embryo at 7.5 dpc.
CC {ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:12438720}.
CC -!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31762.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF515450; AAO22167.1; -; mRNA.
DR EMBL; AK044072; BAC31762.1; ALT_FRAME; mRNA.
DR EMBL; AK048427; BAC33334.1; -; mRNA.
DR EMBL; AK051458; BAC34649.1; -; mRNA.
DR EMBL; AC121094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048405; AAH48405.1; -; mRNA.
DR EMBL; BC052744; AAH52744.1; -; mRNA.
DR EMBL; AF314173; AAK00298.1; -; mRNA.
DR CCDS; CCDS29106.1; -. [Q7TSY6-2]
DR CCDS; CCDS50241.1; -. [Q7TSY6-5]
DR CCDS; CCDS89204.1; -. [Q7TSY6-4]
DR CCDS; CCDS89205.1; -. [Q7TSY6-3]
DR CCDS; CCDS89206.1; -. [Q7TSY6-6]
DR RefSeq; NP_001139764.1; NM_001146292.1. [Q7TSY6-5]
DR RefSeq; NP_001139765.1; NM_001146293.1. [Q7TSY6-3]
DR RefSeq; NP_001139766.1; NM_001146294.1. [Q7TSY6-6]
DR RefSeq; NP_001139767.1; NM_001146295.1.
DR RefSeq; NP_001167545.1; NM_001174074.1. [Q7TSY6-4]
DR RefSeq; NP_573458.2; NM_133195.3. [Q7TSY6-2]
DR RefSeq; XP_006525577.1; XM_006525514.2.
DR AlphaFoldDB; Q7TSY6; -.
DR SMR; Q7TSY6; -.
DR STRING; 10090.ENSMUSP00000111483; -.
DR iPTMnet; Q7TSY6; -.
DR PhosphoSitePlus; Q7TSY6; -.
DR MaxQB; Q7TSY6; -.
DR PaxDb; Q7TSY6; -.
DR PeptideAtlas; Q7TSY6; -.
DR PRIDE; Q7TSY6; -.
DR ProteomicsDB; 281179; -. [Q7TSY6-1]
DR ProteomicsDB; 281180; -. [Q7TSY6-2]
DR ProteomicsDB; 281181; -. [Q7TSY6-3]
DR ProteomicsDB; 281182; -. [Q7TSY6-4]
DR ProteomicsDB; 281183; -. [Q7TSY6-5]
DR ProteomicsDB; 281184; -. [Q7TSY6-6]
DR ProteomicsDB; 281185; -. [Q7TSY6-7]
DR ABCD; Q7TSY6; 1 sequenced antibody.
DR Antibodypedia; 22364; 77 antibodies from 19 providers.
DR DNASU; 108013; -.
DR Ensembl; ENSMUST00000025117; ENSMUSP00000025117; ENSMUSG00000024268. [Q7TSY6-6]
DR Ensembl; ENSMUST00000115816; ENSMUSP00000111483; ENSMUSG00000024268. [Q7TSY6-5]
DR Ensembl; ENSMUST00000223704; ENSMUSP00000153326; ENSMUSG00000024268. [Q7TSY6-3]
DR Ensembl; ENSMUST00000224553; ENSMUSP00000153258; ENSMUSG00000024268. [Q7TSY6-4]
DR Ensembl; ENSMUST00000225477; ENSMUSP00000153226; ENSMUSG00000024268. [Q7TSY6-2]
DR GeneID; 108013; -.
DR KEGG; mmu:108013; -.
DR UCSC; uc008ehk.2; mouse. [Q7TSY6-4]
DR UCSC; uc008ehl.2; mouse. [Q7TSY6-2]
DR UCSC; uc012ban.1; mouse. [Q7TSY6-3]
DR UCSC; uc012bao.1; mouse. [Q7TSY6-5]
DR UCSC; uc012bap.1; mouse. [Q7TSY6-6]
DR UCSC; uc012baq.1; mouse. [Q7TSY6-7]
DR CTD; 56853; -.
DR MGI; MGI:1932407; Celf4.
DR VEuPathDB; HostDB:ENSMUSG00000024268; -.
DR eggNOG; KOG0146; Eukaryota.
DR GeneTree; ENSGT00940000158673; -.
DR HOGENOM; CLU_015367_0_1_1; -.
DR InParanoid; Q7TSY6; -.
DR OMA; LMQMFIP; -.
DR OrthoDB; 1209165at2759; -.
DR PhylomeDB; Q7TSY6; -.
DR TreeFam; TF314924; -.
DR BioGRID-ORCS; 108013; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Celf4; mouse.
DR PRO; PR:Q7TSY6; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q7TSY6; protein.
DR Bgee; ENSMUSG00000024268; Expressed in dorsomedial nucleus of hypothalamus and 198 other tissues.
DR ExpressionAtlas; Q7TSY6; baseline and differential.
DR Genevisible; Q7TSY6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0042835; F:BRE binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0036002; F:pre-mRNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006376; P:mRNA splice site selection; IDA:MGI.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:MGI.
DR GO; GO:1902866; P:regulation of retina development in camera-type eye; IEP:MGI.
DR CDD; cd12632; RRM1_CELF3_4_5_6; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR034648; CELF3/4/5/6_RRM1.
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 Activator; Alternative splicing; Cytoplasm; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..486
FT /note="CUGBP Elav-like family member 4"
FT /id="PRO_0000295223"
FT DOMAIN 54..135
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 152..232
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 406..479
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..298
FT /note="Sufficient for RNA-binding and MSE-dependent
FT splicing activity"
FT /evidence="ECO:0000250"
FT REGION 18..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..258
FT /note="Necessary for TNNT2 exon 5 inclusion"
FT /evidence="ECO:0000250"
FT VAR_SEQ 124..163
FT /note="MNRPIQVKPADSESRGGSSCLRQPPSQDRKLFVGMLNKQQ -> VSGAGRGA
FT AGRAPTGGDFGRSGSDARGGDSRDPAAQDASR (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026833"
FT VAR_SEQ 140..150
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:12438720"
FT /id="VSP_026834"
FT VAR_SEQ 150..151
FT /note="QD -> H (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026835"
FT VAR_SEQ 164..486
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026836"
FT VAR_SEQ 268
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026837"
FT VAR_SEQ 390
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026838"
FT VAR_SEQ 417..444
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026839"
FT VAR_SEQ 443
FT /note="P -> PFGNVISSKVFVDRATNQSKC (in isoform 5 and isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:12438720"
FT /id="VSP_026840"
FT CONFLICT 352
FT /note="P -> R (in Ref. 5; AAK00298)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="A -> R (in Ref. 5; AAK00298)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="A -> T (in Ref. 5; AAK00298)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="P -> S (in Ref. 5; AAK00298)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="S -> T (in Ref. 5; AAK00298)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="Q -> R (in Ref. 2; BAC33334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 51932 MW; 17E4648A6752CF6F CRC64;
MYIKMATLAN GQADNASLST NGLGSSPGSA GHMNGLSHSP GNPSTIPMKD HDAIKLFIGQ
IPRNLDEKDL KPLFEEFGKI YELTVLKDRF TGMHKGCAFL TYCERESALK AQSALHEQKT
LPGMNRPIQV KPADSESRGG SSCLRQPPSQ DRKLFVGMLN KQQSEDDVRR LFEAFGNIEE
CTILRGPDGN SKGCAFVKYS SHAEAQAAIN ALHGSQTMPG ASSSLVVKFA DTDKERTMRR
MQQMAGQMGM FNPMAIPFGA YGAYAQALMQ QQAALMASVA QGGYLNPMAA FAAAQMQQMA
ALNMNGLAAA PMTPTSGGST PPGITAPAVP SIPSPIGVNG FTGLPPQANG QPAAEAVFAN
GIHPYPAQSP TAADPLQQAY AGVQQYAGPA AYPAAYGQIS QAFPQPPPMI PQQQREGPEG
CNLLIYHLPQ EFGDAELMQM FLPFGFVSFD NPASAQTAIQ AMNGFQIGMK RLKVQLKRPK
DANRPY
