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CELF3_MOUSE
ID   CELF3_MOUSE             Reviewed;         465 AA.
AC   Q8CIN6; Q6PFH2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=CUGBP Elav-like family member 3;
DE            Short=CELF-3;
DE   AltName: Full=Bruno-like protein 1;
DE   AltName: Full=CUG-BP- and ETR-3-like factor 3;
DE   AltName: Full=ELAV-type RNA-binding protein 1;
DE            Short=ETR-1;
DE   AltName: Full=RNA-binding protein BRUNOL-1;
DE   AltName: Full=Trinucleotide repeat-containing gene 4 protein;
GN   Name=Celf3; Synonyms=Tnrc4;
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 1).
RC   TISSUE=Brain;
RA   d'Apolito M., Savino M., Grifa A., Quattrone A.;
RT   "The RNA binding protein CELF3 associates to the DMPK mRNA and is a
RT   negative regulator of mRNA stability involved in neuronal
RT   differentiation.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Fetal brain;
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).
CC   -!- FUNCTION: RNA-binding protein involved 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. Activates the splicing of MAPT/Tau exon 10. Binds to
CC       muscle-specific splicing enhancer (MSE) intronic sites flanking the
CC       alternative exon 5 of TNNT2 pre-mRNA (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CIN6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CIN6-2; Sequence=VSP_026826, VSP_026827;
CC   -!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
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DR   EMBL; AY165052; AAN73885.1; -; mRNA.
DR   EMBL; BC057553; AAH57553.1; -; mRNA.
DR   CCDS; CCDS38536.1; -. [Q8CIN6-1]
DR   CCDS; CCDS79972.1; -. [Q8CIN6-2]
DR   RefSeq; NP_001276542.1; NM_001289613.1. [Q8CIN6-2]
DR   RefSeq; NP_001276545.1; NM_001289616.1.
DR   RefSeq; NP_001276549.1; NM_001289620.1.
DR   RefSeq; NP_766022.1; NM_172434.3. [Q8CIN6-1]
DR   RefSeq; XP_006502386.1; XM_006502323.3.
DR   AlphaFoldDB; Q8CIN6; -.
DR   SMR; Q8CIN6; -.
DR   STRING; 10090.ENSMUSP00000029784; -.
DR   iPTMnet; Q8CIN6; -.
DR   PhosphoSitePlus; Q8CIN6; -.
DR   MaxQB; Q8CIN6; -.
DR   PaxDb; Q8CIN6; -.
DR   PRIDE; Q8CIN6; -.
DR   ProteomicsDB; 281576; -. [Q8CIN6-1]
DR   ProteomicsDB; 281577; -. [Q8CIN6-2]
DR   Antibodypedia; 20334; 98 antibodies from 22 providers.
DR   DNASU; 78784; -.
DR   Ensembl; ENSMUST00000029784; ENSMUSP00000029784; ENSMUSG00000028137. [Q8CIN6-1]
DR   Ensembl; ENSMUST00000200342; ENSMUSP00000143344; ENSMUSG00000028137. [Q8CIN6-2]
DR   GeneID; 78784; -.
DR   KEGG; mmu:78784; -.
DR   UCSC; uc008qgl.2; mouse. [Q8CIN6-1]
DR   UCSC; uc008qgm.2; mouse. [Q8CIN6-2]
DR   CTD; 11189; -.
DR   MGI; MGI:1926034; Celf3.
DR   VEuPathDB; HostDB:ENSMUSG00000028137; -.
DR   eggNOG; KOG0146; Eukaryota.
DR   eggNOG; KOG4205; Eukaryota.
DR   GeneTree; ENSGT00940000154716; -.
DR   InParanoid; Q8CIN6; -.
DR   OMA; NYPAYNA; -.
DR   OrthoDB; 1209165at2759; -.
DR   PhylomeDB; Q8CIN6; -.
DR   TreeFam; TF314924; -.
DR   BioGRID-ORCS; 78784; 2 hits in 76 CRISPR screens.
DR   PRO; PR:Q8CIN6; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8CIN6; protein.
DR   Bgee; ENSMUSG00000028137; Expressed in embryonic brain and 109 other tissues.
DR   ExpressionAtlas; Q8CIN6; baseline and differential.
DR   Genevisible; Q8CIN6; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016604; C:nuclear body; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0097322; F:7SK snRNA binding; IPI:MGI.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IPI:MGI.
DR   GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR   GO; GO:0006376; P:mRNA splice site selection; IBA:GO_Central.
DR   GO; GO:0098781; P:ncRNA transcription; IMP:MGI.
DR   GO; GO:0030575; P:nuclear body organization; 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:0008380; P:RNA splicing; ISO:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP: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   2: Evidence at transcript level;
KW   Activator; Alternative splicing; Cytoplasm; mRNA processing; mRNA splicing;
KW   Nucleus; Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..465
FT                   /note="CUGBP Elav-like family member 3"
FT                   /id="PRO_0000295199"
FT   DOMAIN          7..88
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          95..174
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          380..458
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          283..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..360
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         92
FT                   /note="G -> GE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026826"
FT   VAR_SEQ         306
FT                   /note="P -> PDEALSAERSAGGVPIMSQAHSWLVMLSA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026827"
SQ   SEQUENCE   465 AA;  50520 MW;  542DF7AC60CCA705 CRC64;
     MKEPDAIKLF VGQIPRHLEE KDLKPIFEQF GRIFELTVIK DKYTGLHKGC AFLTYCARDS
     ALKAQSALHE QKTLPGMNRP IQVKPADSES RGDRKLFVGM LGKQQTDEDV RKMFEPFGTI
     DECTVLRGPD GTSKGCAFVK FQTHAEAQAA INTLHSSRTL PGASSSLVVK FADTEKERGL
     RRMQQVATQL GMFSPIALQF GAYSAYTQAL MQQQAALVAA HSAYLSPMAT MAAVQMQHMA
     AISANGLIAT PITPSSGTST PPAIAATPVS AIPAALGVNG YSPVPTQPTG QPAPDALYPN
     GVHPYPAQSP AAPVDPLQQA YAGMQHYTAA YPAAYSLVAP AFPQPPALVA QQPPPPPQQQ
     QQQQQQQQQQ QQQREGPDGC NIFIYHLPQE FTDSEILQMF VPFGHVISAK VFVDRATNQS
     KCFGFVSFDN PASAQAAIQA MNGFQIGMKR LKVQLKRPKD ANRPY
 
 
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