ID ELAV4_DANRE Reviewed; 411 AA. AC A0A0R4IEW8; Q6NZU5; Q90409; DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2018, sequence version 2. DT 18-SEP-2019, entry version 25. DE RecName: Full=ELAV-like protein 4 {ECO:0000305}; DE AltName: Full=Protein elrD {ECO:0000303|PubMed:7753842}; GN Name=elavl4 {ECO:0000312|ZFIN:ZDB-GENE-990415-246}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437}; RN [1] {ECO:0000312|EMBL:AAA96940.1} RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7753842; DOI=10.1073/pnas.92.10.4557; RA Good P.J.; RT "A conserved family of elav-like genes in vertebrates."; RL Proc. Natl. Acad. Sci. U.S.A. 92:4557-4561(1995). RN [2] {ECO:0000312|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., RA Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., RA Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., RA Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., RA Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., RA Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., RA Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., RA Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., RA Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., RA Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., RA Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., RA Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., RA Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., RA Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). RN [3] {ECO:0000312|EMBL:AAH65965.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo {ECO:0000312|EMBL:AAH65965.2}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000305} RP FUNCTION, INTERACTION WITH SMN1, TISSUE SPECIFICITY, AND DISRUPTION RP PHENOTYPE. RX PubMed=29061699; DOI=10.1523/JNEUROSCI.1528-17.2017; RA Hao le T., Duy P.Q., An M., Talbot J., Iyer C.C., Wolman M., RA Beattie C.E.; RT "HuD and the Survival Motor Neuron Protein Interact in Motoneurons and RT Are Essential for Motoneuron Development, Function, and mRNA RT Regulation."; RL J. Neurosci. 37:11559-11571(2017). CC -!- FUNCTION: RNA-binding protein that is involved in the post- CC transcriptional regulation of mRNAs (By similarity). Plays a role CC in the regulation of mRNA stability, alternative splicing and CC translation (By similarity). Binds to AU-rich element (ARE) CC sequences in the 3' untranslated region (3'UTR) of target mRNAs CC (By similarity). Mainly plays a role in neuron-specific RNA CC processing (By similarity). Required for the maturation of motor CC neuron axonal branches and dendrites (PubMed:29061699). CC {ECO:0000250|UniProtKB:P26378, ECO:0000250|UniProtKB:Q61701, CC ECO:0000269|PubMed:29061699}. CC -!- SUBUNIT: Interacts with smn1. {ECO:0000269|PubMed:29061699}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O09032}. CC Perikaryon {ECO:0000250|UniProtKB:Q61701}. Cell projection, axon CC {ECO:0000250|UniProtKB:Q61701}. Cell projection, dendrite CC {ECO:0000250|UniProtKB:Q61701}. Cell projection, growth cone CC {ECO:0000250|UniProtKB:Q61701}. CC -!- TISSUE SPECIFICITY: Expressed in motor neurons. CC {ECO:0000269|PubMed:29061699}. CC -!- DISRUPTION PHENOTYPE: Reduced overall movement, decreased CC initiation of swim and turn movements and decreased mean body CC curvature change per swim half-cycle and mean number of swim half- CC cycles per swim (PubMed:29061699). At 2 and 4 dpf, decreased CC axonal branches and at 4 dpf, decreased dendrites in motor neurons CC (PubMed:29061699). Defects on motor neuron extensions persist at CC 26 dph (PubMed:29061699). Decreased GAP43 mRNA levels CC (PubMed:29061699). {ECO:0000269|PubMed:29061699}. CC -!- SIMILARITY: Belongs to the RRM elav family. CC {ECO:0000255|RuleBase:RU361281}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA96940.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=AAH65965.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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; CR931780; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CU467068; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CU929301; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U17602; AAA96940.1; ALT_INIT; mRNA. DR EMBL; BC065965; AAH65965.2; ALT_INIT; mRNA. DR PIR; I50513; I50513. DR RefSeq; NP_001231529.1; NM_001244600.1. DR Ensembl; ENSDART00000172510; ENSDARP00000133629; ENSDARG00000045639. DR GeneID; 30737; -. DR KEGG; dre:30737; -. DR CTD; 1996; -. DR ZFIN; ZDB-GENE-990415-246; elavl4. DR eggNOG; KOG0145; Eukaryota. DR eggNOG; ENOG410XP7S; LUCA. DR GeneTree; ENSGT00940000157399; -. DR HOGENOM; HOG000231162; -. DR KO; K13208; -. DR OrthoDB; 614259at2759; -. DR Proteomes; UP000000437; Chromosome 8. DR ExpressionAtlas; A0A0R4IEW8; baseline. DR GO; GO:0030424; C:axon; TAS:ZFIN. DR GO; GO:0032991; C:protein-containing complex; IPI:ZFIN. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; TAS:ZFIN. DR GO; GO:0007409; P:axonogenesis; IMP:ZFIN. DR CDD; cd12650; RRM1_Hu; 1. DR CDD; cd12656; RRM3_HuD; 1. DR Gene3D; 3.30.70.330; -; 3. DR InterPro; IPR006548; ELAD_HU_SF. DR InterPro; IPR034775; ELAV/Hu_RRM1. DR InterPro; IPR034918; HuD_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 TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1. DR PROSITE; PS50102; RRM; 3. PE 1: Evidence at protein level; KW Cell projection; Complete proteome; Cytoplasm; mRNA processing; KW mRNA splicing; Reference proteome; Repeat; RNA-binding. FT CHAIN 1 411 ELAV-like protein 4. FT /FTId=PRO_0000447878. FT DOMAIN 88 166 RRM 1. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. FT DOMAIN 174 257 RRM 2. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. FT DOMAIN 328 406 RRM 3. {ECO:0000255|PROSITE- FT ProRule:PRU00176}. SQ SEQUENCE 411 AA; 45258 MW; 313C6063DEFE38F4 CRC64; MFEISRTLNA ALLSNEGSTE TQWRQADLPQ LQGWAEKGLL TQPKMIISNM EPQVTNGPNS ATANGPSSNS RSCPSPMQTG GSNDDSKTNL IVNYLPQNMT QEEFRSLFGS IGEIESCKLV RDKITGQSLG YGFVNYIDPK DAEKAINTLN GLRLQTKTIK VSYARPSSAS IRDANLYVSG LPKTMTQKEL EQLFSQYGRI ITSRILVDQV TGPTGGSRGV GFIRFDKRIE AEEAIKGLNG QKPSGAAEPI TVKFANNPSQ KTSQALLSQL YQSPNRRYPG PLHHQAQRFR LDNLLNMAYG VKRFSPITID SMTSLVGMNI PGHTGTGWCI FVYNLSPDSD ESVLWQLFGP FGAVNNVKVI RDFNTNKCKG FGFVTMTNYD EAAMAIASLN GYRLGDRVLQ VSFKTNKTHK S //