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 28-JUN-2023, entry version 44. 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 Danionidae; Danioninae; 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., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., 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., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., RA Raisen C., 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., Babbage A., RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT 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., Beattie C.E.; RT "HuD and the Survival Motor Neuron Protein Interact in Motoneurons and Are RT Essential for Motoneuron Development, Function, and mRNA 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 in CC the regulation of mRNA stability, alternative splicing and translation CC (By similarity). Binds to AU-rich element (ARE) sequences in the 3' CC untranslated region (3'UTR) of target mRNAs (By similarity). Mainly CC plays a role in neuron-specific RNA processing (By similarity). CC Required for the maturation of motor neuron axonal branches and CC dendrites (PubMed:29061699). {ECO:0000250|UniProtKB:P26378, CC ECO:0000250|UniProtKB:Q61701, 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 initiation of CC swim and turn movements and decreased mean body curvature change per CC swim half-cycle and mean number of swim half-cycles per swim CC (PubMed:29061699). At 2 and 4 dpf, decreased axonal branches and at 4 CC dpf, decreased dendrites in motor neurons (PubMed:29061699). Defects on CC motor neuron extensions persist at 26 dph (PubMed:29061699). Decreased CC GAP43 mRNA levels (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=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH65965.2; Type=Erroneous initiation; Note=Truncated N-terminus.; 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 RefSeq; NP_001231530.1; NM_001244601.1. DR RefSeq; NP_571528.2; NM_131453.3. DR AlphaFoldDB; A0A0R4IEW8; -. DR SMR; A0A0R4IEW8; -. DR STRING; 7955.ENSDARP00000116684; -. DR DNASU; 30737; -. DR GeneID; 30737; -. DR KEGG; dre:30737; -. DR CTD; 1996; -. DR ZFIN; ZDB-GENE-990415-246; elavl4. DR InParanoid; A0A0R4IEW8; -. DR OMA; GSEWCIF; -. DR OrthoDB; 129910at2759; -. DR PRO; PR:A0A0R4IEW8; -. DR Proteomes; UP000000437; Chromosome 8. DR Bgee; ENSDARG00000045639; Expressed in central nervous system and 16 other tissues. DR ExpressionAtlas; A0A0R4IEW8; baseline and differential. DR GO; GO:0030424; C:axon; TAS:ZFIN. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell. DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. 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 GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR CDD; cd12652; RRM2_Hu; 1. DR CDD; cd12656; RRM3_HuD; 1. DR Gene3D; 3.30.70.330; -; 3. DR InterPro; IPR006548; ELAD_HU_SF. 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 PANTHER; PTHR10352:SF9; ELAV-LIKE PROTEIN 4; 1. DR PANTHER; PTHR10352; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT G; 1. DR Pfam; PF00076; RRM_1; 3. DR PRINTS; PR00961; HUDSXLRNA. DR SMART; SM00360; RRM; 3. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1. DR PROSITE; PS50102; RRM; 3. PE 1: Evidence at protein level; KW Cell projection; Cytoplasm; mRNA processing; mRNA splicing; KW Reference proteome; Repeat; RNA-binding. FT CHAIN 1..411 FT /note="ELAV-like protein 4" FT /id="PRO_0000447878" FT DOMAIN 88..166 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 174..257 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 328..406 FT /note="RRM 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 50..89 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 //