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   03-AUG-2022, entry version 39.
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};
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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   Ensembl; ENSDART00000172510; ENSDARP00000133629; ENSDARG00000045639.
DR   GeneID; 30737; -.
DR   KEGG; dre:30737; -.
DR   CTD; 1996; -.
DR   ZFIN; ZDB-GENE-990415-246; elavl4.
DR   GeneTree; ENSGT00940000157399; -.
DR   OrthoDB; 614259at2759; -.
DR   PRO; PR:A0A0R4IEW8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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; 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; 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