ELAV4_RAT
ID ELAV4_RAT Reviewed; 385 AA.
AC O09032; A0A140TAF2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ELAV-like protein 4;
DE AltName: Full=Hu-antigen D;
DE Short=HuD;
DE AltName: Full=Paraneoplastic encephalomyelitis antigen HuD;
GN Name=Elavl4; Synonyms=Hud;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8717365; DOI=10.1016/0169-328x(95)00231-g;
RA Steller U., Kohls S., Muller B., Soller R., Muller R., Schlender J.,
RA Blohm D.H.;
RT "The RNA binding protein HuD: rat cDNA and analysis of the alternative
RT spliced mRNA in neuronal differentiating cell lines P19 and PC12.";
RL Brain Res. Mol. Brain Res. 35:285-296(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP FUNCTION.
RX PubMed=10982410; DOI=10.1091/mbc.11.9.3191;
RA Mobarak C.D., Anderson K.D., Morin M., Beckel-Mitchener A., Rogers S.L.,
RA Furneaux H., King P., Perrone-Bizzozero N.I.;
RT "The RNA-binding protein HuD is required for GAP-43 mRNA stability, GAP-43
RT gene expression, and PKC-dependent neurite outgrowth in PC12 cells.";
RL Mol. Biol. Cell 11:3191-3203(2000).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11948657; DOI=10.1002/jnr.10175;
RA Perrone-Bizzozero N., Bolognani F.;
RT "Role of HuD and other RNA-binding proteins in neural development and
RT plasticity.";
RL J. Neurosci. Res. 68:121-126(2002).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY AXOTOMY.
RX PubMed=12957493; DOI=10.1016/s0014-4886(03)00103-1;
RA Anderson K.D., Merhege M.A., Morin M., Bolognani F.,
RA Perrone-Bizzozero N.I.;
RT "Increased expression and localization of the RNA-binding protein HuD and
RT GAP-43 mRNA to cytoplasmic granules in DRG neurons during nerve
RT regeneration.";
RL Exp. Neurol. 183:100-108(2003).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY FEAR
RP CONDITIONING.
RX PubMed=15519747; DOI=10.1016/j.neulet.2004.08.074;
RA Bolognani F., Merhege M.A., Twiss J., Perrone-Bizzozero N.I.;
RT "Dendritic localization of the RNA-binding protein HuD in hippocampal
RT neurons: association with polysomes and upregulation during contextual
RT learning.";
RL Neurosci. Lett. 371:152-157(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16554442; DOI=10.1242/jcs.02852;
RA Ratti A., Fallini C., Cova L., Fantozzi R., Calzarossa C., Zennaro E.,
RA Pascale A., Quattrone A., Silani V.;
RT "A role for the ELAV RNA-binding proteins in neural stem cells:
RT stabilization of Msi1 mRNA.";
RL J. Cell Sci. 119:1442-1452(2006).
RN [8]
RP FUNCTION, AND METHYLATION AT ARG-248.
RX PubMed=16508003; DOI=10.1128/mcb.26.6.2273-2285.2006;
RA Fujiwara T., Mori Y., Chu D.L., Koyama Y., Miyata S., Tanaka H., Yachi K.,
RA Kubo T., Yoshikawa H., Tohyama M.;
RT "CARM1 regulates proliferation of PC12 cells by methylating HuD.";
RL Mol. Cell. Biol. 26:2273-2285(2006).
RN [9]
RP TISSUE SPECIFICITY, AND REPRESSION BY AXOTOMY.
RX PubMed=17234598; DOI=10.1523/jneurosci.4626-06.2007;
RA Deschenes-Furry J., Mousavi K., Bolognani F., Neve R.L., Parks R.J.,
RA Perrone-Bizzozero N.I., Jasmin B.J.;
RT "The RNA-binding protein HuD binds acetylcholinesterase mRNA in neurons and
RT regulates its expression after axotomy.";
RL J. Neurosci. 27:665-675(2007).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY SEIZURE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17577668; DOI=10.1007/s11064-007-9388-8;
RA Bolognani F., Tanner D.C., Nixon S., Okano H.J., Okano H.,
RA Perrone-Bizzozero N.I.;
RT "Coordinated expression of HuD and GAP-43 in hippocampal dentate granule
RT cells during developmental and adult plasticity.";
RL Neurochem. Res. 32:2142-2151(2007).
RN [11]
RP INTERACTION WITH SMN.
RX PubMed=21389246; DOI=10.1523/jneurosci.3631-10.2011;
RA Fallini C., Zhang H., Su Y., Silani V., Singer R.H., Rossoll W.,
RA Bassell G.J.;
RT "The survival of motor neuron (SMN) protein interacts with the mRNA-binding
RT protein HuD and regulates localization of poly(A) mRNA in primary motor
RT neuron axons.";
RL J. Neurosci. 31:3914-3925(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25692578; DOI=10.1371/journal.pone.0117264;
RA Vanevski F., Xu B.;
RT "HuD interacts with Bdnf mRNA and is essential for activity-induced BDNF
RT synthesis in dendrites.";
RL PLoS ONE 10:E0117264-E0117264(2015).
CC -!- FUNCTION: RNA-binding protein that is involved in the post-
CC transcriptional regulation of mRNAs (PubMed:10982410, PubMed:16508003,
CC PubMed:17577668). Plays a role in the regulation of mRNA stability,
CC alternative splicing and translation (PubMed:10982410, PubMed:16508003,
CC PubMed:17577668). Binds to AU-rich element (ARE) sequences in the 3'
CC untranslated region (UTR) of target mRNAs, including GAP43, VEGF, FOS,
CC CDKN1A and ACHE mRNA (PubMed:10982410). Many of the target mRNAs are
CC coding for RNA-binding proteins, transcription factors and proteins
CC involved in RNA processing and/or neuronal development and function (By
CC similarity). By binding to the mRNA 3'UTR, decreases mRNA deadenylation
CC and thereby contributes to the stabilization of mRNA molecules and
CC their protection from decay (By similarity). Also binds to the
CC polyadenylated (poly(A)) tail in the 3'UTR of mRNA, thereby increasing
CC its affinity for mRNA binding (By similarity). Mainly plays a role in
CC neuron-specific RNA processing by stabilization of mRNAs such as GAP43,
CC ACHE and mRNAs of other neuronal proteins, thereby contributing to the
CC differentiation of neural progenitor cells, nervous system development,
CC learning and memory mechanisms (PubMed:10982410, PubMed:17577668).
CC Involved in the negative regulation of the proliferative activity of
CC neuronal stem cells and in the positive regulation of neuronal
CC differentiation of neural progenitor cells (By similarity). Promotes
CC neuronal differentiation of neural stem/progenitor cells in the adult
CC subventricular zone of the hippocampus by binding to and stabilizing
CC SATB1 mRNA (By similarity). Binds and stabilizes MSI1 mRNA in neural
CC stem cells (By similarity). Exhibits increased binding to ACHE mRNA
CC during neuronal differentiation, thereby stabilizing ACHE mRNA and
CC enhancing its expression (By similarity). Protects CDKN1A mRNA from
CC decay by binding to its 3'-UTR (PubMed:16508003). May bind to APP and
CC BACE1 mRNAS and the BACE1AS lncRNA and enhance their stabilization (By
CC similarity). Plays a role in neurite outgrowth and in the establishment
CC and maturation of dendritic arbors, thereby contributing to neocortical
CC and hippocampal circuitry function (By similarity). Stabilizes GAP43
CC mRNA and protects it from decay during postembryonic development in the
CC brain (PubMed:10982410, PubMed:17234598). By promoting the
CC stabilization of GAP43 mRNA, plays a role in NGF-mediated neurite
CC outgrowth (PubMed:10982410). Binds to BDNF long 3'UTR mRNA, thereby
CC leading to its stabilization and increased dendritic translation after
CC activation of PKC (PubMed:25692578). By increasing translation of BDNF
CC after nerve injury, may contribute to nerve regeneration (By
CC similarity). Acts as a stabilizing factor by binding to the 3'UTR of
CC NOVA1 mRNA, thereby increasing its translation and enhancing its
CC functional activity in neuron-specific splicing (By similarity).
CC Stimulates translation of mRNA in a poly(A)- and cap-dependent manner,
CC possibly by associating with the EIF4F cap-binding complex (By
CC similarity). May also negatively regulate translation by binding to the
CC 5'UTR of Ins2 mRNA, thereby repressing its translation (By similarity).
CC Upon glucose stimulation, Ins2 mRNA is released form ELAVL4 and
CC translational inhibition is abolished (By similarity). Also plays a
CC role in the regulation of alternative splicing (By similarity). May
CC regulate alternative splicing of CALCA pre-mRNA into Calcitonin and
CC calcitonin gene-related peptide 1 (CGRP) by competing with splicing
CC regulator TIAR for binding to U-rich sequences of CALCA pre-mRNA (By
CC similarity). {ECO:0000250|UniProtKB:P26378,
CC ECO:0000250|UniProtKB:Q61701, ECO:0000269|PubMed:10982410,
CC ECO:0000269|PubMed:16508003, ECO:0000269|PubMed:17234598,
CC ECO:0000269|PubMed:17577668, ECO:0000269|PubMed:25692578}.
CC -!- SUBUNIT: Component of a TAU mRNP complex, at least composed of IGF2BP1,
CC ELAVL4 and G3BP (By similarity). Associates with the EIF4F cap-binding
CC complex, composed of EIF4G, EIF4A, EIF4E and PABP (By similarity).
CC Within the EIF4F cap-binding complex, interacts with EIF4A (By
CC similarity). Interacts with SMN (via Tudor domain) in an RNA-
CC independent manner; the interaction is required for localization of
CC ELAVL4 to RNA granules (PubMed:21389246). Interacts with MAP1 light
CC chain LC1 (via C-terminus); the interaction contributes to the
CC association of ELAVL4 with microtubules (By similarity). Interacts with
CC MAP1 light chain LC2 (By similarity). {ECO:0000250|UniProtKB:Q61701,
CC ECO:0000269|PubMed:21389246}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11948657,
CC ECO:0000269|PubMed:12957493, ECO:0000269|PubMed:15519747,
CC ECO:0000269|PubMed:16554442}. Perikaryon {ECO:0000269|PubMed:12957493,
CC ECO:0000269|PubMed:25692578}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q61701}. Cell projection, dendrite
CC {ECO:0000269|PubMed:15519747}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q61701}. Note=Co-localizes with ribosomal RNA in
CC polysomes. {ECO:0000269|PubMed:12957493, ECO:0000269|PubMed:15519747}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=At least 3 isoforms are produced.;
CC Name=1;
CC IsoId=O09032-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the hippocampus and cerebral cortex
CC (at protein level) (PubMed:15519747). Expressed in stem and progenitor
CC cells in the subventricular zone of the hippocampus (at protein level)
CC (PubMed:16554442). Expressed in hippocampal neurons, with highest
CC levels of expression in the CA4 and CA3 neurons and lower levels in CA1
CC neurons (at protein level) (PubMed:11948657, PubMed:17577668,
CC PubMed:25692578). Expressed in the dorsal root ganglion (at protein
CC level) (PubMed:12957493). Expressed in the superior cervical ganglion
CC (PubMed:17234598). {ECO:0000269|PubMed:11948657,
CC ECO:0000269|PubMed:12957493, ECO:0000269|PubMed:15519747,
CC ECO:0000269|PubMed:16554442, ECO:0000269|PubMed:17234598,
CC ECO:0000269|PubMed:17577668, ECO:0000269|PubMed:25692578}.
CC -!- DEVELOPMENTAL STAGE: Expression in dentate granule cells of the
CC hippocampus at postnatal day 7, with disappearing expression in dentate
CC granule cells as early as P14. {ECO:0000269|PubMed:17577668}.
CC -!- INDUCTION: Up-regulated by kainic acid-induced seizures
CC (PubMed:17577668). Up-regulated after contextual fear conditioning
CC (PubMed:15519747). Down-regulated at day 2 after axotomy and up-
CC regulated at day 7 after axotomy (PubMed:17234598, PubMed:12957493).
CC {ECO:0000269|PubMed:12957493, ECO:0000269|PubMed:15519747,
CC ECO:0000269|PubMed:17234598, ECO:0000269|PubMed:17577668}.
CC -!- DOMAIN: The RRM 3 domain is required for binding to poly(A) RNA, for
CC the association with polysomes and with the EIF4F cap-binding complex
CC and for the stimulation of translation (By similarity). The RRM 1 and
CC RRM 2 domains may contribute to polysome association and stimulation of
CC translation (By similarity). {ECO:0000250|UniProtKB:Q61701}.
CC -!- PTM: Methylated by CARM1, which leads to reduced RNA-binding activity
CC and enhanced interaction with SMN (By similarity). Methylation at Arg-
CC 248 by CARM1 weakens protective binding to the 3'-UTR of CDKN1A mRNA
CC and down-regulates CDKN1A protein expression, thereby maintaining cells
CC in a proliferative state (PubMed:16508003). Methylation is inhibited by
CC NGF, which facilitates neurite outgrowth (PubMed:16508003).
CC {ECO:0000250|UniProtKB:P26378, ECO:0000269|PubMed:16508003}.
CC -!- DISRUPTION PHENOTYPE: Faster decay of GAP42 mRNA.
CC {ECO:0000269|PubMed:17577668}.
CC -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB50733.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; S83320; AAB50733.1; ALT_INIT; mRNA.
DR EMBL; AABR07049591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07049592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001071119.2; NM_001077651.2. [O09032-1]
DR AlphaFoldDB; O09032; -.
DR SMR; O09032; -.
DR BioGRID; 268628; 1.
DR STRING; 10116.ENSRNOP00000037614; -.
DR iPTMnet; O09032; -.
DR PhosphoSitePlus; O09032; -.
DR jPOST; O09032; -.
DR PaxDb; O09032; -.
DR PRIDE; O09032; -.
DR Ensembl; ENSRNOT00000035252; ENSRNOP00000037614; ENSRNOG00000023601. [O09032-1]
DR GeneID; 432358; -.
DR KEGG; rno:432358; -.
DR UCSC; RGD:1560027; rat. [O09032-1]
DR CTD; 1996; -.
DR RGD; 1560027; Elavl4.
DR eggNOG; KOG0145; Eukaryota.
DR GeneTree; ENSGT00940000157399; -.
DR HOGENOM; CLU_026186_2_0_1; -.
DR InParanoid; O09032; -.
DR OMA; GSEWCIF; -.
DR OrthoDB; 614259at2759; -.
DR PhylomeDB; O09032; -.
DR PRO; PR:O09032; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000023601; Expressed in cerebellum and 9 other tissues.
DR Genevisible; O09032; RN.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0042788; C:polysomal ribosome; IDA:RGD.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:RGD.
DR GO; GO:0003729; F:mRNA binding; IDA:RGD.
DR GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR GO; GO:0097158; F:pre-mRNA intronic pyrimidine-rich binding; ISS:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; IDA:SynGO.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0008306; P:associative learning; IEP:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEP:RGD.
DR GO; GO:0030182; P:neuron differentiation; IMP:RGD.
DR GO; GO:1905870; P:positive regulation of 3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:1900006; P:positive regulation of dendrite development; IMP:RGD.
DR GO; GO:0031099; P:regeneration; IEP:RGD.
DR GO; GO:0043488; P:regulation of mRNA stability; IMP:RGD.
DR GO; GO:0099547; P:regulation of translation at synapse, modulating synaptic transmission; IDA:SynGO.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:RGD.
DR GO; GO:0006396; P:RNA processing; ISS:UniProtKB.
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 Alternative splicing; Cell projection; Cytoplasm; Methylation;
KW mRNA processing; mRNA splicing; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..385
FT /note="ELAV-like protein 4"
FT /id="PRO_0000081585"
FT DOMAIN 51..129
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 137..217
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 302..380
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 12..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61701"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 248
FT /note="Asymmetric dimethylarginine; by CARM1; alternate"
FT /evidence="ECO:0000269|PubMed:16508003"
FT MOD_RES 248
FT /note="Omega-N-methylarginine; by CARM1; alternate"
FT /evidence="ECO:0000269|PubMed:16508003"
SQ SEQUENCE 385 AA; 42368 MW; 1EA9CDAB7E9BC683 CRC64;
MEWNGLKMII STMEPQVSNG PTSNTSNGPS SNNRNCPSPM QTGAATDDSK TNLIVNYLPQ
NMTQEEFRSL FGSIGEIESC KLVRDKITGQ SLGYGFVNYI DPKDAEKAIN TLNGLRLQTK
TIKVSYARPS SASIRDANLY VSGLPKTMTQ KELEQLFSQY GRIITSRILV DQVTGVSRGV
GFIRFDKRIE AEEAIKGLNG QKPSGATEPI TVKFANNPSQ KSSQALLSQL YQSPNRRYPG
PLHHQAQRFR LDNLLNMAYG VKRLMSGPVP PSACPPRFSP ITIDGMTSLV GMNIPGHTGT
GWCIFVYNLS PDSDESVLWQ LFGPFGAVNN VKVIRDFNTN KCKGFGFVTM TNYDEAAMAI
ASLNGYRLGD RVLQVSFKTN KAHKS
