ELAV4_MOUSE
ID ELAV4_MOUSE Reviewed; 385 AA.
AC Q61701; A2A9R6; A2A9R7; A2A9R8; A2A9S0; A2A9S1; A2A9S2; A2A9S3; O55010;
AC Q6PHZ3; Q8BVA9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
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 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), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8535975; DOI=10.1093/dnares/1.4.175;
RA Abe R., Uyeno Y., Yamamoto K., Sakamoto H.;
RT "Tissue-specific expression of the gene encoding a mouse RNA binding
RT protein homologous to human HuD antigen.";
RL DNA Res. 1:175-180(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9096138; DOI=10.1523/jneurosci.17-09-03024.1997;
RA Okano H.J., Darnell R.B.;
RT "A hierarchy of Hu RNA binding proteins in developing and adult neurons.";
RL J. Neurosci. 17:3024-3037(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=ICR;
RX PubMed=9524251; DOI=10.1016/s0378-1119(97)00615-x;
RA Inman M.V., Levy S., Mock B.A., Owens G.C.;
RT "Gene organization and chromosome location of the neural-specific RNA
RT binding protein Elavl4.";
RL Gene 208:139-145(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC37532.1};
RC TISSUE=Diencephalon {ECO:0000312|EMBL:BAC37532.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 5; 6; 7; 8; 9 AND 10),
RP ALTERNATIVE INITIATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22895702; DOI=10.1523/jneurosci.2247-12.2012;
RA Bronicki L.M., Belanger G., Jasmin B.J.;
RT "Characterization of multiple exon 1 variants in mammalian HuD mRNA and
RT neuron-specific transcriptional control via neurogenin 2.";
RL J. Neurosci. 32:11164-11175(2012).
RN [7]
RP TISSUE SPECIFICITY, AND INDUCTION BY MEMORY TRAINING.
RX PubMed=11573004; DOI=10.1073/pnas.191388398;
RA Quattrone A., Pascale A., Nogues X., Zhao W., Gusev P., Pacini A.,
RA Alkon D.L.;
RT "Posttranscriptional regulation of gene expression in learning by the
RT neuronal ELAV-like mRNA-stabilizing proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11668-11673(2001).
RN [8]
RP IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP1 AND G3BP, AND INTERACTION
RP WITH IGF2BP1.
RX PubMed=15086518; DOI=10.1111/j.1471-4159.2004.02371.x;
RA Atlas R., Behar L., Elliott E., Ginzburg I.;
RT "The insulin-like growth factor mRNA binding-protein IMP-1 and the Ras-
RT regulatory protein G3BP associate with tau mRNA and HuD protein in
RT differentiated P19 neuronal cells.";
RL J. Neurochem. 89:613-626(2004).
RN [9]
RP TISSUE SPECIFICITY.
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 [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15764704; DOI=10.1073/pnas.0407523102;
RA Akamatsu W., Fujihara H., Mitsuhashi T., Yano M., Shibata S., Hayakawa Y.,
RA Okano H.J., Sakakibara S., Takano H., Takano T., Takahashi T., Noda T.,
RA Okano H.;
RT "The RNA-binding protein HuD regulates neuronal cell identity and
RT maturation.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4625-4630(2005).
RN [11]
RP FUNCTION, 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 [12]
RP FUNCTION.
RX PubMed=17035636; DOI=10.1091/mbc.e06-02-0099;
RA Zhu H., Hasman R.A., Barron V.A., Luo G., Lou H.;
RT "A nuclear function of Hu proteins as neuron-specific alternative RNA
RT processing regulators.";
RL Mol. Biol. Cell 17:5105-5114(2006).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=18493953; DOI=10.1002/hipo.20442;
RA Tanner D.C., Qiu S., Bolognani F., Partridge L.D., Weeber E.J.,
RA Perrone-Bizzozero N.I.;
RT "Alterations in mossy fiber physiology and GAP-43 expression and function
RT in transgenic mice overexpressing HuD.";
RL Hippocampus 18:814-823(2008).
RN [14]
RP FUNCTION.
RX PubMed=18218628; DOI=10.1074/jbc.m706082200;
RA Ratti A., Fallini C., Colombrita C., Pascale A., Laforenza U.,
RA Quattrone A., Silani V.;
RT "Post-transcriptional regulation of neuro-oncological ventral antigen 1 by
RT the neuronal RNA-binding proteins ELAV.";
RL J. Biol. Chem. 283:7531-7541(2008).
RN [15]
RP FUNCTION, INTERACTION WITH ELF4, DOMAIN, AND MUTAGENESIS OF ARG-277;
RP PHE-278; SER-279; PRO-280 AND 303-CYS--SER-385.
RX PubMed=20064466; DOI=10.1016/j.molcel.2009.11.013;
RA Fukao A., Sasano Y., Imataka H., Inoue K., Sakamoto H., Sonenberg N.,
RA Thoma C., Fujiwara T.;
RT "The ELAV protein HuD stimulates cap-dependent translation in a
RT Poly(A)- and eIF4A-dependent manner.";
RL Mol. Cell 36:1007-1017(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-233, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [17]
RP INTERACTION WITH MAP1 LIGHT CHAIN LC1 AND MAP1 LIGHT CHAIN LC2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21288476; DOI=10.1016/j.biochi.2011.01.008;
RA Fujiwara Y., Kasashima K., Saito K., Fukuda M., Fukao A., Sasano Y.,
RA Inoue K., Fujiwara T., Sakamoto H.;
RT "Microtubule association of a neuronal RNA-binding protein HuD through its
RT binding to the light chain of MAP1B.";
RL Biochimie 93:817-822(2011).
RN [18]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [19]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY GLUCOSE
RP AND BY INSULIN, AND DISRUPTION PHENOTYPE.
RX PubMed=22387028; DOI=10.1016/j.molcel.2012.01.016;
RA Lee E.K., Kim W., Tominaga K., Martindale J.L., Yang X., Subaran S.S.,
RA Carlson O.D., Mercken E.M., Kulkarni R.N., Akamatsu W., Okano H.,
RA Perrone-Bizzozero N.I., de Cabo R., Egan J.M., Gorospe M.;
RT "RNA-binding protein HuD controls insulin translation.";
RL Mol. Cell 45:826-835(2012).
RN [20]
RP FUNCTION.
RX PubMed=23383270; DOI=10.1371/journal.pone.0055718;
RA Allen M., Bird C., Feng W., Liu G., Li W., Perrone-Bizzozero N.I., Feng Y.;
RT "HuD promotes BDNF expression in brain neurons via selective stabilization
RT of the BDNF long 3'UTR mRNA.";
RL PLoS ONE 8:E55718-E55718(2013).
RN [21]
RP TISSUE SPECIFICITY.
RX PubMed=24857657; DOI=10.1016/j.celrep.2014.04.050;
RA Kang M.J., Abdelmohsen K., Hutchison E.R., Mitchell S.J., Grammatikakis I.,
RA Guo R., Noh J.H., Martindale J.L., Yang X., Lee E.K., Faghihi M.A.,
RA Wahlestedt C., Troncoso J.C., Pletnikova O., Perrone-Bizzozero N.,
RA Resnick S.M., de Cabo R., Mattson M.P., Gorospe M.;
RT "HuD regulates coding and noncoding RNA to induce APP[?]Abeta processing.";
RL Cell Rep. 7:1401-1409(2014).
RN [22]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24599466; DOI=10.1523/jneurosci.3703-13.2014;
RA DeBoer E.M., Azevedo R., Vega T.A., Brodkin J., Akamatsu W., Okano H.,
RA Wagner G.C., Rasin M.R.;
RT "Prenatal deletion of the RNA-binding protein HuD disrupts postnatal
RT cortical circuit maturation and behavior.";
RL J. Neurosci. 34:3674-3686(2014).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-149 AND THR-165.
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).
RN [24]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY DIFFERENTIATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26305964; DOI=10.1073/pnas.1513780112;
RA Wang F., Tidei J.J., Polich E.D., Gao Y., Zhao H., Perrone-Bizzozero N.I.,
RA Guo W., Zhao X.;
RT "Positive feedback between RNA-binding protein HuD and transcription factor
RT SATB1 promotes neurogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E4995-E5004(2015).
RN [25]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY NERVE INJURY.
RX PubMed=28111162; DOI=10.1016/j.brainres.2017.01.019;
RA Sanna M.D., Ghelardini C., Galeotti N.;
RT "HuD-mediated distinct BDNF regulatory pathways promote regeneration after
RT nerve injury.";
RL Brain Res. 1659:55-63(2017).
CC -!- FUNCTION: RNA-binding protein that is involved in the post-
CC transcriptional regulation of mRNAs (PubMed:15764704, PubMed:16554442,
CC PubMed:17035636, PubMed:20064466, PubMed:22387028, PubMed:23383270,
CC PubMed:26305964, PubMed:28111162). Plays a role in the regulation of
CC mRNA stability, alternative splicing and translation (PubMed:15764704,
CC PubMed:23383270, PubMed:26305964, PubMed:28111162). Binds to AU-rich
CC element (ARE) sequences in the 3' untranslated region (3'UTR) of target
CC mRNAs, including GAP43, VEGF, FOS, CDKN1A and ACHE mRNA (By
CC similarity). Many of the target mRNAs are coding for RNA-binding
CC proteins, transcription factors and proteins involved in RNA processing
CC and/or neuronal development and function (PubMed:26305964). By binding
CC to the mRNA 3'UTR, decreases mRNA deadenylation and thereby contributes
CC to the stabilization of mRNA molecules and their protection from decay
CC (By similarity). Also binds to the polyadenylated (poly(A)) tail in the
CC 3'UTR of mRNA, thereby increasing its affinity for mRNA binding
CC (PubMed:20064466). Mainly plays a role in neuron-specific RNA
CC processing by stabilization of mRNAs such as GAP43, ACHE and mRNAs of
CC other neuronal proteins, thereby contributing to the differentiation of
CC neural progenitor cells, nervous system development, learning and
CC memory mechanisms (PubMed:15764704, PubMed:16554442, PubMed:18218628,
CC PubMed:23383270, PubMed:24599466, PubMed:25692578, PubMed:26305964,
CC PubMed:28111162). Involved in the negative regulation of the
CC proliferative activity of neuronal stem cells and in the positive
CC regulation of neuronal differentiation of neural progenitor cells
CC (PubMed:15764704). Promotes neuronal differentiation of neural
CC stem/progenitor cells in the adult subventricular zone of the
CC hippocampus by binding to and stabilizing SATB1 mRNA (PubMed:26305964).
CC Binds and stabilizes MSI1 mRNA in neural stem cells (PubMed:16554442).
CC Exhibits increased binding to ACHE mRNA during neuronal
CC differentiation, thereby stabilizing ACHE mRNA and enhancing its
CC expression (By similarity). Protects CDKN1A mRNA from decay by binding
CC to its 3'-UTR (By similarity). May bind to APP and BACE1 mRNAS and the
CC BACE1AS lncRNA and enhance their stabilization (By similarity). Plays a
CC role in neurite outgrowth and in the establishment and maturation of
CC dendritic arbors, thereby contributing to neocortical and hippocampal
CC circuitry function (PubMed:24599466). Stabilizes GAP43 mRNA and
CC protects it from decay during postembryonic development in the brain
CC (PubMed:28111162). By promoting the stabilization of GAP43 mRNA, plays
CC a role in NGF-mediated neurite outgrowth (By similarity). Binds to BDNF
CC long 3'UTR mRNA, thereby leading to its stabilization and increased
CC dendritic translation after activation of PKC (PubMed:23383270,
CC PubMed:25692578). By increasing translation of BDNF after nerve injury,
CC may contribute to nerve regeneration (PubMed:28111162). Acts as a
CC stabilizing factor by binding to the 3'UTR of NOVA1 mRNA, thereby
CC increasing its translation and enhancing its functional activity in
CC neuron-specific splicing (PubMed:18218628). Stimulates translation of
CC mRNA in a poly(A)- and cap-dependent manner, possibly by associating
CC with the EIF4F cap-binding complex (PubMed:20064466). May also
CC negatively regulate translation by binding to the 5'UTR of Ins2 mRNA,
CC thereby repressing its translation (PubMed:22387028). Upon glucose
CC stimulation, Ins2 mRNA is released from ELAVL4 and translational
CC inhibition is abolished (PubMed:22387028). Also plays a role in the
CC regulation of alternative splicing (PubMed:17035636). May regulate
CC alternative splicing of CALCA pre-mRNA into Calcitonin and Calcitonin
CC gene-related peptide 1 (CGRP) by competing with splicing regulator TIAR
CC for binding to U-rich sequences of CALCA pre-mRNA (PubMed:17035636).
CC {ECO:0000250|UniProtKB:O09032, ECO:0000250|UniProtKB:P26378,
CC ECO:0000269|PubMed:15764704, ECO:0000269|PubMed:16554442,
CC ECO:0000269|PubMed:17035636, ECO:0000269|PubMed:18218628,
CC ECO:0000269|PubMed:20064466, ECO:0000269|PubMed:22387028,
CC ECO:0000269|PubMed:23383270, ECO:0000269|PubMed:24599466,
CC ECO:0000269|PubMed:25692578, ECO:0000269|PubMed:26305964,
CC ECO:0000269|PubMed:28111162}.
CC -!- SUBUNIT: Component of a TAU mRNP complex, at least composed of IGF2BP1,
CC ELAVL4 and G3BP (PubMed:15086518). Associates with the EIF4F cap-
CC binding complex, composed of EIF4G, EIF4A, EIF4E and PABP
CC (PubMed:20064466). Within the EIF4F cap-binding complex, interacts with
CC EIF4A (PubMed:20064466). Interacts with SMN (via Tudor domain) in an
CC RNA-independent manner; the interaction is required for localization of
CC ELAVL4 to RNA granules (By similarity). Interacts with MAP1 light chain
CC LC1 (via C-terminus); the interaction contributes to the association of
CC ELAVL4 with microtubules (PubMed:21288476). Interacts with MAP1 light
CC chain LC2 (PubMed:21288476). {ECO:0000250|UniProtKB:P26378,
CC ECO:0000269|PubMed:15086518, ECO:0000269|PubMed:20064466,
CC ECO:0000269|PubMed:21288476}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16554442,
CC ECO:0000269|PubMed:21288476, ECO:0000269|PubMed:22387028}. Perikaryon
CC {ECO:0000269|PubMed:21389246}. Cell projection, dendrite
CC {ECO:0000269|PubMed:25692578}. Cell projection, axon
CC {ECO:0000269|PubMed:21389246}. Cell projection, growth cone
CC {ECO:0000269|PubMed:21389246}. Note=Co-localizes with ribosomal RNA in
CC polysomes. {ECO:0000250|UniProtKB:O09032}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=10;
CC Name=1; Synonyms=Long;
CC IsoId=Q61701-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q61701-2; Sequence=VSP_005792;
CC Name=3; Synonyms=sv1 {ECO:0000303|PubMed:9096138}, E1b
CC {ECO:0000303|PubMed:22895702};
CC IsoId=Q61701-4; Sequence=VSP_060287;
CC Name=4; Synonyms=sv2 {ECO:0000303|PubMed:9096138};
CC IsoId=Q61701-5; Sequence=VSP_060287, VSP_060290;
CC Name=5; Synonyms=E1a {ECO:0000303|PubMed:22895702};
CC IsoId=Q61701-6; Sequence=VSP_060284, VSP_005792;
CC Name=6; Synonyms=E1a1 {ECO:0000303|PubMed:22895702};
CC IsoId=Q61701-7; Sequence=VSP_060285, VSP_060290;
CC Name=7; Synonyms=E1a2 {ECO:0000303|PubMed:22895702};
CC IsoId=Q61701-8; Sequence=VSP_060286, VSP_060289;
CC Name=8; Synonyms=E1a3 {ECO:0000303|PubMed:22895702};
CC IsoId=Q61701-9; Sequence=VSP_060288, VSP_060290;
CC Name=9; Synonyms=E1c {ECO:0000303|PubMed:22895702};
CC IsoId=Q61701-10; Sequence=VSP_060290;
CC Name=10; Synonyms=E1c1 {ECO:0000303|PubMed:22895702};
CC IsoId=Q61701-11; Sequence=VSP_060291;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, including the hippocampus,
CC and in pancreatic beta cells (at protein level) (PubMed:22387028,
CC PubMed:18493953, PubMed:15764704, PubMed:24599466). Expressed in
CC pyramidal neurons of the hippocampal CA3 and CA1 region and in the
CC hilus but not in dentate granule cells (at protein level)
CC (PubMed:15519747). Expressed in the dorsal root ganglion and the spinal
CC cord (at protein level) (PubMed:17035636, PubMed:28111162). Expressed
CC in neural stem and progenitor cells (at protein level)
CC (PubMed:16554442). Expressed in radial glia-like cells and in transient
CC amplifying cells in the subventricular zone (SVZ), and in immature
CC neurons both in the SVZ and the rostral migratory stream as well as in
CC mature neurons in the olfactory bulb (at protein level)
CC (PubMed:26305964). Expressed in testis and in the brain, including the
CC hippocampus, the neocortex and the cerebellum (PubMed:8535975,
CC PubMed:11573004, PubMed:24857657). Expressed in lower- but not upper-
CC layer primary neurons of the mature neocortex, in the hippocampal
CC regions CA1-3 and the dentate gyrus (PubMed:24599466, PubMed:9096138).
CC Expressed in the mitral and granule cells of the olfactory bulb,
CC cerebral cortex, entorhinal cortex, thalamus, medial habenula,
CC amygdala, granule cells of the cerebellum, pons, olivary nucleus,
CC dorsal and ventral spinal cord and in dorsal root ganglia
CC (PubMed:9096138). Expressed in motor neurons (PubMed:21389246). Isoform
CC 4: Expressed in the brain (PubMed:9096138, PubMed:22895702). Isoform 5:
CC Expressed in the brain (PubMed:9096138). Isoform 6: Expressed in the
CC brain (PubMed:22895702). Isoform 7: Expressed in the brain
CC (PubMed:22895702). Isoform 8: Expressed in the brain (PubMed:22895702).
CC Isoform 9: Expressed in the brain (PubMed:22895702). Isoform 10:
CC Expressed in the brain (PubMed:22895702). Isoform 11: Expressed in the
CC brain (PubMed:22895702). {ECO:0000269|PubMed:11573004,
CC ECO:0000269|PubMed:15519747, ECO:0000269|PubMed:15764704,
CC ECO:0000269|PubMed:16554442, ECO:0000269|PubMed:17035636,
CC ECO:0000269|PubMed:18493953, ECO:0000269|PubMed:21389246,
CC ECO:0000269|PubMed:22387028, ECO:0000269|PubMed:22895702,
CC ECO:0000269|PubMed:24599466, ECO:0000269|PubMed:24857657,
CC ECO:0000269|PubMed:26305964, ECO:0000269|PubMed:28111162,
CC ECO:0000269|PubMed:8535975, ECO:0000269|PubMed:9096138}.
CC -!- DEVELOPMENTAL STAGE: At 14 dpc, expressed in the intermediate zone of
CC the cortex (PubMed:9096138). At 15 dpc, high expression in the
CC neocortex, with decreased expression at postnatal day 7 and in
CC adulthood (PubMed:24599466). At 16 dpc and at birth, expressed in the
CC retina, thalamus, hypothalamus, midbrain, pons, dorsal and ventral
CC spinal cord, and the dorsal root ganglia (PubMed:9096138). At birth,
CC expressed in the nasal epithelium, olfactory bulb, trigeminal ganglia,
CC cerebral cortex, the pyramidal cells of the hippocampus and the
CC sympathetic ganglia (PubMed:9096138). Widely expressed in the
CC cerebellum at postnatal day 9 (PubMed:9096138). Isoform 4: Highly
CC expressed in the brain at 10 dpc to 14 dpc, with decreased expression
CC at 16 dpc and at postnatal day 8 (PubMed:9096138). Isoform 5: Highly
CC expressed in the brain at 10 dpc, with decreased expression at 16 dpc
CC and at postnatal day 8 (PubMed:9096138). Isoform 6: Expressed in the
CC brain at 14 dpc (PubMed:22895702). Isoform 7: Expressed in the brain at
CC 14 dpc (PubMed:9096138). Isoform 8: Expressed in the brain at 14 dpc
CC (PubMed:9096138). Isoform 9: Expressed in the brain at 14 dpc
CC (PubMed:9096138). Isoform 10: Expressed in the brain at 14 dpc,
CC including the amygdala, hippocampus and cerebral cortex, and strong
CC expression in the olfactory bulb and retina (PubMed:22895702). Isoform
CC 11: Expressed in the brain at 14 dpc (PubMed:9096138).
CC {ECO:0000269|PubMed:22895702, ECO:0000269|PubMed:24599466,
CC ECO:0000269|PubMed:9096138}.
CC -!- INDUCTION: Up-regulated by glucose and by insulin (PubMed:22387028).
CC Up-regulated after memory training in radial arm maze experiments
CC (PubMed:11573004). Up-regulated after sciatic nerve injury
CC (PubMed:28111162). Up-regulated during adult neuronal stem cell
CC differentiation (PubMed:26305964). {ECO:0000269|PubMed:11573004,
CC ECO:0000269|PubMed:22387028, ECO:0000269|PubMed:26305964,
CC ECO:0000269|PubMed:28111162}.
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 (PubMed:20064466). The RRM 1 and
CC RRM 2 domains may contribute to polysome association and stimulation of
CC translation (PubMed:20064466). {ECO:0000269|PubMed:20064466}.
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 and
CC down-regulates CDKN1A protein expression, thereby maintaining cells in
CC a proliferative state (By similarity). Methylation is inhibited by NGF,
CC which facilitates neurite outgrowth (By similarity).
CC {ECO:0000250|UniProtKB:O09032, ECO:0000250|UniProtKB:P26378}.
CC -!- DISRUPTION PHENOTYPE: Transiently impaired neurite extensions of
CC several cranial nerves, including glossopharyngeal nerve, hypoglossal
CC nerve, trigeminal nerve and acousticofacial nerves in the midembryonic
CC nervous system at 10.5 dpc, however no developmental delays of the
CC nervous system in later-stage embryos at 14 dpc are obvious
CC (PubMed:15764704). By postnatal weeks 4 to 8, 70-80% of the mice
CC exhibit an abnormal clasping reflex of the hind limbs upon being
CC suspended by the tail (PubMed:15764704). Decreased motor coordination,
CC as impaired performance on an accelerating rotarod is observed
CC (PubMed:15764704). Embryonic neural stem cells exhibit enhanced cell
CC renewal capacity and decreased ability to differentiate into neurons
CC (PubMed:15764704). Failure of neural progenitor cells to leave the cell
CC cycle, resulting in increased apoptosis and in reduced production of
CC postmitotic neurons (PubMed:15764704). Increased number of slowly
CC dividing cells in the subventricular zone (PubMed:15764704). High
CC insulin levels in pancreatic beta cells (PubMed:22387028). At 28 dpc, a
CC decreased number of lower layer neocortical neurons is observed and
CC lower layer neocortical neurons and CA3 hippocampal neurons exhibit a
CC decreased dendritic complexity with fewer basal and apical
CC branchpoints, fewer branch endings and shorter basal dendrites
CC (PubMed:24599466). Basal branching deficiency in neocortical lower
CC layer neurons and in hippocampal CA3 neurons persists into adulthood at
CC 90 dpc (PubMed:24599466). Increased time spent in low-energy-expending
CC activities and less in the high-energy activity of locomotion,
CC indicating an anxiety response (PubMed:24599466). Decreased performance
CC in finding a hidden platform in a water bath (Morris water maze test),
CC suggesting difficulty in learning, lack of avoidance of the open arm in
CC a elevated plus maze test, suggesting an aberrant response to anxiety-
CC producing environments, and higher susceptibility to auditory-induced
CC seizures (PubMed:24599466). RNAi-mediated knockdown in the neocortex at
CC 13.5 dpc results in reduced neurite outgrowth (PubMed:24599466). RNAi-
CC mediated knockdown in neural stem/progenitor cells in the adult
CC subventricular zone impairs early neuronal differentiation
CC (PubMed:26305964). {ECO:0000269|PubMed:15764704,
CC ECO:0000269|PubMed:22387028, ECO:0000269|PubMed:24599466,
CC ECO:0000269|PubMed:26305964}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation.
CC {ECO:0000303|PubMed:22895702}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
CC 4. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative initiation.
CC {ECO:0000303|PubMed:22895702}.
CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative initiation.
CC {ECO:0000303|PubMed:22895702}.
CC -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative initiation.
CC {ECO:0000303|PubMed:22895702}.
CC -!- MISCELLANEOUS: [Isoform 8]: Produced by alternative initiation.
CC {ECO:0000303|PubMed:22895702}.
CC -!- MISCELLANEOUS: [Isoform 9]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 10]: Produced by alternative initiation.
CC {ECO:0000303|PubMed:22895702}.
CC -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000305}.
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DR EMBL; D31953; BAA06723.1; -; mRNA.
DR EMBL; AF041341; AAC40080.1; -; mRNA.
DR EMBL; BC052451; AAH52451.2; -; mRNA.
DR EMBL; AK079088; BAC37532.1; -; mRNA.
DR EMBL; AL627425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18470.1; -. [Q61701-4]
DR CCDS; CCDS18471.1; -. [Q61701-1]
DR CCDS; CCDS51261.1; -. [Q61701-10]
DR CCDS; CCDS51262.1; -. [Q61701-6]
DR CCDS; CCDS84777.1; -. [Q61701-5]
DR PIR; JC2298; JC2298.
DR RefSeq; NP_001033787.1; NM_001038698.1. [Q61701-4]
DR RefSeq; NP_001334107.1; NM_001347178.1. [Q61701-5]
DR RefSeq; NP_034618.2; NM_010488.4. [Q61701-1]
DR RefSeq; XP_006502862.1; XM_006502799.3. [Q61701-9]
DR AlphaFoldDB; Q61701; -.
DR SMR; Q61701; -.
DR BioGRID; 200486; 20.
DR IntAct; Q61701; 5.
DR MINT; Q61701; -.
DR STRING; 10090.ENSMUSP00000102207; -.
DR iPTMnet; Q61701; -.
DR PhosphoSitePlus; Q61701; -.
DR MaxQB; Q61701; -.
DR PaxDb; Q61701; -.
DR PeptideAtlas; Q61701; -.
DR PRIDE; Q61701; -.
DR ProteomicsDB; 275737; -. [Q61701-1]
DR ProteomicsDB; 275738; -. [Q61701-2]
DR ProteomicsDB; 320612; -.
DR ProteomicsDB; 333003; -.
DR ProteomicsDB; 345023; -.
DR ProteomicsDB; 345265; -.
DR ProteomicsDB; 349412; -.
DR ProteomicsDB; 349699; -.
DR ProteomicsDB; 350897; -.
DR Antibodypedia; 3839; 254 antibodies from 29 providers.
DR DNASU; 15572; -.
DR Ensembl; ENSMUST00000102722; ENSMUSP00000099783; ENSMUSG00000028546. [Q61701-10]
DR Ensembl; ENSMUST00000102723; ENSMUSP00000099784; ENSMUSG00000028546. [Q61701-4]
DR Ensembl; ENSMUST00000106597; ENSMUSP00000102207; ENSMUSG00000028546. [Q61701-1]
DR Ensembl; ENSMUST00000106598; ENSMUSP00000102208; ENSMUSG00000028546. [Q61701-5]
DR Ensembl; ENSMUST00000106600; ENSMUSP00000102210; ENSMUSG00000028546. [Q61701-9]
DR Ensembl; ENSMUST00000106601; ENSMUSP00000102212; ENSMUSG00000028546. [Q61701-7]
DR Ensembl; ENSMUST00000106603; ENSMUSP00000102214; ENSMUSG00000028546. [Q61701-6]
DR Ensembl; ENSMUST00000142722; ENSMUSP00000121828; ENSMUSG00000028546. [Q61701-8]
DR GeneID; 15572; -.
DR KEGG; mmu:15572; -.
DR UCSC; uc008ucw.1; mouse. [Q61701-1]
DR UCSC; uc008ucx.1; mouse.
DR CTD; 1996; -.
DR MGI; MGI:107427; Elavl4.
DR VEuPathDB; HostDB:ENSMUSG00000028546; -.
DR eggNOG; KOG0145; Eukaryota.
DR GeneTree; ENSGT00940000157399; -.
DR HOGENOM; CLU_026186_2_0_1; -.
DR InParanoid; Q61701; -.
DR OMA; GSEWCIF; -.
DR OrthoDB; 614259at2759; -.
DR PhylomeDB; Q61701; -.
DR TreeFam; TF313377; -.
DR BioGRID-ORCS; 15572; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Elavl4; mouse.
DR PRO; PR:Q61701; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q61701; protein.
DR Bgee; ENSMUSG00000028546; Expressed in habenula and 167 other tissues.
DR ExpressionAtlas; Q61701; baseline and differential.
DR Genevisible; Q61701; MM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0042788; C:polysomal ribosome; ISO:MGI.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
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; ISO:MGI.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IDA:MGI.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0030182; P:neuron differentiation; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0031099; P:regeneration; IEA:Ensembl.
DR GO; GO:0043488; P:regulation of mRNA stability; ISO:MGI.
DR GO; GO:0099547; P:regulation of translation at synapse, modulating synaptic transmission; ISO:MGI.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
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 initiation; Alternative splicing; Cell projection; Cytoplasm;
KW Methylation; mRNA processing; mRNA splicing; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..385
FT /note="ELAV-like protein 4"
FT /id="PRO_0000081584"
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:0007744|PubMed:21183079"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 248
FT /note="Asymmetric dimethylarginine; by CARM1; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26378"
FT MOD_RES 248
FT /note="Omega-N-methylarginine; by CARM1; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26378"
FT VAR_SEQ 1..8
FT /note="MEWNGLKM -> MPNALLFQCLCSR (in isoform 10)"
FT /id="VSP_060291"
FT VAR_SEQ 1..8
FT /note="MEWNGLKM -> MRLQNQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:22895702"
FT /id="VSP_060284"
FT VAR_SEQ 1..8
FT /note="MEWNGLKM -> MEQ (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:22895702"
FT /id="VSP_060285"
FT VAR_SEQ 1..8
FT /note="MEWNGLKM -> MFEISRTLNAALLNNE (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:22895702"
FT /id="VSP_060286"
FT VAR_SEQ 1..7
FT /note="MEWNGLK -> MV (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9096138"
FT /id="VSP_060287"
FT VAR_SEQ 1..7
FT /note="MEWNGLK -> MGLLLLREIVINESRNCSF (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:22895702"
FT /id="VSP_060288"
FT VAR_SEQ 85..385
FT /note="Missing (in isoform 7)"
FT /id="VSP_060289"
FT VAR_SEQ 251..277
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:22895702,
FT ECO:0000303|PubMed:9524251"
FT /id="VSP_005792"
FT VAR_SEQ 264..277
FT /note="Missing (in isoform 4, isoform 6, isoform 8 and
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:22895702,
FT ECO:0000303|PubMed:9096138"
FT /id="VSP_060290"
FT MUTAGEN 1..215
FT /note="Missing: Reduced association with polysomes and
FT reduced stimulation of translation."
FT /evidence="ECO:0000269|PubMed:20064466"
FT MUTAGEN 149
FT /note="T->A: Decreased dendritic localization and decreased
FT translation of reporter mRNA, when associated with Ala-
FT 165."
FT /evidence="ECO:0000269|PubMed:25692578"
FT MUTAGEN 165
FT /note="T->A: Decreased dendritic localization and decreased
FT translation of reporter mRNA, when associated with Ala-
FT 149."
FT /evidence="ECO:0000269|PubMed:25692578"
FT MUTAGEN 277
FT /note="R->A: No impact on interaction with EIF4A."
FT /evidence="ECO:0000269|PubMed:20064466"
FT MUTAGEN 278
FT /note="F->A: Disrupts interaction with EIF4A and fails to
FT stimulate translation."
FT /evidence="ECO:0000269|PubMed:20064466"
FT MUTAGEN 279
FT /note="S->A: No impact on interaction with EIF4A."
FT /evidence="ECO:0000269|PubMed:20064466"
FT MUTAGEN 280
FT /note="P->A: No impact on interaction with EIF4A."
FT /evidence="ECO:0000269|PubMed:20064466"
FT MUTAGEN 303..385
FT /note="Missing: Loss of association with polysomes and loss
FT of translation stimulation."
FT /evidence="ECO:0000269|PubMed:20064466"
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
