ID   ELAV3_MOUSE             Reviewed;         367 AA.
AC   Q60900; Q60901;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=ELAV-like protein 3;
DE   AltName: Full=Hu-antigen C;
DE            Short=HuC;
GN   Name=Elavl3; Synonyms=Huc;
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] (ISOFORMS HUC-L AND HUC-S), FUNCTION, DOMAIN,
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9016658; DOI=10.1093/nar/24.24.4895;
RA   Abe R., Sakashita E., Yamamoto K., Sakamoto H.;
RT   "Two different RNA binding activities for the AU-rich element and the
RT   poly(A) sequence of the mouse neuronal protein mHuC.";
RL   Nucleic Acids Res. 24:4895-4901(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HUC-L).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, INDUCTION BY MEMORY TRAINING, AND DISRUPTION
RP   PHENOTYPE.
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   [4]
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   [5]
RP   INTERACTION WITH MAP1B LIGHT CHAIN LC1.
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   [6]
RP   STRUCTURE BY NMR OF 36-208, RNA-BINDING, FUNCTION, AND DOMAIN.
RX   PubMed=10734193; DOI=10.1093/nar/28.8.1743;
RA   Inoue M., Muto Y., Sakamoto H., Yokoyama S.;
RT   "NMR studies on functional structures of the AU-rich element-binding
RT   domains of Hu antigen C.";
RL   Nucleic Acids Res. 28:1743-1750(2000).
CC   -!- FUNCTION: RNA-binding protein that binds to AU-rich element (ARE)
CC       sequences of target mRNAs, including VEGF mRNA (PubMed:10734193,
CC       PubMed:9016658). May also bind poly-A tracts via RRM 3
CC       (PubMed:9016658). May be involved in neuronal differentiation and
CC       maintenance (PubMed:9016658). Plays a role in the stabilization of
CC       GAP43 mRNA and in spatial learning (PubMed:11573004).
CC       {ECO:0000269|PubMed:10734193, ECO:0000269|PubMed:11573004,
CC       ECO:0000269|PubMed:9016658, ECO:0000303|PubMed:9016658}.
CC   -!- SUBUNIT: Interacts with MAP1B light chain LC1.
CC       {ECO:0000269|PubMed:21288476}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=HuC-L;
CC         IsoId=Q60900-1; Sequence=Displayed;
CC       Name=HuC-S;
CC         IsoId=Q60900-2; Sequence=VSP_005790;
CC   -!- TISSUE SPECIFICITY: Brain specific (PubMed:9016658). Expressed in the
CC       hippocampus with expression in CA1, CA3 and dentate gyrus
CC       (PubMed:11573004). {ECO:0000269|PubMed:11573004,
CC       ECO:0000269|PubMed:9016658}.
CC   -!- INDUCTION: Up-regulated after spatial learning in radial arm maze
CC       experiments and in Morris water maze experiments.
CC       {ECO:0000269|PubMed:11573004}.
CC   -!- DOMAIN: RRM 1 and RRM 2 bind cooperatively to AU-rich sequences in
CC       target mRNAs. RRM 3 binds to poly-A mRNA sequences.
CC       {ECO:0000269|PubMed:10734193, ECO:0000269|PubMed:9016658}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced Gap43
CC       mRNA levels and impaired learning behavior in radial arm maze training.
CC       {ECO:0000269|PubMed:11573004}.
CC   -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000305}.
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DR   EMBL; U29148; AAC52999.1; -; mRNA.
DR   EMBL; U29149; AAC53000.1; -; mRNA.
DR   EMBL; BC052097; AAH52097.1; -; mRNA.
DR   CCDS; CCDS52741.1; -. [Q60900-1]
DR   RefSeq; NP_034617.1; NM_010487.2. [Q60900-1]
DR   RefSeq; XP_006510085.1; XM_006510022.1. [Q60900-2]
DR   PDB; 1D8Z; NMR; -; A=36-123.
DR   PDB; 1D9A; NMR; -; A=124-208.
DR   PDB; 1FNX; NMR; -; H=36-208.
DR   PDBsum; 1D8Z; -.
DR   PDBsum; 1D9A; -.
DR   PDBsum; 1FNX; -.
DR   AlphaFoldDB; Q60900; -.
DR   SMR; Q60900; -.
DR   BioGRID; 200485; 16.
DR   IntAct; Q60900; 4.
DR   MINT; Q60900; -.
DR   STRING; 10090.ENSMUSP00000003501; -.
DR   iPTMnet; Q60900; -.
DR   PhosphoSitePlus; Q60900; -.
DR   SwissPalm; Q60900; -.
DR   MaxQB; Q60900; -.
DR   PaxDb; 10090-ENSMUSP00000003501; -.
DR   PeptideAtlas; Q60900; -.
DR   ProteomicsDB; 275657; -. [Q60900-1]
DR   ProteomicsDB; 275658; -. [Q60900-2]
DR   Antibodypedia; 25887; 207 antibodies from 27 providers.
DR   DNASU; 15571; -.
DR   Ensembl; ENSMUST00000003501.9; ENSMUSP00000003501.8; ENSMUSG00000003410.9. [Q60900-1]
DR   GeneID; 15571; -.
DR   KEGG; mmu:15571; -.
DR   UCSC; uc009onl.2; mouse. [Q60900-1]
DR   UCSC; uc009onn.1; mouse. [Q60900-2]
DR   AGR; MGI:109157; -.
DR   CTD; 1995; -.
DR   MGI; MGI:109157; Elavl3.
DR   VEuPathDB; HostDB:ENSMUSG00000003410; -.
DR   eggNOG; KOG0145; Eukaryota.
DR   GeneTree; ENSGT00940000160389; -.
DR   HOGENOM; CLU_026186_2_2_1; -.
DR   InParanoid; Q60900; -.
DR   OMA; NQCYASS; -.
DR   OrthoDB; 129910at2759; -.
DR   PhylomeDB; Q60900; -.
DR   TreeFam; TF313377; -.
DR   BioGRID-ORCS; 15571; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Elavl3; mouse.
DR   EvolutionaryTrace; Q60900; -.
DR   PRO; PR:Q60900; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q60900; Protein.
DR   Bgee; ENSMUSG00000003410; Expressed in embryonic brain and 119 other cell types or tissues.
DR   ExpressionAtlas; Q60900; baseline and differential.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:InterPro.
DR   GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   CDD; cd12772; RRM1_HuC; 1.
DR   CDD; cd12776; RRM2_HuC; 1.
DR   CDD; cd12655; RRM3_HuC; 1.
DR   Gene3D; 3.30.70.330; -; 3.
DR   InterPro; IPR006548; ELAD_HU_SF.
DR   InterPro; IPR034915; HuC_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   InterPro; IPR003954; RRM_dom_euk.
DR   NCBIfam; TIGR01661; ELAV_HUD_SF; 1.
DR   PANTHER; PTHR10352:SF15; ELAV-LIKE PROTEIN 3; 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   SMART; SM00361; RRM_1; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   PROSITE; PS50102; RRM; 3.
DR   Genevisible; Q60900; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Developmental protein; Differentiation;
KW   Neurogenesis; Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..367
FT                   /note="ELAV-like protein 3"
FT                   /id="PRO_0000081582"
FT   DOMAIN          39..117
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          125..205
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          284..362
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   VAR_SEQ         251..257
FT                   /note="Missing (in isoform HuC-S)"
FT                   /evidence="ECO:0000303|PubMed:9016658"
FT                   /id="VSP_005790"
FT   STRAND          41..44
FT                   /evidence="ECO:0007829|PDB:1D8Z"
FT   HELIX           52..60
FT                   /evidence="ECO:0007829|PDB:1D8Z"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:1FNX"
FT   STRAND          66..70
FT                   /evidence="ECO:0007829|PDB:1D8Z"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:1D8Z"
FT   STRAND          81..86
FT                   /evidence="ECO:0007829|PDB:1D8Z"
FT   HELIX           90..100
FT                   /evidence="ECO:0007829|PDB:1D8Z"
FT   STRAND          101..104
FT                   /evidence="ECO:0007829|PDB:1D8Z"
FT   STRAND          109..113
FT                   /evidence="ECO:0007829|PDB:1D8Z"
FT   STRAND          128..131
FT                   /evidence="ECO:0007829|PDB:1D9A"
FT   HELIX           138..146
FT                   /evidence="ECO:0007829|PDB:1D9A"
FT   STRAND          151..157
FT                   /evidence="ECO:0007829|PDB:1D9A"
FT   STRAND          160..163
FT                   /evidence="ECO:0007829|PDB:1D9A"
FT   STRAND          168..175
FT                   /evidence="ECO:0007829|PDB:1D9A"
FT   HELIX           176..186
FT                   /evidence="ECO:0007829|PDB:1D9A"
FT   TURN            192..195
FT                   /evidence="ECO:0007829|PDB:1D9A"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:1D9A"
SQ   SEQUENCE   367 AA;  39533 MW;  ECD1A266512ADF58 CRC64;
     MVTQILGAME SQVGGGPAGP ALPNGPLLGT NGATDDSKTN LIVNYLPQNM TQDEFKSLFG
     SIGDIESCKL VRDKITGQSL GYGFVNYSDP NDADKAINTL NGLKLQTKTI KVSYARPSSA
     SIRDANLYVS GLPKTMSQKE MEQLFSQYGR IITSRILLDQ ATGVSRGVGF IRFDKRIEAE
     EAIKGLNGQK PLGAAEPITV KFANNPSQKT GQALLTHLYQ SSARRYAGPL HHQTQRFRLD
     NLLNMAYGVK SPLSLIARFS PIAIDGMSGL AGVGLSGGAA GAGWCIFVYN LSPEADESVL
     WQLFGPFGAV TNVKVIRDFT TNKCKGFGFV TMTNYDEAAM AIASLNGYRL GERVLQVSFK
     TSKQHKA
//