ELAV3_MOUSE
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 03-AUG-2022, entry version 169.
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; 15.
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; Q60900; -.
DR PeptideAtlas; Q60900; -.
DR PRIDE; Q60900; -.
DR ProteomicsDB; 275657; -. [Q60900-1]
DR ProteomicsDB; 275658; -. [Q60900-2]
DR Antibodypedia; 25887; 177 antibodies from 27 providers.
DR DNASU; 15571; -.
DR Ensembl; ENSMUST00000003501; ENSMUSP00000003501; ENSMUSG00000003410. [Q60900-1]
DR GeneID; 15571; -.
DR KEGG; mmu:15571; -.
DR UCSC; uc009onl.2; mouse. [Q60900-1]
DR UCSC; uc009onn.1; mouse. [Q60900-2]
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; AGCTEPI; -.
DR OrthoDB; 614259at2759; -.
DR PhylomeDB; Q60900; -.
DR TreeFam; TF313377; -.
DR BioGRID-ORCS; 15571; 2 hits in 74 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 117 other tissues.
DR ExpressionAtlas; Q60900; baseline and differential.
DR Genevisible; Q60900; MM.
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; cd12650; RRM1_Hu; 1.
DR CDD; cd12655; RRM3_HuC; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR006548; ELAD_HU_SF.
DR InterPro; IPR034775; ELAV/Hu_RRM1.
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 Pfam; PF00076; RRM_1; 3.
DR PRINTS; PR00961; HUDSXLRNA.
DR SMART; SM00360; RRM; 3.
DR SMART; SM00361; RRM_1; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1.
DR PROSITE; PS50102; RRM; 3.
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
