ID ELAV3_HUMAN Reviewed; 367 AA. AC Q14576; Q16135; Q96CL8; Q96QS9; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2002, sequence version 3. DT 27-MAR-2024, entry version 190. DE RecName: Full=ELAV-like protein 3; DE AltName: Full=Hu-antigen C; DE Short=HuC; DE AltName: Full=Paraneoplastic cerebellar degeneration-associated antigen; DE AltName: Full=Paraneoplastic limbic encephalitis antigen 21; GN Name=ELAVL3; Synonyms=HUC, PLE21; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain; RA Manley T., Furneaux H.M.; RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Zhang B., Yuan J.G., Qiang B.Q.; RT "Isolation of HuC cDNA."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Brain; RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-367 (ISOFORM 2). RC TISSUE=Hippocampus; RX PubMed=7511893; DOI=10.1006/bbrc.1994.1358; RA Sakai K., Gofuku M., Kitagawa Y., Ogasawara T., Hirose G., Yamazaki M., RA Koh C.S., Yanagisawa N., Steinman L.; RT "A hippocampal protein associated with paraneoplastic neurologic syndrome RT and small cell lung carcinoma."; RL Biochem. Biophys. Res. Commun. 199:1200-1208(1994). RN [6] RP FUNCTION. RX PubMed=10710437; DOI=10.1093/nar/28.7.e20; RA King P.H.; RT "RNA-binding analyses of HuC and HuD with the VEGF and c-myc 3'- RT untranslated regions using a novel ELISA-based assay."; RL Nucleic Acids Res. 28:E20-E20(2000). CC -!- FUNCTION: RNA-binding protein that binds to AU-rich element (ARE) CC sequences of target mRNAs, including VEGF mRNA (PubMed:10710437). May CC also bind poly-A tracts via RRM 3 (By similarity). May be involved in CC neuronal differentiation and maintenance (By similarity). Plays a role CC in the stabilization of GAP43 mRNA and in spatial learning (By CC similarity). {ECO:0000250|UniProtKB:Q60900, CC ECO:0000269|PubMed:10710437}. CC -!- SUBUNIT: Interacts with MAP1B light chain LC1. CC {ECO:0000250|UniProtKB:Q60900}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q14576-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14576-2; Sequence=VSP_005789; CC -!- TISSUE SPECIFICITY: Brain specific. 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 (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L26405; AAA58677.1; -; mRNA. DR EMBL; AY036909; AAK67714.1; -; mRNA. DR EMBL; AC008481; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC014144; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; D26158; BAA21838.1; -; mRNA. DR CCDS; CCDS32912.1; -. [Q14576-1] DR CCDS; CCDS45978.1; -. [Q14576-2] DR RefSeq; NP_001411.2; NM_001420.3. [Q14576-1] DR RefSeq; NP_115657.2; NM_032281.2. [Q14576-2] DR AlphaFoldDB; Q14576; -. DR SMR; Q14576; -. DR BioGRID; 108310; 20. DR IntAct; Q14576; 12. DR MINT; Q14576; -. DR STRING; 9606.ENSP00000352162; -. DR BindingDB; Q14576; -. DR ChEMBL; CHEMBL4105924; -. DR iPTMnet; Q14576; -. DR PhosphoSitePlus; Q14576; -. DR BioMuta; ELAVL3; -. DR DMDM; 21264436; -. DR EPD; Q14576; -. DR jPOST; Q14576; -. DR MassIVE; Q14576; -. DR MaxQB; Q14576; -. DR PaxDb; 9606-ENSP00000352162; -. DR PeptideAtlas; Q14576; -. DR ProteomicsDB; 60054; -. [Q14576-1] DR ProteomicsDB; 60055; -. [Q14576-2] DR Antibodypedia; 25887; 207 antibodies from 27 providers. DR DNASU; 1995; -. DR Ensembl; ENST00000359227.8; ENSP00000352162.1; ENSG00000196361.10. [Q14576-1] DR Ensembl; ENST00000438662.6; ENSP00000390878.1; ENSG00000196361.10. [Q14576-2] DR GeneID; 1995; -. DR KEGG; hsa:1995; -. DR MANE-Select; ENST00000359227.8; ENSP00000352162.1; NM_001420.4; NP_001411.2. DR UCSC; uc002mrx.2; human. [Q14576-1] DR AGR; HGNC:3314; -. DR CTD; 1995; -. DR DisGeNET; 1995; -. DR GeneCards; ELAVL3; -. DR HGNC; HGNC:3314; ELAVL3. DR HPA; ENSG00000196361; Tissue enriched (brain). DR MIM; 603458; gene. DR neXtProt; NX_Q14576; -. DR OpenTargets; ENSG00000196361; -. DR PharmGKB; PA27742; -. DR VEuPathDB; HostDB:ENSG00000196361; -. DR eggNOG; KOG0145; Eukaryota. DR GeneTree; ENSGT00940000160389; -. DR HOGENOM; CLU_026186_2_2_1; -. DR InParanoid; Q14576; -. DR OMA; NQCYASS; -. DR OrthoDB; 129910at2759; -. DR PhylomeDB; Q14576; -. DR TreeFam; TF313377; -. DR PathwayCommons; Q14576; -. DR SignaLink; Q14576; -. DR SIGNOR; Q14576; -. DR BioGRID-ORCS; 1995; 11 hits in 1142 CRISPR screens. DR ChiTaRS; ELAVL3; human. DR GeneWiki; ELAVL3; -. DR GenomeRNAi; 1995; -. DR Pharos; Q14576; Tchem. DR PRO; PR:Q14576; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q14576; Protein. DR Bgee; ENSG00000196361; Expressed in inferior vagus X ganglion and 188 other cell types or tissues. DR ExpressionAtlas; Q14576; 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; Q14576; HS. PE 2: Evidence at transcript level; KW Alternative splicing; Developmental protein; Differentiation; Neurogenesis; KW Reference proteome; Repeat; RNA-binding. FT CHAIN 1..367 FT /note="ELAV-like protein 3" FT /id="PRO_0000081581" 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 2)" FT /evidence="ECO:0000303|PubMed:7511893, ECO:0000303|Ref.1, FT ECO:0000303|Ref.2" FT /id="VSP_005789" FT CONFLICT 20..25 FT /note="PALPNG -> RPAQR (in Ref. 4; BAA21838)" FT /evidence="ECO:0000305" FT CONFLICT 78..79 FT /note="QS -> RD (in Ref. 1; AAA58677 and 2; AAK67714)" FT /evidence="ECO:0000305" FT CONFLICT 88 FT /note="S -> P (in Ref. 1; AAA58677 and 2; AAK67714)" FT /evidence="ECO:0000305" FT CONFLICT 195 FT /note="A -> R (in Ref. 4; BAA21838)" FT /evidence="ECO:0000305" FT CONFLICT 248 FT /note="G -> A (in Ref. 4; BAA21838)" FT /evidence="ECO:0000305" FT CONFLICT 282 FT /note="Missing (in Ref. 1; AAA58677 and 4; BAA21838)" FT /evidence="ECO:0000305" FT CONFLICT 295..297 FT /note="ADE -> PDQ (in Ref. 4; BAA21838)" FT /evidence="ECO:0000305" FT CONFLICT 330 FT /note="V -> M (in Ref. 4; BAA21838)" FT /evidence="ECO:0000305" FT CONFLICT 351 FT /note="G -> A (in Ref. 1; AAA58677)" FT /evidence="ECO:0000305" FT CONFLICT 352 FT /note="E -> Q (in Ref. 4; BAA21838)" FT /evidence="ECO:0000305" SQ SEQUENCE 367 AA; 39547 MW; 03FB3BD4D112B326 CRC64; MVTQILGAME SQVGGGPAGP ALPNGPLLGT NGATDDSKTN LIVNYLPQNM TQDEFKSLFG SIGDIESCKL VRDKITGQSL GYGFVNYSDP NDADKAINTL NGLKLQTKTI KVSYARPSSA SIRDANLYVS GLPKTMSQKE MEQLFSQYGR IITSRILVDQ VTGVSRGVGF IRFDKRIEAE EAIKGLNGQK PLGAAEPITV KFANNPSQKT GQALLTHLYQ SSARRYAGPL HHQTQRFRLD NLLNMAYGVK SPLSLIARFS PIAIDGMSGL AGVGLSGGAA GAGWCIFVYN LSPEADESVL WQLFGPFGAV TNVKVIRDFT TNKCKGFGFV TMTNYDEAAM AIASLNGYRL GERVLQVSFK TSKQHKA //