ID   ELAV1_XENTR             Reviewed;         326 AA.
AC   Q6GLB5;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=ELAV-like protein 1 {ECO:0000250|UniProtKB:Q15717};
DE   AltName: Full=Protein ElrA {ECO:0000250|UniProtKB:Q15717};
GN   Name=elavl1 {ECO:0000312|EMBL:AAH74585.1};
GN   Synonyms=elrA {ECO:0000250|UniProtKB:Q1JQ73};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAH74585.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH74585.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA-binding protein that binds to the 3'-UTR region of mRNAs
CC       and increases their stability. Involved in embryonic stem cells (ESCs)
CC       differentiation: preferentially binds mRNAs that are not methylated by
CC       N6-methyladenosine (m6A), stabilizing them, promoting ESCs
CC       differentiation (By similarity). Binds to poly-U elements and AU-rich
CC       elements (AREs) in the 3'-UTR of target mRNAs. Acts cooperatively with
CC       cribp to stabilize AU-rich sequence (ARE)-containing mRNAs. May play a
CC       role during gastrulation. Required for the vegetal localization of vg1
CC       mRNA (By similarity). {ECO:0000250|UniProtKB:Q15717,
CC       ECO:0000250|UniProtKB:Q1JQ73}.
CC   -!- SUBUNIT: Interacts (via RRM3) with cirbp. Unable to form oligomers.
CC       Part of a ribonucleoprotein (RNP) complex, at least composed of
CC       elavl1/elrA and/or elavl2/elrB, igf2bp3/vg1RBP, ddx6/Xp54, ybx2/frgy2,
CC       lsm14b/rap55b and, in a subset of RNP complexes, stau1/staufen (By
CC       similarity). {ECO:0000250|UniProtKB:Q1JQ73}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q1JQ73}.
CC       Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q1JQ73}. Note=Enriched at
CC       the vegetal cortex in stage III and IV oocytes. Shows very weak nuclear
CC       localization. {ECO:0000250|UniProtKB:Q1JQ73}.
CC   -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000255}.
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DR   EMBL; BC074585; AAH74585.1; -; mRNA.
DR   RefSeq; NP_001005461.1; NM_001005461.1.
DR   AlphaFoldDB; Q6GLB5; -.
DR   SMR; Q6GLB5; -.
DR   STRING; 8364.ENSXETP00000059917; -.
DR   DNASU; 448062; -.
DR   GeneID; 448062; -.
DR   KEGG; xtr:448062; -.
DR   CTD; 1994; -.
DR   Xenbase; XB-GENE-481800; elavl1.
DR   eggNOG; KOG0145; Eukaryota.
DR   InParanoid; Q6GLB5; -.
DR   OrthoDB; 614259at2759; -.
DR   Reactome; R-XTR-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR   Reactome; R-XTR-72163; mRNA Splicing - Major Pathway.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0008266; F:poly(U) RNA binding; ISS:UniProtKB.
DR   GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR   GO; GO:0007369; P:gastrulation; ISS:UniProtKB.
DR   GO; GO:0008298; P:intracellular mRNA localization; ISS:UniProtKB.
DR   GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR   GO; GO:2000036; P:regulation of stem cell population maintenance; ISS:UniProtKB.
DR   CDD; cd12650; RRM1_Hu; 1.
DR   Gene3D; 3.30.70.330; -; 3.
DR   InterPro; IPR006548; ELAD_HU_SF.
DR   InterPro; IPR034775; ELAV/Hu_RRM1.
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   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Gastrulation; Reference proteome; Repeat;
KW   RNA-binding.
FT   CHAIN           1..326
FT                   /note="ELAV-like protein 1"
FT                   /id="PRO_0000391370"
FT   DOMAIN          20..98
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          106..186
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          244..322
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ   SEQUENCE   326 AA;  35950 MW;  8B7734C2672C02CA CRC64;
     MSNGYGDHMD DVCRDDIGRT NLIVNYLPQN MTQDELRSLF SSIGEVESAK LIRDKVAGHS
     LGYGFVNYLN AKDAERAINT LNGLRLQSKT IKVSVARPSS ESIKDANLYI SGLPRTMTQK
     DVEDMFLPFG RIINSRVLVD QATGLSRGVA FIRFDKRSEA EEAIASFNGH KPPGSSEPIT
     VKFAANPNQN KNMALLSQLC HSPARRFGGP VHHQAQRFRF SPMGVDHMSS ISGVNVASSA
     SSGWCIFIYN LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEEAAM
     AIASLNGYRL GDKTLQVFFK TSKSHK