ID   ELV1B_XENLA             Reviewed;         326 AA.
AC   Q5U259;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=ELAV-like protein 1-B;
DE   AltName: Full=Protein ElrA-B;
DE            Short=ElrA {ECO:0000303|PubMed:19458392};
GN   Name=elavl1-b; Synonyms=elavl1, elrA {ECO:0000303|PubMed:19458392};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000312|EMBL:AAH86269.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula {ECO:0000312|EMBL:AAH86269.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   FUNCTION, IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH IGF2BP3;
RP   STAU1; DDX6; LSM14B AND YBX2, AND SUBCELLULAR LOCATION.
RX   PubMed=19458392; DOI=10.1074/jbc.m109.009928;
RA   Arthur P.K., Claussen M., Koch S., Tarbashevich K., Jahn O., Pieler T.;
RT   "Participation of Xenopus Elr-type proteins in vegetal mRNA localization
RT   during oogenesis.";
RL   J. Biol. Chem. 284:19982-19992(2009).
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. {ECO:0000250|UniProtKB:Q15717, ECO:0000269|PubMed:19458392}.
CC   -!- SUBUNIT: Interacts (via RRM3) with cirbp. Unable to form oligomers (By
CC       similarity). Part of a ribonucleoprotein (RNP) complex, at least
CC       composed of elavl1/elrA and/or elavl2/elrB, igf2bp3/vg1RBP, ddx6/Xp54,
CC       ybx2/frgy2, lsm14b/rap55b and, in a subset of RNP complexes,
CC       stau1/staufen. {ECO:0000250|UniProtKB:Q1JQ73,
CC       ECO:0000269|PubMed:19458392}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19458392}.
CC       Cytoplasm, cell cortex {ECO:0000269|PubMed:19458392}. Note=Enriched at
CC       the vegetal cortex in stage III and IV oocytes. Shows very weak nuclear
CC       localization. {ECO:0000269|PubMed:19458392}.
CC   -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000255}.
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DR   EMBL; BC086269; AAH86269.1; -; mRNA.
DR   RefSeq; NP_001088628.1; NM_001095159.1.
DR   AlphaFoldDB; Q5U259; -.
DR   SMR; Q5U259; -.
DR   DNASU; 495680; -.
DR   GeneID; 495680; -.
DR   KEGG; xla:495680; -.
DR   CTD; 495680; -.
DR   Xenbase; XB-GENE-865489; elavl1.S.
DR   OMA; WQKHVTS; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 495680; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IPI:UniProtKB.
DR   GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IDA: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; IMP: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   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Gastrulation; Reference proteome; Repeat;
KW   RNA-binding.
FT   CHAIN           1..326
FT                   /note="ELAV-like protein 1-B"
FT                   /id="PRO_0000391369"
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;  36008 MW;  D4DE7DFD007D4F7F CRC64;
     MSNGYEDHMD DVCRDDIGRT NLIVNYLPQN MTQDELRSLF SSIGEVESAK LIRDKVAGHS
     LGYGFVNYLN AKDAERAINT LNGLRLQSKT IKVSFARPSS ETIKDANLYI SGLPRTMTQK
     DVEDMFLPFG HIINSRVLVD QATGLSRGVA FIRFDKRSEA EEAIASFNGH KPPGSSEPIT
     VKFAANPNQS KNMALLSQIC HSPARRFGGP VHHQAQRFRF SPMGVDHMSS ISSVNVASSA
     SSGWCIFIYN LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEEAAM
     AIASLNGYRL GDKTLQVSFK TSKSHK