ELAV2_XENLA
ID ELAV2_XENLA Reviewed; 389 AA.
AC Q91903; B7ZSI9; Q52KU1; Q91583;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=ELAV-like protein 2;
DE AltName: Full=Elav like-1 {ECO:0000303|PubMed:7547471};
DE Short=Xel-1 {ECO:0000312|EMBL:CAA59430.1};
DE AltName: Full=Protein ElrB {ECO:0000303|PubMed:7753842};
DE AltName: Full=p45 {ECO:0000303|PubMed:11780632};
GN Name=elavl2;
GN Synonyms=el-1 {ECO:0000312|EMBL:CAA59430.1},
GN elavl2-a {ECO:0000312|EMBL:AAH94189.1}, elrB {ECO:0000312|EMBL:AAA96943.1};
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:0000305, ECO:0000312|EMBL:CAA59430.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Brain {ECO:0000312|EMBL:CAA59430.1};
RX PubMed=7547471; DOI=10.1016/0925-4773(95)00368-1;
RA Perron M., Theodore L., Wegnez M.;
RT "Isolation and embryonic expression of Xel-1, a nervous system-specific
RT Xenopus gene related to the elav gene family.";
RL Mech. Dev. 51:235-249(1995).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAA96943.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000312|EMBL:AAA96943.1};
RX PubMed=7753842; DOI=10.1073/pnas.92.10.4557;
RA Good P.J.;
RT "A conserved family of elav-like genes in vertebrates.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4557-4561(1995).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAI70539.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Oocyte {ECO:0000312|EMBL:AAH94189.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=9174163; DOI=10.1089/dna.1997.16.579;
RA Perron M., Bourlitio P., Wegnez M., Theodore L.;
RT "Subcellular distribution of Xenopus XEL-1 protein, a member of the neuron-
RT specific ELAV/Hu family, revealed by epitope tagging.";
RL DNA Cell Biol. 16:579-587(1997).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=10470646;
RA Perron M., Furrer M.P., Wegnez M., Theodore L.;
RT "Misexpression of the RNA-binding protein ELRB in Xenopus presumptive
RT neurectoderm induces proliferation arrest and programmed cell death.";
RL Int. J. Dev. Biol. 43:295-303(1999).
RN [6] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=10473128; DOI=10.1016/s0925-4773(99)00056-8;
RA Perron M., Furrer M.P., Wegnez M., Theodore L.;
RT "Xenopus elav-like genes are differentially expressed during
RT neurogenesis.";
RL Mech. Dev. 84:139-142(1999).
RN [7] {ECO:0000305}
RP RNA-BINDING.
RX PubMed=11780632;
RA Otero L.J., Devaux A., Standart N.;
RT "A 250-nucleotide UA-rich element in the 3' untranslated region of Xenopus
RT laevis Vg1 mRNA represses translation both in vivo and in vitro.";
RL RNA 7:1753-1767(2001).
RN [8] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=15593335; DOI=10.1002/cne.20387;
RA Amato M.A., Boy S., Arnault E., Girard M., Della Puppa A., Sharif A.,
RA Perron M.;
RT "Comparison of the expression patterns of five neural RNA binding proteins
RT in the Xenopus retina.";
RL J. Comp. Neurol. 481:331-339(2005).
RN [9] {ECO:0000305}
RP RNA-BINDING, IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16199879; DOI=10.1128/mcb.25.20.9028-9039.2005;
RA Colegrove-Otero L.J., Devaux A., Standart N.;
RT "The Xenopus ELAV protein ElrB represses Vg1 mRNA translation during
RT oogenesis.";
RL Mol. Cell. Biol. 25:9028-9039(2005).
RN [10] {ECO:0000305}
RP RNA-BINDING, AND HOMOOLIGOMERIZATION.
RX PubMed=16930598; DOI=10.1016/j.febslet.2006.08.012;
RA Devaux A., Colegrove-Otero L.J., Standart N.;
RT "Xenopus ElrB, but not ElrA, binds RNA as an oligomer: possible role of the
RT linker.";
RL FEBS Lett. 580:4947-4952(2006).
RN [11] {ECO:0000305}
RP FUNCTION, RNA-BINDING, AND IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX
RP WITH IGF2BP3; STAU1; DDX6; LSM14B AND YBX2.
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: Binds to poly-U elements and AU-rich elements (AREs) in the
CC 3'-UTR of target mRNAs. Required for the vegetal localization of vg1
CC mRNA. Probably required for nervous system development.
CC {ECO:0000269|PubMed:10470646, ECO:0000269|PubMed:19458392}.
CC -!- SUBUNIT: Part of a ribonucleoprotein (RNP) complex, at least composed
CC 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. Binds RNA as a homooligomer.
CC {ECO:0000269|PubMed:16199879, ECO:0000269|PubMed:19458392}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16199879,
CC ECO:0000269|PubMed:9174163}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:16199879, ECO:0000269|PubMed:9174163}.
CC Note=Enriched at the vegetal cortex in stage III and IV oocytes. Shows
CC both nuclear and cytoplasmic localization in the neural tube at the
CC neurula stage, although endogenous elavl2 is not expressed at this
CC stage. {ECO:0000269|PubMed:16199879, ECO:0000269|PubMed:9174163}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:7547471, ECO:0000269|PubMed:7753842};
CC IsoId=Q91903-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91903-2; Sequence=VSP_038717;
CC -!- TISSUE SPECIFICITY: Expressed in brain, testis and ovary. Ovarian
CC expression is restricted to follicle cells surrounding the oocyte. From
CC the early tailbud stage, expression is neural-specific and is seen in
CC both the central and peripheral nervous system in differentiating
CC neurons but not proliferating precursors. Expressed in the retina from
CC stage 32 with expression becoming restricted to the ganglion cell layer
CC by later stages. {ECO:0000269|PubMed:10473128,
CC ECO:0000269|PubMed:15593335, ECO:0000269|PubMed:7547471,
CC ECO:0000269|PubMed:7753842}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Predominantly expressed in the early stages of oogenesis (stages I to
CC III), with expression levels declining from stage IV onwards. Zygotic
CC expression begins at the early tailbud stage.
CC {ECO:0000269|PubMed:16199879, ECO:0000269|PubMed:7547471}.
CC -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000255}.
CC -!- CAUTION: The 45 kDa RNA-binding proteins identified in PubMed:7969126
CC and PubMed:8873767, and PubMed:11087864 may correspond to elavl2/elrB.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH94189.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X85111; CAA59430.1; -; mRNA.
DR EMBL; U17597; AAA96943.1; -; mRNA.
DR EMBL; BC170539; AAI70539.1; -; mRNA.
DR EMBL; BC094189; AAH94189.1; ALT_INIT; mRNA.
DR PIR; I51676; I51676.
DR RefSeq; NP_001081035.1; NM_001087566.1. [Q91903-1]
DR RefSeq; NP_001081613.1; NM_001088144.1.
DR RefSeq; XP_018083833.1; XM_018228344.1. [Q91903-1]
DR RefSeq; XP_018083899.1; XM_018228410.1. [Q91903-1]
DR RefSeq; XP_018083945.1; XM_018228456.1. [Q91903-1]
DR RefSeq; XP_018083985.1; XM_018228496.1. [Q91903-1]
DR RefSeq; XP_018084043.1; XM_018228554.1. [Q91903-1]
DR RefSeq; XP_018084087.1; XM_018228598.1. [Q91903-1]
DR RefSeq; XP_018084130.1; XM_018228641.1. [Q91903-2]
DR RefSeq; XP_018084175.1; XM_018228686.1. [Q91903-2]
DR AlphaFoldDB; Q91903; -.
DR SMR; Q91903; -.
DR BioGRID; 98944; 1.
DR IntAct; Q91903; 1.
DR MINT; Q91903; -.
DR PRIDE; Q91903; -.
DR DNASU; 394342; -.
DR GeneID; 394342; -.
DR KEGG; xla:394342; -.
DR CTD; 394342; -.
DR Xenbase; XB-GENE-866091; elavl2.L.
DR OMA; YPSCHSA; -.
DR OrthoDB; 775799at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 394342; Expressed in egg cell and 12 other tissues.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0017131; F:uridine-rich cytoplasmic polyadenylylation element binding; IDA:UniProtKB.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR CDD; cd12650; RRM1_Hu; 1.
DR CDD; cd12775; RRM2_HuB; 1.
DR CDD; cd12654; RRM3_HuB; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR006548; ELAD_HU_SF.
DR InterPro; IPR034775; ELAV/Hu_RRM1.
DR InterPro; IPR034999; HuB_RRM2.
DR InterPro; IPR034914; HuB_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 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 Alternative splicing; Cytoplasm; Developmental protein; Reference proteome;
KW Repeat; Ribonucleoprotein; RNA-binding.
FT CHAIN 1..389
FT /note="ELAV-like protein 2"
FT /id="PRO_0000391371"
FT DOMAIN 66..145
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 153..233
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 306..384
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT VAR_SEQ 104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_038717"
FT CONFLICT 128
FT /note="L -> V (in Ref. 1; CAA59430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 42709 MW; 200C18CA6EE0D1BC CRC64;
MAVRLCDVAS LLRSGSWAAE PWTGQVIAAM ETQLSNGPTC NNTANCPNTI NCSSPVESNN
TEDSKTNLIV NYLPQNMTQE ELKSLFGSIG EIESCKLVRD KITEGQSLGY GFVNYIDPKD
AEKAINTLNG LRLQTKTIKV SYARPSSASI RDANLYVSGL PKTMTQKELE QLFSQYGRII
TSRILVDQVT GVSRGVGFIR FDKRIEAEEA IKGLNGQKPP GATEPITVKF ANNPSQKVNH
TILSQLYQSP NRRYPGPLAQ QAQRFRLDNL LNMAYGGIKS RFSPMAIDGM TSLAGINFPG
HAGTGWCIFV YNLAPDADES ILWQMFGPFG AVTNVKVIRD FNTNKCKGFG FVTMTNYDEA
AMAIASLNGY RLGDRVLQVS FKTSKTHKA
