ELV1A_XENLA
ID ELV1A_XENLA Reviewed; 337 AA.
AC Q1JQ73; Q91582;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=ELAV-like protein 1-A;
DE AltName: Full=36 kDa embryonic-type cytoplasmic polyadenylation element-binding protein;
DE Short=36 kDa eCPE-binding protein;
DE Short=36 kDa eCPEB;
DE Short=p36 {ECO:0000303|PubMed:11780632};
DE AltName: Full=Protein ElrA-A {ECO:0000312|EMBL:AAI16460.1};
DE Short=ElrA {ECO:0000312|EMBL:AAI16460.1};
GN Name=elavl1-a;
GN Synonyms=elavl1 {ECO:0000250|UniProtKB:Q15717},
GN elrA {ECO:0000312|EMBL:AAI16460.1};
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:AAA96942.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Tail bud {ECO:0000269|PubMed:7753842};
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAI16460.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Oocyte {ECO:0000312|EMBL:AAI16460.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP RNA-BINDING.
RX PubMed=7969126; DOI=10.1128/mcb.14.12.7867-7875.1994;
RA Simon R., Richter J.D.;
RT "Further analysis of cytoplasmic polyadenylation in Xenopus embryos and
RT identification of embryonic cytoplasmic polyadenylation element-binding
RT proteins.";
RL Mol. Cell. Biol. 14:7867-7875(1994).
RN [4] {ECO:0000305}
RP RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=8873767; DOI=10.1006/dbio.1996.0254;
RA Simon R., Wu L., Richter J.D.;
RT "Cytoplasmic polyadenylation of activin receptor mRNA and the control of
RT pattern formation in Xenopus development.";
RL Dev. Biol. 179:239-250(1996).
RN [5] {ECO:0000305}
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=9343402; DOI=10.1128/mcb.17.11.6402;
RA Wu L., Good P.J., Richter J.D.;
RT "The 36-kilodalton embryonic-type cytoplasmic polyadenylation element-
RT binding protein in Xenopus laevis is ElrA, a member of the ELAV family of
RT RNA-binding proteins.";
RL Mol. Cell. Biol. 17:6402-6409(1997).
RN [6] {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 [7] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH CIRBP.
RX PubMed=13679363; DOI=10.1074/jbc.m308328200;
RA Aoki K., Matsumoto K., Tsujimoto M.;
RT "Xenopus cold-inducible RNA-binding protein 2 interacts with ElrA, the
RT Xenopus homolog of HuR, and inhibits deadenylation of specific mRNAs.";
RL J. Biol. Chem. 278:48491-48497(2003).
RN [8] {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 [9] {ECO:0000305}
RP RNA-BINDING, AND LACK OF OLIGOMERIZATION.
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 [10] {ECO:0000305}
RP PUTATIVE FUNCTION, AND RNA-BINDING.
RX PubMed=17355986; DOI=10.1093/nar/gkm084;
RA Slevin M.K., Gourronc F., Hartley R.S.;
RT "ElrA binding to the 3'UTR of cyclin E1 mRNA requires polyadenylation
RT elements.";
RL Nucleic Acids Res. 35:2167-2176(2007).
RN [11] {ECO:0000305}
RP RNA-BINDING.
RX PubMed=18930026; DOI=10.1016/j.bbrc.2008.10.029;
RA Guo X., Gourronc F., Audic Y., Lyons-Levy G., Mitchell T., Hartley R.S.;
RT "ElrA and AUF1 differentially bind cyclin B2 mRNA.";
RL Biochem. Biophys. Res. Commun. 377:653-657(2008).
RN [12] {ECO:0000305}
RP FUNCTION, RNA-BINDING, IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH
RP IGF2BP3; 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. May be involved in
CC cytoplasmic mRNA polyadenylation. Acts cooperatively with cribp to
CC stabilize AU-rich sequence (ARE)-containing mRNAs. May play a role
CC during gastrulation. Required for the vegetal localization of vg1 mRNA.
CC {ECO:0000250|UniProtKB:Q15717, ECO:0000269|PubMed:13679363,
CC ECO:0000269|PubMed:19458392, ECO:0000269|PubMed:9343402}.
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.
CC {ECO:0000269|PubMed:13679363, ECO:0000269|PubMed:16199879,
CC ECO:0000269|PubMed:19458392}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16199879,
CC ECO:0000269|PubMed:19458392, ECO:0000269|PubMed:8873767,
CC ECO:0000269|PubMed:9343402}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:16199879, ECO:0000269|PubMed:19458392,
CC ECO:0000269|PubMed:8873767, ECO:0000269|PubMed:9343402}. Note=Enriched
CC at the vegetal cortex in stage III and IV oocytes. Shows very weak
CC nuclear localization. {ECO:0000269|PubMed:16199879,
CC ECO:0000269|PubMed:19458392, ECO:0000269|PubMed:8873767,
CC ECO:0000269|PubMed:9343402}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1JQ73-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:7753842};
CC IsoId=Q1JQ73-2; Sequence=VSP_038716;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in adults.
CC {ECO:0000269|PubMed:7753842}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout development in oocytes, eggs, embryos and adults. Expression
CC increases between oogenesis stages III and VI.
CC {ECO:0000269|PubMed:16199879, ECO:0000269|PubMed:7753842,
CC ECO:0000269|PubMed:9343402}.
CC -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000255}.
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DR EMBL; U17596; AAA96942.1; -; mRNA.
DR EMBL; BC116459; AAI16460.1; -; mRNA.
DR PIR; I51675; I51675.
DR RefSeq; NP_001084078.1; NM_001090609.1. [Q1JQ73-1]
DR RefSeq; XP_018098715.1; XM_018243226.1. [Q1JQ73-1]
DR RefSeq; XP_018098723.1; XM_018243234.1. [Q1JQ73-2]
DR AlphaFoldDB; Q1JQ73; -.
DR SMR; Q1JQ73; -.
DR IntAct; Q1JQ73; 2.
DR MINT; Q1JQ73; -.
DR DNASU; 399292; -.
DR GeneID; 399292; -.
DR KEGG; xla:399292; -.
DR CTD; 399292; -.
DR Xenbase; XB-GENE-6254178; elavl1.L.
DR OMA; SASLGCK; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 399292; Expressed in egg cell 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; IDA: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; IDA:UniProtKB.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0007369; P:gastrulation; IMP:UniProtKB.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; IGI:UniProtKB.
DR GO; GO:0031440; P:regulation of mRNA 3'-end processing; IC: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 Alternative splicing; Cytoplasm; Developmental protein; Gastrulation;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..337
FT /note="ELAV-like protein 1-A"
FT /id="PRO_0000391368"
FT DOMAIN 20..109
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 117..197
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 255..333
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT VAR_SEQ 59..69
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7753842"
FT /id="VSP_038716"
SQ SEQUENCE 337 AA; 37199 MW; BEE8BF72CF1F03BE CRC64;
MSNGYEDHMD DVCRDDIGRT NLIVNYLPQN MTQDELRSLF SSIGEVESAK LIRDKVAGFE
MRSSSLSKGH SLGYGFVNYL NAKDAERAIN TLNGLRLQSK TIKVSFARPS SESIKDANLY
ISGLPRTMTQ KDVEDMFLPF GHIINSRVLV DQATGLSRGV AFIRFDKRSE AEEAIASFNG
HKPPGSSEPI TVKFAANPNQ NKNVALLSQI CHSPARRFGG PVHHQAQRFR FSPMGVDHMS
SISSVNVASS ATSGWCIFVY NLGQDADEGI LWQMFGPFGA VTNVKVIRDF NTNKCKGFGF
VTMTNYEEAA MAIASLNGYR LGDKTLQVSF KTSKSHK
