RB24A_XENLA
ID RB24A_XENLA Reviewed; 225 AA.
AC Q6GQD3; Q9I8R5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=RNA-binding protein 24-A {ECO:0000305};
DE AltName: Full=RNA-binding motif protein 24-A;
DE AltName: Full=RRM domain-containing protein SEB-4 {ECO:0000303|PubMed:10842088};
DE Short=SEB-4 {ECO:0000303|PubMed:10842088};
DE AltName: Full=Xseb-4;
GN Name=rbm24-a;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=10842088; DOI=10.1016/s0925-4773(00)00284-7;
RA Fetka I., Radeghieri A., Bouwmeester T.;
RT "Expression of the RNA recognition motif-containing protein SEB-4 during
RT Xenopus embryonic development.";
RL Mech. Dev. 94:283-286(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=20338237; DOI=10.1016/j.mod.2010.03.002;
RA Li H.Y., Bourdelas A., Carron C., Shi D.L.;
RT "The RNA-binding protein Seb4/RBM24 is a direct target of MyoD and is
RT required for myogenesis during Xenopus early development.";
RL Mech. Dev. 127:281-291(2010).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=25217815; DOI=10.1016/j.mod.2014.08.003;
RA Grifone R., Xie X., Bourgeois A., Saquet A., Duprez D., Shi D.L.;
RT "The RNA-binding protein Rbm24 is transiently expressed in myoblasts and is
RT required for myogenic differentiation during vertebrate development.";
RL Mech. Dev. 134:1-15(2014).
CC -!- FUNCTION: Multifunctional RNA-binding protein involved in the
CC regulation of pre-mRNA splicing, mRNA stability and mRNA translation
CC important for cell fate decision and differentiation. Plays a major
CC role in pre-mRNA alternative splicing regulation. Mediates
CC preferentially muscle-specific exon inclusion in numerous mRNAs
CC important for striated cardiac and skeletal muscle cell
CC differentiation. Binds to intronic splicing enhancer (ISE) composed of
CC stretches of GU-rich motifs localized in flanking intron of exon that
CC will be included by alternative splicing. Involved in embryonic stem
CC cell (ESC) transition to cardiac cell differentiation by promoting pre-
CC mRNA alternative splicing events of several pluripotency and/or
CC differentiation genes. Plays a role in the regulation of mRNA stability
CC and mRNA translation to which it is bound. Involved in myogenic
CC differentiation by regulating myog levels (PubMed:20338237). Binds to a
CC huge amount of mRNAs. Required for embryonic heart development,
CC sarcomer and M-band formation in striated muscles (PubMed:20338237).
CC {ECO:0000250|UniProtKB:D3Z4I3, ECO:0000250|UniProtKB:Q9BX46,
CC ECO:0000269|PubMed:20338237}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10842088}. Cytoplasm
CC {ECO:0000269|PubMed:10842088}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC (PubMed:10842088). Zygotic transcription is initiated in the early
CC gastrula embryo in paraxial mesoderm that is fated to give rise to
CC somites (PubMed:10842088). During the course of gastrulation and
CC neurulation, it is expressed in somitic paraxial mesoderm is centered
CC within the myoD expression domain (PubMed:10842088). Expressed in
CC developing somites at larval stages (PubMed:25217815). As development
CC proceeds it is also expressed in the cardiac primordium and the lens
CC vesicle (PubMed:10842088, PubMed:25217815). Expressed in hypaxial
CC migrating cells and branchiomeric cranial muscles (PubMed:25217815). In
CC the heart expression is confined to the myocardium (PubMed:10842088).
CC {ECO:0000269|PubMed:10842088, ECO:0000269|PubMed:25217815}.
CC -!- INDUCTION: Up-regulated by the myogenic factor myoD during
CC gastrulation. {ECO:0000269|PubMed:20338237}.
CC -!- DOMAIN: The RRM domain is necessary for mRNA stability and mRNA
CC translation regulation. {ECO:0000250|UniProtKB:Q9BX46}.
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DR EMBL; AF223427; AAF81070.1; -; mRNA.
DR EMBL; BC072812; AAH72812.1; -; mRNA.
DR RefSeq; NP_001080995.1; NM_001087526.1.
DR AlphaFoldDB; Q6GQD3; -.
DR SMR; Q6GQD3; -.
DR DNASU; 394318; -.
DR GeneID; 394318; -.
DR KEGG; xla:394318; -.
DR CTD; 394318; -.
DR Xenbase; XB-GENE-866276; rbm24.L.
DR OrthoDB; 1579773at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 394318; Expressed in muscle tissue and 18 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:1990715; F:mRNA CDS binding; ISS:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; ISS:UniProtKB.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0061157; P:mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:1905870; P:positive regulation of 3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB.
DR GO; GO:1902811; P:positive regulation of skeletal muscle fiber differentiation; ISS:UniProtKB.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0010830; P:regulation of myotube differentiation; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 1.
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; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Differentiation; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; RNA-binding; Translation regulation.
FT CHAIN 1..225
FT /note="RNA-binding protein 24-A"
FT /id="PRO_0000273373"
FT DOMAIN 11..88
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT CONFLICT 13..14
FT /note="IF -> TS (in Ref. 1; AAF81070)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="S -> SAA (in Ref. 1; AAF81070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 24027 MW; 72AB9432CBB4DADE CRC64;
MHTTQKDTTY TKIFVGGLPY HTTDSSLRKY FEVFGDIEEA VVITDRQTGK SRGYGFVTMA
DRAAAERACK DPNPIIDGRK ANVNLAYLGA KPRIMQPGFA FGVQQIHPAL IQRPFGIPAH
YVYPQAYVQP GVVIPHVQPT AATSTSPYID YTSAAYAQYS AAAAAAAYDQ YPYAASPAAT
GYVTAAGYGY AVPQPLTAAA PGSAAAAAAA FGQYQPQQLQ ADRMQ
