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RBM24_XENTR
ID   RBM24_XENTR             Reviewed;         226 AA.
AC   Q6P8A7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=RNA-binding protein 24 {ECO:0000305};
DE   AltName: Full=RNA-binding motif protein 24 {ECO:0000250|UniProtKB:Q9BX46};
GN   Name=rbm24;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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. Binds to a huge amount of
CC       mRNAs. Required for embryonic heart development, sarcomer and M-band
CC       formation in striated muscles. {ECO:0000250|UniProtKB:D3Z4I3,
CC       ECO:0000250|UniProtKB:Q9BX46}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6GQD3}. Cytoplasm
CC       {ECO:0000250|UniProtKB:D3Z4I3}.
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; BC061322; AAH61322.1; -; mRNA.
DR   RefSeq; NP_989016.1; NM_203685.1.
DR   AlphaFoldDB; Q6P8A7; -.
DR   SMR; Q6P8A7; -.
DR   STRING; 8364.ENSXETP00000053069; -.
DR   PaxDb; Q6P8A7; -.
DR   DNASU; 394612; -.
DR   Ensembl; ENSXETT00000053069; ENSXETP00000053069; ENSXETG00000024618.
DR   GeneID; 394612; -.
DR   KEGG; xtr:394612; -.
DR   CTD; 221662; -.
DR   Xenbase; XB-GENE-493647; rbm24.
DR   eggNOG; KOG0149; Eukaryota.
DR   HOGENOM; CLU_065652_0_1_1; -.
DR   InParanoid; Q6P8A7; -.
DR   OrthoDB; 1579773at2759; -.
DR   PhylomeDB; Q6P8A7; -.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000024618; Expressed in skeletal muscle tissue and 16 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; ISS: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..226
FT                   /note="RNA-binding protein 24"
FT                   /id="PRO_0000273375"
FT   DOMAIN          11..88
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ   SEQUENCE   226 AA;  24136 MW;  2542F10C6FE1FD72 CRC64;
     MHTTQKDTTY TKIFVGGLPY HTTDSSLRKY FEVFGDIEEA VVITDRQTGK SRGYGFVTMA
     DRAAAERACK DPNPIIDGRK ANVNLAYLGA KPRIMQPGFA FGVQQIHPAL IQRPFGIPAH
     YVYPHAFVQP GVVIPHVQQA AAASTSPYID YTSAAYAQYS AAAAAAAAYD QYPYAASPAT
     TGYVTTAGYG YAVPQPLTAA APGTAAAAAA AFGQYQPQQL QADRMQ
 
 
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