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RBM24_CHICK
ID   RBM24_CHICK             Reviewed;         225 AA.
AC   Q5ZMA3;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=RNA-binding protein 24 {ECO:0000305};
DE   AltName: Full=RNA-binding motif protein 24 {ECO:0000250|UniProtKB:Q9BX46};
GN   Name=RBM24 {ECO:0000250|UniProtKB:Q9BX46}; ORFNames=RCJMB04_2l21;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2]
RP   FUNCTION, AND 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. Binds to a huge amount of
CC       mRNAs (By similarity). Involved in embryonic heart development and
CC       myogenic differentiation of somitic muscle progenitors
CC       (PubMed:25217815). {ECO:0000250|UniProtKB:D3Z4I3,
CC       ECO:0000250|UniProtKB:Q9BX46, ECO:0000269|PubMed:25217815}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6GQD3}. Cytoplasm
CC       {ECO:0000250|UniProtKB:D3Z4I3}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in differentiated myotomal muscle
CC       progenitors in embryos at 3 days of development (at protein level).
CC       Expressed in somites in embryos at 3 and 3.5 days of development.
CC       Expressed in the mesodermal core of the first and second branchial
CC       arches at 3 days of development. Expressed in forelimbs and hindlimbs
CC       at 3.5 days of development. Expressed in non-muscle territories
CC       including lens and otic vesicle at 3 days of development.
CC       {ECO:0000269|PubMed:25217815}.
CC   -!- DOMAIN: The RRM domain is necessary for mRNA stability and mRNA
CC       translation regulation. {ECO:0000250|UniProtKB:Q9BX46}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG31140.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ719481; CAG31140.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001012881.2; NM_001012863.2.
DR   AlphaFoldDB; Q5ZMA3; -.
DR   SMR; Q5ZMA3; -.
DR   STRING; 9031.ENSGALP00000042563; -.
DR   PaxDb; Q5ZMA3; -.
DR   GeneID; 420846; -.
DR   KEGG; gga:420846; -.
DR   CTD; 221662; -.
DR   VEuPathDB; HostDB:geneid_420846; -.
DR   eggNOG; KOG0149; Eukaryota.
DR   InParanoid; Q5ZMA3; -.
DR   OrthoDB; 1579773at2759; -.
DR   PhylomeDB; Q5ZMA3; -.
DR   PRO; PR:Q5ZMA3; -.
DR   Proteomes; UP000000539; Unplaced.
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; IMP: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   1: Evidence at protein 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"
FT                   /id="PRO_0000273371"
FT   DOMAIN          11..88
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ   SEQUENCE   225 AA;  23892 MW;  976D19C0739DB443 CRC64;
     MHTTQKDTTY TKIFVGGLPY HTTDSSLRKY FEVFGDIEEA VVITDRQTGK SRGYGFVTMA
     DRAAAERACK DPNPIIDGRK ANVNLAYLGA KPRIMQPGFA FGVQQLHPAL IQRPFGIPAH
     YVYPQAFVQP GVVIPHVQPA AAAASTTPYI GYTGAAYAQY SAAAAAYEQY PYAASPAAAA
     GYVAAGGYGY AVQQPITAAA PGTAAAAAAA FGQYQPQQLQ TDRMQ
 
 
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