RBM24_RAT
ID RBM24_RAT Reviewed; 236 AA.
AC M0R7T6;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 4.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=RNA-binding protein 24 {ECO:0000305};
DE AltName: Full=RNA-binding motif protein 24 {ECO:0000305};
GN Name=Rbm24 {ECO:0000303|PubMed:27289039, ECO:0000312|RGD:1584029};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION.
RX PubMed=27289039; DOI=10.1002/1873-3468.12251;
RA Ito J., Iijima M., Yoshimoto N., Niimi T., Kuroda S., Maturana A.D.;
RT "RBM20 and RBM24 cooperatively promote the expression of short enh splice
RT variants.";
RL FEBS Lett. 590:2262-2274(2016).
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 (PubMed:27289039).
CC Plays a major role in pre-mRNA alternative splicing regulation (By
CC similarity). Mediates preferentially muscle-specific exon inclusion in
CC numerous mRNAs important for striated cardiac and skeletal muscle cell
CC differentiation (By similarity). Binds to intronic splicing enhancer
CC (ISE) composed of stretches of GU-rich motifs localized in flanking
CC intron of exon that will be included by alternative splicing (By
CC similarity). Involved in embryonic stem cell (ESC) transition to
CC cardiac cell differentiation by promoting pre-mRNA alternative splicing
CC events of several pluripotency and/or differentiation genes (By
CC similarity). Plays a role in the regulation of mRNA stability (By
CC similarity). Binds to 3'-untranslated region (UTR) AU-rich elements in
CC target transcripts, such as CDKN1A and MYOG, leading to maintain their
CC stabilities (By similarity). Involved in myogenic differentiation by
CC regulating MYOG levels (By similarity). Binds to multiple regions in
CC the mRNA 3'-UTR of TP63 isoform 2, hence inducing its destabilization
CC (By similarity). Promotes also the destabilization of the CHRM2 mRNA
CC via its binding to a region in the coding sequence (By similarity).
CC Plays a role in the regulation of mRNA translation (By similarity).
CC Mediates repression of p53/TP53 mRNA translation through its binding to
CC U-rich element in the 3'-UTR, hence preventing EIF4E from binding to
CC p53/TP53 mRNA and translation initiation (By similarity). Binds to a
CC huge amount of mRNAs (By similarity). Required for embryonic heart
CC development, sarcomer and M-band formation in striated muscles (By
CC similarity). Together with RBM20, promotes the expression of short
CC isoforms of PDLIM5/ENH in cardiomyocytes (PubMed:27289039).
CC {ECO:0000250|UniProtKB:D3Z4I3, ECO:0000250|UniProtKB:Q9BX46,
CC ECO:0000269|PubMed:27289039}.
CC -!- SUBUNIT: Interacts with EIF4E; this interaction prevents EIF4E from
CC binding to p53/TP53 mRNA and inhibits the assembly of translation
CC initiation complex. {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 AlphaFoldDB; M0R7T6; -.
DR SMR; M0R7T6; -.
DR STRING; 10116.ENSRNOP00000065520; -.
DR PaxDb; M0R7T6; -.
DR Ensembl; ENSRNOT00000072682.3; ENSRNOP00000065520.3; ENSRNOG00000046547.3.
DR RGD; 1584029; Rbm24.
DR VEuPathDB; HostDB:ENSRNOG00000046547; -.
DR eggNOG; KOG0149; Eukaryota.
DR GeneTree; ENSGT00940000156245; -.
DR HOGENOM; CLU_065652_0_1_1; -.
DR InParanoid; M0R7T6; -.
DR OMA; IPAHYMY; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000046547; Expressed in skeletal muscle tissue and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:RGD.
DR GO; GO:1990715; F:mRNA CDS binding; ISO:RGD.
DR GO; GO:0097157; F:pre-mRNA intronic binding; ISO:RGD.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISO:RGD.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0003197; P:endocardial cushion development; ISO:RGD.
DR GO; GO:0061157; P:mRNA destabilization; ISO:RGD.
DR GO; GO:0048255; P:mRNA stabilization; ISO:RGD.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISO:RGD.
DR GO; GO:1905870; P:positive regulation of 3'-UTR-mediated mRNA stabilization; ISO:RGD.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; ISO:RGD.
DR GO; GO:1902811; P:positive regulation of skeletal muscle fiber differentiation; ISO:RGD.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; ISO:RGD.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISO:RGD.
DR GO; GO:0010830; P:regulation of myotube differentiation; ISO:RGD.
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 3: Inferred from homology;
KW Cytoplasm; Differentiation; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; RNA-binding; Translation regulation.
FT CHAIN 1..236
FT /note="RNA-binding protein 24"
FT /id="PRO_0000456217"
FT DOMAIN 11..88
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 175..199
FT /note="Necessary for interaction with EIF4E"
FT /evidence="ECO:0000250|UniProtKB:Q9BX46"
SQ SEQUENCE 236 AA; 24852 MW; 770ECF3F8A089495 CRC64;
MHTTQKDTTY TKIFVGGLPY HTTDASLRKY FEVFGDIEEA VVITDRQTGK SRGYGFVTMA
DRAAAERACK DPNPIIDGRK ANVNLAYLGA KPRIMQPGFA FGVQQLHPAL IQRPFGIPAH
YVYPQAFVQP GVVIPHVQPT AAAASTTPYI DYTGAAYAQY SAAAAAAAAA AAYDQYPYAA
SPAATGYVTT GGYSYAVQQP ITAAAPGTAA AAAAAAAAAA AFGQYQPQQL QTDRMQ
