ID   RBM8A_RAT               Reviewed;         174 AA.
AC   Q27W01;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=RNA-binding protein 8A;
DE   AltName: Full=RNA-binding motif protein 8A;
DE   AltName: Full=Ribonucleoprotein RBM8A;
GN   Name=Rbm8a; Synonyms=Rbm8;
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 [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RX   PubMed=16275927; DOI=10.1073/pnas.0503783102;
RA   Glanzer J., Miyashiro K.Y., Sul J.-Y., Barrett L., Belt B., Haydon P.,
RA   Eberwine J.;
RT   "RNA splicing capability of live neuronal dendrites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:16859-16864(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-56, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC       spliceosome (By similarity). Core component of the splicing-dependent
CC       multiprotein exon junction complex (EJC) deposited at splice junctions
CC       on mRNAs. The EJC is a dynamic structure consisting of core proteins
CC       and several peripheral nuclear and cytoplasmic associated factors that
CC       join the complex only transiently either during EJC assembly or during
CC       subsequent mRNA metabolism. The EJC marks the position of the exon-exon
CC       junction in the mature mRNA for the gene expression machinery and the
CC       core components remain bound to spliced mRNAs throughout all stages of
CC       mRNA metabolism thereby influencing downstream processes including
CC       nuclear mRNA export, subcellular mRNA localization, translation
CC       efficiency and nonsense-mediated mRNA decay (NMD). Its removal from
CC       cytoplasmic mRNAs requires translation initiation from EJC-bearing
CC       spliced mRNAs. Associates preferentially with mRNAs produced by
CC       splicing. Does not interact with pre-mRNAs, introns, or mRNAs produced
CC       from intronless cDNAs. Associates with both nuclear mRNAs and newly
CC       exported cytoplasmic mRNAs (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y5S9}.
CC   -!- SUBUNIT: Heterodimer with either MAGOH or MAGOHB. Part of the mRNA
CC       splicing-dependent exon junction complex (EJC) complex; the core
CC       complex contains CASC3, EIF4A3, MAGOH or MAGOHB, and RBM8A. Interacts
CC       with PYM1; the interaction is direct and dissociates the EJC from
CC       spliced mRNAs. Part of a complex that contains the EJC core components
CC       CASC3, EIF4A3, MAGOH and RBM8A plus proteins involved in nonsense-
CC       mediated mRNA decay, such as UPF1, UPF2, UPF3A and UPF3B. Found in a
CC       post-splicing complex with NXF1, MAGOH, UPF1, UPF2, UPF3A, UPF3B and
CC       RNPS1. Interacts with DDX39B, MAGOH, DPH1, UPF3B, RNPS1, SRRM1 and
CC       ALYREF/THOC4. Interacts with IPO13; the interaction mediates the
CC       nuclear import of the MAGOH-RBM8A heterodimer. Identified in the
CC       spliceosome C complex. Associates with polysomes.
CC       {ECO:0000250|UniProtKB:Q9Y5S9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16275927}. Nucleus
CC       speckle {ECO:0000269|PubMed:16275927}. Cytoplasm
CC       {ECO:0000269|PubMed:16275927}. Note=Nucleocytoplasmic shuttling
CC       protein. Travels to the cytoplasm as part of the exon junction complex
CC       (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1
CC       and UAP56 in the nucleus and nuclear speckles.
CC       {ECO:0000250|UniProtKB:Q9Y5S9}.
CC   -!- SIMILARITY: Belongs to the RBM8A family. {ECO:0000305}.
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DR   EMBL; DQ359102; ABD46661.1; -; mRNA.
DR   RefSeq; NP_001258067.1; NM_001271138.1.
DR   AlphaFoldDB; Q27W01; -.
DR   SMR; Q27W01; -.
DR   BioGRID; 254951; 2.
DR   IntAct; Q27W01; 2.
DR   STRING; 10116.ENSRNOP00000028807; -.
DR   iPTMnet; Q27W01; -.
DR   PhosphoSitePlus; Q27W01; -.
DR   jPOST; Q27W01; -.
DR   PaxDb; 10116-ENSRNOP00000028807; -.
DR   Ensembl; ENSRNOT00000028807.8; ENSRNOP00000028807.4; ENSRNOG00000021215.8.
DR   Ensembl; ENSRNOT00055056129; ENSRNOP00055046282; ENSRNOG00055032492.
DR   Ensembl; ENSRNOT00060021407; ENSRNOP00060016906; ENSRNOG00060012608.
DR   Ensembl; ENSRNOT00065055410; ENSRNOP00065045582; ENSRNOG00065032176.
DR   GeneID; 295284; -.
DR   KEGG; rno:295284; -.
DR   UCSC; RGD:1310099; rat.
DR   AGR; RGD:1310099; -.
DR   CTD; 9939; -.
DR   RGD; 1310099; Rbm8a.
DR   eggNOG; KOG0130; Eukaryota.
DR   GeneTree; ENSGT00730000111185; -.
DR   HOGENOM; CLU_012062_18_3_1; -.
DR   InParanoid; Q27W01; -.
DR   OMA; CEFGDIK; -.
DR   OrthoDB; 36315at2759; -.
DR   PhylomeDB; Q27W01; -.
DR   TreeFam; TF314933; -.
DR   Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-RNO-72187; mRNA 3'-end processing.
DR   Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR   Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:Q27W01; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000021215; Expressed in thymus and 20 other cell types or tissues.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0035145; C:exon-exon junction complex; ISO:RGD.
DR   GO; GO:1990501; C:exon-exon junction subcomplex mago-y14; ISO:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; ISS:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:RGD.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0050684; P:regulation of mRNA processing; ISO:RGD.
DR   GO; GO:2000622; P:regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:RGD.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR   CDD; cd12324; RRM_RBM8; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR008111; RNA-bd_8.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR033744; RRM_RBM8.
DR   PANTHER; PTHR45894; RNA-BINDING PROTEIN 8A; 1.
DR   PANTHER; PTHR45894:SF1; RNA-BINDING PROTEIN 8A; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PRINTS; PR01738; RNABINDINGM8.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   Genevisible; Q27W01; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Isopeptide bond; mRNA processing; mRNA splicing;
KW   mRNA transport; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; Spliceosome; Translation regulation;
KW   Transport; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5S9"
FT   CHAIN           2..174
FT                   /note="RNA-binding protein 8A"
FT                   /id="PRO_0000378563"
FT   DOMAIN          73..151
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..174
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5S9"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5S9"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CROSSLNK        27
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5S9"
SQ   SEQUENCE   174 AA;  19889 MW;  70BBD03CDDFEECFE CRC64;
     MADVLDLHEA GGEDFAMDED GDESIHKLKE KAKKRKGRGF GSEEGSRARM REDYDSVEQD
     GDEPGPQRSV EGWILFVTGV HEEATEEDIH DKFAEYGEIK NIHLNLDRRT GYLKGYTLVE
     YETYKEAQAA MEGLNGQDLM GQPISVDWCF VRGPPKGKRR GGRRRSRSPD RRRR
//