ID A0A8B8XDM1_BALMU Unreviewed; 501 AA. AC A0A8B8XDM1; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 02-OCT-2024, entry version 13. DE RecName: Full=RNA-binding protein 8A {ECO:0000256|RuleBase:RU361239}; GN Name=LIX1L {ECO:0000313|RefSeq:XP_036707788.1}; OS Balaenoptera musculus (Blue whale). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti; OC Balaenopteridae; Balaenoptera. OX NCBI_TaxID=9771 {ECO:0000313|Proteomes:UP000694857, ECO:0000313|RefSeq:XP_036707788.1}; RN [1] {ECO:0000313|RefSeq:XP_036707788.1} RP IDENTIFICATION. RC TISSUE=Epidermis and Blubber {ECO:0000313|RefSeq:XP_036707788.1}; RG RefSeq; RL Submitted (JUN-2024) to UniProtKB. CC -!- FUNCTION: Core component of the splicing-dependent multiprotein exon CC junction complex (EJC) deposited at splice junctions on mRNAs. CC {ECO:0000256|RuleBase:RU361239}. CC -!- SUBUNIT: Heterodimer with MAGOH. Part of the mRNA splicing-dependent CC exon junction complex (EJC) complex; the core complex contains CASC3, CC EIF4A3, MAGOH and RBM8A. {ECO:0000256|RuleBase:RU361239}. CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324, CC ECO:0000256|RuleBase:RU361239}. Nucleus CC {ECO:0000256|RuleBase:RU361239}. Cytoplasm CC {ECO:0000256|RuleBase:RU361239}. CC -!- SIMILARITY: Belongs to the LIX1 family. CC {ECO:0000256|ARBA:ARBA00007468}. CC -!- SIMILARITY: Belongs to the RBM8A family. CC {ECO:0000256|ARBA:ARBA00007987, ECO:0000256|RuleBase:RU361239}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_036707788.1; XM_036851893.1. DR KEGG; bmus:118895019; -. DR Proteomes; UP000694857; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW. DR GO; GO:0003729; F:mRNA binding; IEA:InterPro. DR GO; GO:0097352; P:autophagosome maturation; IEA:TreeGrafter. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR CDD; cd12324; RRM_RBM8; 1. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR051436; Autophagy-related_EPG5. DR InterPro; IPR029270; LIX1. 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; PTHR31139; ECTOPIC P GRANULES PROTEIN 5 HOMOLOG; 1. DR PANTHER; PTHR31139:SF3; LIX1-LIKE PROTEIN; 1. DR Pfam; PF14954; LIX1; 1. DR Pfam; PF00076; RRM_1; 1. DR PRINTS; PR01738; RNABINDINGM8. DR SMART; SM00360; RRM; 1. DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|RuleBase:RU361239}; KW mRNA processing {ECO:0000256|RuleBase:RU361239}; KW mRNA splicing {ECO:0000256|RuleBase:RU361239}; KW mRNA transport {ECO:0000256|RuleBase:RU361239}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361239}; KW Reference proteome {ECO:0000313|Proteomes:UP000694857}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE- KW ProRule:PRU00176}; Spliceosome {ECO:0000256|ARBA:ARBA00022728}; KW Transport {ECO:0000256|RuleBase:RU361239}. FT DOMAIN 400..478 FT /note="RRM" FT /evidence="ECO:0000259|PROSITE:PS50102" FT REGION 1..64 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 356..395 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 478..501 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 39..61 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 363..392 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 483..501 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 501 AA; 55134 MW; 5CA191A09D8173A0 CRC64; METLRAQRLQ PGVGTSGRGT LRALRPGVTG AAAATATPQA GPPPAPPPPA PPPPPLLLSG AAGLPLPPGA AGSPAVLREA VEAVVRSFAK HTQGYGRVNV VEALQEFWQM KQSRGADLKN GALVVYEMVP SNSPPYVCYV TLPGGSCFGS FQFCPTKAEA RRSAAKIALM NSVFNEHPSR RITDEFIEKS VSEALASFNG NREEADNPNT GIGAFRFMLE SNKGKSMLEF QELMTVFQLL HWNGSLKAMR ERQCSRQEVL AHYSHRALDD DIRHQMALDW VSREQSVPGA LSRELASTER ELDEARLAVS RGAKCLSVTE ESSSLGKMAD VLDLHEAGGE DFAMDEDGDE SIHKLKEKAK KRKGRGFGSE EGSRARMRED YDSVEQDGDE PGPQRSVEGW ILFVTGVHEE ATEEDIHDKF AEYGEIKNIH LNLDRRTGYL KGYTLVEYET YKEAQAAMEG LNGQDLMGQP ISVDWCFVRG PPKGKRRGGR RRSRSPDRRR R //