ID A0A7F8Q5C7_LEPWE Unreviewed; 649 AA. AC A0A7F8Q5C7; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 03-MAY-2023, entry version 10. DE RecName: Full=RNA-binding protein with serine-rich domain 1 {ECO:0000256|ARBA:ARBA00014789}; GN Name=LOC102728895 {ECO:0000313|RefSeq:XP_030876462.1}; OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Leptonychotes. OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_030876462.1}; RN [1] {ECO:0000313|RefSeq:XP_030876462.1} RP IDENTIFICATION. RC TISSUE=Liver {ECO:0000313|RefSeq:XP_030876462.1}; RG RefSeq; RL Submitted (JAN-2023) to UniProtKB. CC -!- SUBUNIT: Found in mRNA splicing-dependent exon junction complexes CC (EJC). Found in a post-splicing complex with NXF1, RBM8A, UPF1, UPF2, CC UPF3A, UPF3B and RNPS1. Component of the heterotrimeric ASAP CC (apoptosis- and splicing-associated protein) and PSAP complexes CC consisting of RNPS1, SAP18 and either ACIN1 or PNN, respectively; the CC ASAP and PSAP complexes probably are formed mutually exclusive. CC Component of the active spliceosome. Associates with polysomes. CC Interacts with the cleaved p110 isoform of CDC2L1, CSNK2A1, PNN, SART3, CC SRP54, SRRM1 and TRA2B/SFRS10. {ECO:0000256|ARBA:ARBA00026044}. CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}. CC -!- SIMILARITY: Belongs to the splicing factor SR family. CC {ECO:0000256|ARBA:ARBA00010269}. 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_030876462.1; XM_031020602.1. DR AlphaFoldDB; A0A7F8Q5C7; -. DR OrthoDB; 12385at2759; -. DR Proteomes; UP000245341; Unplaced. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR CDD; cd12365; RRM_RNPS1; 1. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR026082; ABCA. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR034201; RNPS1_RRM. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1. DR PANTHER; PTHR19229:SF98; PHOSPHOLIPID-TRANSPORTING ATPASE ABCA3; 1. DR Pfam; PF12698; ABC2_membrane_3; 1. DR Pfam; PF00076; RRM_1; 1. DR SMART; SM00360; RRM; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000313|RefSeq:XP_030876462.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000313|RefSeq:XP_030876462.1}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Reference proteome {ECO:0000313|Proteomes:UP000245341}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE- KW ProRule:PRU00176}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 22..42 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 265..283 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 303..329 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 345..368 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 374..393 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 505..584 FT /note="RRM" FT /evidence="ECO:0000259|PROSITE:PS50102" FT REGION 583..649 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 584..609 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 610..649 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 649 AA; 74584 MW; 5188B4DDF7AAA593 CRC64; MAVLRQLVLL LWKNYTVQKR KVLVTVLELF LPLLFSGILI WLRLKIQSEN VPNATIYPGQ SIQELPLFFS FPPPGDTWEL AYIPSQSDAV KTITEMARRT LVINMRARGF PSEKDFEDYI RYNNRSSNVL AALVFEHTFN HSGEPLPLAV KYHLRFSDTR RNYMWTQTGS FFLKETEGWH TTSLFPLFPN PGPREPASPD GGEPGYIREG FLAVQHAVDR AIMQYHANAS TRQLFEKLTV IAKRFPYPPF ISDPFLVAIQ YQLPLLLMLS FTYTSLTIIR AVVQEKERKL KEYMRMMGLS SWLHWSAWFL LFFFFLLVAV SCVTLLFCVK VKKDVAVLTH SDPSLVLVFL LCFATSSVSF SFMVSTFFSK ANMAAAIGGF LYFFTYIPYF FVAPRYNWMT LSQKLLSCLL SNVAMAMGAQ LIGKFEAKEP TCWGVSSRED LGGVEGAVAA KRRQEGEHEL LHGCGVVLAF PKLIVSGVLF FSIRSKPPKR DEKERKRRSP SPKPTKVHIG RLTRNVTKDH IMEIFSTYGK IKMIDMPVER MHPHLSKGYA YVEFENPDEA EKALKHMDGG QIDGQEITAT AVLAPWPRPP PRRFSPPRRM LPPPPMWRRS PPRMRRRSRS PRRRSPVRRR SRSPGRRRHR SRSSSNSSR //