ID   RNPS1_DANRE             Reviewed;         283 AA.
AC   Q6PG31; Q6NZV7;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=RNA-binding protein with serine-rich domain 1;
GN   Name=rnps1; ORFNames=wu:fa19a11, zgc:65775;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of a splicing-dependent multiprotein exon junction
CC       complex (EJC) deposited at splice junction on mRNAs. The EJC is a
CC       dynamic structure consisting of a few core proteins and several more
CC       peripheral nuclear and cytoplasmic associated factors that join the
CC       complex only transiently either during EJC assembly or during
CC       subsequent mRNA metabolism. Putative component of the spliceosome which
CC       enhances the formation of the ATP-dependent A complex of the
CC       spliceosome. May participate in mRNA 3'-end cleavage. Also mediates
CC       increase of mRNA abundance and translational efficiency (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the active spliceosome. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC       {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Nucleocytoplasmic
CC       shuttling protein. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR   EMBL; BC057251; AAH57251.1; -; mRNA.
DR   EMBL; BC065953; AAH65953.1; -; mRNA.
DR   RefSeq; NP_956055.1; NM_199761.1.
DR   RefSeq; XP_009296550.1; XM_009298275.2.
DR   AlphaFoldDB; Q6PG31; -.
DR   SMR; Q6PG31; -.
DR   STRING; 7955.ENSDARP00000111476; -.
DR   PaxDb; Q6PG31; -.
DR   PRIDE; Q6PG31; -.
DR   GeneID; 327020; -.
DR   KEGG; dre:103909923; -.
DR   KEGG; dre:327020; -.
DR   CTD; 10921; -.
DR   ZFIN; ZDB-GENE-030131-5228; rnps1.
DR   eggNOG; KOG4209; Eukaryota.
DR   HOGENOM; CLU_076438_0_0_1; -.
DR   InParanoid; Q6PG31; -.
DR   OMA; DPCKNTG; -.
DR   OrthoDB; 1516210at2759; -.
DR   TreeFam; TF314165; -.
DR   Reactome; R-DRE-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-DRE-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-DRE-72187; mRNA 3'-end processing.
DR   Reactome; R-DRE-73856; RNA Polymerase II Transcription Termination.
DR   Reactome; R-DRE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:Q6PG31; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0061574; C:ASAP complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   CDD; cd12365; RRM_RNPS1; 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; IPR034201; RNPS1_RRM.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR003954; RRM_dom_euk.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00361; RRM_1; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..283
FT                   /note="RNA-binding protein with serine-rich domain 1"
FT                   /id="PRO_0000378575"
FT   DOMAIN          137..216
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..241
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..283
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        44
FT                   /note="S -> N (in Ref. 1; AAH65953)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   283 AA;  31739 MW;  901A925940E9F148 CRC64;
     MAPSPTKRRE RSEDKPRERG KEKAPAKEGA EKERGRDKIR KRRSNSTGSS SSRSSSSSSS
     SSGSSSGSSS GSSSSSGSSR SGSSSSSRSS SSSGSSGSPS PSRRRHDNRR RSRSKSKSQK
     RTDEKERKRR SPSPKPTKLY LGRLTRNVTK DHIQEIFATY GKIKMIDMPS DRLHPNVSKG
     YAYVEYESPE DAQKALKHMD GGQIDGQEIT ATAILAQRIR PAPRRLSPPR RMPPPPPMWR
     RTPPRMRRRS RSPRRRSPVR RRSRSRSPGR RRHRSRSSSN SSR