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RNP1A_XENLA
ID   RNP1A_XENLA             Reviewed;         283 AA.
AC   Q5XG24;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=RNA-binding protein with serine-rich domain 1-A;
GN   Name=rnps1-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) 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; BC084646; AAH84646.1; -; mRNA.
DR   RefSeq; NP_001088379.1; NM_001094910.1.
DR   AlphaFoldDB; Q5XG24; -.
DR   SMR; Q5XG24; -.
DR   DNASU; 495230; -.
DR   GeneID; 495230; -.
DR   KEGG; xla:495230; -.
DR   CTD; 495230; -.
DR   Xenbase; XB-GENE-941532; rnps1.S.
DR   OrthoDB; 1524222at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 495230; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 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-A"
FT                   /id="PRO_0000081821"
FT   DOMAIN          161..240
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..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..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..243
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..283
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   283 AA;  31805 MW;  1606CC74076F2B7F CRC64;
     MAPSPSKRKE RSEDRAKERG KEKAPGKEVT EKDRGRDKAK KRRSGSSGSS SSSHSRSSSS
     SSSSSGSSSG SSSGSSSSAS SRSGSSSSSR SSSSSSSSGS PSPSRRRHDN RRRSRSKSKQ
     PKRDEKERKR RSPSPRPTKV HIGRLTRNVT KDHILEIFST YGKIKMIDMP VDRYHPHLSK
     GYAYVEFEAP EEAEKALKHM DGGQIDGQEI TASAVLTPWP MRPMPRRFSP PRRMLPPPPM
     WRRSPPRMRR RSRSPRRRSP VRRRSRSPAR RRHRSRSSSN SSR
 
 
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