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