SRSF1_XENTR
ID SRSF1_XENTR Reviewed; 267 AA.
AC Q6DII2;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Serine/arginine-rich splicing factor 1;
DE AltName: Full=Splicing factor, arginine/serine-rich 1;
GN Name=srsf1; Synonyms=sfrs1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in preventing exon skipping, ensuring the
CC accuracy of splicing and regulating alternative splicing.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q07955}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q07955}. Note=In nuclear speckles.
CC Shuttles between the nucleus and the cytoplasm.
CC {ECO:0000250|UniProtKB:Q07955}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; BC075558; AAH75558.1; -; mRNA.
DR RefSeq; NP_001006919.1; NM_001006918.1.
DR AlphaFoldDB; Q6DII2; -.
DR BMRB; Q6DII2; -.
DR SMR; Q6DII2; -.
DR PRIDE; Q6DII2; -.
DR DNASU; 448766; -.
DR GeneID; 448766; -.
DR KEGG; xtr:448766; -.
DR CTD; 6426; -.
DR Xenbase; XB-GENE-486875; srsf1.
DR eggNOG; KOG0105; Eukaryota.
DR InParanoid; Q6DII2; -.
DR OrthoDB; 1321443at2759; -.
DR PhylomeDB; Q6DII2; -.
DR Reactome; R-XTR-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-XTR-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-XTR-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-XTR-72187; mRNA 3'-end processing.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000008954; Expressed in gastrula and 25 other tissues.
DR ExpressionAtlas; Q6DII2; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd12597; RRM1_SRSF1; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034520; SRSF1_RRM1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; RNA-binding.
FT CHAIN 1..267
FT /note="Serine/arginine-rich splicing factor 1"
FT /id="PRO_0000081916"
FT DOMAIN 16..91
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 140..214
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 90..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..244
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 267 AA; 28832 MW; 9F58AF0CF9F88E29 CRC64;
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE
FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGAGGRGG GGGGGGGGGG GGGGGGGGGG
GGGGGAPRGR YGPPSRRSEY RVVVSGLPPS GSWQDLKDHM REAGDVCYAD VFRDGTGVVE
FVRKEDMTYA VRKLDNTKFR SHEGETAYIR VKVDGPRSPS YGRSRSRSRS RSRSRSRSNS
RSRSYSPRRS RGSPRYSPRH SRSRSRT