SRSF1_PIG
ID SRSF1_PIG Reviewed; 248 AA.
AC Q3YLA6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Serine/arginine-rich splicing factor 1;
DE AltName: Full=Splicing factor, arginine/serine-rich 1;
GN Name=SRSF1; Synonyms=SFRS1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Fetal skeletal muscle;
RX PubMed=16293136; DOI=10.1111/j.1365-2052.2005.01370.x;
RA Wang H., Wang H.L., Zhu Z.M., Yang S.L., Li K.;
RT "Molecular cloning, polymorphism and mapping of the porcine SFRS1 gene.";
RL Anim. Genet. 36:526-527(2005).
CC -!- FUNCTION: Plays a role in preventing exon skipping, ensuring the
CC accuracy of splicing and regulating alternative splicing. Interacts
CC with other spliceosomal components, via the RS domains, to form a
CC bridge between the 5'- and 3'-splice site binding components, U1 snRNP
CC and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-
CC containing pre-mRNA. Binds to purine-rich RNA sequences, either the
CC octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers,
CC AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif
CC in vitro. Three copies of the octamer constitute a powerful splicing
CC enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can
CC specifically activate ASE-dependent splicing. May function as export
CC adapter involved in mRNA nuclear export through the TAP/NXF1 pathway
CC (By similarity). {ECO:0000250|UniProtKB:Q07955}.
CC -!- SUBUNIT: Consists of two polypeptides of p32 and p33. Identified in the
CC spliceosome C complex. Component of a ribonucleoprotein complex
CC containing mRNAs and RNA-binding proteins including DDX5, HNRNPH2 and
CC SRSF1 as well as splicing regulator ARVCF. In vitro, self-associates
CC and binds SRSF2, SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12.
CC Interacts with SAFB/SAFB1. Interacts with PSIP1/LEDGF. Interacts with
CC RSRC1 (via Arg/Ser-rich domain). Interacts with ZRSR2/U2AF1-RS2.
CC Interacts with CCDC55 (via C-terminus). Interacts with SRPK1 and a
CC sliding docking interaction is essential for its sequential and
CC processive phosphorylation by SRPK1. Interacts with NXF1. Interacts
CC with CCNL1, CCNL2 and CDK11B. Interacts with RRP1B. Interacts (when
CC phosphorylated in its RS domain) with TNPO3; promoting nuclear import.
CC Interacts with ILDR1 (via C-terminus) and ILDR2.
CC {ECO:0000250|UniProtKB:Q07955, ECO:0000250|UniProtKB:Q6PDM2}.
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. Nuclear import is
CC mediated via interaction with TNPO3. {ECO:0000250|UniProtKB:Q07955}.
CC -!- DOMAIN: The RRM 2 domain plays an important role in governing both the
CC binding mode and the phosphorylation mechanism of the RS domain by
CC SRPK1. RS domain and RRM 2 are uniquely positioned to initiate a highly
CC directional (C-terminus to N-terminus) phosphorylation reaction in
CC which the RS domain slides through an extended electronegative channel
CC separating the docking groove of SRPK1 and the active site. RRM 2 binds
CC toward the periphery of the active site and guides the directional
CC phosphorylation mechanism. Both the RS domain and an RRM domain are
CC required for nucleocytoplasmic shuttling (By similarity).
CC {ECO:0000250|UniProtKB:Q07955}.
CC -!- PTM: Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Phosphorylated by
CC SRPK1 at multiple serines in its RS domain via a directional (C-
CC terminal to N-terminal) and a dual-track mechanism incorporating both
CC processive phosphorylation (in which the kinase stays attached to the
CC substrate after each round of phosphorylation) and distributive
CC phosphorylation steps (in which the kinase and substrate dissociate
CC after each phosphorylation event). The RS domain of SRSF1 binds to a
CC docking groove in the large lobe of the kinase domain of SRPK1 and this
CC induces certain structural changes in SRPK1 and/or RRM 2 domain of
CC SRSF1, allowing RRM 2 to bind the kinase and initiate phosphorylation.
CC The cycles continue for several phosphorylation steps in a processive
CC manner (steps 1-8) until the last few phosphorylation steps
CC (approximately steps 9-12). During that time, a mechanical stress
CC induces the unfolding of the beta-4 motif in RRM 2, which then docks at
CC the docking groove of SRPK1. This also signals RRM 2 to begin to
CC dissociate, which facilitates SRSF1 dissociation after phosphorylation
CC is completed (By similarity). {ECO:0000250|UniProtKB:Q07955}.
CC -!- PTM: Asymmetrically dimethylated at arginines, probably by PRMT1,
CC methylation promotes localization to nuclear speckles.
CC {ECO:0000250|UniProtKB:Q07955}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; DQ098951; AAZ86089.1; -; Genomic_DNA.
DR EMBL; DQ098950; AAZ86088.1; -; mRNA.
DR RefSeq; NP_001033096.1; NM_001038007.1.
DR AlphaFoldDB; Q3YLA6; -.
DR BMRB; Q3YLA6; -.
DR SMR; Q3YLA6; -.
DR STRING; 9823.ENSSSCP00000018680; -.
DR PaxDb; Q3YLA6; -.
DR PeptideAtlas; Q3YLA6; -.
DR PRIDE; Q3YLA6; -.
DR Ensembl; ENSSSCT00000043811; ENSSSCP00000057414; ENSSSCG00000017626.
DR Ensembl; ENSSSCT00015085769; ENSSSCP00015034868; ENSSSCG00015063911.
DR Ensembl; ENSSSCT00025025450; ENSSSCP00025010750; ENSSSCG00025018725.
DR Ensembl; ENSSSCT00030071795; ENSSSCP00030032731; ENSSSCG00030051510.
DR Ensembl; ENSSSCT00035089681; ENSSSCP00035037508; ENSSSCG00035066552.
DR Ensembl; ENSSSCT00040020695; ENSSSCP00040008693; ENSSSCG00040015341.
DR Ensembl; ENSSSCT00045035907; ENSSSCP00045024966; ENSSSCG00045020995.
DR Ensembl; ENSSSCT00050046484; ENSSSCP00050019237; ENSSSCG00050034576.
DR Ensembl; ENSSSCT00055034498; ENSSSCP00055027403; ENSSSCG00055017510.
DR Ensembl; ENSSSCT00060028231; ENSSSCP00060012096; ENSSSCG00060020808.
DR Ensembl; ENSSSCT00065037964; ENSSSCP00065016013; ENSSSCG00065028144.
DR GeneID; 654327; -.
DR KEGG; ssc:654327; -.
DR CTD; 6426; -.
DR VGNC; VGNC:99084; SRSF1.
DR eggNOG; KOG0105; Eukaryota.
DR GeneTree; ENSGT00940000155585; -.
DR HOGENOM; CLU_012062_34_0_1; -.
DR InParanoid; Q3YLA6; -.
DR OMA; HRMQISG; -.
DR OrthoDB; 1321443at2759; -.
DR TreeFam; TF106261; -.
DR Reactome; R-SSC-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-SSC-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-SSC-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-SSC-72187; mRNA 3'-end processing.
DR Reactome; R-SSC-73856; RNA Polymerase II Transcription Termination.
DR Proteomes; UP000008227; Chromosome 12.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000017626; Expressed in hindlimb bud and 43 other tissues.
DR ExpressionAtlas; Q3YLA6; baseline and differential.
DR Genevisible; Q3YLA6; SS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
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 Acetylation; Cytoplasm; Isopeptide bond; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT CHAIN 2..248
FT /note="Serine/arginine-rich splicing factor 1"
FT /id="PRO_0000247977"
FT DOMAIN 16..91
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 121..195
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 88..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..247
FT /note="Interaction with SAFB1"
FT /evidence="ECO:0000250"
FT COMPBIAS 205..225
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955, ECO:0000255"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 38
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 93
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 93
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 97
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 97
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 109
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 109
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 111
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 202
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT CROSSLNK 30
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT CROSSLNK 38
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
SQ SEQUENCE 248 AA; 27745 MW; C28A0B2F112EA713 CRC64;
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE
FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE
NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF
RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR
HSRSRSRT
