SRSF3_MOUSE
ID SRSF3_MOUSE Reviewed; 164 AA.
AC P84104; O08831; P23152; Q564E9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Serine/arginine-rich splicing factor 3;
DE AltName: Full=Pre-mRNA-splicing factor SRP20;
DE AltName: Full=Protein X16;
DE AltName: Full=Splicing factor, arginine/serine-rich 3;
GN Name=Srsf3; Synonyms=Sfrs3, Srp20, X16;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=2030943; DOI=10.1093/nar/19.6.1273;
RA Ayane M., Preuss U., Koehler G., Nielsen P.J.;
RT "A differentially expressed murine RNA encoding a protein with similarities
RT to two types of nucleic acid binding motifs.";
RL Nucleic Acids Res. 19:1273-1278(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=MRL/MpJ; TISSUE=Lymphoid tissue;
RX PubMed=9154810; DOI=10.1128/mcb.17.6.3116;
RA Jumaa H., Guenet J.-L., Nielsen P.J.;
RT "Regulated expression and RNA processing of transcripts from the Srp20
RT splicing factor gene during the cell cycle.";
RL Mol. Cell. Biol. 17:3116-3124(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=C57BL/6J, and DBA/2J;
RC TISSUE=Bone marrow, Colon, Mammary gland, Placenta, Thymus, and
RC Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION BY CLK1; CLK2; CLK3 AND CLK4.
RX PubMed=9307018; DOI=10.1042/bj3260693;
RA Nayler O., Stamm S., Ullrich A.;
RT "Characterization and comparison of four serine- and arginine-rich (SR)
RT protein kinases.";
RL Biochem. J. 326:693-700(1997).
RN [6]
RP INTERACTION WITH YTHDC1.
RX PubMed=29799838; DOI=10.1371/journal.pgen.1007412;
RA Kasowitz S.D., Ma J., Anderson S.J., Leu N.A., Xu Y., Gregory B.D.,
RA Schultz R.M., Wang P.J.;
RT "Nuclear m6A reader YTHDC1 regulates alternative polyadenylation and
RT splicing during mouse oocyte development.";
RL PLoS Genet. 14:e1007412-e1007412(2018).
CC -!- FUNCTION: Splicing factor that specifically promotes exon-inclusion
CC during alternative splicing. Interaction with YTHDC1, a RNA-binding
CC protein that recognizes and binds N6-methyladenosine (m6A)-containing
CC RNAs, promotes recruitment of SRSF3 to its mRNA-binding elements
CC adjacent to m6A sites, leading to exon-inclusion during alternative
CC splicing. Also functions as export adapter involved in mRNA nuclear
CC export. Binds mRNA which is thought to be transferred to the NXF1-NXT1
CC heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-
CC binding activity. Involved in nuclear export of m6A-containing mRNAs
CC via interaction with YTHDC1: interaction with YTHDC1 facilitates m6A-
CC containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear
CC export. RNA-binding is semi-sequence specific.
CC {ECO:0000250|UniProtKB:P84103}.
CC -!- SUBUNIT: Interacts with CPSF6 (By similarity). Interacts with RBMY1A1
CC (By similarity). Interacts with SREK1/SFRS12 (By similarity). Interacts
CC with NXF1 (By similarity). Interacts with YTHDC1, leading to
CC recruitment to RNA elements adjacent to m6A sites (PubMed:29799838).
CC {ECO:0000250|UniProtKB:P84103, ECO:0000269|PubMed:29799838}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P84103}. Nucleus
CC speckle {ECO:0000250|UniProtKB:P84103}. Cytoplasm
CC {ECO:0000250|UniProtKB:P84103}. Note=Recruited to nuclear speckles
CC following interaction with YTHDC1. {ECO:0000250|UniProtKB:P84103}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P84104-1, P23152-1;
CC Sequence=Displayed;
CC Name=Short;
CC IsoId=P84104-2, P23152-2;
CC Sequence=VSP_005861, VSP_005862;
CC -!- TISSUE SPECIFICITY: Highest expression in thymus and pre-B cell lines;
CC high, in testis, brain and spleen; very low in heart and not detectable
CC in liver and kidney. {ECO:0000269|PubMed:2030943}.
CC -!- INDUCTION: Isoform long is induced by serum; in a tissue culture.
CC {ECO:0000269|PubMed:2030943}.
CC -!- PTM: Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Extensively
CC phosphorylated on serine residues in the RS domain.
CC {ECO:0000269|PubMed:9307018}.
CC -!- MISCELLANEOUS: [Isoform Short]: May be produced at very low levels due
CC to a premature stop codon in the mRNA, leading to nonsense-mediated
CC mRNA decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; X53824; CAA37821.1; -; mRNA.
DR EMBL; X91656; CAA62844.1; -; Genomic_DNA.
DR EMBL; X91656; CAA62845.1; -; Genomic_DNA.
DR EMBL; AK011657; BAB27762.1; -; mRNA.
DR EMBL; AK078891; BAC37445.1; -; mRNA.
DR EMBL; AK134177; BAE22040.1; -; mRNA.
DR EMBL; AK135298; BAE22483.1; -; mRNA.
DR EMBL; AK145089; BAE26230.1; -; mRNA.
DR EMBL; AK145715; BAE26606.1; -; mRNA.
DR EMBL; AK146010; BAE26830.1; -; mRNA.
DR EMBL; AK146253; BAE27015.1; -; mRNA.
DR EMBL; AK150912; BAE29950.1; -; mRNA.
DR EMBL; AK153209; BAE31808.1; -; mRNA.
DR EMBL; BC068111; AAH68111.1; -; mRNA.
DR EMBL; BC071196; AAH71196.1; -; mRNA.
DR EMBL; BC083316; AAH83316.1; -; mRNA.
DR CCDS; CCDS28590.1; -.
DR PIR; S14016; S14016.
DR RefSeq; NP_038691.1; NM_013663.5. [P84104-1]
DR AlphaFoldDB; P84104; -.
DR SMR; P84104; -.
DR BioGRID; 203189; 53.
DR IntAct; P84104; 6.
DR MINT; P84104; -.
DR STRING; 10090.ENSMUSP00000117045; -.
DR GlyConnect; 2703; 1 N-Linked glycan (1 site).
DR GlyGen; P84104; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; P84104; -.
DR PhosphoSitePlus; P84104; -.
DR SwissPalm; P84104; -.
DR CPTAC; non-CPTAC-3749; -.
DR EPD; P84104; -.
DR jPOST; P84104; -.
DR MaxQB; P84104; -.
DR PaxDb; P84104; -.
DR PeptideAtlas; P84104; -.
DR PRIDE; P84104; -.
DR ProteomicsDB; 258615; -.
DR ProteomicsDB; 258616; -. [P84104-2]
DR Antibodypedia; 29693; 286 antibodies from 31 providers.
DR DNASU; 20383; -.
DR Ensembl; ENSMUST00000037776; ENSMUSP00000049025; ENSMUSG00000071172. [P84104-2]
DR Ensembl; ENSMUST00000130216; ENSMUSP00000117045; ENSMUSG00000071172. [P84104-1]
DR GeneID; 20383; -.
DR KEGG; mmu:20383; -.
DR UCSC; uc008bsd.2; mouse.
DR CTD; 6428; -.
DR MGI; MGI:98285; Srsf3.
DR VEuPathDB; HostDB:ENSMUSG00000071172; -.
DR eggNOG; KOG0107; Eukaryota.
DR GeneTree; ENSGT00910000144115; -.
DR HOGENOM; CLU_012062_20_6_1; -.
DR InParanoid; P84104; -.
DR OMA; EMHRDSC; -.
DR OrthoDB; 1533297at2759; -.
DR PhylomeDB; P84104; -.
DR TreeFam; TF351858; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 20383; 25 hits in 72 CRISPR screens.
DR ChiTaRS; Srsf3; mouse.
DR PRO; PR:P84104; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P84104; protein.
DR Bgee; ENSMUSG00000071172; Expressed in undifferentiated genital tubercle and 257 other tissues.
DR ExpressionAtlas; P84104; baseline and differential.
DR Genevisible; P84104; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043274; F:phospholipase binding; IPI:BHF-UCL.
DR GO; GO:0070878; F:primary miRNA binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:BHF-UCL.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0031053; P:primary miRNA processing; IEA:Ensembl.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:BHF-UCL.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; mRNA processing;
KW mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Transport.
FT CHAIN 1..164
FT /note="Serine/arginine-rich splicing factor 3"
FT /id="PRO_0000081924"
FT DOMAIN 10..83
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 119..133
FT /note="B-1"
FT REPEAT 149..164
FT /note="B-2"
FT REGION 1..90
FT /note="Sufficient for interaction with NXF1"
FT /evidence="ECO:0000250"
FT REGION 81..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..164
FT /note="2 X approximate repeats, basic"
FT COMPBIAS 95..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P84103"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84103"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P84103"
FT VAR_SEQ 115..124
FT /note="SPRRRSFSRS -> VTIMSLLTTL (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_005861"
FT VAR_SEQ 125..164
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_005862"
SQ SEQUENCE 164 AA; 19330 MW; 02F0A5EE33FF28A0 CRC64;
MHRDSCPLDC KVYVGNLGNN GNKTELERAF GYYGPLRSVW VARNPPGFAF VEFEDPRDAA
DAVRELDGRT LCGCRVRVEL SNGEKRSRNR GPPPSWGRRP RDDYRRRSPP PRRRSPRRRS
FSRSRSRSLS RDRRRERSLS RERNHKPSRS FSRSRSRSRS NERK
