ID   SRSF9_RAT               Reviewed;         221 AA.
AC   Q5PPI1;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Serine/arginine-rich splicing factor 9;
DE   AltName: Full=Splicing factor, arginine/serine-rich 9;
GN   Name=Srsf9; Synonyms=Sfrs9;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
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   [2]
RP   INTERACTION WITH KHDRBS3.
RX   PubMed=11118435; DOI=10.1074/jbc.m006851200;
RA   Stoss O., Olbrich M., Hartmann A.M., Koenig H., Memmott J., Andreadis A.,
RA   Stamm S.;
RT   "The STAR/GSG family protein rSLM-2 regulates the selection of alternative
RT   splice sites.";
RL   J. Biol. Chem. 276:8665-8673(2001).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-211 AND SER-216, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Plays a role in constitutive splicing and can modulate the
CC       selection of alternative splice sites. Represses the splicing of
CC       MAPT/Tau exon 10 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with KHDRBS3. Interacts with HABP4. Interacts with
CC       NOL3/ARC/NOP30. Interacts with NSEP1/YB-1/YB1. Interacts with
CC       SAFB/SAFB1. Interacts with SRSF6/SFRS6. Interacts with TRA2B/SFRS10.
CC       Interacts with C1QBP. May also interact with DUSP11/PIR1.
CC       {ECO:0000250|UniProtKB:Q13242, ECO:0000250|UniProtKB:Q9D0B0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR   EMBL; BC087684; AAH87684.1; -; mRNA.
DR   RefSeq; NP_001009255.1; NM_001009255.1.
DR   AlphaFoldDB; Q5PPI1; -.
DR   SMR; Q5PPI1; -.
DR   STRING; 10116.ENSRNOP00000001539; -.
DR   iPTMnet; Q5PPI1; -.
DR   PhosphoSitePlus; Q5PPI1; -.
DR   PaxDb; Q5PPI1; -.
DR   PRIDE; Q5PPI1; -.
DR   Ensembl; ENSRNOT00000001539; ENSRNOP00000001539; ENSRNOG00000001163.
DR   GeneID; 288701; -.
DR   KEGG; rno:288701; -.
DR   UCSC; RGD:1309495; rat.
DR   CTD; 8683; -.
DR   RGD; 1309495; Srsf9.
DR   eggNOG; KOG0105; Eukaryota.
DR   GeneTree; ENSGT00940000156839; -.
DR   HOGENOM; CLU_012062_34_0_1; -.
DR   InParanoid; Q5PPI1; -.
DR   OMA; SYIRVCP; -.
DR   OrthoDB; 1315388at2759; -.
DR   PhylomeDB; Q5PPI1; -.
DR   TreeFam; TF106261; -.
DR   Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-RNO-72187; mRNA 3'-end processing.
DR   Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR   PRO; PR:Q5PPI1; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000001163; Expressed in ovary and 20 other tissues.
DR   Genevisible; Q5PPI1; RN.
DR   GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
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   GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0043279; P:response to alkaloid; IEP:RGD.
DR   GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR   CDD; cd12768; RRM2_SRSF9; 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; IPR034995; SRSF9_RRM2.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; RNA-binding; Ubl conjugation.
FT   CHAIN           1..221
FT                   /note="Serine/arginine-rich splicing factor 9"
FT                   /id="PRO_0000081937"
FT   DOMAIN          14..89
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          111..187
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          187..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..200
FT                   /note="Interaction with SAFB1"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        190..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13242"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13242"
FT   MOD_RES         195
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13242"
FT   MOD_RES         204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13242"
FT   MOD_RES         211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16641100,
FT                   ECO:0007744|PubMed:22673903"
FT   MOD_RES         214
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13242"
FT   MOD_RES         216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CROSSLNK        36
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13242"
SQ   SEQUENCE   221 AA;  25498 MW;  1B4E6F847D7A97A9 CRC64;
     MSGWADERGG EGDGRIYVGN LPTDVREKDL EDLFYKYGRI REIELKNRHG LVPFAFVRFE
     DPRDAEDAIY GRNGYDYGQC RLRVEFPRAY GGRGGWPRAS RNGPPTRRSD FRVLVSGLPP
     SGSWQDLKDH MREAGDVCYA DVQKDGMGMV EYLRKEDMEY ALRKLDDTKF RSHEGETSYI
     RVYPERGTSY GCSRSRSGSR GRDSPYQSRG SPHYFSPFRP Y