SRSF4_MOUSE
ID SRSF4_MOUSE Reviewed; 489 AA.
AC Q8VE97; Q9JJC3;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Serine/arginine-rich splicing factor 4;
DE AltName: Full=Splicing factor, arginine/serine-rich 4;
GN Name=Srsf4; Synonyms=Sfrs4; ORFNames=MNCb-2616;
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 [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-489.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in alternative splice site selection during pre-
CC mRNA splicing. Represses the splicing of MAPT/Tau exon 10 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a pre-mRNA splicing complex with SRSF4/SFRS4,
CC SRSF5/SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. Interacts with PNN (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95070.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC019437; AAH19437.1; -; mRNA.
DR EMBL; AB041587; BAA95070.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q8VE97; -.
DR SMR; Q8VE97; -.
DR IntAct; Q8VE97; 2.
DR STRING; 10090.ENSMUSP00000061474; -.
DR iPTMnet; Q8VE97; -.
DR PhosphoSitePlus; Q8VE97; -.
DR EPD; Q8VE97; -.
DR jPOST; Q8VE97; -.
DR MaxQB; Q8VE97; -.
DR PaxDb; Q8VE97; -.
DR PeptideAtlas; Q8VE97; -.
DR PRIDE; Q8VE97; -.
DR ProteomicsDB; 257072; -.
DR MGI; MGI:1890577; Srsf4.
DR eggNOG; KOG0106; Eukaryota.
DR InParanoid; Q8VE97; -.
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 ChiTaRS; Srsf4; mouse.
DR PRO; PR:Q8VE97; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VE97; protein.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISO:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
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 CDD; cd12337; RRM1_SRSF4_like; 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; IPR035585; RRM1_SRSF4-like.
DR InterPro; IPR000504; RRM_dom.
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 mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-binding.
FT CHAIN 1..489
FT /note="Serine/arginine-rich splicing factor 4"
FT /id="PRO_0000081926"
FT DOMAIN 2..72
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 104..177
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 72..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..242
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..353
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08170"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08170"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08170"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08170"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08170"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08170"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08170"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08170"
FT CONFLICT 341
FT /note="S -> SKVGS (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 389..390
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="G -> E (in Ref. 2; BAA95070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 55979 MW; 8D5FE8D1EF4624B3 CRC64;
MPRVYIGRLS YQARERDVER FFKGYGKILE VDLKNGYGFV EFDDLRDADD AVYELNGKDL
CGERVIVEHA RGPRRDGSYG SGRSGYGYRR SGRDKYGPPT RTEYRLIVEN LSSRCSWQDL
KDYMRQAGEV TYADAHKGRK NEGVIEFVSY SDMKRALEKL DGTEVNGRKI RLVEDKPGSR
RRRSYSRSRS HSRSRSRSRH SRKSRSRSGS SKSSHSKSRS RSRSGSHSRS KSRSRSQSRS
RSKKEKSRSP SKDNKSRSRS RSPDKSRSKS KDHAEDKLQN NDSAGKAKSH SPSRHDSKSR
SRSQERRAEE ERRRSVSRAR SQEKSRSQEK SLLKSRSRSR SRSRSRSKDK RKGRKRSRDE
SRSRSRSKSE RSRKHSSKRD SKVSSSSSSS KKKKDTDHSR SPSRSVSKER EHAKAESGQR
GSRAEGESEA PNPEPRARSR STSKSKPNVP AESRSRSKSA SKTRSRSKSP SRSASRSPSR
SRSRSHSRS
