SRSF2_BOVIN
ID SRSF2_BOVIN Reviewed; 221 AA.
AC Q3MHR5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Serine/arginine-rich splicing factor 2;
DE AltName: Full=Splicing component, 35 kDa;
DE AltName: Full=Splicing factor SC35;
DE Short=SC-35;
DE AltName: Full=Splicing factor, arginine/serine-rich 2;
GN Name=SRSF2; Synonyms=SFRS2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Necessary for the splicing of pre-mRNA. It is required for
CC formation of the earliest ATP-dependent splicing complex and interacts
CC with spliceosomal components bound to both the 5'- and 3'-splice sites
CC during spliceosome assembly. It also is required for ATP-dependent
CC interactions of both U1 and U2 snRNPs with pre-mRNA. Interacts with
CC other spliceosomal components, via the RS domains, to form a bridge
CC between the 5'- and 3'-splice site binding components, U1 snRNP and
CC U2AF. Binds to purine-rich RNA sequences, either 5'-AGSAGAGTA-3' (S=C
CC or G) or 5'-GTTCGAGTA-3'. Can bind to beta-globin mRNA and commit it to
CC the splicing pathway. The phosphorylated form (by SRPK2) is required
CC for cellular apoptosis in response to cisplatin treatment (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: In vitro, self-associates and binds SRSF1/SFRS1 (ASF/SF2),
CC SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12. Interacts with
CC CCNL1 and CCNL2. Interacts with SCAF11. Interacts with ZRSR2/U2AF1-RS2.
CC Interacts with CCDC55 (via C-terminus). Interacts with BRDT (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleoplasm
CC {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Phosphorylation by
CC SRPK2 provokes its redistribution from the nuclear speckle to
CC nucleoplasm. {ECO:0000250}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC Phosphorylated by SRPK2 and this causes its redistribution from the
CC nuclear speckle to nucleoplasm and controls cell fate decision in
CC response to cisplatin treatment. KAT5/TIP60 inhibits its
CC phosphorylation by preventing SRPK2 nuclear translocation (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Acetylation on Lys-52 by KAT5/TIP60 promotes its proteasomal
CC degradation. This effect is counterbalanced by HDAC6, which positively
CC controls SRSF2 protein level by deacetylating it and preventing its
CC proteasomal degradation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; BC105138; AAI05139.1; -; mRNA.
DR RefSeq; NP_001029490.1; NM_001034318.1.
DR RefSeq; XP_005221227.1; XM_005221170.2.
DR RefSeq; XP_005221228.1; XM_005221171.2.
DR RefSeq; XP_005221229.1; XM_005221172.2.
DR AlphaFoldDB; Q3MHR5; -.
DR BMRB; Q3MHR5; -.
DR SMR; Q3MHR5; -.
DR STRING; 9913.ENSBTAP00000024299; -.
DR PaxDb; Q3MHR5; -.
DR PeptideAtlas; Q3MHR5; -.
DR PRIDE; Q3MHR5; -.
DR Ensembl; ENSBTAT00000024299; ENSBTAP00000024299; ENSBTAG00000018258.
DR Ensembl; ENSBTAT00000081424; ENSBTAP00000071252; ENSBTAG00000018258.
DR GeneID; 508312; -.
DR KEGG; bta:508312; -.
DR CTD; 6427; -.
DR VEuPathDB; HostDB:ENSBTAG00000018258; -.
DR VGNC; VGNC:55875; SRSF2.
DR eggNOG; KOG4207; Eukaryota.
DR GeneTree; ENSGT00940000154883; -.
DR HOGENOM; CLU_012062_10_3_1; -.
DR InParanoid; Q3MHR5; -.
DR OMA; PLIRCDV; -.
DR OrthoDB; 1524134at2759; -.
DR TreeFam; TF106262; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000018258; Expressed in retropharyngeal lymph node and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IEA:Ensembl.
DR GO; GO:0036002; F:pre-mRNA binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:Ensembl.
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 InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR034893; SRSF2-like.
DR PANTHER; PTHR23147:SF119; PTHR23147:SF119; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Acetylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT CHAIN 2..221
FT /note="Serine/arginine-rich splicing factor 2"
FT /id="PRO_0000245578"
FT DOMAIN 14..92
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 92..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..187
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
SQ SEQUENCE 221 AA; 25476 MW; 68121AC4D35714FA CRC64;
MSYGRPPPDV EGMTSLKVDN LTYRTSPDTL RRVFEKYGRV GDVYIPRDRY TKESRGFAFV
RFHDKRDAED AMDAMDGAVL DGRELRVQMA RYGRPPDSHH SRRGPPPRRY GGGGYGRRSR
SPRRRRRSRS RSRSRSRSRS RSRYSRSKSR SRTRSRSRST SKSRSARRSK SKSSSVSRSR
SRSRSRSRSR SPPPVSKRES KSRSRSKSPP KSPEEEGAVS S
