ID   SRSF6_RABIT             Reviewed;          81 AA.
AC   O18776;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Serine/arginine-rich splicing factor 6;
DE   AltName: Full=Pre-mRNA-splicing factor SRP55;
DE   AltName: Full=Splicing factor, arginine/serine-rich 6;
DE   Flags: Fragment;
GN   Name=SRSF6; Synonyms=SFRS6, SRP55;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white;
RA   Brunet A., Henrion G., Duranthon V., Renard J.P.;
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in constitutive splicing and modulates the
CC       selection of alternative splice sites. Plays a role in the alternative
CC       splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-
CC       mRNA and promotes the expression of alternatively spliced TNC. Plays a
CC       role in wound healing and in the regulation of keratinocyte
CC       differentiation and proliferation via its role in alternative splicing
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds SREK1/SFRS12. Interacts with DYRK1A (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC       {ECO:0000250}.
CC   -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC       Phosphorylated by DYRK1A, probably in the RS domain. Phosphorylation by
CC       DYRK1A modulates alternative splice site selection and inhibits the
CC       expression of MAPT/Tau exon 10 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR   EMBL; AF011564; AAB66467.1; -; mRNA.
DR   AlphaFoldDB; O18776; -.
DR   eggNOG; KOG0106; Eukaryota.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0036002; F:pre-mRNA binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0006376; P:mRNA splice site selection; ISS:UniProtKB.
DR   GO; GO:0045617; P:negative regulation of keratinocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0010837; P:regulation of keratinocyte proliferation; ISS:UniProtKB.
DR   GO; GO:0061041; P:regulation of wound healing; ISS:UniProtKB.
PE   2: Evidence at transcript level;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; RNA-binding.
FT   CHAIN           <1..>81
FT                   /note="Serine/arginine-rich splicing factor 6"
FT                   /id="PRO_0000081931"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..47
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         81
SQ   SEQUENCE   81 AA;  9521 MW;  20D9F8A9D08C7CA0 CRC64;
     RSRSRSRRSS RSRSRSISKS RSRSRSRSKG RSRSRSKGRK SRSKSKSKPK SDRGSRSRSR
     SRSKDEYEKS RSRSRSRSRS P