SRSF6_BOVIN
ID SRSF6_BOVIN Reviewed; 345 AA.
AC Q3B7L6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Serine/arginine-rich splicing factor 6;
DE AltName: Full=Splicing factor, arginine/serine-rich 6;
GN Name=SRSF6; Synonyms=SFRS6;
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=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) 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|UniProtKB:Q13247}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q13247}.
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; BC107553; AAI07554.1; -; mRNA.
DR RefSeq; NP_001030349.1; NM_001035272.1.
DR AlphaFoldDB; Q3B7L6; -.
DR SMR; Q3B7L6; -.
DR STRING; 9913.ENSBTAP00000011240; -.
DR PaxDb; Q3B7L6; -.
DR PeptideAtlas; Q3B7L6; -.
DR PRIDE; Q3B7L6; -.
DR GeneID; 507828; -.
DR KEGG; bta:507828; -.
DR CTD; 6431; -.
DR eggNOG; KOG0106; Eukaryota.
DR InParanoid; Q3B7L6; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
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.
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; IPR029541; SRSF6.
DR PANTHER; PTHR23147:SF82; PTHR23147:SF82; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..345
FT /note="Serine/arginine-rich splicing factor 6"
FT /id="PRO_0000287721"
FT DOMAIN 1..72
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 110..183
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 75..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..249
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3TWW8"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT MOD_RES 305
FT /note="Phosphoserine; by DYRK1A"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
SQ SEQUENCE 345 AA; 39647 MW; D3F4A9DDD3EA8769 CRC64;
MPRVYIGRLS YNVREKDIQR FFSGYGRLLG IDLKNGYGFV EFEDSRDADD AVYELNGKEL
CGERVIVEHA RGPRRDRDGY SYGSRSGGGG YSSRRTSGRD KYGPPVRTEF RLIVENLSSR
CSWQDLKDFM RQAGEVTYAD AHKERTNEGV IEFRSYSDMK RALDKLDGTE INGRNIRLIE
DKPRTSHRRS YSGSRSRSRS RRRSRSRSRR SSRSRSRSIS KSRSRSRSRS KGRSRSRSKG
RKSRSKSKSK PKSDRGSRSR SRSRSKDEYE KSRSRSRSRS RSPKENGKGD IKSKSRSRSQ
SRSDSPLPAP PSKARSVSPP PKRASRSHSR SRSKSRSRSR SSSRD
