SRSF7_BOVIN
ID SRSF7_BOVIN Reviewed; 235 AA.
AC Q3T106;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Serine/arginine-rich splicing factor 7;
DE AltName: Full=Splicing factor, arginine/serine-rich 7;
GN Name=SRSF7; Synonyms=SFRS7;
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 (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for pre-mRNA splicing. Represses the splicing of
CC MAPT/Tau exon 10. May function as export adapter involved in mRNA
CC nuclear export such as of histone H2A. Binds mRNA which is thought to
CC be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1
CC pathway); enhances NXF1-NXT1 RNA-binding activity. RNA-binding is semi-
CC sequence specific (By similarity). {ECO:0000250|UniProtKB:Q16629}.
CC -!- SUBUNIT: Found in large molecular weight complexes containing CCNL1 and
CC the p110 isoforms of either CDC2L1 or CDC2L2. Interacts with CCNL2 and
CC CPSF6. Interacts with NXF1 (By similarity). Interacts with YTHDC1 (By
CC similarity). {ECO:0000250|UniProtKB:Q16629,
CC ECO:0000250|UniProtKB:Q8BL97}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q16629}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q16629}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; BC102184; AAI02185.1; -; mRNA.
DR RefSeq; NP_001029449.1; NM_001034277.2.
DR AlphaFoldDB; Q3T106; -.
DR BMRB; Q3T106; -.
DR SMR; Q3T106; -.
DR STRING; 9913.ENSBTAP00000033048; -.
DR PaxDb; Q3T106; -.
DR PeptideAtlas; Q3T106; -.
DR PRIDE; Q3T106; -.
DR Ensembl; ENSBTAT00000033124; ENSBTAP00000033048; ENSBTAG00000014891.
DR GeneID; 507066; -.
DR KEGG; bta:507066; -.
DR CTD; 6432; -.
DR VEuPathDB; HostDB:ENSBTAG00000014891; -.
DR VGNC; VGNC:35303; SRSF7.
DR eggNOG; KOG0107; Eukaryota.
DR GeneTree; ENSGT00910000144115; -.
DR HOGENOM; CLU_012062_20_0_1; -.
DR InParanoid; Q3T106; -.
DR OMA; VERSHGM; -.
DR OrthoDB; 1533297at2759; -.
DR TreeFam; TF351858; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000014891; Expressed in retropharyngeal lymph node and 107 other tissues.
DR ExpressionAtlas; Q3T106; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR CDD; cd12646; RRM_SRSF7; 1.
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; IPR034651; SRSF7_RRM.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Isopeptide bond; Metal-binding; mRNA processing;
KW mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; RNA-binding; Transport; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..235
FT /note="Serine/arginine-rich splicing factor 7"
FT /id="PRO_0000284385"
FT DOMAIN 11..84
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 153..160
FT /note="1"
FT REPEAT 161..168
FT /note="2"
FT REPEAT 169..176
FT /note="3"
FT REPEAT 177..184
FT /note="4"
FT REPEAT 208..215
FT /note="5; approximate"
FT REPEAT 216..223
FT /note="6; approximate"
FT ZN_FING 104..120
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 81..98
FT /note="Sufficient for interaction with NXF1"
FT /evidence="ECO:0000250"
FT REGION 123..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..223
FT /note="6 X 8 AA repeats of R-R-S-R-S-X-S-X"
FT COMPBIAS 123..176
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..214
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BL97"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BL97"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16629"
SQ SEQUENCE 235 AA; 26941 MW; E55CFB883E2A9822 CRC64;
MSRYGRYGGE TKVYVGNLGT GAGKGELERA FSYYGPLRTV WIARNPPGFA FVEFEDPRDA
EDAVRGLDGK VICGSRVRVE LSTGMPRRSR FDRPPARRPF DPNDRCYECG EKGHYAYDCH
RYSRRRRSRS RSRSHSRSRG RRYSRSRSRS RGRRSRSASP RRSRSVSLRR SRSASLRRSR
SGSIKGSRSR SRSRSRSRSL SRPRSSRSKS RSPSPKRSRS PSGSPRRSAS PERVD
