Overview
| Uniprot ID | A0A286XIK7 |
|---|
| Protein Name | Serine/arginine-rich splicing factor 3 |
|---|
| Gene Name | SRSF3 |
|---|
| Organism | Cavia porcellus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 85 |
VELSNGEKRSRNRGP |
Function
Splicing factor, which binds the consensus motif 5'-C[ACU][AU]C[ACU][AC]C-3' within pre-mRNA and promotes specific exons inclusion during alternative splicing. Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites within exons. Also functions as an adapter involved in mRNA nuclear export. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. Involved in nuclear export of m6A-containing mRNAs via interaction with YTHDC1: interaction with YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export
Protein Sequence
10
MHRDSCPLDC
20
KVYVGNLGNN
30
GNKTELERAF
40
GYYGPLRSVW
50
VARNPPGFAF
60
VEFEDPRDAA
70
DAVRELDGRT
80
LCGCRVRVEL
90
SNGEKRSRNR
100
GPPPSWGRRP
110
RDDYRRRSPP
120
PRRRSPRRRS
130
FSRSRSRSLS
140
RDRRRERSLS
150
RERNHKPSRS
160
FSRSRSRSRS
NERK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0016607 |
nuclear speck |
| Molecular Function |
GO:0043274 |
phospholipase binding |
| Molecular Function |
GO:0070878 |
primary miRNA binding |
| Molecular Function |
GO:0160134 |
protein-RNA sequence-specific adaptor activity |
| Biological Process |
GO:0006406 |
mRNA export from nucleus |
| Biological Process |
GO:0006397 |
mRNA processing |
| Biological Process |
GO:0031053 |
primary miRNA processing |
| Biological Process |
GO:0048024 |
regulation of mRNA splicing, via spliceosome |
| Biological Process |
GO:0008380 |
RNA splicing |
Reference
[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.