Overview
| Uniprot ID | A6M931 |
|---|
| Protein Name | Eukaryotic initiation factor 4A-III |
|---|
| Gene Name | EIF4A3 |
|---|
| Organism | Sus scrofa |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 152 |
NVGEDIRKLDYGQHV |
| 198 |
EMLNKGFKEQIYDVY |
| 374 |
RSGRYGRKGVAINFV |
| 70 |
AIQQRAIKQIIKGRD |
Function
ATP-dependent RNA helicase. Involved in pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms; the function is different from the established EJC assembly. Involved in craniofacial development
Protein Sequence
10
MAATATMATS
20
GSARKRLLKE
30
EDMTKVEFET
40
SEEVDVTPTF
50
DTMGLREDLL
60
RGIYAYGFEK
70
PSAIQQRAIK
80
QIIKGRDVIA
90
QSQSGTGKTA
100
TFSISVLQCL
110
DIQVRETQAL
120
ILAPTRELAV
130
QIQKGLLALG
140
DYMNVQCHAC
150
IGGTNVGEDI
160
RKLDYGQHVV
170
AGTPGRVFDM
180
IRRRSLRTRA
190
IKMLVLDEAD
200
EMLNKGFKEQ
210
IYDVYRYLPP
220
ATQVVLISAT
230
LPHEILEMTN
240
KFMTDPIRIL
250
VKRDELTLEG
260
IKQFFVAVER
270
EEWKFDTLCD
280
LYDTLTITQA
290
VIFCNTKRKV
300
DWLTEKMREA
310
NFTVSSMHGD
320
MPQKERESIM
330
KEFRSGASRV
340
LISTDVWARG
350
LDVPQVSLII
360
NYDLPNNREL
370
YIHRIGRSGR
380
YGRKGVAINF
390
VKNDDIRILR
400
DIEQYYSTQI
410
DEMPMNVADL
I
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0071013 |
catalytic step 2 spliceosome |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0035145 |
exon-exon junction complex |
| Cellular Component |
GO:0016607 |
nuclear speck |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0071006 |
U2-type catalytic step 1 spliceosome |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0016887 |
ATP hydrolysis activity |
| Molecular Function |
GO:0003729 |
mRNA binding |
| Molecular Function |
GO:0008143 |
poly(A) binding |
| Molecular Function |
GO:0003724 |
RNA helicase activity |
| Biological Process |
GO:0048701 |
embryonic cranial skeleton morphogenesis |
| Biological Process |
GO:0006406 |
mRNA export from nucleus |
| Biological Process |
GO:0000398 |
mRNA splicing, via spliceosome |
| Biological Process |
GO:0017148 |
negative regulation of translation |
| Biological Process |
GO:0000184 |
nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
| Biological Process |
GO:0045727 |
positive regulation of translation |
| Biological Process |
GO:0000381 |
regulation of alternative mRNA splicing, via spliceosome |
| Biological Process |
GO:2000622 |
regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
| Biological Process |
GO:0006364 |
rRNA processing |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.