IF4A3_CHICK
ID IF4A3_CHICK Reviewed; 412 AA.
AC Q5ZM36;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Eukaryotic initiation factor 4A-III;
DE Short=eIF-4A-III;
DE Short=eIF4A-III;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P38919};
DE AltName: Full=ATP-dependent RNA helicase DDX48;
DE AltName: Full=ATP-dependent RNA helicase eIF4A-3;
DE AltName: Full=DEAD box protein 48;
DE AltName: Full=Eukaryotic translation initiation factor 4A isoform 3;
GN Name=EIF4A3; Synonyms=DDX48; ORFNames=RCJMB04_3e17;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: ATP-dependent RNA helicase. Involved in pre-mRNA splicing as
CC component of the spliceosome. Core component of the splicing-dependent
CC multiprotein exon junction complex (EJC) deposited at splice junctions
CC on mRNAs. The EJC is a dynamic structure consisting of core proteins
CC and several peripheral nuclear and cytoplasmic associated factors that
CC join the complex only transiently either during EJC assembly or during
CC subsequent mRNA metabolism. The EJC marks the position of the exon-exon
CC junction in the mature mRNA for the gene expression machinery and the
CC core components remain bound to spliced mRNAs throughout all stages of
CC mRNA metabolism thereby influencing downstream processes including
CC nuclear mRNA export, subcellular mRNA localization, translation
CC efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent
CC ATPase and RNA-helicase activities are induced by CASC3, but abolished
CC in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-
CC bound EJC core onto spliced mRNA in a stable conformation. The
CC inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases
CC the RNA-binding affinity of the EJC. Involved in translational
CC enhancement of spliced mRNAs after formation of the 80S ribosome
CC complex. Binds spliced mRNA in sequence-independent manner, 20-24
CC nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity
CC for single-stranded RNA in an ATP-bound core EJC complex than after the
CC ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X
CC (and probably other apoptotic genes); specifically inhibits formation
CC of proapoptotic isoforms; the function is different from the
CC established EJC assembly. Involved in craniofacial development.
CC {ECO:0000250|UniProtKB:P38919}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:P38919};
CC -!- SUBUNIT: Identified in the spliceosome C complex. Part of the mRNA
CC splicing-dependent exon junction complex (EJC) complex; the core
CC complex contains CASC3, EIF4A3, MAGOH and RBM8A. Interacts with CASC3,
CC MAGOH, NXF1, RBM8A and ALYREF/THOC4. May interact with NOM1. Interacts
CC with POLDIP3. Interacts with CWC22 and PRPF19 in an RNA-independent
CC manner. Direct interaction with CWC22 is mediated by the helicase C-
CC terminal domain. Full interaction with CWC22 occurs only when EIF4A3 is
CC not part of the EJC and prevents EIF4A3 binding to RNA. Interacts with
CC NCBP3. {ECO:0000250|UniProtKB:P38919}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3B8Q2}. Nucleus
CC speckle {ECO:0000250|UniProtKB:P38919}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q3B8Q2}. Note=Nucleocytoplasmic shuttling
CC protein. Travels to the cytoplasm as part of the exon junction complex
CC (EJC) bound to mRNA. {ECO:0000250|UniProtKB:Q3B8Q2}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ719548; CAG31207.1; -; mRNA.
DR RefSeq; NP_001025820.1; NM_001030649.1.
DR AlphaFoldDB; Q5ZM36; -.
DR SMR; Q5ZM36; -.
DR STRING; 9031.ENSGALP00000038179; -.
DR Ensembl; ENSGALT00000038969; ENSGALP00000038179; ENSGALG00000008530.
DR GeneID; 416704; -.
DR KEGG; gga:416704; -.
DR CTD; 9775; -.
DR VEuPathDB; HostDB:geneid_416704; -.
DR eggNOG; KOG0328; Eukaryota.
DR GeneTree; ENSGT00940000155037; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q5ZM36; -.
DR OMA; FGCQALV; -.
DR OrthoDB; 726081at2759; -.
DR PhylomeDB; Q5ZM36; -.
DR Reactome; R-GGA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-GGA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-GGA-429947; Deadenylation of mRNA.
DR Reactome; R-GGA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-GGA-72187; mRNA 3'-end processing.
DR Reactome; R-GGA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-GGA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:Q5ZM36; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000008530; Expressed in colon and 12 other tissues.
DR ExpressionAtlas; Q5ZM36; baseline and differential.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding; Spliceosome;
KW Translation regulation; Transport.
FT CHAIN 1..412
FT /note="Eukaryotic initiation factor 4A-III"
FT /id="PRO_0000379478"
FT DOMAIN 70..240
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 251..412
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..67
FT /note="Q motif"
FT MOTIF 188..191
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
FT BINDING 83..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 86..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
FT BINDING 368..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
SQ SEQUENCE 412 AA; 46816 MW; 5B619FF6CE453766 CRC64;
MSGSAGSGGT TGSARKRIMK EEDMTKVEFE TSEEVDVTPT FDTMGLREDL LRGIYAYGFE
KPSAIQQRAI KQIIKGRDVI AQSQSGTGKT ATFSISVLQC LDIQVRETQA LILAPTRELA
VQIQKGLLAL GDYMNVQCHA CIGGTNVGED IRKLDYGQHV VAGTPGRVFD MIRRRSLRTR
AIKMLVLDEA DEMLNKGFKE QIYDVYRYLP PATQVVLISA TLPHEILEMT NKFMTDPIRI
LVKRDELTLE GIKQFFVAVE REEWKFDTLC DLYDTLTITQ AVIFCNTKRK VDWLTEKMRE
ANFTVSSMHG DMPQKERESI MKEFRSGASR VLISTDVWAR GLDVPQVSLI INYDLPNNRE
LYIHRIGRSG RYGRKGVAIN FVKNDDIRIL RDIEQYYSTQ IDEMPMNVAD LI
