IF4A3_SALSA
ID IF4A3_SALSA Reviewed; 406 AA.
AC B5DG42;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
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;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=White muscle;
RA Andreassen R., Hoyheim B.;
RT "Characterization of full-length sequenced inserts (FLIcs) from a salmo
RT salar white muscle specific cDNA library.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Head kidney;
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
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). Binds spliced mRNA
CC in sequence-independent manner, 20-24 nucleotides upstream of mRNA
CC exon-exon junctions (By similarity). Involved in craniofacial
CC development (By similarity). {ECO:0000250|UniProtKB:P38919,
CC ECO:0000250|UniProtKB:Q7ZVA6}.
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.
CC {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; BT043601; ACH70716.1; -; mRNA.
DR EMBL; BT047669; ACI67470.1; -; mRNA.
DR RefSeq; NP_001134430.1; NM_001140958.1.
DR RefSeq; XP_013986627.1; XM_014131152.1.
DR AlphaFoldDB; B5DG42; -.
DR SMR; B5DG42; -.
DR STRING; 8030.ENSSSAP00000000725; -.
DR GeneID; 100195929; -.
DR GeneID; 106564785; -.
DR KEGG; sasa:100195929; -.
DR KEGG; sasa:106564785; -.
DR CTD; 100195929; -.
DR OMA; FGCQALV; -.
DR OrthoDB; 726081at2759; -.
DR Proteomes; UP000087266; Chromosome ssa02.
DR Proteomes; UP000087266; Chromosome ssa12.
DR Bgee; ENSSSAG00000000352; Expressed in semen and 16 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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..406
FT /note="Eukaryotic initiation factor 4A-III"
FT /id="PRO_0000379481"
FT DOMAIN 64..234
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 245..406
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 33..61
FT /note="Q motif"
FT MOTIF 182..185
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
FT BINDING 77..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 80..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
FT BINDING 337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
FT BINDING 362..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P38919"
SQ SEQUENCE 406 AA; 46582 MW; 7E4EC7404C13E31C CRC64;
MEVATVPRTR RLLKEEDMTK IEFETSEEVD VTPTFDTMGL REDLLRGIYA YGFEKPSAIQ
QRAIKQIIKG RDVIAQSQSG TGKTATFCVS VLQCLDIQVR ETQALILAPT RELAGQIQKV
LLALGDYMNV QCHSCIGGTN VGEDIRKLDY GQHVVAGTPG RVFDMIRRRS LRTRAIKMLV
LDEADEMLNK GFKEQIYDVY RYLPPATQVC LISATLPHEI LEMTNKFMTD PIRILVKRDE
LTLEGIKQFF VAVEREEWKF DTLCDLYDTL TITQAVIFCN TKRKVDWLTE KMREANFTVS
SMHGDMPQKE RESIMKEFRS GASRVLISTD VWARGLDVPQ VSLIINYDLP NNRELYIHRI
GRSGRYGRKG VAINFVKNDD IRILRDIEQY YSTQIDEMPM NVADLI
