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Database: UniProt
Entry: Q4R3Q1
LinkDB: Q4R3Q1
Original site: Q4R3Q1 
ID   IF4A3_MACFA             Reviewed;         411 AA.
AC   Q4R3Q1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 85.
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;
DE   Contains:
DE     RecName: Full=Eukaryotic initiation factor 4A-III, N-terminally processed;
GN   Name=EIF4A3; Synonyms=DDX48; ORFNames=QtsA-15322;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- ACTIVITY REGULATION: The ATPase activity is increased some 4-fold in
CC       the presence of RNA. {ECO:0000250|UniProtKB:P38919}.
CC   -!- SUBUNIT: Identified in the spliceosome C complex. Core component of the
CC       mRNA splicing-dependent exon junction complex (EJC); the core complex
CC       contains CASC3, EIF4A3, MAGOH or MAGOHB, and RBM8A. Interacts with
CC       CASC3, MAGOH, NXF1, RBM8A and ALYREF/THOC4. May interact with NOM1.
CC       Interacts with POLDIP3. Interacts with CWC22 and PRPF19 in an RNA-
CC       independent manner. Direct interaction with CWC22 is mediated by the
CC       helicase C-terminal domain. Full interaction with CWC22 occurs only
CC       when EIF4A3 is not part of the EJC and prevents EIF4A3 binding to RNA.
CC       Identified in a complex composed of the EJC core, UPF3B and UPF2. The
CC       EJC core can also interact with UPF3A (in vitro). Interacts with NCBP3.
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. Detected in dendritic layer as well as the nuclear
CC       and cytoplasmic (somatic) compartments of neurons. Colocalizes with
CC       STAU1 and FMR1 in dendrites. {ECO:0000250|UniProtKB:Q3B8Q2}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC       {ECO:0000305}.
DR   EMBL; AB179214; BAE02265.1; -; mRNA.
DR   RefSeq; NP_001271847.1; NM_001284918.1.
DR   SMR; Q4R3Q1; -.
DR   STRING; 9541.XP_005585250.1; -.
DR   PRIDE; Q4R3Q1; -.
DR   GeneID; 101867456; -.
DR   KEGG; mcf:101867456; -.
DR   CTD; 9775; -.
DR   KO; K13025; -.
DR   OrthoDB; 726081at2759; -.
DR   Proteomes; UP000233100; Unplaced.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:UniProtKB.
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   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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   Acetylation; ATP-binding; Cytoplasm; Helicase; Hydrolase; Isopeptide bond;
KW   mRNA processing; mRNA splicing; mRNA transport;
KW   Nonsense-mediated mRNA decay; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; rRNA processing; Spliceosome;
KW   Translation regulation; Transport; Ubl conjugation.
FT   CHAIN           1..411
FT                   /note="Eukaryotic initiation factor 4A-III"
FT                   /id="PRO_0000423268"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P38919"
FT   CHAIN           2..411
FT                   /note="Eukaryotic initiation factor 4A-III, N-terminally
FT                   processed"
FT                   /id="PRO_0000054943"
FT   DOMAIN          69..239
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          250..411
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         85..90
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   NP_BIND         367..371
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           38..66
FT                   /note="Q motif"
FT   MOTIF           187..190
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000305"
FT   BINDING         60
FT                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000250|UniProtKB:P38919"
FT   BINDING         65
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P38919"
FT   BINDING         342
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P38919"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P38919"
FT   MOD_RES         2
FT                   /note="N-acetylalanine; in Eukaryotic initiation factor 4A-
FT                   III, N-terminally processed"
FT                   /evidence="ECO:0000250|UniProtKB:P38919"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38919"
FT   MOD_RES         124
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   MOD_RES         163
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P38919"
FT   MOD_RES         198
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P60843"
FT   MOD_RES         296
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P38919"
FT   MOD_RES         321
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P38919"
FT   CROSSLNK        19
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38919"
FT   CROSSLNK        152
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   CROSSLNK        314
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38919"
FT   CROSSLNK        374
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   CROSSLNK        382
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P38919"
SQ   SEQUENCE   411 AA;  46871 MW;  4DEFE98DE699B4E8 CRC64;
     MATTATMATS GSARKRLLKE EDMTKVEFET SEEVDVTPTF DTMGLREDLL RGIYAYGFEK
     PSAIQQRAIK QIIKGRDVIA QSQSGTGKTA TFSISVLQCL DIQVRETQAL ILAPARELAV
     QIQKGLLTLG DYMNVQCHAC IGGTNVGEDI RKLDYGQHVV AGTPGRVFDM IRRRSLRTRA
     IKMLVLDEAD EMLNKGFKEQ IYDVYRYLPP ATQVVLISAT LPHEILEMTN KFMTDPIRIL
     VKRDELTLEG IKQFFVAVER EEWKFDTLCD LYDTLTITQA VIFCNTKRKV DWLTEKMREA
     NFTVSSMHGD MPQKERESIM KEFRSGASRV LISTDVWARG LDVPQVSLII NYDLPNNREL
     YIHRIGRSGR YGRKGVAINF VKNDDIRILR DIEQYYSTQI DEMPMNVADL I
//
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