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Database: UniProt
Entry: A6M931
LinkDB: A6M931
Original site: A6M931 
ID   IF4A3_PIG               Reviewed;         411 AA.
AC   A6M931;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   16-OCT-2019, entry version 89.
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;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=17226078; DOI=10.1007/s10528-006-9065-7;
RA   Wang H., Wang H., Zhu Z., Yang S., Li K.;
RT   "Molecular cloning, mapping, and expression analysis of the EIF4A2
RT   gene in pig.";
RL   Biochem. Genet. 45:51-62(2007).
CC   -!- FUNCTION: ATP-dependent RNA helicase. Involved in pre-mRNA
CC       splicing as component of the spliceosome. Core component of the
CC       splicing-dependent multiprotein exon junction complex (EJC)
CC       deposited at splice junctions on mRNAs. The EJC is a dynamic
CC       structure consisting of core proteins and several peripheral
CC       nuclear and cytoplasmic associated factors that join the complex
CC       only transiently either during EJC assembly or during subsequent
CC       mRNA metabolism. The EJC marks the position of the exon-exon
CC       junction in the mature mRNA for the gene expression machinery and
CC       the core components remain bound to spliced mRNAs throughout all
CC       stages of mRNA metabolism thereby influencing downstream processes
CC       including nuclear mRNA export, subcellular mRNA localization,
CC       translation efficiency and nonsense-mediated mRNA decay (NMD). Its
CC       RNA-dependent ATPase and RNA-helicase activities are induced by
CC       CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer,
CC       thereby trapping the ATP-bound EJC core onto spliced mRNA in a
CC       stable conformation. The inhibition of ATPase activity by the
CC       MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the
CC       EJC. Involved in translational enhancement of spliced mRNAs after
CC       formation of the 80S ribosome complex. Binds spliced mRNA in
CC       sequence-independent manner, 20-24 nucleotides upstream of mRNA
CC       exon-exon junctions. Shows higher affinity for single-stranded RNA
CC       in an ATP-bound core EJC complex than after the ATP is hydrolyzed.
CC       Involved in the splicing modulation of BCL2L1/Bcl-X (and probably
CC       other apoptotic genes); specifically inhibits formation of
CC       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
CC       in the presence of RNA. {ECO:0000250|UniProtKB:P38919}.
CC   -!- SUBUNIT: Identified in the spliceosome C complex. Core component
CC       of the mRNA splicing-dependent exon junction complex (EJC); the
CC       core complex contains CASC3, EIF4A3, MAGOH or MAGOHB, and RBM8A.
CC       Interacts with CASC3, MAGOH, NXF1, RBM8A and ALYREF/THOC4. May
CC       interact with NOM1. Interacts with POLDIP3. Interacts with CWC22
CC       and PRPF19 in an RNA-independent manner. Direct interaction with
CC       CWC22 is mediated by the helicase C-terminal domain. Full
CC       interaction with CWC22 occurs only when EIF4A3 is not part of the
CC       EJC and prevents EIF4A3 binding to RNA. Identified in a complex
CC       composed of the EJC core, UPF3B and UPF2. The EJC core can also
CC       interact with UPF3A (in vitro). Interacts with NCBP3.
CC       {ECO:0000250|UniProtKB:P38919}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3B8Q2}.
CC       Nucleus 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
CC       complex (EJC) bound to mRNA. Detected in dendritic layer as well
CC       as the nuclear and cytoplasmic (somatic) compartments of neurons.
CC       Colocalizes with STAU1 and FMR1 in dendrites.
CC       {ECO:0000250|UniProtKB:Q3B8Q2}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A
CC       subfamily. {ECO:0000305}.
DR   EMBL; DQ351286; ABC84196.1; -; mRNA.
DR   RefSeq; NP_001093663.1; NM_001100193.1.
DR   SMR; A6M931; -.
DR   STRING; 9823.ENSSSCP00000018178; -.
DR   PaxDb; A6M931; -.
DR   PeptideAtlas; A6M931; -.
DR   PRIDE; A6M931; -.
DR   Ensembl; ENSSSCT00000018679; ENSSSCP00000018178; ENSSSCG00000017155.
DR   Ensembl; ENSSSCT00070033973; ENSSSCP00070028370; ENSSSCG00070017212.
DR   GeneID; 100101926; -.
DR   KEGG; ssc:100101926; -.
DR   CTD; 9775; -.
DR   eggNOG; KOG0327; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   GeneTree; ENSGT00940000155037; -.
DR   HOGENOM; HOG000268797; -.
DR   InParanoid; A6M931; -.
DR   KO; K13025; -.
DR   OMA; TRFHDFK; -.
DR   OrthoDB; 726081at2759; -.
DR   Proteomes; UP000008227; Chromosome 12.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035145; C:exon-exon junction complex; IEA:Ensembl.
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:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0008143; F:poly(A) binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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:0017148; P:negative regulation of translation; IEA:Ensembl.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR   GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
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; Complete proteome; Cytoplasm; Helicase;
KW   Hydrolase; Isopeptide bond; mRNA processing; mRNA splicing;
KW   mRNA transport; Nonsense-mediated mRNA decay; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW   rRNA processing; Spliceosome; Translation regulation; Transport;
KW   Ubl conjugation.
FT   CHAIN         1    411       Eukaryotic initiation factor 4A-III.
FT                                /FTId=PRO_0000423270.
FT   INIT_MET      1      1       Removed; alternate.
FT                                {ECO:0000250|UniProtKB:P38919}.
FT   CHAIN         2    411       Eukaryotic initiation factor 4A-III, N-
FT                                terminally processed.
FT                                /FTId=PRO_0000379477.
FT   DOMAIN       69    239       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      250    411       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      85     90       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   NP_BIND     367    371       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        38     66       Q motif.
FT   MOTIF       187    190       DEAD box. {ECO:0000305}.
FT   BINDING      60     60       ATP; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P38919}.
FT   BINDING      65     65       ATP. {ECO:0000250|UniProtKB:P38919}.
FT   BINDING     342    342       ATP. {ECO:0000250|UniProtKB:P38919}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:P38919}.
FT   MOD_RES       2      2       N-acetylalanine; in Eukaryotic initiation
FT                                factor 4A-III, N-terminally processed.
FT                                {ECO:0000250|UniProtKB:P38919}.
FT   MOD_RES      10     10       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P60842}.
FT   MOD_RES      12     12       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P38919}.
FT   MOD_RES     124    124       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P60842}.
FT   MOD_RES     163    163       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P38919}.
FT   MOD_RES     198    198       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P60843}.
FT   MOD_RES     296    296       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P38919}.
FT   MOD_RES     321    321       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P38919}.
FT   CROSSLNK     19     19       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P38919}.
FT   CROSSLNK    152    152       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P60842}.
FT   CROSSLNK    314    314       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P38919}.
FT   CROSSLNK    374    374       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P60842}.
FT   CROSSLNK    382    382       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P38919}.
SQ   SEQUENCE   411 AA;  46841 MW;  987DAF10824DEC4D CRC64;
     MAATATMATS GSARKRLLKE EDMTKVEFET SEEVDVTPTF DTMGLREDLL RGIYAYGFEK
     PSAIQQRAIK QIIKGRDVIA QSQSGTGKTA TFSISVLQCL DIQVRETQAL ILAPTRELAV
     QIQKGLLALG 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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