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Eukaryotic initiation factor 4A-III (eIF-4A-III) (eIF4A-III) (EC 3.6.4.13) (ATP-dependent RNA helicase DDX48) (ATP-dependent RNA helicase eIF4A-3) (DEAD box protein 48) (Eukaryotic translation initiation factor 4A isoform 3) [Cleaved into: Eukaryotic initiation factor 4A-III, N-terminally processed]

 IF4A3_MOUSE             Reviewed;         411 AA.
Q91VC3; B2RY38; Q3TEZ8; Q3UD29; Q8BVY3;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
31-JAN-2018, entry version 143.
RecName: Full=Eukaryotic initiation factor 4A-III;
Short=eIF-4A-III;
Short=eIF4A-III;
EC=3.6.4.13;
AltName: Full=ATP-dependent RNA helicase DDX48;
AltName: Full=ATP-dependent RNA helicase eIF4A-3;
AltName: Full=DEAD box protein 48;
AltName: Full=Eukaryotic translation initiation factor 4A isoform 3;
Contains:
RecName: Full=Eukaryotic initiation factor 4A-III, N-terminally processed;
Name=Eif4a3; Synonyms=Ddx48;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=BALB/cJ, C57BL/6J, DBA/2J, and NOD;
TISSUE=Bone marrow, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: ATP-dependent RNA helicase. 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; the function is different from the established EJC
assembly (By similarity). Involved in craniofacial development (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- ENZYME REGULATION: The ATPase activity is increased some 4-fold in
the presence of RNA.
-!- SUBUNIT: Part of the mRNA splicing-dependent exon junction complex
(EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and
RBM8A. Interacts with CASC3, MAGOH, NXF1, RBM8A and ALYREF/THOC4.
Identified in the spliceosome C complex. May interact with NOM1.
Interacts with POLDIP3. Interacts with CWC22 and PRPF19 in an RNA-
independent manner. Direct interaction with CWC22 is mediated by
the helicase C-terminal domain. Full interaction with CWC22 occurs
only when EIF4A3 is not part of the EJC and prevents EIF4A3
binding to RNA. Interacts with NCBP3 (By similarity).
{ECO:0000250|UniProtKB:P38919}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
{ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Nucleocytoplasmic
shuttling protein. Travels to the cytoplasm as part of the exon
junction complex (EJC) bound to mRNA. Detected in dendritic layer
as well as the nuclear and cytoplasmic (somatic) compartments of
neurons. Colocalizes with STAU1 and FMR1 in dendrites (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A
subfamily. {ECO:0000305}.
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EMBL; AK075920; BAC36054.1; -; mRNA.
EMBL; AK146385; BAE27130.1; -; mRNA.
EMBL; AK150277; BAE29433.1; -; mRNA.
EMBL; AK152824; BAE31525.1; -; mRNA.
EMBL; AK153359; BAE31931.1; -; mRNA.
EMBL; AK157855; BAE34233.1; -; mRNA.
EMBL; AK167107; BAE39256.1; -; mRNA.
EMBL; AK168319; BAE40258.1; -; mRNA.
EMBL; AK169350; BAE41100.1; -; mRNA.
EMBL; AK169815; BAE41387.1; -; mRNA.
EMBL; AL672140; CAM14996.1; -; Genomic_DNA.
EMBL; AL645911; CAM14996.1; JOINED; Genomic_DNA.
EMBL; AL645911; CAM18884.1; -; Genomic_DNA.
EMBL; AL672140; CAM18884.1; JOINED; Genomic_DNA.
EMBL; CH466558; EDL34693.1; -; Genomic_DNA.
EMBL; BC008132; AAH08132.1; -; mRNA.
EMBL; BC012862; AAH12862.1; -; mRNA.
EMBL; BC158083; AAI58084.1; -; mRNA.
CCDS; CCDS25714.1; -.
RefSeq; NP_619610.1; NM_138669.1.
UniGene; Mm.197555; -.
UniGene; Mm.490978; -.
ProteinModelPortal; Q91VC3; -.
SMR; Q91VC3; -.
BioGrid; 228659; 4.
IntAct; Q91VC3; 5.
MINT; MINT-1864166; -.
STRING; 10090.ENSMUSP00000026667; -.
ChEMBL; CHEMBL3751651; -.
iPTMnet; Q91VC3; -.
PhosphoSitePlus; Q91VC3; -.
SwissPalm; Q91VC3; -.
EPD; Q91VC3; -.
MaxQB; Q91VC3; -.
PaxDb; Q91VC3; -.
PeptideAtlas; Q91VC3; -.
PRIDE; Q91VC3; -.
Ensembl; ENSMUST00000026667; ENSMUSP00000026667; ENSMUSG00000025580.
GeneID; 192170; -.
KEGG; mmu:192170; -.
UCSC; uc007mqj.1; mouse.
CTD; 9775; -.
MGI; MGI:1923731; Eif4a3.
eggNOG; KOG0327; Eukaryota.
eggNOG; COG0513; LUCA.
GeneTree; ENSGT00530000062880; -.
HOGENOM; HOG000268797; -.
HOVERGEN; HBG107989; -.
InParanoid; Q91VC3; -.
KO; K13025; -.
OMA; DEMPVNA; -.
OrthoDB; EOG091G07OI; -.
PhylomeDB; Q91VC3; -.
TreeFam; TF300466; -.
Reactome; R-MMU-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-MMU-429947; Deadenylation of mRNA.
Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
Reactome; R-MMU-72187; mRNA 3'-end processing.
Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
PRO; PR:Q91VC3; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000025580; -.
ExpressionAtlas; Q91VC3; baseline and differential.
Genevisible; Q91VC3; MM.
GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; ISO:MGI.
GO; GO:0003729; F:mRNA binding; ISO:MGI.
GO; GO:0008143; F:poly(A) binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
CDD; cd00079; HELICc; 1.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
Pfam; PF00270; DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51195; Q_MOTIF; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome; Cytoplasm; Helicase;
Hydrolase; Isopeptide bond; mRNA processing; mRNA splicing;
mRNA transport; Nonsense-mediated mRNA decay; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
rRNA processing; Spliceosome; Translation regulation; Transport;
Ubl conjugation.
CHAIN 1 411 Eukaryotic initiation factor 4A-III.
/FTId=PRO_0000423269.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:P38919}.
CHAIN 2 411 Eukaryotic initiation factor 4A-III, N-
terminally processed.
/FTId=PRO_0000054944.
DOMAIN 69 239 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 250 411 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 85 90 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
NP_BIND 367 371 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 38 66 Q motif.
MOTIF 187 190 DEAD box.
BINDING 60 60 ATP; via carbonyl oxygen. {ECO:0000250}.
BINDING 65 65 ATP. {ECO:0000250}.
BINDING 342 342 ATP. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P38919}.
MOD_RES 2 2 N-acetylalanine; in Eukaryotic initiation
factor 4A-III, N-terminally processed.
{ECO:0000250|UniProtKB:P38919}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P60842}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000250|UniProtKB:P38919}.
MOD_RES 124 124 N6-acetyllysine.
{ECO:0000250|UniProtKB:P60842}.
MOD_RES 163 163 Phosphothreonine.
{ECO:0000250|UniProtKB:P38919}.
MOD_RES 198 198 N6-acetyllysine.
{ECO:0000250|UniProtKB:P60843}.
MOD_RES 296 296 N6-acetyllysine.
{ECO:0000250|UniProtKB:P38919}.
MOD_RES 321 321 N6-acetyllysine.
{ECO:0000250|UniProtKB:P38919}.
CROSSLNK 19 19 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38919}.
CROSSLNK 152 152 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P60842}.
CROSSLNK 314 314 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38919}.
CROSSLNK 374 374 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P60842}.
CROSSLNK 382 382 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P38919}.
CONFLICT 3 4 AN -> TT (in Ref. 4; AAI58084).
{ECO:0000305}.
CONFLICT 6 6 T -> R (in Ref. 4; AAI58084).
{ECO:0000305}.
CONFLICT 11 11 G -> V (in Ref. 4; AAI58084).
{ECO:0000305}.
CONFLICT 22 22 D -> G (in Ref. 4; AAI58084).
{ECO:0000305}.
CONFLICT 36 36 V -> R (in Ref. 4; AAI58084).
{ECO:0000305}.
CONFLICT 38 38 P -> L (in Ref. 4; AAI58084).
{ECO:0000305}.
CONFLICT 47 47 E -> G (in Ref. 1; BAC36054).
{ECO:0000305}.
CONFLICT 94 94 V -> I (in Ref. 4; AAI58084).
{ECO:0000305}.
CONFLICT 177 177 R -> P (in Ref. 4; AAI58084).
{ECO:0000305}.
CONFLICT 200 200 Q -> L (in Ref. 1; BAE41100).
{ECO:0000305}.
CONFLICT 235 235 D -> H (in Ref. 4; AAI58084).
{ECO:0000305}.
CONFLICT 285 285 N -> I (in Ref. 4; AAI58084).
{ECO:0000305}.
CONFLICT 407 407 V -> L (in Ref. 4; AAI58084).
{ECO:0000305}.
SEQUENCE 411 AA; 46840 MW; 2639EA64F5332A54 CRC64;
MAANATMATS GSARKRLLKE EDMTKVEFET SEEVDVTPTF DTMGLREDLL RGIYAYGFEK
PSAIQQRAIK QIIKGRDVIA QSQSGTGKTA TFSVSVLQCL 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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U1885r CLIA eIF3a,Eif3a,Eif3s10,eIF-3-theta,Eukaryotic translation initiation factor 3 subunit 10,Eukaryotic translation initiation factor 3 subunit A,Rat,Rattus norvegicus 96T
EIAAB12722 eIF3 p66,eIF3d,Eif3d,Eif3s7,eIF-3-zeta,Eukaryotic translation initiation factor 3 subunit 7,Eukaryotic translation initiation factor 3 subunit D,Mouse,Mus musculus
U1885r CLIA kit eIF3a,Eif3a,Eif3s10,eIF-3-theta,Eukaryotic translation initiation factor 3 subunit 10,Eukaryotic translation initiation factor 3 subunit A,Rat,Rattus norvegicus 96T
EIAAB12718 eIF3 p110,eIF3c,Eif3c,Eif3s8,Eukaryotic translation initiation factor 3 subunit 8,Eukaryotic translation initiation factor 3 subunit C,Mouse,Mus musculus


 

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