Q91VC3 (IF4A3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic initiation factor 4A-III
Short name=eIF-4A-III
Short name=eIF4A-III
EC=3.6.4.13

Alternative name(s):
ATP-dependent RNA helicase DDX48
ATP-dependent RNA helicase eIF4A-3
DEAD box protein 48
Eukaryotic translation initiation factor 4A isoform 3

Gene names

Name:	Eif4a3
Synonyms:	Ddx48

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	ATP-dependent RNA helicase. Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction in the mature mRNA and thereby influences downstream processes of gene expression including mRNA splicing, nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Constitutes at least part of the platform anchoring other EJC proteins to spliced mRNAs. 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 By similarity.
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Part of the EJC core complex that contains CASC3, EIF4A3, MAGOH and RBM8A. Found in a mRNA splicing-dependent exon junction complex (EJC), at least composed of ACIN1, CASC3, EIF4A3, MAGOH, PNN, RBM8A, RNPS1, SAP18 and ALYREF/THOC4. Interacts with CASC3, MAGOH, NXF1, RBM8A and ALYREF/THOC4. Identified in the spliceosome C complex. May interact with NOM1 By similarity.
Subcellular location	Nucleus By similarity. Nucleus speckle By similarity. Cytoplasm By similarity. 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.
Sequence similarities	Belongs to the DEAD box helicase family. eIF4A subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay Translation regulation Transport mRNA processing mRNA splicing mRNA transport rRNA processing
Cellular component	Cytoplasm Nucleus Spliceosome
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of translation Inferred from electronic annotation. Source: Compara nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of translation Inferred from electronic annotation. Source: Compara rRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	catalytic step 2 spliceosome Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell exon-exon junction complex Inferred from electronic annotation. Source: Compara nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent RNA helicase activity Inferred from electronic annotation. Source: Compara poly(A) RNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 411	410	Eukaryotic initiation factor 4A-III		PRO_0000054944
Regions
	Domain	69 – 239	171	Helicase ATP-binding
	Domain	250 – 411	162	Helicase C-terminal
	Nucleotide binding	85 – 90	6	ATP By similarity
	Nucleotide binding	367 – 371	5	ATP By similarity
	Motif	38 – 66	29	Q motif
	Motif	187 – 190	4	DEAD box
Sites
	Binding site	60	1	ATP; via carbonyl oxygen By similarity
	Binding site	65	1	ATP By similarity
	Binding site	342	1	ATP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	12	1	Phosphoserine By similarity
	Modified residue	163	1	Phosphothreonine By similarity
	Modified residue	296	1	N6-acetyllysine By similarity
	Modified residue	321	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	3 – 4	2	AN → TT in AAI58084. Ref.4
	Sequence conflict	6	1	T → R in AAI58084. Ref.4
	Sequence conflict	11	1	G → V in AAI58084. Ref.4
	Sequence conflict	22	1	D → G in AAI58084. Ref.4
	Sequence conflict	36	1	V → R in AAI58084. Ref.4
	Sequence conflict	38	1	P → L in AAI58084. Ref.4
	Sequence conflict	47	1	E → G in BAC36054. Ref.1
	Sequence conflict	94	1	V → I in AAI58084. Ref.4
	Sequence conflict	177	1	R → P in AAI58084. Ref.4
	Sequence conflict	200	1	Q → L in BAE41100. Ref.1
	Sequence conflict	235	1	D → H in AAI58084. Ref.4
	Sequence conflict	285	1	N → I in AAI58084. Ref.4
	Sequence conflict	407	1	V → L in AAI58084. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q91VC3 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 2639EA64F5332A54	FASTA	411	46,840
	10 20 30 40 50 60 MAANATMATS GSARKRLLKE EDMTKVEFET SEEVDVTPTF DTMGLREDLL RGIYAYGFEK 70 80 90 100 110 120 PSAIQQRAIK QIIKGRDVIA QSQSGTGKTA TFSVSVLQCL DIQVRETQAL ILAPTRELAV 130 140 150 160 170 180 QIQKGLLALG DYMNVQCHAC IGGTNVGEDI RKLDYGQHVV AGTPGRVFDM IRRRSLRTRA 190 200 210 220 230 240 IKMLVLDEAD EMLNKGFKEQ IYDVYRYLPP ATQVVLISAT LPHEILEMTN KFMTDPIRIL 250 260 270 280 290 300 VKRDELTLEG IKQFFVAVER EEWKFDTLCD LYDTLTITQA VIFCNTKRKV DWLTEKMREA 310 320 330 340 350 360 NFTVSSMHGD MPQKERESIM KEFRSGASRV LISTDVWARG LDVPQVSLII NYDLPNNREL 370 380 390 400 410 YIHRIGRSGR YGRKGVAINF VKNDDIRILR DIEQYYSTQI DEMPMNVADL I

References

[1]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c, C57BL/6J, DBA/2 and NOD. Tissue: Bone marrow and Thymus.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK075920 mRNA. Translation: BAC36054.1. AK146385 mRNA. Translation: BAE27130.1. AK150277 mRNA. Translation: BAE29433.1. AK152824 mRNA. Translation: BAE31525.1. AK153359 mRNA. Translation: BAE31931.1. AK157855 mRNA. Translation: BAE34233.1. AK167107 mRNA. Translation: BAE39256.1. AK168319 mRNA. Translation: BAE40258.1. AK169350 mRNA. Translation: BAE41100.1. AK169815 mRNA. Translation: BAE41387.1. AL672140, AL645911 Genomic DNA. Translation: CAM14996.1. AL645911, AL672140 Genomic DNA. Translation: CAM18884.1. CH466558 Genomic DNA. Translation: EDL34693.1. BC008132 mRNA. Translation: AAH08132.1. BC012862 mRNA. Translation: AAH12862.1. BC158083 mRNA. Translation: AAI58084.1.
IPI	IPI00126716.
RefSeq	NP_619610.1. NM_138669.1.
UniGene	Mm.197555. Mm.490978.
3D structure databases
ProteinModelPortal	Q91VC3.
SMR	Q91VC3. Positions 21-411.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q91VC3. 2 interactions.
PTM databases
PhosphoSite	Q91VC3.
Proteomic databases
PaxDb	Q91VC3.
PRIDE	Q91VC3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026667; ENSMUSP00000026667; ENSMUSG00000025580.
GeneID	192170.
KEGG	mmu:192170.
UCSC	uc007mqj.1. mouse.
Organism-specific databases
CTD	9775.
MGI	MGI:1923731. Eif4a3.
Phylogenomic databases
eggNOG	COG0513.
GeneTree	ENSGT00530000062880.
HOGENOM	HOG000268797.
HOVERGEN	HBG107989.
InParanoid	Q8BVY3.
KO	K13025.
OMA	EDWKFDT.
OrthoDB	EOG4229JV.
Gene expression databases
ArrayExpress	Q91VC3.
Bgee	Q91VC3.
Genevestigator	Q91VC3.
GermOnline	ENSMUSG00000025580. Mus musculus.
Family and domain databases
InterPro	IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR000629. RNA-helicase_DEAD-box_CS. IPR014014. RNA_helicase_DEAD_Q_motif. [Graphical view]
Pfam	PF00270. DEAD. 1 hit. PF00271. Helicase_C. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
PROSITE	PS00039. DEAD_ATP_HELICASE. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS51195. Q_MOTIF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	371176.
SOURCE	Search...

Entry information

Entry name

IF4A3_MOUSE

Accession

Primary (citable) accession number: Q91VC3
Secondary accession number(s): B2RY38 , Q3TEZ8, Q3UD29, Q8BVY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program