IF4A2_MOUSE
ID IF4A2_MOUSE Reviewed; 407 AA.
AC P10630; Q61513; Q61514;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Eukaryotic initiation factor 4A-II;
DE Short=eIF-4A-II;
DE Short=eIF4A-II;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase eIF4A-2;
GN Name=Eif4a2; Synonyms=Ddx2b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
RX PubMed=3046931; DOI=10.1002/j.1460-2075.1988.tb03049.x;
RA Nielsen P.J., Trachsel H.;
RT "The mouse protein synthesis initiation factor 4A gene family includes two
RT related functional genes which are differentially expressed.";
RL EMBO J. 7:2097-2105(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Nielsen P.J.;
RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 291-323.
RC TISSUE=Liver;
RX PubMed=9092667; DOI=10.1093/nar/25.8.1591;
RA Selvamurugan N., Joost O.H., Haas E.S., Brown J.W., Galvin N.J.,
RA Eliceiri G.L.;
RT "Intracellular localization and unique conserved sequences of three small
RT nucleolar RNAs.";
RL Nucleic Acids Res. 25:1591-1596(1997).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: ATP-dependent RNA helicase which is a subunit of the eIF4F
CC complex involved in cap recognition and is required for mRNA binding to
CC ribosome. In the current model of translation initiation, eIF4A unwinds
CC RNA secondary structures in the 5'-UTR of mRNAs which is necessary to
CC allow efficient binding of the small ribosomal subunit, and subsequent
CC scanning for the initiator codon.
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 -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions. It is
CC composed of at least EIF4A, EIF4E and EIF4G1/EIFFG3. Interacts with
CC EIF4E. May interact with NOM1 (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P10630-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P10630-2; Sequence=VSP_009630;
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC {ECO:0000305}.
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DR EMBL; X12507; CAA31025.1; -; mRNA.
DR EMBL; X14422; CAA32585.1; -; Genomic_DNA.
DR EMBL; X56953; CAA40269.1; -; Genomic_DNA.
DR EMBL; X56953; CAA40268.1; -; Genomic_DNA.
DR EMBL; AK076509; BAC36372.1; -; mRNA.
DR EMBL; U64706; AAC53180.1; -; Genomic_DNA.
DR CCDS; CCDS28074.1; -. [P10630-1]
DR CCDS; CCDS84218.1; -. [P10630-2]
DR PIR; S00985; S00985.
DR RefSeq; NP_001116509.1; NM_001123037.2.
DR RefSeq; NP_001116510.1; NM_001123038.2.
DR RefSeq; NP_001334108.1; NM_001347179.1. [P10630-2]
DR RefSeq; NP_038534.2; NM_013506.3. [P10630-1]
DR AlphaFoldDB; P10630; -.
DR SMR; P10630; -.
DR BioGRID; 199419; 15.
DR ComplexPortal; CPX-5862; Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G1 variant.
DR ComplexPortal; CPX-5864; Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G3 variant.
DR IntAct; P10630; 6.
DR STRING; 10090.ENSMUSP00000023599; -.
DR ChEMBL; CHEMBL3751650; -.
DR iPTMnet; P10630; -.
DR PhosphoSitePlus; P10630; -.
DR SwissPalm; P10630; -.
DR EPD; P10630; -.
DR jPOST; P10630; -.
DR MaxQB; P10630; -.
DR PaxDb; P10630; -.
DR PeptideAtlas; P10630; -.
DR PRIDE; P10630; -.
DR ProteomicsDB; 267260; -. [P10630-1]
DR ProteomicsDB; 267261; -. [P10630-2]
DR Antibodypedia; 3189; 313 antibodies from 33 providers.
DR DNASU; 13682; -.
DR Ensembl; ENSMUST00000023599; ENSMUSP00000023599; ENSMUSG00000022884. [P10630-1]
DR GeneID; 13682; -.
DR KEGG; mmu:13682; -.
DR UCSC; uc007ytd.3; mouse. [P10630-1]
DR CTD; 1974; -.
DR MGI; MGI:106906; Eif4a2.
DR VEuPathDB; HostDB:ENSMUSG00000022884; -.
DR eggNOG; KOG0327; Eukaryota.
DR GeneTree; ENSGT00940000153783; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; P10630; -.
DR OMA; EHKDGQR; -.
DR OrthoDB; 726081at2759; -.
DR PhylomeDB; P10630; -.
DR TreeFam; TF101524; -.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-429947; Deadenylation of mRNA.
DR Reactome; R-MMU-72649; Translation initiation complex formation.
DR Reactome; R-MMU-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR BioGRID-ORCS; 13682; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Eif4a2; mouse.
DR PRO; PR:P10630; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P10630; protein.
DR Bgee; ENSMUSG00000022884; Expressed in dentate gyrus of hippocampal formation granule cell and 76 other tissues.
DR ExpressionAtlas; P10630; baseline and differential.
DR Genevisible; P10630; MM.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IC:ComplexPortal.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR GO; GO:1900260; P:negative regulation of RNA-directed 5'-3' RNA polymerase activity; ISO:MGI.
DR GO; GO:0006413; P:translational initiation; IC:ComplexPortal.
DR CDD; cd18046; DEADc_EIF4AII_EIF4AI_DDX2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044728; EIF4A_DEADc.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Helicase; Hydrolase; Initiation factor;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..407
FT /note="Eukaryotic initiation factor 4A-II"
FT /id="PRO_0000054940"
FT DOMAIN 64..235
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 246..407
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 33..61
FT /note="Q motif"
FT MOTIF 183..186
FT /note="DEAD box"
FT BINDING 77..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14240"
FT VAR_SEQ 9
FT /note="N -> NS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_009630"
FT CONFLICT 200..201
FT /note="IF -> RV (in Ref. 1; CAA31025)"
FT /evidence="ECO:0000305"
FT CONFLICT 294..297
FT /note="HARD -> QAIY (in Ref. 1; CAA31025)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="D -> H (in Ref. 1; CAA31025)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="V -> G (in Ref. 1; CAA31025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 46402 MW; FAA7D3BA9D8C6DA0 CRC64;
MSGGSADYNR EHGGPEGMDP DGVIESNWNE IVDNFDDMNL KESLLRGIYA YGFEKPSAIQ
QRAIIPCIKG YDVIAQAQSG TGKTATFAIS ILQQLEIEFK ETQALVLAPT RELAQQIQKV
ILALGDYMGA TCHACIGGTN VRNEMQKLQA EAPHIVVGTP GRVFDMLNRR YLSPKWIKMF
VLDEADEMLS RGFKDQIYEI FQKLNTSIQV VLLSATMPTD VLEVTKKFMR DPIRILVKKE
ELTLEGIKQF YINVEREEWK LDTLCDLYET LTITQAVIFL NTRRKVDWLT EKMHARDFTV
SALHGDMDQK ERDVIMREFR SGSSRVLITT DLLARGIDVQ QVSLVINYDL PTNRENYIHR
IGRGGRFGRK GVAINFVTEE DKRILRDIET FYNTTVEEMP MNVADLI
