IF4A1_MOUSE
ID IF4A1_MOUSE Reviewed; 406 AA.
AC P60843; P04765; Q61516;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Eukaryotic initiation factor 4A-I;
DE Short=eIF-4A-I;
DE Short=eIF4A-I;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase eIF4A-1;
GN Name=Eif4a1; Synonyms=Ddx2a, Eif4a;
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 [MRNA].
RX PubMed=3840589; DOI=10.1093/nar/13.19.6867;
RA Nielsen P.J., McMaster G.K., Trachsel H.;
RT "Cloning of eukaryotic protein synthesis initiation factor genes: isolation
RT and characterization of cDNA clones encoding factor eIF-4A.";
RL Nucleic Acids Res. 13:6867-6880(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3215517; DOI=10.1016/0378-1119(88)90195-3;
RA Reddy N.S., Roth W.W., Bragg P.W., Wahba A.J.;
RT "Isolation and mapping of a gene for protein synthesis initiation factor 4A
RT and its expression during differentiation of murine erythroleukemia
RT cells.";
RL Gene 70:231-243(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RA Miyashita A., Shimizu N., Nakajima T., Odani S., Kuwano R.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP MUTAGENESIS.
RX PubMed=1378397; DOI=10.1002/j.1460-2075.1992.tb05330.x;
RA Pause A., Somenberg N.;
RT "Mutational analysis of a DEAD box RNA helicase: the mammalian translation
RT initiation factor eIF-4A.";
RL EMBO J. 11:2643-2654(1992).
RN [7]
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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-193 AND LYS-238, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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/EIF4G3. Interacts with
CC PAIP1, EIF4E and UPF2. Found in a complex with XPO7, EIF4A1, ARHGAP1,
CC VPS26A, VPS29, VPS35 and SFN. May interact with NOM1. Interacts with
CC PDCD4; this interferes with the interaction between EIF4A and EIF4G.
CC Interacts with RBM4 (By similarity). Interacts with DDX3X in an RNA-
CC independent manner (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P60842}.
CC -!- INTERACTION:
CC P60843; Q6NZJ6: Eif4g1; NbExp=2; IntAct=EBI-6665935, EBI-8175606;
CC P60843; Q61823: Pdcd4; NbExp=4; IntAct=EBI-6665935, EBI-296473;
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA26842.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA26843.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA26845.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA26846.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X03039; CAA26842.1; ALT_INIT; mRNA.
DR EMBL; X03039; CAA26843.1; ALT_INIT; mRNA.
DR EMBL; X03040; CAA26845.1; ALT_INIT; mRNA.
DR EMBL; X03040; CAA26846.1; ALT_INIT; mRNA.
DR EMBL; L36611; AAA50407.1; -; Genomic_DNA.
DR EMBL; M22873; AAA50407.1; JOINED; Genomic_DNA.
DR EMBL; L36608; AAA50407.1; JOINED; Genomic_DNA.
DR EMBL; L36609; AAA50407.1; JOINED; Genomic_DNA.
DR EMBL; L36610; AAA50407.1; JOINED; Genomic_DNA.
DR EMBL; AB011595; BAA25075.1; -; Genomic_DNA.
DR EMBL; AK077429; BAC36796.1; -; mRNA.
DR EMBL; BC049915; AAH49915.1; -; mRNA.
DR CCDS; CCDS24904.1; -.
DR PIR; JS0039; FIMS4A.
DR RefSeq; NP_659207.1; NM_144958.4.
DR PDB; 6XKI; X-ray; 2.87 A; A=19-406.
DR PDB; 7DDX; X-ray; 2.50 A; B=1-238.
DR PDBsum; 6XKI; -.
DR PDBsum; 7DDX; -.
DR AlphaFoldDB; P60843; -.
DR SMR; P60843; -.
DR BioGRID; 199418; 33.
DR ComplexPortal; CPX-5863; Eukaryotic translation initiation factor 4F, EIF4A1 and EIF4G1 variant.
DR ComplexPortal; CPX-5865; Eukaryotic translation initiation factor 4F, EIF4A1 and EIF4G3 variant.
DR IntAct; P60843; 9.
DR MINT; P60843; -.
DR STRING; 10090.ENSMUSP00000127034; -.
DR ChEMBL; CHEMBL3309046; -.
DR iPTMnet; P60843; -.
DR PhosphoSitePlus; P60843; -.
DR SwissPalm; P60843; -.
DR REPRODUCTION-2DPAGE; P60843; -.
DR CPTAC; non-CPTAC-3823; -.
DR EPD; P60843; -.
DR jPOST; P60843; -.
DR PaxDb; P60843; -.
DR PeptideAtlas; P60843; -.
DR PRIDE; P60843; -.
DR ProteomicsDB; 267098; -.
DR Antibodypedia; 24168; 231 antibodies from 27 providers.
DR DNASU; 13681; -.
DR Ensembl; ENSMUST00000163666; ENSMUSP00000127034; ENSMUSG00000059796.
DR GeneID; 13681; -.
DR KEGG; mmu:13681; -.
DR UCSC; uc007jra.2; mouse.
DR CTD; 1973; -.
DR MGI; MGI:95303; Eif4a1.
DR VEuPathDB; HostDB:ENSMUSG00000059796; -.
DR eggNOG; KOG0327; Eukaryota.
DR GeneTree; ENSGT00940000153889; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; P60843; -.
DR OMA; HLGDYMN; -.
DR OrthoDB; 726081at2759; -.
DR PhylomeDB; P60843; -.
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; 13681; 30 hits in 72 CRISPR screens.
DR ChiTaRS; Eif4a1; mouse.
DR PRO; PR:P60843; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P60843; protein.
DR Bgee; ENSMUSG00000059796; Expressed in embryonic post-anal tail and 74 other tissues.
DR ExpressionAtlas; P60843; baseline and differential.
DR Genevisible; P60843; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IC:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
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:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
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 3D-structure; Acetylation; ATP-binding; Helicase; Hydrolase;
KW Initiation factor; Isopeptide bond; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CHAIN 2..406
FT /note="Eukaryotic initiation factor 4A-I"
FT /id="PRO_0000054935"
FT DOMAIN 63..234
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 245..406
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 32..60
FT /note="Q motif"
FT MOTIF 182..185
FT /note="DEAD box"
FT BINDING 76..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT MOD_RES 174
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT MOD_RES 193
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 238
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CROSSLNK 309
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CROSSLNK 369
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CONFLICT 300
FT /note="S -> C (in Ref. 2; AAA50407)"
FT /evidence="ECO:0000305"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:7DDX"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:7DDX"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:7DDX"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:7DDX"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:7DDX"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:7DDX"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:7DDX"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:7DDX"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:7DDX"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:7DDX"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:7DDX"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:7DDX"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:7DDX"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:7DDX"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:7DDX"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:7DDX"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:7DDX"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:7DDX"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:6XKI"
FT STRAND 244..255
FT /evidence="ECO:0007829|PDB:6XKI"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:6XKI"
FT HELIX 259..265
FT /evidence="ECO:0007829|PDB:6XKI"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:6XKI"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:6XKI"
FT HELIX 282..293
FT /evidence="ECO:0007829|PDB:6XKI"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:6XKI"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:6XKI"
FT HELIX 308..319
FT /evidence="ECO:0007829|PDB:6XKI"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:6XKI"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:6XKI"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:6XKI"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:6XKI"
FT STRAND 370..377
FT /evidence="ECO:0007829|PDB:6XKI"
FT HELIX 378..391
FT /evidence="ECO:0007829|PDB:6XKI"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:6XKI"
SQ SEQUENCE 406 AA; 46154 MW; 6EF89939F3045420 CRC64;
MSASQDSRSR DNGPDGMEPE GVIESNWNEI VDSFDDMNLS ESLLRGIYAY GFEKPSAIQQ
RAILPCIKGY DVIAQAQSGT GKTATFAISI LQQIELDLKA TQALVLAPTR ELAQQIQKVV
MALGDYMGAS CHACIGGTNV RAEVQKLQME APHIIVGTPG RVFDMLNRRY LSPKYIKMFV
LDEADEMLSR GFKDQIYDIF QKLNSNTQVV LLSATMPSDV LEVTKKFMRD PIRILVKKEE
LTLEGIRQFY INVEREEWKL DTLCDLYETL TITQAVIFIN TRRKVDWLTE KMHARDFTVS
AMHGDMDQKE RDVIMREFRS GSSRVLITTD LLARGIDVQQ VSLVINYDLP TNRENYIHRI
GRGGRFGRKG VAINMVTEED KRTLRDIETF YNTSIEEMPL NVADLI
