IF4A2_RAT
ID IF4A2_RAT Reviewed; 407 AA.
AC Q5RKI1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [2]
RP PROTEIN SEQUENCE OF 101-111 AND 326-335, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
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 (By similarity). {ECO:0000250}.
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 (By similarity).
CC Interacts with EIF4E. May interact with NOM1 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC {ECO:0000305}.
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DR EMBL; BC085859; AAH85859.1; -; mRNA.
DR RefSeq; NP_001008336.1; NM_001008335.1.
DR AlphaFoldDB; Q5RKI1; -.
DR SMR; Q5RKI1; -.
DR BioGRID; 257691; 3.
DR IntAct; Q5RKI1; 2.
DR MINT; Q5RKI1; -.
DR STRING; 10116.ENSRNOP00000002484; -.
DR iPTMnet; Q5RKI1; -.
DR PhosphoSitePlus; Q5RKI1; -.
DR World-2DPAGE; 0004:Q5RKI1; -.
DR jPOST; Q5RKI1; -.
DR PaxDb; Q5RKI1; -.
DR PeptideAtlas; Q5RKI1; -.
DR PRIDE; Q5RKI1; -.
DR GeneID; 303831; -.
DR KEGG; rno:303831; -.
DR UCSC; RGD:1309225; rat.
DR CTD; 1974; -.
DR RGD; 1309225; Eif4a2.
DR VEuPathDB; HostDB:ENSRNOG00000001815; -.
DR eggNOG; KOG0327; Eukaryota.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q5RKI1; -.
DR OMA; EHKDGQR; -.
DR OrthoDB; 726081at2759; -.
DR PhylomeDB; Q5RKI1; -.
DR Reactome; R-RNO-1169408; ISG15 antiviral mechanism.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-429947; Deadenylation of mRNA.
DR Reactome; R-RNO-72649; Translation initiation complex formation.
DR Reactome; R-RNO-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Reactome; R-RNO-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR PRO; PR:Q5RKI1; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001815; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; Q5RKI1; baseline and differential.
DR Genevisible; Q5RKI1; RN.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:RGD.
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; ISO:RGD.
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:RGD.
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 ATP-binding; Direct protein sequencing; Helicase; Hydrolase;
KW Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..407
FT /note="Eukaryotic initiation factor 4A-II"
FT /id="PRO_0000252335"
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"
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
