IF4A1_RABIT
ID IF4A1_RABIT Reviewed; 398 AA.
AC P29562;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 127.
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;
DE Flags: Fragment;
GN Name=EIF4A1; Synonyms=DDX2A, EIF4A;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-398, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2241157; DOI=10.1016/0003-9861(90)90130-q;
RA Conroy S.C., Dever T.E., Owens C.L., Merrick W.C.;
RT "Characterization of the 46,000-dalton subunit of eIF-4F.";
RL Arch. Biochem. Biophys. 282:363-371(1990).
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC {ECO:0000305}.
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DR PIR; S13269; S13269.
DR AlphaFoldDB; P29562; -.
DR SMR; P29562; -.
DR STRING; 9986.ENSOCUP00000008940; -.
DR ChEMBL; CHEMBL2052029; -.
DR eggNOG; KOG0327; Eukaryota.
DR InParanoid; P29562; -.
DR BRENDA; 3.6.4.13; 1749.
DR SABIO-RK; P29562; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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; IEA:UniProtKB-KW.
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 Acetylation; ATP-binding; Direct protein sequencing; Helicase; Hydrolase;
KW Initiation factor; Isopeptide bond; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN <1..398
FT /note="Eukaryotic initiation factor 4A-I"
FT /id="PRO_0000054937"
FT DOMAIN 55..226
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 237..398
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 24..52
FT /note="Q motif"
FT MOTIF 174..177
FT /note="DEAD box"
FT BINDING 68..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT MOD_RES 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT MOD_RES 166
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT MOD_RES 185
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60843"
FT MOD_RES 230
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P60843"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CROSSLNK 217
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CROSSLNK 301
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT CROSSLNK 373
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P60842"
FT NON_TER 1
SQ SEQUENCE 398 AA; 45291 MW; 8CE1C18DE7AC7D37 CRC64;
SRDNGPDGME PEGVIESNWN EIVDSFDDMN LSESLLRGIY AYGFEKPSAI QQRAILPCIK
GYDVIAQAQS GTGKTATFAI SILQQIELDL KATQALVLAP TRELAQQIQK VVMALGDYMG
ASCHACIGGT NVRAEVQKLQ MEAPHIIVGT PGRVFDMLNR RYLSPKYIKM FVLDEADEML
SRGFKDQIYD IFQKLNSNTQ VVLLSATMPS DVLEVTKKFM RDPIRILVKK EELTLEGIRQ
FYINVEREEW KLDTLCDLYE TLTITQAVIF INTRRKVDWL TEKMHARDFT VSAMHGDMDQ
KERDVIMREF RSGSSRVLIT TDLLARGIDV QQVSLVINYD LPTNRENYIH RIGRGGRFGR
KGVAINMVTE EDKRTLRDIE TFYNTSIEEM PLNVADLI
