ID IF4A1_BOVIN Reviewed; 406 AA. AC Q3SZ54; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 31-JAN-2018, entry version 94. 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; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Fetal liver; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ATP-dependent RNA helicase which is a subunit of the CC eIF4F complex involved in cap recognition and is required for mRNA CC binding to ribosome. In the current model of translation CC initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR CC of mRNAs which is necessary to allow efficient binding of the CC small ribosomal subunit, and subsequent scanning for the initiator CC codon (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of CC which varies with external and internal environmental conditions. CC It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. CC Interacts with PAIP1, EIF4E and UPF2. Found in a complex with CC XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. May interact CC with NOM1. Interacts with PDCD4; this interferes with the CC interaction between EIF4A and EIF4G. Interacts with RBM4 (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC103130; AAI03131.1; -; mRNA. DR RefSeq; NP_001029400.1; NM_001034228.1. DR UniGene; Bt.14169; -. DR ProteinModelPortal; Q3SZ54; -. DR SMR; Q3SZ54; -. DR STRING; 9913.ENSBTAP00000000144; -. DR PaxDb; Q3SZ54; -. DR PeptideAtlas; Q3SZ54; -. DR PRIDE; Q3SZ54; -. DR Ensembl; ENSBTAT00000000144; ENSBTAP00000000144; ENSBTAG00000000132. DR GeneID; 504958; -. DR KEGG; bta:504958; -. DR CTD; 1973; -. DR eggNOG; KOG0327; Eukaryota. DR eggNOG; COG0513; LUCA. DR GeneTree; ENSGT00530000062880; -. DR HOGENOM; HOG000268797; -. DR HOVERGEN; HBG107989; -. DR InParanoid; Q3SZ54; -. DR KO; K03257; -. DR OMA; FTHRNGR; -. DR OrthoDB; EOG091G07OI; -. DR TreeFam; TF101524; -. DR Reactome; R-BTA-1169408; ISG15 antiviral mechanism. DR Reactome; R-BTA-156827; L13a-mediated translational silencing of Ceruloplasmin expression. DR Reactome; R-BTA-429947; Deadenylation of mRNA. DR Reactome; R-BTA-72649; Translation initiation complex formation. DR Reactome; R-BTA-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S. DR Reactome; R-BTA-72702; Ribosomal scanning and start codon recognition. DR Reactome; R-BTA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit. DR Proteomes; UP000009136; Chromosome 19. DR Bgee; ENSBTAG00000000132; -. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl. DR GO; GO:0016020; C:membrane; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central. DR GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central. DR GO; GO:0006413; P:translational initiation; IBA:GO_Central. DR CDD; cd00079; HELICc; 1. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR037583; EIF4A. 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 PANTHER; PTHR24031:SF226; PTHR24031:SF226; 1. 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 2: Evidence at transcript level; KW Acetylation; ATP-binding; Complete proteome; Helicase; Hydrolase; KW Initiation factor; Isopeptide bond; Nucleotide-binding; KW Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding; KW Ubl conjugation. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P60842}. FT CHAIN 2 406 Eukaryotic initiation factor 4A-I. FT /FTId=PRO_0000244559. FT DOMAIN 63 234 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 245 406 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 76 83 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 32 60 Q motif. FT MOTIF 182 185 DEAD box. FT MOD_RES 2 2 N-acetylserine. FT {ECO:0000250|UniProtKB:P60842}. FT MOD_RES 4 4 Phosphoserine. FT {ECO:0000250|UniProtKB:P60842}. FT MOD_RES 118 118 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P60842}. FT MOD_RES 158 158 Phosphothreonine. FT {ECO:0000250|UniProtKB:P60842}. FT MOD_RES 174 174 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P60842}. FT MOD_RES 193 193 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P60843}. FT MOD_RES 238 238 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P60843}. FT CROSSLNK 146 146 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:P60842}. FT CROSSLNK 225 225 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:P60842}. FT CROSSLNK 238 238 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. FT {ECO:0000250|UniProtKB:P60842}. FT CROSSLNK 309 309 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:P60842}. FT CROSSLNK 369 369 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:P60842}. FT CROSSLNK 381 381 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000250|UniProtKB:P60842}. 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 //