GenomeNet

Database: UniProt
Entry: Q3SZ54
LinkDB: Q3SZ54
Original site: Q3SZ54 
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   16-OCT-2019, entry version 106.
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:
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
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}.
DR   EMBL; BC103130; AAI03131.1; -; mRNA.
DR   RefSeq; NP_001029400.1; NM_001034228.1.
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   VGNC; VGNC:28404; EIF4A1.
DR   eggNOG; KOG0327; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   GeneTree; ENSGT00940000153889; -.
DR   HOGENOM; HOG000268797; -.
DR   InParanoid; Q3SZ54; -.
DR   KO; K03257; -.
DR   OMA; AEYDNRD; -.
DR   OrthoDB; 726081at2759; -.
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   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000000132; Expressed in 10 organ(s), highest expression level in spleen.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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   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
//
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