IF4A1_ARATH
ID IF4A1_ARATH Reviewed; 412 AA.
AC P41376; Q0WWD9; Q546P0; Q8LBZ6; Q8RXF3; Q94CM1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Eukaryotic initiation factor 4A-1 {ECO:0000303|PubMed:1398145, ECO:0000303|Ref.2};
DE Short=eIF-4A-1 {ECO:0000303|PubMed:1398145, ECO:0000303|Ref.2};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P10081};
DE AltName: Full=ATP-dependent RNA helicase eIF4A-1 {ECO:0000303|PubMed:1398145, ECO:0000303|Ref.2};
DE AltName: Full=DEAD-box ATP-dependent RNA helicase 4 {ECO:0000303|PubMed:17168887};
DE Short=AtRH04 {ECO:0000303|PubMed:17168887};
GN Name=EIF4A1 {ECO:0000303|PubMed:1398145, ECO:0000303|Ref.2};
GN Synonyms=RH4 {ECO:0000303|PubMed:17168887}, TIF4A-1;
GN OrderedLocusNames=At3g13920 {ECO:0000312|Araport:AT3G13920};
GN ORFNames=MDC16.4 {ECO:0000312|EMBL:BAB02322.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1398145; DOI=10.1016/0378-1119(92)90112-3;
RA Metz A.M., Timmer R.T., Browning K.S.;
RT "Sequences for two cDNAs encoding Arabidopsis thaliana eukaryotic protein
RT synthesis initiation factor 4A.";
RL Gene 120:313-314(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. C24;
RA De Greve H., Nguyen V., Deboeck F., Thia-Toong L., Karimi M.,
RA Hernalsteens J.P.;
RT "T-DNA tagging of the translation initiation factor eIF-4A1 from
RT Arabidopsis thaliana.";
RL Plant Sci. 161:685-693(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INTERACTION WITH CDKA-1.
RX PubMed=14706832; DOI=10.1016/s0014-5793(03)01382-6;
RA Hutchins A.P., Roberts G.R., Lloyd C.W., Doonan J.H.;
RT "In vivo interaction between CDKA and eIF4A: a possible mechanism linking
RT translation and cell proliferation.";
RL FEBS Lett. 556:91-94(2004).
RN [9]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=17168887; DOI=10.1111/j.1467-7652.2004.00084.x;
RA Mingam A., Toffano-Nioche C., Brunaud V., Boudet N., Kreis M., Lecharny A.;
RT "DEAD-box RNA helicases in Arabidopsis thaliana: establishing a link
RT between quantitative expression, gene structure and evolution of a family
RT of genes.";
RL Plant Biotechnol. J. 2:401-415(2004).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP GENE FAMILY.
RX PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA Xu R., Zhang S., Huang J., Zheng C.;
RT "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT sativa.";
RL PLoS ONE 8:E78982-E78982(2013).
RN [12]
RP INTERACTION WITH MRF1; MRF2; MRF3/ECIP1 AND MRF4.
RC STRAIN=cv. Columbia;
RX PubMed=29084871; DOI=10.1105/tpc.17.00563;
RA Lee D.-H., Park S.J., Ahn C.S., Pai H.-S.;
RT "MRF family genes are involved in translation control, especially under
RT energy-deficient conditions, and their expression and functions are
RT modulated by the TOR signaling pathway.";
RL Plant Cell 29:2895-2920(2017).
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. {ECO:0000250|UniProtKB:P10081}.
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 Evidence={ECO:0000250|UniProtKB:P10081};
CC -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions (By
CC similarity). It is composed of at least EIF4A, EIF4E and EIF4G (By
CC similarity). Interacts with CDKA-1 (PubMed:14706832). Interacts with
CC MRF1, MRF2, MRF3/ECIP1 and MRF4 (PubMed:29084871).
CC {ECO:0000250|UniProtKB:P60842, ECO:0000269|PubMed:14706832,
CC ECO:0000269|PubMed:29084871}.
CC -!- INTERACTION:
CC P41376; P24100: CDKA-1; NbExp=2; IntAct=EBI-371706, EBI-371713;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P10081}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P41376-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in the whole plant.
CC {ECO:0000269|PubMed:17168887}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000250|UniProtKB:P10081}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC43286.1; Type=Erroneous gene model prediction; Evidence={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; X65052; CAA46188.1; -; mRNA.
DR EMBL; AJ298137; CAC43286.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ298138; CAC43288.1; -; mRNA.
DR EMBL; AB019229; BAB02322.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75438.1; -; Genomic_DNA.
DR EMBL; AY050957; AAK93634.1; -; mRNA.
DR EMBL; AY052344; AAK96536.1; -; mRNA.
DR EMBL; AY081287; AAL91176.1; -; mRNA.
DR EMBL; AY091304; AAM14243.1; -; mRNA.
DR EMBL; AY098962; AAM19972.1; -; mRNA.
DR EMBL; AY139981; AAM98124.1; -; mRNA.
DR EMBL; BT000655; AAN31802.1; -; mRNA.
DR EMBL; AK226414; BAE98559.1; -; mRNA.
DR EMBL; AY086907; AAM63951.1; -; mRNA.
DR PIR; JC1452; JC1452.
DR RefSeq; NP_566469.1; NM_112246.4. [P41376-1]
DR AlphaFoldDB; P41376; -.
DR SMR; P41376; -.
DR BioGRID; 5939; 15.
DR IntAct; P41376; 3.
DR iPTMnet; P41376; -.
DR PRIDE; P41376; -.
DR EnsemblPlants; AT3G13920.1; AT3G13920.1; AT3G13920. [P41376-1]
DR GeneID; 820605; -.
DR Gramene; AT3G13920.1; AT3G13920.1; AT3G13920. [P41376-1]
DR KEGG; ath:AT3G13920; -.
DR Araport; AT3G13920; -.
DR InParanoid; P41376; -.
DR PhylomeDB; P41376; -.
DR PRO; PR:P41376; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P41376; baseline and differential.
DR Genevisible; P41376; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Helicase;
KW Hydrolase; Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..412
FT /note="Eukaryotic initiation factor 4A-1"
FT /id="PRO_0000054949"
FT DOMAIN 70..240
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 251..412
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 39..67
FT /note="Q motif"
FT MOTIF 188..191
FT /note="DEAD box"
FT BINDING 83..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94A52"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CAI7"
FT CONFLICT 91
FT /note="A -> T (in Ref. 6; BAE98559)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="G -> S (in Ref. 6; BAE98559)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="L -> V (in Ref. 5; AAL91176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 46704 MW; E407BA7CBC967458 CRC64;
MAGSAPEGTQ FDARQFDQKL NEVLEGQDEF FTSYDDVHES FDAMGLQENL LRGIYAYGFE
KPSAIQQRGI VPFCKGLDVI QQAQSGTGKT ATFCSGVLQQ LDFSLIQCQA LVLAPTRELA
QQIEKVMRAL GDYLGVKVHA CVGGTSVRED QRILQAGVHV VVGTPGRVFD MLKRQSLRAD
NIKMFVLDEA DEMLSRGFKD QIYDIFQLLP PKIQVGVFSA TMPPEALEIT RKFMSKPVRI
LVKRDELTLE GIKQFYVNVE KEEWKLETLC DLYETLAITQ SVIFVNTRRK VDWLTDKMRS
RDHTVSATHG DMDQNTRDII MREFRSGSSR VLITTDLLAR GIDVQQVSLV INFDLPTQPE
NYLHRIGRSG RFGRKGVAIN FVTRDDERML FDIQKFYNVV VEELPSNVAD LL
