GenomeNet

Database: UniProt
Entry: P41377
LinkDB: P41377
Original site: P41377 
ID   IF4A2_ARATH             Reviewed;         412 AA.
AC   P41377; Q0WWK5;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-OCT-2019, entry version 159.
DE   RecName: Full=Eukaryotic initiation factor 4A-2;
DE            Short=eIF-4A-2;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent RNA helicase eIF4A-2;
DE   AltName: Full=DEAD-box ATP-dependent RNA helicase 19;
GN   Name=TIF4A-2; Synonyms=RH19; OrderedLocusNames=At1g54270;
GN   ORFNames=F20D21.9, F20D21_52;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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
RT   protein synthesis initiation factor 4A.";
RL   Gene 120:313-314(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
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.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
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.,
RA   Lecharny A.;
RT   "DEAD-box RNA helicases in Arabidopsis thaliana: establishing a link
RT   between quantitative expression, gene structure and evolution of a
RT   family of genes.";
RL   Plant Biotechnol. J. 2:401-415(2004).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., 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   [9]
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
RT   family in Zea mays and Glycine max: a comparison with Arabidopsis and
RT   Oryza sativa.";
RL   PLoS ONE 8:E78982-E78982(2013).
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 EIF4G (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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=P41377-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Preferentially expressed in
CC       flowers, young leaves and roots. {ECO:0000269|PubMed:17168887}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A
CC       subfamily. {ECO:0000305}.
DR   EMBL; X65053; CAA46189.1; -; mRNA.
DR   EMBL; AC005287; AAD25605.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33073.1; -; Genomic_DNA.
DR   EMBL; AF386923; AAK62368.1; -; mRNA.
DR   EMBL; AF428462; AAL16231.1; -; mRNA.
DR   EMBL; BT008504; AAP37863.1; -; mRNA.
DR   EMBL; AK226344; BAE98493.1; -; mRNA.
DR   EMBL; AY087965; AAM65512.1; -; mRNA.
DR   PIR; JC1453; JC1453.
DR   RefSeq; NP_175829.1; NM_104305.4. [P41377-1]
DR   SMR; P41377; -.
DR   BioGrid; 27093; 3.
DR   IntAct; P41377; 1.
DR   MINT; P41377; -.
DR   STRING; 3702.AT1G54270.1; -.
DR   iPTMnet; P41377; -.
DR   SwissPalm; P41377; -.
DR   PaxDb; P41377; -.
DR   PRIDE; P41377; -.
DR   EnsemblPlants; AT1G54270.1; AT1G54270.1; AT1G54270. [P41377-1]
DR   GeneID; 841868; -.
DR   Gramene; AT1G54270.1; AT1G54270.1; AT1G54270. [P41377-1]
DR   KEGG; ath:AT1G54270; -.
DR   Araport; AT1G54270; -.
DR   TAIR; locus:2020078; AT1G54270.
DR   eggNOG; KOG0327; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268797; -.
DR   InParanoid; P41377; -.
DR   KO; K03257; -.
DR   OrthoDB; 726081at2759; -.
DR   PhylomeDB; P41377; -.
DR   PRO; PR:P41377; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P41377; baseline and differential.
DR   Genevisible; P41377; AT.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
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   GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
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; Complete proteome;
KW   Cytoplasm; Helicase; Hydrolase; Initiation factor; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22223895}.
FT   CHAIN         2    412       Eukaryotic initiation factor 4A-2.
FT                                /FTId=PRO_0000054950.
FT   DOMAIN       70    240       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      251    412       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      83     90       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        39     67       Q motif.
FT   MOTIF       188    191       DEAD box.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:22223895}.
FT   MOD_RES     145    145       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9CAI7}.
SQ   SEQUENCE   412 AA;  46763 MW;  30335E5E6BAC33A1 CRC64;
     MAGSAPEGTQ FDTRQFDQRL NEVLDGQDEF FTSYDEVHES FDAMGLQENL LRGIYAYGFE
     KPSAIQQRGI VPFCKGLDVI QQAQSGTGKT ATFCSGVLQQ LDYALLQCQA LVLAPTRELA
     QQIEKVMRAL GDYQGVKVHA CVGGTSVRED QRILQAGVHV VVGTPGRVFD MLRRQSLRPD
     CIKMFVLDEA DEMLSRGFKD QIYDIFQLLP PKIQVGVFSA TMPPEALEIT RKFMSKPVRI
     LVKRDELTLE GIKQFYVNVE KEDWKLETLC DLYETLAITQ SVIFVNTRRK VDWLTDKMRS
     RDHTVSATHG DMDQNTRDII MREFRSGSSR VLITTDLLAR GIDVQQVSLV INFDLPTQPE
     NYLHRIGRSG RFGRKGVAIN FVTLDDQRML FDIQKFYNVV VEELPSNVAD LL
//
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