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IF4A3_ORYSJ
ID   IF4A3_ORYSJ             Reviewed;         414 AA.
AC   Q6Z2Z4; B7EMF9; Q9AR32;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Eukaryotic initiation factor 4A-3;
DE            Short=eIF-4A-3;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent RNA helicase eIF4A-3;
DE   AltName: Full=DEAD-box ATP-dependent RNA helicase 23;
DE   AltName: Full=eIF4A-2;
GN   OrderedLocusNames=Os02g0146600, LOC_Os02g05330;
GN   ORFNames=OJ1008_C03.10, OsJ_05367 {ECO:0000312|EMBL:EEE56296.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=11913775; DOI=10.3109/10425170109084453;
RA   Kato A., Fujita S., Komeda Y.;
RT   "Identification and characterization of two genes encoding the eukaryotic
RT   initiation factor 4A in rice.";
RL   DNA Seq. 12:295-303(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Ilpoombyeo; TISSUE=Immature seed;
RA   Yoon U.H.;
RT   "Structural and expression analysis of immature seed genes in Oryza sativa
RT   L.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [8]
RP   INTERACTION WITH DRM2, AND SUBCELLULAR LOCATION.
RX   PubMed=23732981; DOI=10.1016/j.jmb.2013.05.021;
RA   Dangwal M., Malik G., Kapoor S., Kapoor M.;
RT   "De novo methyltransferase, OsDRM2, interacts with the ATP-dependent RNA
RT   helicase, OseIF4A, in rice.";
RL   J. Mol. Biol. 425:2853-2866(2013).
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 (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 which
CC       varies with external and internal environmental conditions. It is
CC       composed of at least EIF4A, EIF4E and EIF4G (By similarity). Interacts
CC       with DRM2 (via UBA domains) (PubMed:23732981). {ECO:0000250,
CC       ECO:0000269|PubMed:23732981}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000269|PubMed:23732981}. Note=Localizes to the nucleus when
CC       interacting with DRM2. {ECO:0000269|PubMed:23732981}.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB21258.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB21259.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB046414; BAB21258.1; ALT_FRAME; mRNA.
DR   EMBL; AB046415; BAB21259.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; KC140119; AGT42311.1; -; mRNA.
DR   EMBL; AP005288; BAD13081.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF07792.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS76965.1; -; Genomic_DNA.
DR   EMBL; CM000139; EEE56296.1; -; Genomic_DNA.
DR   EMBL; AK073620; BAG93556.1; -; mRNA.
DR   RefSeq; XP_015626460.1; XM_015770974.1.
DR   AlphaFoldDB; Q6Z2Z4; -.
DR   SMR; Q6Z2Z4; -.
DR   STRING; 4530.OS02T0146600-01; -.
DR   PaxDb; Q6Z2Z4; -.
DR   PRIDE; Q6Z2Z4; -.
DR   EnsemblPlants; Os02t0146600-01; Os02t0146600-01; Os02g0146600.
DR   GeneID; 4328286; -.
DR   Gramene; Os02t0146600-01; Os02t0146600-01; Os02g0146600.
DR   KEGG; osa:4328286; -.
DR   eggNOG; KOG0327; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; Q6Z2Z4; -.
DR   OMA; HLGDYMN; -.
DR   OrthoDB; 726081at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6Z2Z4; OS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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   ATP-binding; Cytoplasm; Helicase; Hydrolase; Initiation factor;
KW   Nucleotide-binding; Nucleus; Protein biosynthesis; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..414
FT                   /note="Eukaryotic initiation factor 4A-3"
FT                   /id="PRO_0000282441"
FT   DOMAIN          72..242
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          253..414
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           41..69
FT                   /note="Q motif"
FT   MOTIF           190..193
FT                   /note="DEAD box"
FT   BINDING         85..92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   CONFLICT        38..39
FT                   /note="EV -> DL (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="Q -> K (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="D -> Q (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        228
FT                   /note="A -> G (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        233..234
FT                   /note="RK -> LR (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237
FT                   /note="N -> D (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        251
FT                   /note="L -> R (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        276..277
FT                   /note="ET -> DS (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290..292
FT                   /note="RRK -> LRM (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        317
FT                   /note="N -> I (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        341
FT                   /note="A -> D (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        358
FT                   /note="P -> S (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        361
FT                   /note="P -> T (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        382
FT                   /note="N -> I (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        401
FT                   /note="V -> G (in Ref. 1; BAB21258/BAB21259)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   414 AA;  47138 MW;  B440EF6727D791DD CRC64;
     MAGMAPEGSQ FDAKHYDSKM QELLHQGDNE EFFTSYDEVF ESFDDMGLQE NLLRGIYAYG
     FEKPSAIQQR GIVPFCKGLD VIQQAQSGTG KTATFCSGIL QQLDYGLVEC QSLVLAPTRE
     LAQQIEKVMR ALGDYLGVKV HACVGGTSVR EDQRILASGV HVVVGTPGRV FDMLRRQSLR
     PDHIKMFVLD EADEMLSRGF KDQIYDIFQL LPPKIQVGVF SATMPPEALE ITRKFMNKPV
     RILVKRDELT LEGIKQFYVN VEKEDWKLDT LCDLYETLAI TQSVIFVNTR RKVDWLTDKM
     RSRDHTVSAT HGDMDQNTRD IIMREFRSGS SRVLITTDLL ARGIDVQQVS LVINYDLPTQ
     PENYLHRIGR SGRFGRKGVA INFVTRDDER MLFDIQRFYN VTIEELPANV ADLL
 
 
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