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IF4E1_ORYSJ
ID   IF4E1_ORYSJ             Reviewed;         227 AA.
AC   P48599; B9EWY9; Q0JFN9; Q7F2S7;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:17898986, ECO:0000303|PubMed:8973371};
DE            Short=eIF-4E-1 {ECO:0000303|PubMed:17898986, ECO:0000303|PubMed:8973371};
DE            Short=eIF4E-1 {ECO:0000303|PubMed:17898986, ECO:0000303|PubMed:8973371};
DE   AltName: Full=eIF-4F 25 kDa subunit {ECO:0000303|PubMed:8973371};
DE   AltName: Full=eIF-4F p26 subunit {ECO:0000303|PubMed:8973371};
DE   AltName: Full=mRNA cap-binding protein {ECO:0000303|PubMed:17898986, ECO:0000303|PubMed:8973371};
GN   Name=eIF4E {ECO:0000303|PubMed:17898986, ECO:0000303|PubMed:8973371};
GN   OrderedLocusNames=Os01g0970400 {ECO:0000305}, LOC_Os01g73880 {ECO:0000305};
GN   ORFNames=OJ1656_A11.43 {ECO:0000312|EMBL:BAB85343.1},
GN   OsJ_04917 {ECO:0000312|EMBL:EEE56085.1};
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 [MRNA].
RC   STRAIN=cv. Nipponbare; TISSUE=Root;
RX   PubMed=8973371; DOI=10.1016/s0378-1119(96)00418-0;
RA   Aliyeva E., Metz A.M., Browning K.S.;
RT   "Sequences of two expressed sequence tags (EST) from rice encoding
RT   different cap-binding proteins.";
RL   Gene 180:221-223(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND GENE FAMILY.
RC   STRAIN=cv. Azucena; TISSUE=Leaf;
RX   PubMed=17898986; DOI=10.1007/s00122-007-0646-6;
RA   Boisnard A., Albar L., Thiemele D., Rondeau M., Ghesquiere A.;
RT   "Evaluation of genes from eIF4E and eIF4G multigenic families as potential
RT   candidates for partial resistance QTLs to Rice yellow mottle virus in
RT   rice.";
RL   Theor. Appl. Genet. 116:53-62(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [4]
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   [5]
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   [6]
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   [7]
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   [8]
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   [9]
RP   GENE FAMILY, AND REVIEW.
RX   PubMed=24309680; DOI=10.1016/j.meegid.2013.11.024;
RA   Moury B., Charron C., Janzac B., Simon V., Gallois J.L., Palloix A.,
RA   Caranta C.;
RT   "Evolution of plant eukaryotic initiation factor 4E (eIF4E) and potyvirus
RT   genome-linked protein (VPg): a game of mirrors impacting resistance
RT   spectrum and durability.";
RL   Infect. Genet. Evol. 27:472-480(2014).
CC   -!- FUNCTION: Component of the protein complex eIF4F, which is involved in
CC       the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal
CC       secondary structure and recruitment of mRNA to the ribosome
CC       (PubMed:17898986). Recognizes and binds the 7-methylguanosine-
CC       containing mRNA cap during an early step in the initiation of protein
CC       synthesis and facilitates ribosome binding by inducing the unwinding of
CC       the mRNAs secondary structures (PubMed:17898986).
CC       {ECO:0000303|PubMed:17898986}.
CC   -!- SUBUNIT: EIF4F is a multi-subunit complex, the composition of which
CC       varies with external and internal environmental conditions
CC       (PubMed:17898986). It is composed of at least EIF4A, EIF4E and EIF4G.
CC       EIF4E is also known to interact with other partners (PubMed:17898986).
CC       In higher plants two isoforms of EIF4F have been identified, named
CC       isoform EIF4F and isoform EIF(iso)4F (PubMed:17898986). Isoform EIF4F
CC       has subunits p220 and p26, whereas isoform EIF(iso)4F has subunits p82
CC       and p28 (PubMed:17898986). {ECO:0000303|PubMed:17898986}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm
CC       {ECO:0000250|UniProtKB:C6ZJZ3}.
CC   -!- PTM: According to the redox status, the Cys-125-Cys-163 disulfide
CC       bridge may have a role in regulating protein function by affecting its
CC       ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC       {ECO:0000305}.
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DR   EMBL; U34597; AAB40348.1; -; mRNA.
DR   EMBL; AM411441; CAL69635.1; -; mRNA.
DR   EMBL; AP003448; BAB85343.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF07439.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS76420.1; -; Genomic_DNA.
DR   EMBL; CM000138; EEE56085.1; -; Genomic_DNA.
DR   EMBL; AK069207; BAG91316.1; -; mRNA.
DR   EMBL; AK099169; BAG93969.1; -; mRNA.
DR   PIR; JC5330; JC5330.
DR   RefSeq; XP_015629641.1; XM_015774155.1.
DR   AlphaFoldDB; P48599; -.
DR   SMR; P48599; -.
DR   STRING; 4530.OS01T0970400-01; -.
DR   PaxDb; P48599; -.
DR   PRIDE; P48599; -.
DR   EnsemblPlants; Os01t0970400-01; Os01t0970400-01; Os01g0970400.
DR   GeneID; 4323837; -.
DR   Gramene; Os01t0970400-01; Os01t0970400-01; Os01g0970400.
DR   KEGG; osa:4323837; -.
DR   eggNOG; KOG1670; Eukaryota.
DR   HOGENOM; CLU_043552_2_1_1; -.
DR   InParanoid; P48599; -.
DR   OMA; NKFGGRW; -.
DR   OrthoDB; 1394271at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000007752; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   ExpressionAtlas; P48599; baseline and differential.
DR   Genevisible; P48599; OS.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR   Gene3D; 3.30.760.10; -; 1.
DR   InterPro; IPR023398; TIF_eIF4e-like.
DR   InterPro; IPR001040; TIF_eIF_4E.
DR   InterPro; IPR019770; TIF_eIF_4E_CS.
DR   PANTHER; PTHR11960; PTHR11960; 1.
DR   Pfam; PF01652; IF4E; 1.
DR   SUPFAM; SSF55418; SSF55418; 1.
DR   PROSITE; PS00813; IF4E; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Disulfide bond; Initiation factor; Nucleus;
KW   Protein biosynthesis; Reference proteome; RNA-binding;
KW   Translation regulation.
FT   CHAIN           1..227
FT                   /note="Eukaryotic translation initiation factor 4E-1"
FT                   /id="PRO_0000193660"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..55
FT                   /note="EIF4G-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT   REGION          62..98
FT                   /note="EIF4G-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT   REGION          146..155
FT                   /note="EIF4G-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT   BINDING         70..75
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT                   /ligand_part_id="ChEBI:CHEBI:74429"
FT                   /ligand_part_note="m7GTP residue in mRNA cap"
FT                   /evidence="ECO:0000250|UniProtKB:P29557"
FT   BINDING         102
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT                   /ligand_part_id="ChEBI:CHEBI:74429"
FT                   /ligand_part_note="m7GTP residue in mRNA cap"
FT                   /evidence="ECO:0000250|UniProtKB:P29557"
FT   BINDING         120..121
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT                   /ligand_part_id="ChEBI:CHEBI:74429"
FT                   /ligand_part_note="m7GTP residue in mRNA cap"
FT                   /evidence="ECO:0000250|UniProtKB:P29557"
FT   BINDING         170..175
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT                   /ligand_part_id="ChEBI:CHEBI:74429"
FT                   /ligand_part_note="m7GTP residue in mRNA cap"
FT                   /evidence="ECO:0000250|UniProtKB:P29557"
FT   BINDING         215..219
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT                   /ligand_part_id="ChEBI:CHEBI:74429"
FT                   /ligand_part_note="m7GTP residue in mRNA cap"
FT                   /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT   DISULFID        125..163
FT                   /evidence="ECO:0000250|UniProtKB:P29557"
SQ   SEQUENCE   227 AA;  25465 MW;  FD9E13367E2FA36B CRC64;
     MAEEHETRPP SAGRPPSSGR GRADDADERE EGEIADDDSG HAPPQANPAA PHPLEHAWTF
     WFDNPQGKSK QATWGSSIRP IHTFSTVEDF WSLYNNIHHP SKLVVGADFH CFKNKIEPKW
     EDPICANGGK WTFSCGRGKS DTMWLHTLLA MIGEQFDYGD EICGAVVSVR GKQERIAIWT
     KNAANEAAQI SIGKQWKEFL DYKDSIGFIV HDDAKKMDKG LKNRYTV
 
 
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