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EIF3D_ARATH
ID   EIF3D_ARATH             Reviewed;         591 AA.
AC   P56820; B5X0N5; Q9C5Y8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit D {ECO:0000255|HAMAP-Rule:MF_03003};
DE            Short=eIF3d {ECO:0000255|HAMAP-Rule:MF_03003};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 7 {ECO:0000255|HAMAP-Rule:MF_03003};
DE   AltName: Full=eIF-3-zeta {ECO:0000255|HAMAP-Rule:MF_03003};
DE   AltName: Full=p66;
GN   Name=TIF3D1; OrderedLocusNames=At4g20980; ORFNames=T13K14.140;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 174-591, AND SUBUNIT.
RC   STRAIN=cv. Columbia;
RX   PubMed=11042177; DOI=10.1074/jbc.m007236200;
RA   Burks E.A., Bezerra P.P., Le H., Gallie D.R., Browning K.S.;
RT   "Plant initiation factor 3 subunit composition resembles mammalian
RT   initiation factor 3 and has a novel subunit.";
RL   J. Biol. Chem. 276:2122-2131(2001).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
CC   -!- FUNCTION: mRNA cap-binding component of the eukaryotic translation
CC       initiation factor 3 (eIF-3) complex, which is involved in protein
CC       synthesis of a specialized repertoire of mRNAs and, together with other
CC       initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC       the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation. In the
CC       eIF-3 complex, eif3d specifically recognizes and binds the 7-
CC       methylguanosine cap of a subset of mRNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_03003}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is composed of at least 13 different subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_03003, ECO:0000269|PubMed:11042177}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.
CC   -!- DOMAIN: The RNA gate region regulates mRNA cap recognition to prevent
CC       promiscuous mRNA-binding before assembly of eif3d into the full
CC       eukaryotic translation initiation factor 3 (eIF-3) complex.
CC       {ECO:0000255|HAMAP-Rule:MF_03003}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit D family. {ECO:0000255|HAMAP-
CC       Rule:MF_03003}.
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DR   EMBL; AL080282; CAB45893.1; -; Genomic_DNA.
DR   EMBL; AL161554; CAB79098.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84381.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84382.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84383.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84384.1; -; Genomic_DNA.
DR   EMBL; AK317111; BAH19799.1; -; mRNA.
DR   EMBL; BT044604; ACI31304.1; -; mRNA.
DR   EMBL; AF291714; AAG53638.1; -; mRNA.
DR   PIR; T10640; T10640.
DR   RefSeq; NP_001031683.1; NM_001036606.1.
DR   RefSeq; NP_001031684.1; NM_001036607.1.
DR   RefSeq; NP_001190783.1; NM_001203854.1.
DR   RefSeq; NP_193830.1; NM_118216.4.
DR   AlphaFoldDB; P56820; -.
DR   SMR; P56820; -.
DR   BioGRID; 13136; 21.
DR   STRING; 3702.AT4G20980.2; -.
DR   iPTMnet; P56820; -.
DR   PaxDb; P56820; -.
DR   PRIDE; P56820; -.
DR   ProteomicsDB; 222230; -.
DR   EnsemblPlants; AT4G20980.1; AT4G20980.1; AT4G20980.
DR   EnsemblPlants; AT4G20980.2; AT4G20980.2; AT4G20980.
DR   EnsemblPlants; AT4G20980.3; AT4G20980.3; AT4G20980.
DR   EnsemblPlants; AT4G20980.4; AT4G20980.4; AT4G20980.
DR   GeneID; 827845; -.
DR   Gramene; AT4G20980.1; AT4G20980.1; AT4G20980.
DR   Gramene; AT4G20980.2; AT4G20980.2; AT4G20980.
DR   Gramene; AT4G20980.3; AT4G20980.3; AT4G20980.
DR   Gramene; AT4G20980.4; AT4G20980.4; AT4G20980.
DR   KEGG; ath:AT4G20980; -.
DR   Araport; AT4G20980; -.
DR   TAIR; locus:2133104; AT4G20980.
DR   eggNOG; KOG2479; Eukaryota.
DR   HOGENOM; CLU_024521_2_0_1; -.
DR   InParanoid; P56820; -.
DR   OMA; NIHHQRR; -.
DR   OrthoDB; 1030308at2759; -.
DR   PhylomeDB; P56820; -.
DR   PRO; PR:P56820; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; P56820; baseline and differential.
DR   Genevisible; P56820; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0098808; F:mRNA cap binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0002191; P:cap-dependent translational initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR   HAMAP; MF_03003; eIF3d; 1.
DR   InterPro; IPR007783; eIF3d.
DR   PANTHER; PTHR12399; PTHR12399; 1.
DR   Pfam; PF05091; eIF-3_zeta; 1.
DR   PIRSF; PIRSF016281; EIF-3_zeta; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..591
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   D"
FT                   /id="PRO_0000123522"
FT   REGION          100..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..323
FT                   /note="RNA gate"
FT                   /evidence="ECO:0000250|UniProtKB:K7IM66"
FT   REGION          549..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..565
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..591
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   591 AA;  66725 MW;  9C5E673F04E9845C CRC64;
     MVTEAFEFVA VPFNSDGWGP PDASDVSSSA SPTSVAAANL LPNVPFASFS RSDKLGRVAD
     WTRNLSNPSA RPNTGSKSDP SAVFDFSAFA IDEGFGLASS GGNPDEDAAF RLVDGKPPPR
     PKFGPKWRFN PHHNRNQLPQ RRDEEVEAKK RDAEKERARR DRLYNNNRNN IHHQRREAAA
     FKSSVDIQPE WNMLEQIPFS TFSKLSYTVQ EPEDLLLCGG LEYYNRLFDR ITPKNERRLE
     RFKNRNFFKV TTSDDPVIRR LAKEDKATVF ATDAILAALM CAPRSVYSWD IVIQRVGNKL
     FFDKRDGSQL DLLSVHETSQ EPLPESKDDI NSAHSLGVEA AYINQNFSQQ VLVRDGKKET
     FDEANPFANE GEEIASVAYR YRRWKLDDNM HLVARCELQS VADLNNQRSF LTLNALNEFD
     PKYSGVDWRQ KLETQRGAVL ATELKNNGNK LAKWTAQALL ANADMMKIGF VSRVHPRDHF
     NHVILSVLGY KPKDFAGQIN LNTSNMWGIV KSIVDLCMKL SEGKYVLVKD PSKPQVRIYE
     VPPDAFENDY VEEPLPEDEQ VQPTEENTEG AEASVAATKE TEEKKADDAQ A
 
 
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