EI3D1_DROWI
ID EI3D1_DROWI Reviewed; 561 AA.
AC B4NLG2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit D-1 {ECO:0000255|HAMAP-Rule:MF_03003};
DE Short=eIF3d-1 {ECO:0000255|HAMAP-Rule:MF_03003};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 7-1 {ECO:0000255|HAMAP-Rule:MF_03003};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit p66;
GN Name=eIF3d1 {ECO:0000255|HAMAP-Rule:MF_03003}; Synonyms=eIF-3p66;
GN ORFNames=GK13187;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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. The eIF-3 complex interacts with pix.
CC {ECO:0000255|HAMAP-Rule:MF_03003}.
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; CH964272; EDW84365.1; -; Genomic_DNA.
DR RefSeq; XP_002073379.1; XM_002073343.2.
DR AlphaFoldDB; B4NLG2; -.
DR SMR; B4NLG2; -.
DR STRING; 7260.FBpp0242330; -.
DR EnsemblMetazoa; FBtr0243838; FBpp0242330; FBgn0215196.
DR GeneID; 6650643; -.
DR KEGG; dwi:6650643; -.
DR eggNOG; KOG2479; Eukaryota.
DR HOGENOM; CLU_024521_2_0_1; -.
DR InParanoid; B4NLG2; -.
DR OMA; PDGWGPC; -.
DR OrthoDB; 1030308at2759; -.
DR PhylomeDB; B4NLG2; -.
DR ChiTaRS; eIF-3p66; fly.
DR Proteomes; UP000007798; Unassembled WGS sequence.
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; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblMetazoa.
DR GO; GO:0098808; F:mRNA cap binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
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:0006446; P:regulation of translational initiation; ISS:UniProtKB.
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 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..561
FT /note="Eukaryotic translation initiation factor 3 subunit
FT D-1"
FT /id="PRO_0000364162"
FT REGION 98..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..303
FT /note="RNA gate"
FT /evidence="ECO:0000250|UniProtKB:K7IM66"
FT COMPBIAS 102..116
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 128
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 561 AA; 63852 MW; 79F4C751B16B9D66 CRC64;
MSETINTSAQ FPTFEKPTVQ FNEKGWGPCE LPDTFKDVPY QPFSKNDRLG KICDWTNTSN
NDKKYQNKYA SSFGTGIQYS YYHEEDETTF HLVDTARVQK PPHQRGRFRN MRNSRSGRGR
NARGGINTHG MTTLSGKNVK ARDPRRGMGK KFGNRGPPPK MRESSVAVRS DWASIEEMDF
PRLIKLSLPN IKEGVDIATC GTLEYYDKTY DRINVKNEKP LQKIDRIVHT VTTTDDPVIR
RLSKTVGNVF ATDAILATIM CSTRSNYSWD IVIEKVGDKI FMDKRDHTEF DLLTVNETSV
EPPTDDDSSC NSPRNLAIEA TFINHNFSQQ VLKTGDQEAK FKFEESNPFI SEDEDIQVAS
VGYRYKKWEL GSDIVLVARC EHDGVLQTPS GEPQFMSIKA LNEWDSKMAN GVEWRQKLDT
QRGAVLANEL RNNACKLAKW TVQAVLAGSD QLKLGYVSRI NPRDHSRHVI LGTQQFKPHE
FATQINLSMD NAWGILRCII DLVMKQRDGK YLIMKDPNKP IIRLYDIPDN TFDSDDSDDG
EGDDGEGFQQ VYNYANNSNK I