EI3D1_DROPE
ID EI3D1_DROPE Reviewed; 541 AA.
AC B4GP93;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 61.
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=GL13650;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479186; EDW38976.1; -; Genomic_DNA.
DR RefSeq; XP_002020164.1; XM_002020128.1.
DR AlphaFoldDB; B4GP93; -.
DR SMR; B4GP93; -.
DR STRING; 7234.FBpp0177757; -.
DR EnsemblMetazoa; FBtr0179265; FBpp0177757; FBgn0151255.
DR eggNOG; KOG2479; Eukaryota.
DR HOGENOM; CLU_024521_2_0_1; -.
DR OMA; PDGWGPC; -.
DR PhylomeDB; B4GP93; -.
DR ChiTaRS; eIF-3p66; fly.
DR Proteomes; UP000008744; 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; 2.
DR PIRSF; PIRSF016281; EIF-3_zeta; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW RNA-binding.
FT CHAIN 1..541
FT /note="Eukaryotic translation initiation factor 3 subunit
FT D-1"
FT /id="PRO_0000364152"
FT REGION 98..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 61452 MW; E959F29E84BDADF4 CRC64;
MSETINTAAQ FPSFEKPTVQ FNERGWGPCE LPDTFKDVPY QPFSKNDRLG KICDWTSTSN
NDKKYQNKYA SSFGTGNQYS YYHEEDETTF HLVDTARVQK PPHQRGRFRN MRGRGGRGRN
PRGGLNNHHH HGMTTLNGKN VKARDTRRGM GKKFGHRGPP PKMRESSVAV RADWASIEEM
DFPRLIKLSL PNIKDGVDIA TCGTLEYYDK TYDRINVKNE KPLQKIDRIV HTVTTTDDPV
IRRLSKTVGN VFATDAILAT IMCSTRSNYS WDIVIEKVGD KPPTDDDSSC NSPRNLAIEA
TFINHNFSQQ VLKTGDQEAK FKFEEPNPFI SEDEDIQVAS VGYRYKKWEL GSDIVLVARC
EHDGVLQTPS GEPQFMSIKA LNEWDSKLAN GVEWRQKLDT QRGAVLANEL RNNACKLAKW
TVQAVLAGSD QLKLGYVSRI NPRDHSRHVI LGTQQFKPHE FATQINLSMD NAWGVLRCII
DLVMKQKDGK YLIMKDPNKP IIRLYDIPDN TFDSDDSDDG EGDDGEGFQQ VYNYANNSNK
I