ID   EI3D2_DROSI             Reviewed;         551 AA.
AC   B4QT07;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit D-2 {ECO:0000255|HAMAP-Rule:MF_03003};
DE            Short=eIF3d-2 {ECO:0000255|HAMAP-Rule:MF_03003};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 7-2 {ECO:0000255|HAMAP-Rule:MF_03003};
GN   Name=eIF3d2 {ECO:0000255|HAMAP-Rule:MF_03003};
GN   Synonyms=eIF3-S7-2 {ECO:0000255|HAMAP-Rule:MF_03003}; ORFNames=GD20597;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM000364; EDX13267.1; -; Genomic_DNA.
DR   RefSeq; XP_002103764.1; XM_002103728.2.
DR   AlphaFoldDB; B4QT07; -.
DR   SMR; B4QT07; -.
DR   STRING; 7240.B4QT07; -.
DR   EnsemblMetazoa; FBtr0220507; FBpp0218999; FBgn0192064.
DR   GeneID; 6728418; -.
DR   HOGENOM; CLU_024521_2_0_1; -.
DR   OMA; CKHNGVI; -.
DR   PhylomeDB; B4QT07; -.
DR   Proteomes; UP000000304; Chromosome 3r.
DR   Bgee; FBgn0192064; Expressed in male reproductive system and 2 other tissues.
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: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; Protein biosynthesis; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..551
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   D-2"
FT                   /id="PRO_0000364159"
FT   REGION          108..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..304
FT                   /note="RNA gate"
FT                   /evidence="ECO:0000250|UniProtKB:K7IM66"
FT   REGION          527..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..545
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  62778 MW;  7194EF372EF2CA13 CRC64;
     MSNYAPFIKP YVEYNEHGWG PCEVPELDVP YQPFCKSDRL GKICDWTAMV PEKKFPSKYA
     STFGNNSQYA YFYEDDDSTF HLVDTTGSKA TKPYQRGRYR TNMRNNVRTR GRTGRGTPNI
     ASLGGSTAGG ATASSTKYGK GRHTRNTQNV GRRFGRNAPT RIRESSVMVQ SNWVSIEEID
     FPRLLKLALP NIKEGKDIAT CGSLEFYDKL YDRVNLRNEK PLQKMARVVH TVTTTDDPVI
     RRLSKTMGNV FATDEILSTI MCCTRSNYSW DVVVEKLGTK VFLDKRYNDQ FDLLTVNETS
     VEPPMEEEGS INSAHSLAME ATLINHNFSQ QVLRIGDQEQ RFMFEEPNPF EEPGVDLASI
     GYRYRQWDLG NDVVLIARCK HNAVIQGPNG DMQFLSIKAL NEWDSKVTNS VEWRQKLDTQ
     RGAVLASELR NNACKLARWT VEAVLAGSDQ LKLGYVSRMN PRDHLRHVIL GTQQFKPQEF
     ATQINLNMDN SWGVLRCLID LVMKQPDGKY LIMKDPNKPM IRLYDVPENA FDSDRDEEEE
     SSEPLSNSND N