ID   EI3D2_DROER             Reviewed;         551 AA.
AC   B3P1F9;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
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=GG17155;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01;
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; CH954181; EDV49418.1; -; Genomic_DNA.
DR   RefSeq; XP_001980460.1; XM_001980424.2.
DR   AlphaFoldDB; B3P1F9; -.
DR   SMR; B3P1F9; -.
DR   STRING; 7220.FBpp0135701; -.
DR   PRIDE; B3P1F9; -.
DR   EnsemblMetazoa; FBtr0137209; FBpp0135701; FBgn0109382.
DR   GeneID; 6553887; -.
DR   KEGG; der:6553887; -.
DR   eggNOG; KOG2479; Eukaryota.
DR   HOGENOM; CLU_024521_2_0_1; -.
DR   OMA; CKHNGVI; -.
DR   OrthoDB; 1030308at2759; -.
DR   PhylomeDB; B3P1F9; -.
DR   Proteomes; UP000008711; 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: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; RNA-binding.
FT   CHAIN           1..551
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   D-2"
FT                   /id="PRO_0000364145"
FT   REGION          105..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   COMPBIAS        129..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  62433 MW;  791C26F81F58C195 CRC64;
     MSNYAPFIKP YVEYNEHGWG PCEVPELDVP YQPFCKGDRL GKICDWTVSL PEKKFPSKYA
     STFGNSSQYA YFYEDDDSTF HLVDTTGSKA FKPYQRGRYR PNVRNNVRAR GRTGRGSQAV
     GGPGGPAAGG STANSTKYGK GRNTRNTQNV GRRFGRSAPT RLRESSVMVQ SDWVSIEEID
     FARLLKLALP NIKEGKDIAT CGSLEYYDKL YDRVNLRNEK PLLKMDRVVH TVTTTDDPVI
     RRLSKTMGNV FATDEILATI MCCTRSNYSW DVVIEKLGTK VFLDKRDNDQ FDLLTVNETS
     LEPPMDEEGS INSAHSLAME ATLINHNFSQ QVLRIGDQEP RFKFEEPNPF EEQGVDLASM
     GYRYRQWDLG NEVVLIARCK HNGVIQGPNG EMQFLSIKAL NEWDSKGSNS VEWRQKLDTQ
     RGAVLASELR NNACKLARWT VEAVLAGSDQ LKLGYVSRVN PRDHLRHVIL GTQQFKPQEF
     ATQINLNMDN AWGVLRCLID IVMKQPDGKY LIMKDPNKSM IRLYDIPENA FDSDCNDDTE
     SSETFVHSND N