EI3D2_DROPE
ID EI3D2_DROPE Reviewed; 545 AA.
AC B4GFS1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-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=GL21571;
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; CH479182; EDW34456.1; -; Genomic_DNA.
DR RefSeq; XP_002017356.1; XM_002017320.1.
DR AlphaFoldDB; B4GFS1; -.
DR SMR; B4GFS1; -.
DR STRING; 7234.FBpp0185678; -.
DR EnsemblMetazoa; FBtr0187186; FBpp0185678; FBgn0159164.
DR GeneID; 6591866; -.
DR KEGG; dpe:6591866; -.
DR eggNOG; KOG2479; Eukaryota.
DR HOGENOM; CLU_024521_2_0_1; -.
DR OMA; CKHNGVI; -.
DR PhylomeDB; B4GFS1; -.
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: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..545
FT /note="Eukaryotic translation initiation factor 3 subunit
FT D-2"
FT /id="PRO_0000364153"
FT REGION 99..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..301
FT /note="RNA gate"
FT /evidence="ECO:0000250|UniProtKB:K7IM66"
FT COMPBIAS 135..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 62205 MW; 265414198194144B CRC64;
MSGRAPFIKP VLEYNEHGWG PCEELSVDVP YQPFCKSDRV GKISDWTAPP TERKFANKYV
SSFGNSNQYA YFHEDDESTY HLVDTSGFKG FRPFQRGRFR GNIRNNPRTR GRTGRGGAVT
GIGGNQPGVG VNERTKYGKG RDNRRQMGRR FGRNAPTRMR ESSVVVRSDW VSIEEIDFPR
LLKLSLPNVK EGQDVVTCGS LEYYDKTYDR INVKNERPLL KTDRIIHTLT TTDDPVIRRL
SKTIGNIFAT DEILATIMCC TRSNYSWDVV FDKVGNKIFL DKRDNAQFDL LTVNETALEP
PLDEEGSINS PHSLAMEATL INHNFCQQVL RGGDQKKYQF EEPYPLEESG VDLVSIGYRY
KQWDLGNNII LIARCKHNGV LQGPNGEVQF LSIRALNEWD SKASNSLEWR QKLDTQHGAV
LASELRNNAC KLARWTVESV LSGSDQLKLG YVSRVIPRDH LRHVILRTQQ FKPQEFSTQI
NLSMDNAWGI LRCLIDIVMK QPDGKYLLMK DPNKPMVRLY DVPENAFESS DEDDLSDDKL
FLLSN
