EI3D2_DROVI
ID EI3D2_DROVI Reviewed; 554 AA.
AC B4M5A7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=GJ10066;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
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; CH940652; EDW59818.1; -; Genomic_DNA.
DR RefSeq; XP_002056706.1; XM_002056670.2.
DR AlphaFoldDB; B4M5A7; -.
DR SMR; B4M5A7; -.
DR STRING; 7244.FBpp0224483; -.
DR EnsemblMetazoa; FBtr0225991; FBpp0224483; FBgn0197356.
DR GeneID; 6632344; -.
DR KEGG; dvi:6632344; -.
DR eggNOG; KOG2479; Eukaryota.
DR HOGENOM; CLU_024521_2_0_1; -.
DR InParanoid; B4M5A7; -.
DR OMA; CKHNGVI; -.
DR OrthoDB; 1030308at2759; -.
DR PhylomeDB; B4M5A7; -.
DR Proteomes; UP000008792; 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..554
FT /note="Eukaryotic translation initiation factor 3 subunit
FT D-2"
FT /id="PRO_0000364161"
FT REGION 116..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..305
FT /note="RNA gate"
FT /evidence="ECO:0000250|UniProtKB:K7IM66"
FT REGION 532..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 62723 MW; A258958D5F349C1C CRC64;
MSQYAPFIKP YIEYNQFGWG PCDMPDMEVP YQPFCKSDRL GKISDWMMPV QEKKYANKYA
STFGSNNSQY AYFHEDDDAT FHLVDGGNPR ALKPYQRNRY RPNQRNNVRV HGRNVRGNAA
IGGGQGGAGG TGGAGVGNKY GKGRDMRRGN MGRRFMRNAP VRLRESSVVV RSDWVSIEEI
DFPRLLKLSL PNIKDGVDVV TCGTLEYYDK QCDRINVKNE RPLQKIDRII NVPGTIDDPI
IRRLSKSMGN VFATDDIIAT LMCCTRSNYS WDIVIEKLGT KVFLDKRDNA QFDLLTVNET
ALEPPQDEEG SINSPQSLSL EATLINHNFS QQVLKIGEQE PKHKFDEPNP FEEPGVELAS
VAYRYKEWQL GDDVVLIARC KHNGVIKSPA GELQFLSIKA LNEWDSKAAN SVEWRQKLDS
QRGAVLASEL RNNACKLAKW TVEAVLAGSD QLKLGYVSRV NRKDHLRHVI LGMQQFKPQE
FATQINLNMD NAWGVLRCLV DIVLKQPDGK YLIMKDPNKP MIRLYDIPDN AFDSDGNDDE
ETSDDRPFLK SLGN
