EI3D2_DROGR
ID EI3D2_DROGR Reviewed; 557 AA.
AC B4JUM0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=GH15488;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916374; EDV91190.1; -; Genomic_DNA.
DR RefSeq; XP_001994561.1; XM_001994525.1.
DR AlphaFoldDB; B4JUM0; -.
DR SMR; B4JUM0; -.
DR STRING; 7222.FBpp0149394; -.
DR EnsemblMetazoa; FBtr0150902; FBpp0149394; FBgn0122960.
DR GeneID; 6568607; -.
DR KEGG; dgr:6568607; -.
DR eggNOG; KOG2479; Eukaryota.
DR HOGENOM; CLU_024521_2_0_1; -.
DR InParanoid; B4JUM0; -.
DR OMA; NNMWGIL; -.
DR OrthoDB; 1030308at2759; -.
DR PhylomeDB; B4JUM0; -.
DR Proteomes; UP000001070; 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..557
FT /note="Eukaryotic translation initiation factor 3 subunit
FT D-2"
FT /id="PRO_0000364147"
FT REGION 292..306
FT /note="RNA gate"
FT /evidence="ECO:0000250|UniProtKB:K7IM66"
FT REGION 533..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 63181 MW; 9C5EDD3A849F9204 CRC64;
MSQYAPFVKP YIEYNEFGWG PSDLPDLEVP YQPFCKGDRL GKISDWTTPV QERKYNNNKY
MSTFGSSNSQ YAYFHGNDDA SFHLVNGNNM RALKPYQRNR YRPTQRNNLR LHGRNGRFNA
AIGAGHGGAG AAGGAGASNK YGKGRDMRRG QTGRRFMRAA PVRQRQSSVV VRSDWVSIEE
IDFPRLLKLT LPNIQEGADL ITCGTLEFFD KQCDRINVKN ERPLQKIDRI INVPGTIDDP
IIRRLSKSLG NVFATDDIIA TLMCCTRSNY SWDIVIDKVG TKLFLDKRDN AQFDMLTVNE
TALEPPLEEE GSINSPQSLS LEATIINHNF SQQVLKIGEL EPKHKFDEPN PFEEPGVELA
SIGYRYKQWQ LGDDMVLVAR CKHNGVLRSP GGELQFLSIR ALNEWDSKAA NSVEWRQKLD
SQRGAVLASE LRNNACKLAK WTVEAVLAGS DQLKLGYVSR LNRKDHLHHV ILGMQQFKPQ
EFATQINLNM DNAWGVLRCL VDIMLKQPDG KYLIMKDPNK PMIRLYDIPE NAFDSDNNDG
EETSDDRPFL NSKDNKL
