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EIF3D_DICDI
ID   EIF3D_DICDI             Reviewed;         527 AA.
AC   Q554U9; Q86AR8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit D {ECO:0000255|HAMAP-Rule:MF_03003};
DE            Short=eIF3d {ECO:0000255|HAMAP-Rule:MF_03003};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 7 {ECO:0000255|HAMAP-Rule:MF_03003};
DE   AltName: Full=eIF-3-zeta {ECO:0000255|HAMAP-Rule:MF_03003};
GN   Name=eif3d; Synonyms=moe1; ORFNames=DDB_G0274627;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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. {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; AAFI02000012; EAL70206.1; -; Genomic_DNA.
DR   RefSeq; XP_644224.1; XM_639132.1.
DR   AlphaFoldDB; Q554U9; -.
DR   SMR; Q554U9; -.
DR   STRING; 44689.DDB0219927; -.
DR   PaxDb; Q554U9; -.
DR   EnsemblProtists; EAL70206; EAL70206; DDB_G0274627.
DR   GeneID; 8619653; -.
DR   KEGG; ddi:DDB_G0274627; -.
DR   dictyBase; DDB_G0274627; eif3D.
DR   eggNOG; KOG2479; Eukaryota.
DR   HOGENOM; CLU_024521_2_0_1; -.
DR   InParanoid; Q554U9; -.
DR   OMA; PDGWGPC; -.
DR   PhylomeDB; Q554U9; -.
DR   Reactome; R-DDI-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-DDI-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-DDI-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-DDI-72702; Ribosomal scanning and start codon recognition.
DR   PRO; PR:Q554U9; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005813; C:centrosome; TAS:dictyBase.
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:0045335; C:phagocytic vesicle; HDA:dictyBase.
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:0009617; P:response to bacterium; HEP:dictyBase.
DR   GO; GO:0006413; P: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..527
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   D"
FT                   /id="PRO_0000327633"
FT   REGION          100..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..277
FT                   /note="RNA gate"
FT                   /evidence="ECO:0000250|UniProtKB:K7IM66"
FT   REGION          503..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..518
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  60298 MW;  4A55DA19462A7132 CRC64;
     MSLELNTIKV NPTGWGPVGK LEKFTDIPYA PFSKGDKIGK CSDWNSNVRN YQRQNYGSNA
     FNPFTFKLED DEDSFTLVDY TRVQNKLKNK GKTYQKQFYQ QNKRGGSNAG GRGGRGGMRG
     GRFGSNNKYW NDRRQRNRES SIEILSSWES KEEFDLSTFK QYTVEQLPEP ETIGTYGQVK
     YYNKVYDRIN AKNEKKLQKT ENSVPLIPTS DDKVIRSEYM NGNVYATDSI LAVLMSAQKS
     VYSWDIVVQK VGARLFFELR PGTSEHLTVN ENLTAHHQDD KDPINTTSSL SQEATQVNLN
     YWQQVLSQNV EPFKFDNELP EGDEFENCVD VGYAYKKWDL GDDIVVLART EIDGVVEGLP
     GQPPKFISIK AINEHDSNRF GIEFRKKLDS QRAAILATEI KNNSTKFAKW SIQSTLAGCE
     MLNLGFVSRD SIRDNNNHVI LGTQFYPVAD LNKQNGVDMK NCWGILKHIA QTCMKLANGK
     YLLHRDPNRN VINLYSVPEN AFDQIEEETQ EEEEEEQSKG WVEESRE
 
 
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