ID   EIF3C_DROAN             Reviewed;         906 AA.
AC   B3MIF1;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000255|HAMAP-Rule:MF_03002};
DE            Short=eIF3c {ECO:0000255|HAMAP-Rule:MF_03002};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 8 {ECO:0000255|HAMAP-Rule:MF_03002};
GN   Name=eIF3c {ECO:0000255|HAMAP-Rule:MF_03002};
GN   Synonyms=eIF3-S8 {ECO:0000255|HAMAP-Rule:MF_03002}; ORFNames=GF11658;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13;
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: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is involved in protein synthesis of a
CC       specialized repertoire of mRNAs and, together with other initiation
CC       factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC       ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
CC       {ECO:0000255|HAMAP-Rule:MF_03002}.
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_03002}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000255|HAMAP-
CC       Rule:MF_03002}.
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DR   EMBL; CH902619; EDV36999.1; -; Genomic_DNA.
DR   RefSeq; XP_001960177.1; XM_001960141.2.
DR   RefSeq; XP_014762823.1; XM_014907337.1.
DR   AlphaFoldDB; B3MIF1; -.
DR   SMR; B3MIF1; -.
DR   STRING; 7217.FBpp0114850; -.
DR   EnsemblMetazoa; FBtr0116358; FBpp0114850; FBgn0088698.
DR   EnsemblMetazoa; FBtr0387564; FBpp0347336; FBgn0088698.
DR   GeneID; 6494522; -.
DR   KEGG; dan:6494522; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_0_1; -.
DR   InParanoid; B3MIF1; -.
DR   OMA; VVMHRSE; -.
DR   OrthoDB; 273138at2759; -.
DR   PhylomeDB; B3MIF1; -.
DR   ChiTaRS; eIF3-S8; fly.
DR   Proteomes; UP000007801; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03002; eIF3c; 1.
DR   InterPro; IPR027516; EIF3C.
DR   InterPro; IPR008905; EIF3C_N_dom.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13937; PTHR13937; 1.
DR   Pfam; PF05470; eIF-3c_N; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..906
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000365385"
FT   DOMAIN          641..817
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..873
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          887..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..182
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..234
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..906
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
FT   MOD_RES         176
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
SQ   SEQUENCE   906 AA;  105434 MW;  7AC096C620B4DDD2 CRC64;
     MSRFFANGSD SESESSEEEV QATNFNKASA FQFSDDEEEV KRVVRSTKEK RYENLTNIIK
     TIRNHKKIKD IPNTLSSFED LTKAYTKALP VISKEENGIT PRFYIRCLAE LEDFINEVWE
     DREGRKNLSK NNSKSLGTLR QKVRKYIKDF EDDLSRFREA PDQESEAEDE EAAQDSDGGD
     AGDDSDAGIK REPAEAAPKV AKTVPAKAAP ADDDDSDDSI DWDSDSETET ESSDDENQYQ
     NMRERFLKRT TEKEEKDDDK RKDKRKEQKI KIRKRPEDDE DGEWETVVKG HVVEKPKMFE
     KDAEIDIPLV LAKLVEIMSA RGKKRTDRRL QIDLLFELRD ISDQHNLGTA VSVKIHFNII
     SAIFDYNQKI SEPMKLEHWA LLLEVMQSML KLLLVNPDIH MSESVAEEHE ELATSPFYVR
     GCPLAAVERL DDEFTKLLKE CDPHSNDYVS RLKDEVNVVK TIELVLQYFE NDGNNNERCR
     IYLRKIEHLY YKFDPEVLKK KRGEIPQNTQ TSVDVMDRLC KFIYAKDDTD RIRTRAILAH
     IYHHAMHDNW FQARDLVLMS HLQDNIDAAD PATRILYNRM MANLGLCAFR QENIKDAHHC
     LVDLMVTGKP KELLAQGLLP QRQHERSAEQ EKIEKQRQMP FHMHINLELL ECVYLVSAML
     LEIPYIAAHE FDARRRMISK TFYQQLRSSE RQSLVGPPES MREHVVAAAK AMRCGNWQAC
     ANFIVNKKMN TKVWDLFYES DRVREMLTKF IKEESLRTYL FTYSNVYTSI SIPSLAQMYE
     LPVQKVHSII SKMIINEELM ASLDDPTETV VMHRSEPSRL QALAMQFVDK VTNLVDVNEK
     VFDMKQGNFF QRGNMGNRGD RGYNRNQDGN WGGQLRDIKR IRGQRIQRGR KHQQQQQQQV
     QTIDEE