ID   EIF3C_DROPS             Reviewed;         911 AA.
AC   Q28Z41;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=GA18551;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
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; CM000071; EAL25774.1; -; Genomic_DNA.
DR   RefSeq; XP_001361196.1; XM_001361159.3.
DR   RefSeq; XP_015040097.1; XM_015184611.1.
DR   AlphaFoldDB; Q28Z41; -.
DR   SMR; Q28Z41; -.
DR   STRING; 7237.FBpp0276360; -.
DR   EnsemblMetazoa; FBtr0277922; FBpp0276360; FBgn0078553.
DR   EnsemblMetazoa; FBtr0375078; FBpp0336552; FBgn0078553.
DR   GeneID; 4804672; -.
DR   KEGG; dpo:Dpse_GA18551; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_0_1; -.
DR   InParanoid; Q28Z41; -.
DR   OMA; VVMHRSE; -.
DR   PhylomeDB; Q28Z41; -.
DR   ChiTaRS; eIF3-S8; fly.
DR   Proteomes; UP000001819; Chromosome 3.
DR   Bgee; FBgn0078553; Expressed in female reproductive system and 3 other tissues.
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..911
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000365391"
FT   DOMAIN          642..818
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          851..911
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..233
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..880
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        894..911
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         175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
SQ   SEQUENCE   911 AA;  105941 MW;  144637612185FD0B CRC64;
     MSRFFANGSD SESESSEEEV QAPNFNKASA FQFSDDEEEV KRVVRSTKEK RYENLTSIIK
     TIRNHKKIKD IPNTLSSFED LTRAYTKALP VISKEENGIT PRFYIRCLAE LEDFINEIWE
     DREGRRNLSK NNTKSLGTLR QKVRKYIKDF EEDLSRFREA PDQESEAEDE EAHVSDAGEA
     ADDSYAGFKK EASVTAPKIA KSAPAKSVPA DDEDSDDSID WDSDSESETE SSEDENQYQN
     MRERFLKRST EKGEDKGDDD KRKDKRKEQK LKIRKRAEDD EDGEWETVVK GHVVEKPKMF
     EKDAEIDIPL VLAKLVEIMS ARGKKRTDRR LQIDLLFELR DISDQHNLGV PVSVKIHFNI
     ISAIFDYNQK ISEPMKMEHW ALLLEVMQSM MKLLLANADI SISESVAEEH EEYITAPYYI
     RGCPLAAVER LDDEFTKLLK ECDPHSNDYV SRLKDEMNVV KTIELVLQYF EQCGNPNERC
     RIYLRKIEHL YYKFDPEVLK KKRGELPATT ATSVDVMDKL CKFIYAKDDT DRIRTRAILA
     HIYHHAMHDN WFQARDLVLM SHLQDNIDAA DPATRILYNR MMANLGLCAF RQENVKDAHH
     CLVDLMVTGK PKELLAQGLL PQRQHERSAE QEKIEKQRQM PFHMHINLEL LECVYLVSAM
     LLEIPYIAAH EFDARRRMIS KTFYQQLRSS ERQSLVGPPE SMREHVVAAA KAMRCGNWQA
     CANFIVNKKM NTKVWDLFYE SDRVREMLVK FIKEESLRTY LFTYSNVYTS ISIPSLAQMY
     ELPVPKVHSI ISKMIINEEL MASLDDPSET VVMHRSEPSR LQALAMQFVD KVTNLVDVNE
     KVFDMKQGNF FQRGNMGNRG DRGYNRNQNN QGGNWGGQRR DNRNQRNRNQ RGHHKNQQQQ
     QQQQVQTIDE E