ID   EIF3C_DROME             Reviewed;         910 AA.
AC   A1ZAX1; Q8MR49;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   04-NOV-2026, entry version 138.
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};
GN   ORFNames=CG4954 {ECO:0000312|FlyBase:FBgn0034258};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH PIX, AND ASSOCIATION WITH THE 40S RIBOSOME.
RX   PubMed=17392269; DOI=10.1074/jbc.m701361200;
RA   Andersen D.S., Leevers S.J.;
RT   "The essential Drosophila ATP-binding cassette domain protein, pixie, binds
RT   the 40 S ribosome in an ATP-dependent manner and is required for
RT   translation initiation.";
RL   J. Biol. Chem. 282:14752-14760(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA   Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy for
RT   (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT   Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-176 AND SER-185, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
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, ECO:0000269|PubMed:17392269}.
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; AE013599; AAF57818.1; -; Genomic_DNA.
DR   EMBL; AY122125; AAM52637.1; -; mRNA.
DR   EMBL; BT044242; ACH92307.1; -; mRNA.
DR   RefSeq; NP_001286545.1; NM_001299616.1.
DR   RefSeq; NP_611242.1; NM_137398.2.
DR   AlphaFoldDB; A1ZAX1; -.
DR   SMR; A1ZAX1; -.
DR   BioGRID; 62691; 31.
DR   FunCoup; A1ZAX1; 1999.
DR   IntAct; A1ZAX1; 23.
DR   STRING; 7227.FBpp0309235; -.
DR   GlyGen; A1ZAX1; 1 site.
DR   iPTMnet; A1ZAX1; -.
DR   PaxDb; 7227-FBpp0309235; -.
DR   PeptideAtlas; A1ZAX1; -.
DR   DNASU; 37005; -.
DR   EnsemblMetazoa; FBtr0086836; FBpp0086013; FBgn0034258.
DR   EnsemblMetazoa; FBtr0340269; FBpp0309235; FBgn0034258.
DR   GeneID; 37005; -.
DR   KEGG; dme:Dmel_CG4954; -.
DR   UCSC; CG4954-RA; d. melanogaster.
DR   AGR; FB:FBgn0034258; -.
DR   CTD; 8663; -.
DR   FlyBase; FBgn0034258; eIF3c.
DR   VEuPathDB; VectorBase:FBgn0034258; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_0_1; -.
DR   InParanoid; A1ZAX1; -.
DR   OMA; AACNWNQ; -.
DR   OrthoDB; 29647at2759; -.
DR   PhylomeDB; A1ZAX1; -.
DR   Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-DME-72649; Translation initiation complex formation.
DR   Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-DME-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR   SignaLink; A1ZAX1; -.
DR   BioGRID-ORCS; 37005; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 37005; -.
DR   PRO; PR:A1ZAX1; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0034258; Expressed in adult enteroendocrine precursor cell in adult midgut (Drosophila) and 247 other cell types or tissues.
DR   ExpressionAtlas; A1ZAX1; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:FlyBase.
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:FlyBase.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:FlyBase.
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   GO; GO:0006413; P:translational initiation; ISS:FlyBase.
DR   HAMAP; MF_03002; eIF3c; 1.
DR   InterPro; IPR027516; EIF3C.
DR   InterPro; IPR008905; EIF3C_N_dom.
DR   InterPro; IPR058999; EIF3CL_C.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13937; EUKARYOTIC TRANSLATION INITATION FACTOR 3, SUBUNIT 8 EIF3S8 -RELATED; 1.
DR   PANTHER; PTHR13937:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C-RELATED; 1.
DR   Pfam; PF05470; eIF-3c_N; 1.
DR   Pfam; PF26569; EIF3CL_C; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..910
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000365388"
FT   DOMAIN          639..815
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          847..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..20
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..186
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..207
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..235
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        862..874
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..891
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..910
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03002,
FT                   ECO:0000269|PubMed:17372656"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03002,
FT                   ECO:0000269|PubMed:18327897"
FT   MOD_RES         176
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03002,
FT                   ECO:0000269|PubMed:18327897"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03002,
FT                   ECO:0000269|PubMed:18327897"
FT   CONFLICT        293
FT                   /note="K -> N (in Ref. 3; AAM52637)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   910 AA;  105654 MW;  FC05D6478712684A CRC64;
     MSRFFANGSE SESESSEEEI QATNFNKASA FQFSDDEEEV KRVVRSTKEK RYENLTSIIK
     TIRNHKKIKD IPNTLSSFED LTRAYQKALP VISKEENGIT PRFYIRCLAE LEDFINEVWE
     DREGRKNLSK NNSKSLGTLR QKVRKYIKDF EDDLSRFREA PDQESEAEDE VVALESDGGD
     AGDDSDAGVK PTEAVPKAVK SAPAKAAPAD DDDSDDSIDW DSDSESETES SDDENQYQNM
     RERFLKRTTE KEEKDDDKRK DKRKEQKTKI RKRAEDDEDG EWETVVKGHV VEKPKMFEKD
     AEIDVPLVLA KLLEIMSARG KKRTDRRLQI DLLFELRDIS DQHNLGTAVS VKIHFNIISA
     IYDYNQKISE PMKLEHWALL LEVMQSMMKL LLANADIIMS ESVAEEHEEY ATSPFYVRGC
     PLAAVERLDD EFVKLLKECD PHSNDYVSRL KDEVNVVKTI ELVLQYFERS GTNNERCRIY
     LRKIEHLYYK FDPEVLKKKR GELPATTSTS VDVMDKLCKF IYAKDDTDRI RTRAILAHIY
     HHAMHDNWFQ ARDLVLMSHL QDNIDAADPA TRILYNRMMA NLGLCAFRQG NVKDAHHCLV
     DLMVTGKPKE LLAQGLLPQR QHERSAEQEK IEKQRQMPFH MHINLELLEC VYLVSAMLLE
     IPYIAAHEFD ARRRMISKTF YQQLRSSERQ SLVGPPESMR EHVVAAAKAM RCGNWQACAN
     FIVNKKMNTK VWDLFYESDR VREMLTKFIK EESLRTYLFT YSNVYTSISI PSLAQMYELP
     VPKVHSIISK MIINEELMAS LDDPSETVGM HRSEPSRLQA LAMQFVDKVT NLVDVNEKVF
     DMKQGNFFQR GNMGNRGDRG YNRNQNNQGG NWLGQRRDRN NRNRNQRGHH KNNQDRQQQQ
     QQQVQTIDEE
//