ID   EIF3C_KLULA             Reviewed;         819 AA.
AC   Q6CLH3;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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 93 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03002};
DE            Short=eIF3 p93 {ECO:0000255|HAMAP-Rule:MF_03002};
DE   AltName: Full=Translation initiation factor eIF3, p93 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03002};
GN   Name=NIP1 {ECO:0000255|HAMAP-Rule:MF_03002};
GN   OrderedLocusNames=KLLA0F03014g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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. {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; CR382126; CAG97924.1; -; Genomic_DNA.
DR   RefSeq; XP_455216.1; XM_455216.1.
DR   AlphaFoldDB; Q6CLH3; -.
DR   SMR; Q6CLH3; -.
DR   STRING; 28985.XP_455216.1; -.
DR   EnsemblFungi; CAG97924; CAG97924; KLLA0_F03014g.
DR   GeneID; 2895780; -.
DR   KEGG; kla:KLLA0_F03014g; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_2_1; -.
DR   InParanoid; Q6CLH3; -.
DR   OMA; VVMHRSE; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:EnsemblFungi.
DR   GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:EnsemblFungi.
DR   GO; GO:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:UniProt.
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:EnsemblFungi.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProt.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_03002; eIF3c; 1.
DR   InterPro; IPR027516; EIF3C.
DR   InterPro; IPR008905; EIF3C_N_dom.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13937; PTHR13937; 1.
DR   Pfam; PF05470; eIF-3c_N; 2.
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; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..819
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000364284"
FT   DOMAIN          620..795
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..57
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   819 AA;  94187 MW;  6150B1790B7FAC64 CRC64;
     MSRFFLKTYE YDSTSSGEEE DLLSQSEEDL VSSSSEEELS DDSFFNDSDE SSDNDEDNDS
     DSKPYGPDWF KKPEFRKGGG SGANKFLKST NYSSDEDSSD EEDGKKVVKS AKEKLLDEMK
     SIYQKIDSAE AQQDWESLLN HLETILKLYT KAQQQNYGTP NIFVKSLARF EDAVSATSQD
     EIKNKAVARA YNTTKQRVKK LIRENETSVK AYRENPEDFD KEPVLDADID SRDVSATPFS
     LSGKKNLDLA SVANNISELD FFKTLNIIID SRGKKNTDHT EQIKTTEELL KIAKTPYEKI
     CTYLNLIPIR FDASVSLSYQ PLEQWKASKD NLDGLLEVLE QEIDHYQVTE FAPRNDFIED
     EPEANEHGVK EILGSIFSMV ERLDDEFSKS LLNIDTRSSE YMERLRDEQS IYNLIIRSQL
     YFERVTAEEH RDRLLARVFN RRLEHIYYKS DKLISIMETV AWKQIREGTA SLESSFVRLN
     ESDSADADYN FKVISELSDF LIKQKSNNVF NYRKGTLYKT YYIALNQEYA PAKKIMLSSD
     IAKFISGSDA ALQILYNRCV IQLGLAAFKA GLINECHQVL NGLCINPHLR EILGQQSLQR
     ANANSNVVQG APVEQLCLPF HQHINLDLID TVYMTCSLLL DVPHMAAYYS GIKVKRIPVF
     QKSIRRILES SEKAIFHGPP ETLRDHILYA AKSMQKGDYL QSIEYLRKIS VWSLLSKSDD
     IINQLSEKVQ IETLKTYIFT YKRFYSKISI SKLSKLFDLD IEKVLAVAQN IINDYEVKAK
     LDENNEYIIF ERGEEITKLE EVAIKLVKET KYHSERLRQ