ID   EIF3C_CANGA             Reviewed;         810 AA.
AC   Q6FIJ6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=CAGL0M13893g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380959; CAG62928.1; -; Genomic_DNA.
DR   RefSeq; XP_449948.1; XM_449948.1.
DR   AlphaFoldDB; Q6FIJ6; -.
DR   SMR; Q6FIJ6; -.
DR   STRING; 5478.XP_449948.1; -.
DR   EnsemblFungi; CAG62928; CAG62928; CAGL0M13893g.
DR   GeneID; 2891610; -.
DR   KEGG; cgr:CAGL0M13893g; -.
DR   CGD; CAL0137483; CAGL0M13893g.
DR   VEuPathDB; FungiDB:CAGL0M13893g; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_2_1; -.
DR   InParanoid; Q6FIJ6; -.
DR   OMA; VVMHRSE; -.
DR   Proteomes; UP000002428; Chromosome M.
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: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   HAMAP; MF_03002; eIF3c; 1.
DR   InterPro; IPR027516; EIF3C.
DR   InterPro; IPR008905; EIF3C_N_dom.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR13937; PTHR13937; 1.
DR   Pfam; PF05470; eIF-3c_N; 2.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..810
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000364279"
FT   DOMAIN          605..780
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..56
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   810 AA;  92915 MW;  6F84E9CFBF1C2F03 CRC64;
     MSRFFATNYN YDETSSSSEE DLLSSSEELL SSSEEGELSD DSLFNDESES ESDFDSDDSD
     AKPYGPDWFK KPEFRKGGNK FLKGASYSDS DESDEEDGKK VVKSAREKLL DEMQAVYDKI
     ETAEMSDDWM TILNEFDSIT RLLVRAQQQN FGIPKIFVKV VAQVEDLVSN SEQTEIKNKA
     VSKAFNTTKQ RVKKIARENE ALLAKFREDP QSFDKEDTVE PELPPLNEEN KVFTGKGVNL
     SSLASASSEF SFMASLQIVN DSRGKKNSNQ AELIKTLEEL LNIAKTPYER ILAYLTLIPT
     RLEESTNLSY QPIDQWKSTH DDLNKLFDIL DENISSYQVT ELAARNDDLE TEPEPNANGI
     REILGSLLSF TERLDDEFKK SLLNIDPHSS DYLERLRDEQ NMYNLLLRTQ LYMEATIPEE
     RQEQLLARAF VRRLDHIYYK SNKLISIIEN SAWKAVPSSY KSKYIPFSGN ADEEYCSQLV
     EGLSKSLANQ DNVFLQKRAT LSHIYYTALN GEFEVAKELL LKTKVQSNIN KSDPSLQILF
     NRVVVQLGLS AFKLCKIEEC HQILNELLAS SHLREILGQQ SLQRIASNSS SSSSSEDREK
     QCLPYHQHIN LDLVDLVFMT SSLLIEIPQM TAYLTGIKTK KVPVYQKSVR RLVESFDKSF
     FHGPPESIKE HVLYAAKSMQ KGDWKGCLEY LKSVKTWNLL PNSVEVLDNL TERIQIETMK
     TYVFTYRRFY EKISIKKFSE LFSLPEDKIV TTMEKVIADL ELNIKLDDNK TYIVIEKGDE
     VSKLEEVAVK LNKEIRATRE RLNPSHHNHR