ID   EIF3C_VANPO             Reviewed;         809 AA.
AC   A7TML4;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, 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 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}; ORFNames=Kpol_513p28;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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. {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; DS480423; EDO16512.1; -; Genomic_DNA.
DR   RefSeq; XP_001644370.1; XM_001644320.1.
DR   AlphaFoldDB; A7TML4; -.
DR   SMR; A7TML4; -.
DR   STRING; 436907.A7TML4; -.
DR   EnsemblFungi; EDO16512; EDO16512; Kpol_513p28.
DR   GeneID; 5544645; -.
DR   KEGG; vpo:Kpol_513p28; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_2_1; -.
DR   InParanoid; A7TML4; -.
DR   OMA; VVMHRSE; -.
DR   OrthoDB; 273138at2759; -.
DR   PhylomeDB; A7TML4; -.
DR   Proteomes; UP000000267; 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   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..809
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000364290"
FT   DOMAIN          605..780
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..57
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  91518 MW;  90E9A065A7EB068A CRC64;
     MSRFFAASYE YDSASSSSEE DLLSSSEEEL LSSSSLSEEE SDDSFFNDSE SESDFDSDDS
     DAKPYGPDWF KKQEFRRGGG GGNKFLKGAS YSDSDESDEA SKKVVKSAKE KLLDEMQTSS
     GKIDAAELTN DWITILNEFD SVTRLLTRAQ QQNFGTPNIF VKVVAQVEDA VAASQEEINN
     KAVAKAFNTA KQRVKKISRE HQTLLAKYRE DPESFEKETS VEVDATPELA QFAVGKKTTD
     LSSIATTSSE TGFFPALSIV LDSRGKKNID QQALAQSMDD LLQTTKTPYE KIIAYLTLIP
     IRLDSSTNLS YQPIDQWKAT YNDVSSLLSI LDENINTYQV SELAPFNDSL ENEPEANEKG
     VKTILGSILS FVDRLDDEFT KSLLNTDPHS SDYLIRLRDE QAIYNLILRT QLYLEATLPE
     DRQIDLLSRI FVRRLNHIYY KSNELIRIME VAAWKVAPSS YTSKLTPYDG AVSDSYLSGV
     ISTLTDALSK QQNQSLRKRA VLYNVYYTAL NKEFQVAKDM LIESKVQSFI NKSDPSLQIL
     FNRVVVQLGL SAFKLCLIEE CHQILNDLLA SSHLREILGQ QTLQRVTAHS NSSNADEREK
     LCLPFHEHIN LDLIDVVFMT CSLLIEIPQM TAFYSGIKIK KIPYSQKSIR RALEHYEKSS
     FQGPPETLRD YILHSAKEMQ KGNWKKSFEL LKSIQAWALL PNSASVLDNL AERLQVESLK
     TYFFTNKRFY SKLSMKKLSD LFNLPEDKIV ESLQAVITEY EIDASFNEDK SVLSIAKGAE
     ITKLEEVASK LNKEVKITKE RLHPSRGRR