EIF3C_LODEL
ID EIF3C_LODEL Reviewed; 790 AA.
AC A5E3Q2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=LELG_04240;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981529; EDK46060.1; -; Genomic_DNA.
DR RefSeq; XP_001524269.1; XM_001524219.1.
DR AlphaFoldDB; A5E3Q2; -.
DR SMR; A5E3Q2; -.
DR STRING; 379508.A5E3Q2; -.
DR EnsemblFungi; EDK46060; EDK46060; LELG_04240.
DR GeneID; 5231599; -.
DR KEGG; lel:LELG_04240; -.
DR VEuPathDB; FungiDB:LELG_04240; -.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_2_1; -.
DR InParanoid; A5E3Q2; -.
DR OMA; VVMHRSE; -.
DR OrthoDB; 273138at2759; -.
DR Proteomes; UP000001996; 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; 2.
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..790
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000366882"
FT DOMAIN 556..728
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 90330 MW; B31C9EFEFC36E24B CRC64;
MSRFFVSGYN SESSSEEEDL LSSEEELLTS SGEENEDSDF FNDDDESSSD EEDGRPSGPA
YFLKKSFLKG AGGDSDSDSD DEGRKVVKSA KEKLLDDMKA SIEVINVNKR TNNWIVVLSE
FEKLGKLINR ANQQNFGTPK FYVKLLASLD DSITETVNNE KDDKTMKADE ARAFNTLRQR
VKKQIKEFQV YFDLYKDVPE NFDQEDESLD SFAKNQETRE ETRTLSPIFH NLKLINESRG
KKNIDKSEQV TTLEGLISDE ASDFELISLY QSLLSVRFDA SSNQSFMAIQ DWRSNKRDLN
NLLDILVKSK VYQLSEEGQT TDDIDIEPTA NEDGVKVIYG SVTSLIDRLD DEFTKSLQNT
DPHSMEYVER LKDETEIYNL IVRGQAYIES IVADKQQSNQ LARVVLRRLE HIYYKPNQLI
KANEEEAWKN IKPSTQTPSE VIESLTQFLQ SNKVFAKQAL LYSIYYYAVN GDYNKAKELF
LSAHFNLSDS ALQVSYNRAL VQLGLSAFRS GAIEESHKIL NEMVNSQRSK ELLGQGFNSK
FPNQATVVEK QRLLPFHQHI NLELLECVYM TCSLLIEIPA LASNKDPKRR NASLKSFKSK
LEFHDRQYFT GPPESIKDHI VHASIALQKG DWSKAYNLLS SIKIWHLFPD HDNLLAMMKN
QLQIEGLRTY IFTYKAVYSK LSISKLSSIF GLLQENVSEV LTQMIEKLDI NGEVSGDYIV
FTTDSQRSKL QELAIVMNDK IQLLTEKNEK TSSNGYAKKN QSQTQPQAQS KEVEENKFRY
ANVNTNTDEF
