EIF3C_DROWI
ID EIF3C_DROWI Reviewed; 919 AA.
AC B4MRZ8;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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}; ORFNames=GK15661;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(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. The eIF-3 complex interacts with pix.
CC {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; CH963850; EDW74887.1; -; Genomic_DNA.
DR RefSeq; XP_002063901.1; XM_002063865.2.
DR AlphaFoldDB; B4MRZ8; -.
DR SMR; B4MRZ8; -.
DR STRING; 7260.FBpp0244804; -.
DR EnsemblMetazoa; FBtr0246312; FBpp0244804; FBgn0217666.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_0_1; -.
DR InParanoid; B4MRZ8; -.
DR OMA; VVMHRSE; -.
DR OrthoDB; 273138at2759; -.
DR PhylomeDB; B4MRZ8; -.
DR ChiTaRS; eIF3-S8; fly.
DR Proteomes; UP000007798; 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 InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13937; PTHR13937; 1.
DR Pfam; PF05470; eIF-3c_N; 1.
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; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..919
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000365394"
FT DOMAIN 640..816
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
SQ SEQUENCE 919 AA; 107326 MW; 4AA3A982AA794195 CRC64;
MSRFFANGSD SESESSEEEV QAPNFNKATA FQFSDDEEEV KRVVRSTKEK RYENLTAIIK
SIRNHKKIRD ISNTLTSFED LTKAYQKALP VISKEENGIT PRFYIRCLAE LEDFINEVWE
DRDGRKNLSK NNAKSLGTLR QKVRKYIKDF EDDLSRFREN PQEESENEDE EAAAHDSDGG
LDAGSDIEKR EPTVAATKLA KSVPSKLPVA DDEDSDESID WDPDTESETE SSEDENQYQN
MRERFLKRST EKDDKDDDKR KDKRKEQKIK LRKRAEDEDG EGWETVVKGH VVEKPKMFEK
DAEIDIPLVL AKLLEIMSAR GKKRTDRRLQ IDLLFELRDI SDQHELGVPI SVKIHFNIIS
AIFDYNQKIS EPMKLEHWAL LLEVMQSMMK LLLANPDIQL SESVAEEHEE YNATPYLIRG
CPLAAVERLD DEFTKLLKEC DPHSNDYVSR LKDEINVVKT IELVLQYFEV NGSNNERCRI
YLRKVEHLYY KFDPEVFKKK RGDIPNTTQT SVDIMDRLCK FIYAKDDTDR IRTRAILTHI
YHHAMHDNWF QARDLILMSH LQDNIDAADP STRILYNRMM ANLGLCAFRQ ENVKDAHHCL
VDLMVTGKAK ELLAQGLLPQ RQHERSAEQE KIEKQRQMPF HMHINLELLE CVYLVSAMLL
EIPYIAAHEF DARRRMISKT FYQQLRSSER QSLVGPPESM REHVVAAAKA MRCGNWQACA
NFIVNKKMNT KVWDLFYESD RVRDMLVKFI KEESLRTYLF TYSNVYTSIS IPSLAEMYEL
PVQKVHSIIS KMIINEELMA SLDDPSETVV MHRSEPSRLQ ALAMQFVDKV TNLVDVNEKV
FDMKQGNFFQ RGNMGNRGDR GYNRNQNNQG GNWGGQRRDN RNQRNRNQRG HHKNQQNQNQ
QQQQQHQREQ QQVQTIDEE
