EIF3C_DROPE
ID EIF3C_DROPE Reviewed; 911 AA.
AC B4GIB1;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=GL16787;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479183; EDW36231.1; -; Genomic_DNA.
DR RefSeq; XP_002018392.1; XM_002018356.1.
DR AlphaFoldDB; B4GIB1; -.
DR SMR; B4GIB1; -.
DR STRING; 7234.FBpp0180894; -.
DR EnsemblMetazoa; FBtr0182402; FBpp0180894; FBgn0154391.
DR GeneID; 6592668; -.
DR KEGG; dpe:6592668; -.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_0_1; -.
DR OMA; VVMHRSE; -.
DR PhylomeDB; B4GIB1; -.
DR ChiTaRS; eIF3-S8; fly.
DR Proteomes; UP000008744; 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..911
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000365390"
FT DOMAIN 642..818
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..911
FT /note="Disordered"
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..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..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 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
SQ SEQUENCE 911 AA; 105911 MW; 93CD3BE66C4AEE9C CRC64;
MSRFFANGSD SESESSEEEV QAPNFNKASA FQFSDDEEEV KRVVRSTKEK RYENLTSIIK
TIRNHKKIKD IPNTLSSFED LTRAYTKALP VISKEENGIT PRFYIRCLAE LEDFINEIWE
DREGRRNLSK NNTKSLGTLR QKVRKYIKDF EEDLSRFREA PDQESEAEDE EAHVSDAGEA
ADDSYAGFKK EASVTAPKIA KSAPAKSVPA DDEDSDDSID WDSDSESETE SSEDENQYQN
MRERFLKRST EKGEDKGDDD KRKDKRKEQK LKIRKRAEDD EDGEWETVVK GHVVEKPKMF
EKDAEIDIPL VLAKLVEIMS ARGKKRTDRR LQIDLLFELR DISDQHNLGV PVSVKIHFNI
ISAIFDYNQK ISEPMKMEHW ALLLEVMQSM MKLLLANADI SISESVAEEH EEYITAPFYI
RGCPLAAVER LDDEFTKLLK ECDPHSNDYV SRLKDEMNVV KTIELVLQYF EQCGNPNERC
RIYLRKIEHL YYKFDPEVLK KKRGEVPATT ATSVDVMDKL CKFIYAKDDT DRIRTRAILA
HIYHHAMHDN WFQARDLVLM SHLQDNIDAA DPATRILYNR MMANLGLCAF RQENVKDAHH
CLVDLMVTGK PKELLAQGLL PQRQHERSAE QEKIEKQRQM PFHMHINLEL LECVYLVSAM
LLEIPYIAAH EFDARRRMIS KTFYQQLRSS ERQSLVGPPE SMREHVVAAA KAMRCGNWQA
CANFIVNKKM NTKVWDLFYE SDRVREMLVK FIKEESLRTY LFTYSNVYTS ISIPSLAQMY
ELPVPKVHSI ISKMIINEEL MASLDDPSET VVMHRSEPSR LQALAMQFVD KVTNLVDVNE
KVFDMKQGNF FQRGNMGNRG DRGYNRNQNN QGGNWGGQRR DNRNQRNRNQ RGHHKNQQQQ
QQQQVQTIDE E
