EIF3C_DROVI
ID EIF3C_DROVI Reviewed; 913 AA.
AC B4LNA1;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=GJ21821;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
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; CH940648; EDW61053.1; -; Genomic_DNA.
DR RefSeq; XP_002049860.1; XM_002049824.2.
DR AlphaFoldDB; B4LNA1; -.
DR SMR; B4LNA1; -.
DR STRING; 7244.FBpp0236238; -.
DR PRIDE; B4LNA1; -.
DR EnsemblMetazoa; FBtr0237746; FBpp0236238; FBgn0208939.
DR GeneID; 6625912; -.
DR KEGG; dvi:6625912; -.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_0_1; -.
DR InParanoid; B4LNA1; -.
DR OMA; VVMHRSE; -.
DR OrthoDB; 273138at2759; -.
DR PhylomeDB; B4LNA1; -.
DR ChiTaRS; eIF3-S8; fly.
DR Proteomes; UP000008792; 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..913
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000365393"
FT DOMAIN 645..821
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..236
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..913
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"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
SQ SEQUENCE 913 AA; 106058 MW; 2BF7962023A375E8 CRC64;
MSRFFANGSD SESESSEEEV QASNFNKANN FQFSDDEEEV KRVVRSTKEK RYENLTGIIK
TIRNHKKIKD IPNTLSSFED LTRAYTKALP VISKEENGIT PRFYIRCLAE LEDFINEVWE
DREGRKNLSK NNSKSLGTLR QKVRKYIKDF EEDLARFREA PDQESDVDEG EGEAHDSDAE
RAGADSDGGI GAGTGKLAEL PKAAKLVPTK VAADEDDSDD SIDWDSDTES ETESSEDENL
YQNMRERFLK RTTEKEDKDD DKRKDKRKEQ KHKVRKRADD DEDGEWETVV KGNVVEKPKM
FEKDAEIDIP LVLAKLVEIM SARGKKRTDR RLQIDLLFEL RDISEQHELG TPISVKIHFN
IISAIFDYNQ KISEPMKLEH WALLLEVMQS MLKLLLANPE INMNESVAEE HEEYGAAPYF
IRGCPLAAVE RLDDEFTKLL KECDPHSNDY VSRLKDEINV VKTIELVVQY FERCGSNNER
CRIYLRKIEH LYYKFDPEVL KRKRGELPAA GTAPSSVEVM DKLCKFIYAK DDTDRIRTRA
ILAHIYHHAM HDNWFQARDL VLMSHLQDNI DAADPSTRIL YNRMMANLGL CAFRQENIKD
AHHCLVDLMV TGKPKELLAQ GLLPQRQHER SAEQEKIEKQ RQMPFHMHIN LELLECVYLV
SAMLLEIPYI AAHEFDARRR MISKTFYQQL RSSERQSLVG PPESMREHVV AAAKAMRCGN
WQACANFIVN KKMNTKVWDL FYESERVREM LVKFIKEESL RTYLFTYSNV YTSISIPSLA
QMYELPLPKV HSIISKMIIN EELMASLDDP SETVVMHRSE PSRLQALAMQ FVDKVTNLVD
VNEKVFDMKQ GNFFQRGNMG NRDRGYNRNQ NNQGGNWGGQ RRDNRNQRNR NQRGHHKQQQ
QQQQQQVQTI EEE
