EIF3C_DROGR
ID EIF3C_DROGR Reviewed; 928 AA.
AC B4J789;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=GH20077;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916367; EDW02107.1; -; Genomic_DNA.
DR RefSeq; XP_001987240.1; XM_001987204.1.
DR AlphaFoldDB; B4J789; -.
DR SMR; B4J789; -.
DR STRING; 7222.FBpp0153983; -.
DR PRIDE; B4J789; -.
DR EnsemblMetazoa; FBtr0155491; FBpp0153983; FBgn0127541.
DR GeneID; 6559214; -.
DR KEGG; dgr:6559214; -.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_0_1; -.
DR InParanoid; B4J789; -.
DR OMA; VVMHRSE; -.
DR OrthoDB; 273138at2759; -.
DR PhylomeDB; B4J789; -.
DR ChiTaRS; eIF3-S8; fly.
DR Proteomes; UP000001070; 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..928
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000365387"
FT DOMAIN 656..832
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..237
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..922
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 928 AA; 107695 MW; 2237CFCFBE7F7D05 CRC64;
MSRFFANGSD SESESSEEEV PTQFNNKAQN FQFSDDEEEV KRVVRSTKEK RYENLTSIIK
TIRNHKKIKD IPNTLSSFED LTRAYTKALP VISKEENGIT PRFYIRCLAE LEDFINEVWE
DREGRKNLSK NNSKSLGTLR QKVRKYIKDF EDDLARFREA PDQESDVDEG EGDVHDSDAD
RAGDDSDTGF GVGAKMAELP KAAKSSVQPT KIIADDDDSE DSIDWDPDTE SETESSEDEN
MYQNMRERFL KRTTEKEDKD DDKRKDKRKE QKHKVRKRAD DDEDGEGWET VVKGNVVEKP
KMFEKDAEID VPLVLAKLIE IMSARGKKRT DRRLQIDLLF ELRDISEQHS LGTAVAIKIH
FSIISAIFDY NLKISEPMKL EHWALLLEVM QSMMKLLLAN PDINMNESIA EEHEEYATAP
FYVRGCPLAA VERLDDEFTK LLKECDPHSN DYVSRLKDEV NVVKTIELVV QYFELSGSNN
ERCRIYLRKI EHLYYKFDPE VLKRKRGEQQ PATGAAGATP AAPVQSSVEV MDKLCKFIYA
KDDTDRIRTR AILAHIYHHA MHDNWFQARD LVLMSHLQDN IDAADPSTRI LYNRMMANLG
LCAFRQENIK DAHHCLVDLM VTGKPKELLA QGLLPQRQHE RSAEQEKIEK QRQMPFHMHI
NLELLECVYL VSAMLLEIPY IAAHEFDARR RMISKTFYQQ LRSSERQSLV GPPESMREHV
VAAAKAMRCG NWQACANFIV NKKMNTKVWD LFYESERVRE MLVKFIKEES LRTYLFTYSN
VYTSISIPSL SQMYELPLPK VHSIISKMII NEELMASLDD PSETVVMHRS EPSRLQALAM
QFVDKVTNLV DVNEKVFDMK QGNFFQRGNM GNRDRGYNRN QNNQGGNWGG QRRDNRSQRN
RNQRGHHKQN QQQNQQQQQQ QVHTIDEE
