EIF3C_DROSE
ID EIF3C_DROSE Reviewed; 910 AA.
AC B4HMY3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=GM21808;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25;
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; CH480816; EDW48333.1; -; Genomic_DNA.
DR RefSeq; XP_002034320.1; XM_002034284.1.
DR AlphaFoldDB; B4HMY3; -.
DR SMR; B4HMY3; -.
DR STRING; 7238.B4HMY3; -.
DR EnsemblMetazoa; FBtr0204793; FBpp0203285; FBgn0176685.
DR GeneID; 6609646; -.
DR KEGG; dse:6609646; -.
DR HOGENOM; CLU_004304_0_0_1; -.
DR OMA; VVMHRSE; -.
DR PhylomeDB; B4HMY3; -.
DR ChiTaRS; eIF3-S8; fly.
DR Proteomes; UP000001292; 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..910
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000365392"
FT DOMAIN 639..815
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..232
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..910
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 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03002"
SQ SEQUENCE 910 AA; 105626 MW; 69BAA2F3FCA9FD54 CRC64;
MSRFFANGSE SESESSEEEI QATNFNKASA FQFSDDEEEV KRVVRSTKEK RYENLTSIIK
TIRNHKKIKD IPNTLSSFED LTRAYQKALP VISKEENGIT PRFYIRCLAE LEDFINEVWE
DREGRKNLSK NNSKSLGTLR QKVRKYIKDF EDDLSRFREA PDQESEAEDE VVALESDGGD
AGDDSDAGVK PTEAAPKAVK SAPAKAAPAD DDDSDDSIDW DSDSESETES SDDENQYQNM
RERFLKRTTE KEEKDDDKRK DKRKEQKTKI RKRAEDDEDG EWETVVKGHV VEKPKMFEKD
AEIDVPLVLA KLLEIMSARG KKRTDRRLQI DLLFELRDIS DQHNLGTAVS VKIHFNIISA
IYDYNQKISE PMKLEHWALL LEVMQSMMKL LLANADIIMS ESVAEEHEEY ATSPFYVRGC
PLAAVERLDD EFVKLLKECD PHSNDYVSRL KDEVNVVKTI ELVLQYFERS GTNNERCRIY
LRKIEHLYYK FDPEVLKKKR GELPATTSTS VDVMDKLCKF IYAKDDTDRI RTRAILAHIY
HHAMHDNWFQ ARDLVLMSHL QDNIDAADPA TRILYNRMMA NLGLCAFRQG NVKDAHHCLV
DLMVTGKPKE LLAQGLLPQR QHERSAEQEK IEKQRQMPFH MHINLELLEC VYLVSAMLLE
IPYIAAHEFD ARRRMISKTF YQQLRSSERQ SLVGPPESMR EHVVAAAKAM RCGNWQACAN
FIVNKKMNTK VWDLFYESDR VREMLTKFIK EESLRTYLFT YSNVYTSISI PSLAQMYELP
VPKVHSIISK MIINEELMAS LDDPSETVGM HRSEPSRLQA LAMQFVDKVT NLVDVNEKVF
DMKQGNFFQR GNMGNRGDRG YNRNQNNQGG NWLGQRRDRN NRNRNQRGHH KNNQDRQQQQ
QQQVQTIDEE
