ID A0A0R3W1I5_TAEAS Unreviewed; 871 AA.
AC A0A0R3W1I5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000256|HAMAP-Rule:MF_03002};
DE Short=eIF3c {ECO:0000256|HAMAP-Rule:MF_03002};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 8 {ECO:0000256|HAMAP-Rule:MF_03002};
GN ORFNames=TASK_LOCUS3599 {ECO:0000313|EMBL:VDK32063.1};
OS Taenia asiatica (Asian tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000359801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TASK_0000359801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK32063.1, ECO:0000313|Proteomes:UP000282613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_03002}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000256|HAMAP-
CC Rule:MF_03002}.
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DR EMBL; UYRS01018305; VDK32063.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3W1I5; -.
DR STRING; 60517.A0A0R3W1I5; -.
DR WBParaSite; TASK_0000359801-mRNA-1; TASK_0000359801-mRNA-1; TASK_0000359801.
DR Proteomes; UP000046400; Unplaced.
DR Proteomes; UP000282613; 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; EUKARYOTIC TRANSLATION INITATION FACTOR 3, SUBUNIT 8 EIF3S8 -RELATED; 1.
DR PANTHER; PTHR13937:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C-RELATED; 1.
DR Pfam; PF05470; eIF-3c_N; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03002};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03002};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03002}; Reference proteome {ECO:0000313|Proteomes:UP000282613}.
FT DOMAIN 646..822
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..178
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..212
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 100532 MW; ABB2E55E53B79AC2 CRC64;
MAMTSRLYTA AYSSSDDESS DEISGKAPVK RFMRPVQSDS EDEKRVVRSA KDKRHEEIQN
ILRNLNNHKK IKDMSKVETD FDELVKVYEK AHKMNEVDVY PKFYIRVLAQ LEDFVNESWS
QKKALSKVGA KSLTVLKQKI RKYNKDFEEQ IKKYRENPEL YEEEAEEEIE EGEESAEEEE
VITKPVVASV SKGSDESSDE DDEDDDDYFR TSDESESSDS GPEIDMEHPY TYFLKVEGKP
KKEETKKKAP KPKPVKQVVK PSSEESGDEW RVVAPGDGSA LEPTVQAFEK GVEITQELVF
KKVTEIIANR GKRTSSIAEQ ICLLDQVCQK AGEFPLYASV RIIHHIHQEL HLGVGINVKA
ILSLITVLFD YESRHPAFMP VAKFQRTIEQ LKKLFEILKN NPKDLEISES ITEETESVLE
RPYRIRGSIL GCVGRLDDEY FKILQNANGH EMEYDERLRD EPRVCELIDL LIEYLERIKA
PPEALCVAYL RKVEHLYYKF DFEWGKKVES EGLEAAGLNP YYEVVERLCH YIYKNDKTDR
LRTRAILCHI YFLALFDHWY KARDLMLMSN LQATIDHADH STMILYNRAM VQMGLCAFRQ
GHIKDAHSAL SDLTGSSKIR ELLAQGQRYE RTPEEEKREK ALQMPYHMHI NTELIETVFL
ICAMLQEVPI LAASQDDTRA RVFSKAFSTV LRIQDRATLI GPPESPRDHV IAASKAMRFG
NWHNATKYIF SPKMDAKIWV LFYDPSSVKK MLEEKIKEEC LRCYLFTYSS VHESVSLSRL
AEHFEFPRSQ IYSIISKMII NQELAASLEV PADFLTMHKG ERSRLQNLAI QLADKVNSIM
EMNEKLIDNR GGMISGPKGN YFILQSILIT F
//
