ID A0A0B0PE64_GOSAR Unreviewed; 918 AA.
AC A0A0B0PE64;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 45.
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};
DE AltName: Full=eIF3 p110 {ECO:0000256|HAMAP-Rule:MF_03002};
GN ORFNames=F383_03032 {ECO:0000313|EMBL:KHG23222.1};
OS Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG23222.1, ECO:0000313|Proteomes:UP000032142};
RN [1] {ECO:0000313|Proteomes:UP000032142}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA Wilkins T.A.;
RL Submitted (SEP-2014) 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; KN424214; KHG23222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0PE64; -.
DR Proteomes; UP000032142; 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:UP000032142}.
FT DOMAIN 616..788
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..221
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 103723 MW; 269077CFBDBF2DC1 CRC64;
MASKFWTQGG SDTEEEETDI EDEIENGGAG ETTAAAAGSR YLQTNASDSD DSDGQKRVVR
SAKDKRFEEM ASTVDQMKNA MKINDWVSLQ ESFDKINKQL EKVMRVTESD RVPNLYIKCL
VMLEDFLAEA LANKEAKKKM SSSNHKALNA MKQKLKKNNK QYEELINKYR ENPESEKEKF
EDEDEDEDED ESGSELEDPS QIAAESSDED DEGEDMDDDD ADGAWEKKLS KKEKLMDREF
KKDPSEITWD TVNKKFKEVV AARGRKGTGK FEQVEQLTFL TKVAKTPAQK LEILFSVISA
QFDVNPGLSG HMPINVWKKC VQNMLVILDI LVQYPNIVVD DMVEPDENET QKGADYDGTI
RVWGNLVAFL ERIDNEFFKS LQCIDPHTRE YVERLRDEPL FLVLAQNVQE YLERIGDLKS
AAKVALRRVE LVYYKPQEVY DAMRKLAELS EDGETDGDET KVEETRGTSA FVVTPELVSR
KPTFPENSRA LMDILVTLIY KSGDERTKAR AMLCDIYHHA LFDEFSIARD LLLMSHLQDN
IQHMDVSTQI LFNRAMAQVG LCAFRVGLIA EGHGCLSELY SGGRAKELLA QGVSQSRYHE
KTPEQERLER RRQMPYHMHI NLELLEAVHL ICAMLLEVPN MAANSLDAKR KVISKTFSRL
LEVSERQPFT GPPENVRDHV MAATRALCKG DFQKAFDIIN SLDVWKLLRN RESVLEMLKA
KIKEEALRTY LFTYCSSYDT LGLDQLTRMF DLSDAQIHSI VSKMLVNEEL HASWDQPTRC
IIFHDVEYSR LQALAFQLTE KLSILAESNE RAVEARFGGG GLDLPLRRRD NQEYASGTAG
GSGSRWPDLS YNQGRQGSSG RAAYTGGGRP LALGRASRDR SGQLRGTGGY SGRAGSGIRG
SQMDASARMV SLNRGVRG
//
