ID A0A3Q7EPB0_SOLLC Unreviewed; 917 AA.
AC A0A3Q7EPB0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc01g102585.1.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc01g102585.1.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc01g102585.1.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc01g102585.1.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc01g102585.1.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) to UniProtKB.
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 AlphaFoldDB; A0A3Q7EPB0; -.
DR STRING; 4081.A0A3Q7EPB0; -.
DR PaxDb; 4081-Solyc01g102600-2-1; -.
DR EnsemblPlants; Solyc01g102585.1.1; Solyc01g102585.1.1; Solyc01g102585.1.
DR Gramene; Solyc01g102585.1.1; Solyc01g102585.1.1; Solyc01g102585.1.
DR InParanoid; A0A3Q7EPB0; -.
DR OMA; FRCGLIK; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000004994; Chromosome 1.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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:UP000004994}.
FT DOMAIN 614..786
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..199
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 103535 MW; 76ED97D9B6D8D35B CRC64;
MASRFWTQGD SDTEEEEESD YEVEDDAPAE NPDAPSGPGA RYLAADDSDS DESDGQKRVV
RSAKDKRFEE LSATVDQMKN AMKINDWVSL QESFDKINKQ LEKVMRITES IKPPNLYIKA
LVMLEDFLNQ ALANKETRKK MSSSNAKALN SMKQKLKKNN KQYEELINKY RENPPVSEEE
GGDDEESEEE EEEDDFEEDP TKIAAASASD DDDDPDTIGD GWEKKVNKKD KLLDKQFKDP
SQITWEIVNK KFKEIVAARG RKGTGKMELV EQLTFLTKVA KTPAQKLEIL FGVVSAQFDI
NPGLSGHMPI NVWKRCVQNM LTILDVLTQY PNIVVDDMVE PDENETQKGA DHSGTIRIWG
NLVAFVERID VEFFKSLQVI DPHTSQYVER LRDEPLFLVL AQNVQRYLEQ VGDYKGAAKV
ALKQVEFIYY KPQGVYDAMR KLAELTEGGE AESVEENKVV EESRGPSAFI ATPELVPRKP
AFEENSRTLM DSLVSLIYKY GDERTKARAM LCDIYHHAIL DEFSTSRDLL LMSHLQENIQ
HMDISTQILF NRAMAQLGLC AFRMALVAEA HGCLAELYSA GRVKELLAQG VSQSRYHEKT
PEQERMERRR QMPYHMHINL ELLEAVHLTC AMLLEVPNMA ANSHDMKRRV ISKTFRRLLE
ISERQTFTGP PENVRDHVMA ATRSLRQGDF QKAFDVINSL DVWRLLRNKD SVLEMLRGKI
KEEALRTYLF TYSASYNSLS LDQVAGMFDL SVSQIHSIVS KMMISEELHA SWDQPSQCMV
FHDVEHTRLQ ALAFQLTEKL SVLAESNERA TESRIGGGAL EGLPPRRRDG QDYAAAAGGG
GRWQDFSFSQ GRQGSSGGRT GYAGSRSTSG QTSRDRTNQA RGTLGGQGSR YQSGTTSKGS
QMDGSGRMVN LNRGGRY
//
