ID A0A067KLP9_JATCU Unreviewed; 927 AA.
AC A0A067KLP9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=JCGZ_09905 {ECO:0000313|EMBL:KDP35933.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP35933.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP35933.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP35933.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
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; KK914463; KDP35933.1; -; Genomic_DNA.
DR RefSeq; XP_012074557.1; XM_012219167.1.
DR AlphaFoldDB; A0A067KLP9; -.
DR STRING; 180498.A0A067KLP9; -.
DR GeneID; 105636005; -.
DR KEGG; jcu:105636005; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000027138; 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:UP000027138}.
FT DOMAIN 615..787
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 137..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Polar 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 137..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..217
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 104731 MW; 3A057FE9AB18F656 CRC64;
MASRFWGQGG SDSEEEESDY EEEVDNEAGD STTQAPQNRY LRGTASDSDD SDDQKRVVRS
AKDKRFEEMS ATVDQMKNAM KINDWVSLQE SFDKINKQLE KVMRVTESDK VPSLYIKALV
MLEDFLNQAL ANKEAKKKMS SSNAKALNSM KQKLKKNNKQ YEDLINKFRE NPESEEEQEA
DEETEEEEDS DLEFVEDPSK IAVSDEDEED EEDRQDGRTE VEGDWQKMLS RKEKLMDRQF
MKDPSEITWD TVNKKFKEVV AARGRKGTGR FEQVEQLTFL TKVAKTPAQK LEILFSVVSA
QFDVNPGLSG HMPINVWKKC VHNMLIILDI LVQYPNIVVD DMVEPDENET QKGADFDGTI
RVWGNLVAFL EKIDSEFFKS LQCIDPHTRD FVERLQDEPM FLVLAQDVQE YLERAGDFKA
ASKVALRRVE LIYYKPQEVY DAMRKLAEQT DDGDGVKSGE VEESRGPSAF VVTPELVPRK
PTFPESSRTM MDMLVSLIYK CGDERTKARA MLCDIYHHAL LDEFSTSRDL LLMSHLQDSI
QHMDISTQIL FNRAMAQLGL CAFRVGLITE GHGCLSELYS GGRVKELLAQ GVSQSRYHEK
TPEQERLERR RQMPYHMHIN LELLEAVHLI CAMLLEVPHM AANTHDAKRK VISKTFRRLL
EVSERQTFIG PPENVRDHVM AATRALTKGD FQKAFDVIKS LDVWRLLKSK DSVLEMLKAK
IKEEALRTYL FTYSSSYESL SLDQLTKMFD LSGTQTHSVV SKMMINEELH ASWDQPTQCI
IFHDVAHSRL QLLAFQLTEK LSVLAESNER AIEARVGGGG GLDLPVRRKE GQDYASMAAA
GGKWQDSYTP GRQGSGRSGY NVGGGRPPAL GQATGGGYSR GQSRTGGYSG GSRYLDGAYG
GSGRTSARGS QLDGSNQMVS LNRGVRA
//
