ID A0A0D2QA22_GOSRA Unreviewed; 918 AA.
AC A0A0D2QA22;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=B456_006G145700 {ECO:0000313|EMBL:KJB36178.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB36178.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB36178.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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; CM001745; KJB36178.1; -; Genomic_DNA.
DR RefSeq; XP_012485668.1; XM_012630214.1.
DR AlphaFoldDB; A0A0D2QA22; -.
DR STRING; 29730.A0A0D2QA22; -.
DR EnsemblPlants; KJB36178; KJB36178; B456_006G145700.
DR GeneID; 105799579; -.
DR Gramene; KJB36178; KJB36178; B456_006G145700.
DR KEGG; gra:105799579; -.
DR eggNOG; KOG1076; Eukaryota.
DR OMA; GMITEAH; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000032304; Chromosome 6.
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:UP000032304}.
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..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..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 176..220
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 103774 MW; D7508F550E2F6465 CRC64;
MASKFWTQGG SDTEEEETDI EDEIENGGAG ETTAAAAGSR YLQTNASDSD DSDGQKRVVR
SAKDKRFEEM ASTVDQMKNA MKINDWVSLQ ESFDKINKQL EKVMRVTESD RVPNLYIKCL
VMLEDFLAEA LANKEAKKKM SSSNHKALNA MKQKLKKNNK QYEELINKYR ENPESEEEKF
EDEDEDEDED ESGSELEDPS QIAAESSDED DEGEDVDDDD ANGAWEKKLS KKEKLMDREF
KKDPSEITWD TVNKKFKEVV AARGRKGTGK FEQVEQLTFL TKVAKTPAQK LEIFFSVISA
QFDVNPGLSG HMPINVWKKC VQNMLVILDI LVQYPNIVVD DMVEPDENET QKGADYDGTI
RVWGNLVAFL ERIDNEFFKS LQCIDPHTRE YVERLRDEPL FLVLAQNVQE YLERIGDLKS
AAKVALRRVE LVYYKPQEVY DAMRQLAVLS EDGEKDGDET KVEETRGTSA FVVTPELVSR
KLTFPENSRA LMDILVTLIY KSGDERTKAR AMLCDIYHHA LFDEFSIARD LLLMSHLQDT
IQHMDVSTQI LFNRAMAQVG LCAFRVGLIA EGHGCLSELY SGGRVKELLA QGVSQSRYHE
KTPEQERLER RRQMPYHMHI NLELLEAVHL ICAMLLEVPN MAANSLDAKR KVISKTFRRL
LEVSERQPFT GPPENVRDHV MAATRALCKG DFQKAFDVIN SLDVWKLLRN RESVLEMLKA
KIKEEALRTY LFTYCSSYDT LGLDQLTKMF DLSDAQIHSI VSKMLVNEEL HASWDQPTRC
IIFHDVEYSR LQALAFQLTE KLSILAESNE RAVEARFGGG GLDLPLRRRD NQEYAAGTAG
GGGGRWPDLS YNQGRQGSSG RAAYTGGGRP LALGQASRDR SSQSRGTGGY SGRAGSGMRG
YQMDASARMV SLNRGVRG
//
