ID C1MVZ0_MICPC Unreviewed; 996 AA.
AC C1MVZ0;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=MICPUCDRAFT_59561 {ECO:0000313|EMBL:EEH55787.1};
OS Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876};
RN [1] {ECO:0000313|EMBL:EEH55787.1, ECO:0000313|Proteomes:UP000001876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH55787.1,
RC ECO:0000313|Proteomes:UP000001876};
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG663741; EEH55787.1; -; Genomic_DNA.
DR RefSeq; XP_003059835.1; XM_003059789.1.
DR AlphaFoldDB; C1MVZ0; -.
DR STRING; 564608.C1MVZ0; -.
DR GeneID; 9685274; -.
DR KEGG; mpp:MICPUCDRAFT_59561; -.
DR eggNOG; KOG1076; Eukaryota.
DR OMA; FRCGLIK; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000001876; 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:UP000001876}.
FT DOMAIN 668..840
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..218
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 996 AA; 109708 MW; CA5944F767C787A2 CRC64;
MASKFWGGDS SDSGSDSGSE SSSSSSNGSG SSSSGSSSSG SSSSSESDAG PSKYLQAGSS
DSSSDEGVRV VRSAKDKRFI EARAIADEMR NKIKNNDWIS LQTLFDKLNK QLERVMRLQN
EVGGGVPKFY YRALATLEDA IEATFANKPA IKKMSSTNAK AFNAMRQRLK KHQRDDPTVE
AGIRAAHEKM ESTDEDESEP ESDSDSDADD DDDEKENKQS ADADDGFETV GKGGKTKGKG
AAAAAAAQPP KELDVMTAPK EKITYEMVDK KLKDIIASRG KKGTDRHENA ENLAYLATVS
TCASQEIESL IMLISAQFDI SGSMSAHMPI PIWKRCVNNL LRIDKLLSEN KQITLTEDVE
PQPKPPPEDI VAGAPVQLWG SLCAFTERLD DEYFKSMQSI DPHSKEYLFR MQDESLFIVL
CAAVVRYYEN RDDATEIHCK LSLRLLEHLY YKPEPVYEAL RKFATAKLED ADALEAKLAA
DAVAAAAAAK AKEEAKRIRD KQAEEEDEEY LDDEDADQAE AKEAQEIPYP AGFRFPAPSL
PETLKKLSLT IYKDGDTRSK ARAMLCEIFQ KGLVGDFRAG RDLMLMSHLQ ENISHMDIST
QILFNRAMAQ LGLAAFRGGL FAEAQSCLGE MYQGGRVREL LAQGVTQSRF HERSIEQEKL
ERRRQMPFHM HINLELLESV HLVTSTLAEV PYMTQTSTRR ARSTNKPFTR ICDNYERQTF
NGPPENVRDN VMAAVRFLLD GRWSHAKDII LGLEAWKLLP GDAAPVLEKV VNRLKEEAMR
TYLFQFAAQY NSVSMDVIGN MFDLDQKSAH SIVSRMIINE ELRGMCDAVT NSVVMSHAEP
TRLQSLAMTF AEKCAVLLDA NERALELHVG TGGAQLFDYD DDGGGDGGRR GGRGGRGGRG
GRGAGGEWED DGGGGRGGRG RGGRGGRGGG RGRGDRDGRD GGGRRRQESY SNFSTRRGAE
GDFAKRGGGK FKKDPKEDQR DPTERMVSLK AGNWRR
//