ID D8TLC8_VOLCA Unreviewed; 940 AA.
AC D8TLC8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
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 Name=eif3C {ECO:0000313|EMBL:EFJ51713.1};
GN ORFNames=VOLCADRAFT_103345 {ECO:0000313|EMBL:EFJ51713.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ51713.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
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; GL378326; EFJ51713.1; -; Genomic_DNA.
DR RefSeq; XP_002947123.1; XM_002947077.1.
DR AlphaFoldDB; D8TLC8; -.
DR STRING; 3068.D8TLC8; -.
DR GeneID; 9620224; -.
DR KEGG; vcn:VOLCADRAFT_103345; -.
DR eggNOG; KOG1076; Eukaryota.
DR InParanoid; D8TLC8; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000001058; 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:UP000001058}.
FT DOMAIN 608..780
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 104963 MW; 0C692CADCD6D49D4 CRC64;
MSKFWGRDSS DEEEEETTEE ESSSEEETSN DDDSSSEEES SSGSDSDSDS DSDSDDEGPN
KFLAGSSDSD SDDDRRVVKS EKDKRMGELA QTAEDIRNKI KINDWSTIQE LFDILNQRLE
KTRKFLVGLT VPRVYLKCLI ELEDYLNETL GNKDLKKKMS QTNAKAFNTM RQRLKKHNVN
FADQMAKVRE NPDEDDEEDA AESASSDSES GDEREQEDRK NQQQQQKAKD KLLTMDPKEI
TYEMVARKLR EIVVSRGRRG TDKQEQVEML TYLVTVARGP AQRFEVLAQL TSSLFDLNPG
MMGHLQTGLW KKCVVNLLEM LRILQDNPNI KVDENADALE ERTEQPPDGA EVRVWGNVVA
FVERLDDELF KSLQVIDPHT HEYMARLRDE PVYLALGTKV LEYLQRVGDM VGSPKVALRL
VEHLYYKTDT VYDAMRKLAM AQQQTASAPA PAMEDGDEEE PGAKVEVLVP SDYAMAENCH
ELMLSLVGGV IFKYGDERTK ARAMMCYIYH KAIHDDFHGA RDLLLMSHLQ DSIQHMDVST
MILYNRAMAQ LGLAAFRAGL IHEAHACLNE LYGSGHIKEL LAQGMSMGKY HEKTPEQELA
EKRRQMPFHM HITLELLESA YLTCAMLLEV PNMAANPLNP KKKMISKSFH RVWDTYARQA
FTGPPENVRD HIMAASRALA QGDWAKSFNY LKSLNAWNLL PKKEQVLAML KVKVQEEAVR
TYLLSYSNQY ASLSLDQLAS MFELPDKQIY SIASKMMIAE ELPGSWDQPT RTIVMHSSES
SRVQRVALQL ADKAAVIVDL NERALAYRTG GLRDADDEGG AMAGSSRRRG GQWDDEGGAG
GRSRGGVKLG MVRNIGGRGD RGDRGSVRSG PRPGGMGGRG GGYRRDGGMG GGSYGDRVGG
GPRGYGRPGM GSNMSSMSAL GSLRGPSMGS RGDLRDSQRP
//
