ID H2TCV9_TAKRU Unreviewed; 931 AA.
AC H2TCV9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 24-JAN-2024, entry version 74.
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};
GN Name=LOC101078446 {ECO:0000313|Ensembl:ENSTRUP00000022501.2};
GN Synonyms=EIF3C {ECO:0000256|HAMAP-Rule:MF_03002}, EIF3S8
GN {ECO:0000256|HAMAP-Rule:MF_03002};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000022501.2, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000022501.2, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000022501.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) 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, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC EIF3M. {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 RefSeq; XP_011601148.1; XM_011602846.1.
DR AlphaFoldDB; H2TCV9; -.
DR STRING; 31033.ENSTRUP00000058571; -.
DR Ensembl; ENSTRUT00000022595.3; ENSTRUP00000022501.2; ENSTRUG00000008951.3.
DR GeneID; 101078446; -.
DR KEGG; tru:101078446; -.
DR CTD; 8663; -.
DR eggNOG; KOG1076; Eukaryota.
DR GeneTree; ENSGT00390000017900; -.
DR HOGENOM; CLU_004304_0_0_1; -.
DR OrthoDB; 5482362at2759; -.
DR TreeFam; TF101520; -.
DR Proteomes; UP000005226; 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; 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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_03002; eIF3c; 1.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
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:UP000005226}.
FT DOMAIN 673..849
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 107085 MW; 4395F8D7C2A5D620 CRC64;
MSRFFATGSD SESEESSSAD EITPKATGTP FKQALLLSDD EEDTKRVVRS AKDKRFEELT
NIIKTIRNAM KIRDMAKCLE EFEQLCRAFL KSKNIVDKEG IPPFYIRLLA DLEDYLNQLW
EDKEGKKKMN KNNAKALSTL RQKIRKYNRD YENEIASYKE NPQESADEEE EREAGDSGSS
SDSDDEGKDE GLSAKSFLKK KPEPSSEASK FLKSAKGSGD ESSTSDDDED DEDWGSDTVD
SSSESSDDGE EKSTSLAVVF LKKTQEAEKA DKKLGKKRKP KKKERLEEEM EEEAGEEAEG
GWEKVKGGAP LVKEKPKMFA KGTEINVPVV VKKLNEILQA RGKKGTDRAA QIELLHALAA
ISNENNLGQG VLVKIKFNII ASLYDYNPNL AAFMKPDMWK KCLDCIEELQ TILFEHNNIF
IGENIAEDSE SLANTDQPFR VRGCILTLVE RMDEEFTKIM QNTDPHSQEY VDNLKDEGRV
CAIIDRLLNY LENKGSTEEI CRIYLRRIMH TYYKFDYKAH RRSLGLQVES KSEHDQEESE
GEDSAVIMDR FCKFIYAKDR TDRIRTCAIL CHIYHHALHS RWYQARDLML MSHLQDNIQH
ADPPVQILYN RTMVQLGICA FRQGMIKDAH NALLDIQSSG RAKELLGQGL LMRNMQERNA
EQEKIEKRRQ VPFHMHINLE LLECVYLVSA MLLEIPYMAA HEFDARRRMI SKQFHHQLRV
GERQPLLGPP ESMREHVVAA SKAMKMGDWR TCHSFIINEK MNMKVWDLFP ETQRVQEMLV
RKIQEESLRT YLFTYSSVYD SISMETLSEM FQLEIPTVHS IISKMIINEE LMASLDQPTQ
TVVMHRTEPT SLQNMALQLA EKLGSLVENN ERVFDLKQGV YGGYFNRDQK GGYQQKQSYQ
RDQKSGYQQN KGGYQRGGYR NQNQRRAAHP V
//