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Database: UniProt
Entry: H2TCV9_TAKRU
LinkDB: H2TCV9_TAKRU
Original site: H2TCV9_TAKRU 
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
//
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