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EIF3J_DROER
ID   EIF3J_DROER             Reviewed;         236 AA.
AC   Q8I1G8;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit J {ECO:0000255|HAMAP-Rule:MF_03009};
DE            Short=eIF3j {ECO:0000255|HAMAP-Rule:MF_03009};
GN   Name=eIF3j {ECO:0000255|HAMAP-Rule:MF_03009};
GN   Synonyms=Adam {ECO:0000255|HAMAP-Rule:MF_03009}; ORFNames=GG24124;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12537575; DOI=10.1186/gb-2002-3-12-research0086;
RA   Bergman C.M., Pfeiffer B.D., Rincon-Limas D.E., Hoskins R.A., Gnirke A.,
RA   Mungall C.J., Wang A.M., Kronmiller B., Pacleb J.M., Park S., Stapleton M.,
RA   Wan K.H., George R.A., de Jong P.J., Botas J., Rubin G.M., Celniker S.E.;
RT   "Assessing the impact of comparative genomic sequence data on the
RT   functional annotation of the Drosophila genome.";
RL   Genome Biol. 3:RESEARCH0086.1-RESEARCH0086.20(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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:0000255|HAMAP-Rule:MF_03009}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. The eIF-3 complex interacts with pix.
CC       {ECO:0000255|HAMAP-Rule:MF_03009}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit J family. {ECO:0000255|HAMAP-
CC       Rule:MF_03009}.
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DR   EMBL; AY190939; AAO01001.1; -; Genomic_DNA.
DR   EMBL; CH954177; EDV58178.1; -; Genomic_DNA.
DR   RefSeq; XP_001969119.1; XM_001969083.2.
DR   AlphaFoldDB; Q8I1G8; -.
DR   SMR; Q8I1G8; -.
DR   STRING; 7220.FBpp0142670; -.
DR   EnsemblMetazoa; FBtr0144178; FBpp0142670; FBgn0064657.
DR   GeneID; 6541940; -.
DR   KEGG; der:6541940; -.
DR   eggNOG; KOG4813; Eukaryota.
DR   HOGENOM; CLU_085806_2_0_1; -.
DR   OMA; HYGLFLE; -.
DR   OrthoDB; 1565510at2759; -.
DR   PhylomeDB; Q8I1G8; -.
DR   ChiTaRS; Adam; fly.
DR   Proteomes; UP000008711; 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:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006446; P:regulation of translational initiation; IEA:EnsemblMetazoa.
DR   Gene3D; 1.10.246.60; -; 1.
DR   HAMAP; MF_03009; eIF3j; 1.
DR   InterPro; IPR023194; eIF3-like_dom_sf.
DR   InterPro; IPR013906; eIF3j.
DR   PANTHER; PTHR21681; PTHR21681; 1.
DR   Pfam; PF08597; eIF3_subunit; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis.
FT   CHAIN           1..236
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   J"
FT                   /id="PRO_0000365133"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..42
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   236 AA;  26570 MW;  21878CE066A80025 CRC64;
     MADDWESAAD SEVVIRPTAA ASVNKWEGED EDEDIKDSWE DEEEKKDEEK PTKTEAPAKP
     KPNKALKAKL EQQARLEEEA EAQRVASLSP AEKLAEKLRL QKIQEASDLK HAQEAFGVTS
     TCGGLDAFNP ESKEEFKEFG ATLSWKVAQF RESEHFPQFV EDLVRSLCVN LSAADIKKVK
     MNVEILHSEK LKLEKANAKK PAGKGKGKVT LRTENDDIDG YQKYGNDFTE DYDDFM
 
 
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