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EIF3J_DROWI
ID   EIF3J_DROWI             Reviewed;         236 AA.
AC   B4MP81; Q8I166;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=GK21662;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
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 14030-0811.24;
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; AY190959; AAO01104.1; -; Genomic_DNA.
DR   EMBL; CH963849; EDW73920.1; -; Genomic_DNA.
DR   RefSeq; XP_002062934.1; XM_002062898.2.
DR   AlphaFoldDB; B4MP81; -.
DR   SMR; B4MP81; -.
DR   STRING; 7260.FBpp0250805; -.
DR   EnsemblMetazoa; FBtr0252313; FBpp0250805; FBgn0064303.
DR   GeneID; 6640598; -.
DR   KEGG; dwi:6640598; -.
DR   eggNOG; KOG4813; Eukaryota.
DR   HOGENOM; CLU_085806_2_1_1; -.
DR   InParanoid; B4MP81; -.
DR   OMA; HYGLFLE; -.
DR   OrthoDB; 1565510at2759; -.
DR   PhylomeDB; B4MP81; -.
DR   ChiTaRS; Adam; fly.
DR   Proteomes; UP000007798; 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; Reference proteome.
FT   CHAIN           1..236
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   J"
FT                   /id="PRO_0000365142"
FT   REGION          20..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..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        119
FT                   /note="T -> A (in Ref. 1; AAO01104)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="L -> V (in Ref. 1; AAO01104)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   236 AA;  27120 MW;  3E6D83D75B1FACF6 CRC64;
     MADDWESAAD SEVVILPNAA NNINKWEGED DDEDVKESWE DEEEKKDEEK PTKTEVPVKP
     KPTRALKAKL EEEERLREAE EEKRLANLTP EEKFAEKLRV KKMQEESDMK HTLDTFGVTS
     ISGGLESFNP ESKEEFKEFG DTLSWKVAQF KESPHFPQFV EDLVRSICVN LSAADIKKVK
     INVELLHSEK LKLEKANTKK PIGKGKGKVS LRTENDDIDG YQKYGNDFTD DYDDFM
 
 
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