ID   EIF3J_XENLA             Reviewed;         255 AA.
AC   Q6INR1;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
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};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 1 {ECO:0000255|HAMAP-Rule:MF_03009};
DE   AltName: Full=eIF-3-alpha {ECO:0000255|HAMAP-Rule:MF_03009};
DE   AltName: Full=eIF3 p35 {ECO:0000255|HAMAP-Rule:MF_03009};
GN   Name=eif3j; Synonyms=eif3s1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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, which is composed of 13 subunits: eif3a, eif3b, eif3c,
CC       eif3d, eif3e, eif3f, eif3g, eif3h, eif3i, eif3j, eif3k, eif3l and
CC       eif3m. {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC072212; AAH72212.1; -; mRNA.
DR   RefSeq; NP_001085202.1; NM_001091733.1.
DR   AlphaFoldDB; Q6INR1; -.
DR   SMR; Q6INR1; -.
DR   BioGRID; 101661; 1.
DR   IntAct; Q6INR1; 1.
DR   DNASU; 432295; -.
DR   GeneID; 432295; -.
DR   KEGG; xla:432295; -.
DR   CTD; 432295; -.
DR   Xenbase; XB-GENE-999882; eif3j.S.
DR   OMA; HYGLFLE; -.
DR   OrthoDB; 1565510at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 432295; Expressed in blastula and 19 other tissues.
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; ISS:UniProtKB.
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   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   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..255
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   J"
FT                   /id="PRO_0000365126"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          69..131
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT   COMPBIAS        34..54
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   255 AA;  29339 MW;  BF36B0E37F762B85 CRC64;
     MAENDSWDAD DFEAEDLNQK GAASGPVIVK DRWEGEDEEE DVKDNWDDEE EAQDATKQEP
     QKTELKVPEK KKLQEKIKEK ENLQKKRKEE LKKQALESSN LPEITPEEQL AEKLRQQKLQ
     EDSDLELAKE AFGVNVPVTG IDAMNPSTRE DFTEFGKLLK EKITQYERSL YYPGFLEALV
     RDVCLSLEVE DLKKINSSLT VLCFEKQKQE KQQTKTKKKK KGVVPGGGLK GNMKDYLEDY
     GGMDEGYGRE FDDFM