ID   EIF3J_XENTR             Reviewed;         256 AA.
AC   Q5I0B5;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 89.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-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   -!- SEQUENCE CAUTION:
CC       Sequence=CF222250; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BC088509; AAH88509.1; -; mRNA.
DR   EMBL; CF222250; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001263434.1; NM_001276505.2.
DR   AlphaFoldDB; Q5I0B5; -.
DR   SMR; Q5I0B5; -.
DR   PaxDb; Q5I0B5; -.
DR   GeneID; 496929; -.
DR   KEGG; xtr:496929; -.
DR   CTD; 8669; -.
DR   Xenbase; XB-GENE-999878; eif3j.
DR   eggNOG; KOG4813; Eukaryota.
DR   HOGENOM; CLU_085806_2_1_1; -.
DR   InParanoid; Q5I0B5; -.
DR   OrthoDB; 1565510at2759; -.
DR   PhylomeDB; Q5I0B5; -.
DR   Reactome; R-XTR-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-XTR-72649; Translation initiation complex formation.
DR   Reactome; R-XTR-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-XTR-72702; Ribosomal scanning and start codon recognition.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   ExpressionAtlas; Q5I0B5; baseline.
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..256
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   J"
FT                   /id="PRO_0000365127"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          70..99
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT   COMPBIAS        35..55
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        65
FT                   /note="Missing (in Ref. 1; CF222250)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="K -> Q (in Ref. 1; CF222250)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232..233
FT                   /note="AN -> PT (in Ref. 1; CF222250)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   256 AA;  29241 MW;  96A72F3C4FAE6638 CRC64;
     MAENDSWDAD DFEPEVSNQK GAVSGPPPAG RDRWEGEDEE EDVKDNWDDE EEAEAATKQE
     AQKTVEPKVS EKKKLLEKIR EKEKLHKKRQ EEVNQQEKEG TAPELSPEEQ LAEKLRLKKL
     QEDSDLELAK EAFGDNVTVT GIDAMNPSSR EDFTEFGKLL KEKITQYERS LFYPGFLEVL
     VREVCVSLEV DDLKKINNSL TVLCFEKQKQ EKQQSKAKKK KKGVVPGGGL KANMKNDLED
     YGGMDEGYGR EYDDFM