ID   EI3JB_DANRE             Reviewed;         263 AA.
AC   Q803P1;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit J-B {ECO:0000255|HAMAP-Rule:MF_03009};
DE            Short=eIF3j-B {ECO:0000255|HAMAP-Rule:MF_03009};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 1-B {ECO:0000255|HAMAP-Rule:MF_03009};
DE   AltName: Full=eIF-3-alpha-B {ECO:0000255|HAMAP-Rule:MF_03009};
DE   AltName: Full=eIF3 p35-B {ECO:0000255|HAMAP-Rule:MF_03009};
GN   Name=eif3jb; Synonyms=eif3s1b; ORFNames=zgc:55443;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) 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}.
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DR   EMBL; BC044399; AAH44399.1; -; mRNA.
DR   RefSeq; NP_998667.1; NM_213502.1.
DR   AlphaFoldDB; Q803P1; -.
DR   SMR; Q803P1; -.
DR   STRING; 7955.ENSDARP00000069883; -.
DR   PaxDb; Q803P1; -.
DR   PeptideAtlas; Q803P1; -.
DR   GeneID; 406823; -.
DR   KEGG; dre:406823; -.
DR   CTD; 406823; -.
DR   ZFIN; ZDB-GENE-040426-2900; eif3jb.
DR   eggNOG; KOG4813; Eukaryota.
DR   InParanoid; Q803P1; -.
DR   OrthoDB; 1565510at2759; -.
DR   PhylomeDB; Q803P1; -.
DR   PRO; PR:Q803P1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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..263
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   J-B"
FT                   /id="PRO_0000365125"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          30..127
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT   COMPBIAS        30..50
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   263 AA;  29887 MW;  7A3E1A8A5C4C833E CRC64;
     MADSDEWDAD NFEPNEPIKI ATAGRLDRWE GEDEEEDVKD NWDDEEEEKE EEKKVEQKIA
     EVKPPEKKKL SDKIKEKELL QKKKQEELKK NQETAASESL TLEEQLAEKA RLKKLQEEAD
     MELAREAFGV DPAAANASTT VNTTNASGIE AMCPSSKDDF VTFEKLLKEK ITQFEKSVHY
     PSFLESLFRE LCISLEVDDL KKISTSLSVL LTEKQKQEKE KKANKKKKKG VVPGGGLKAN
     MKDDFADYGG FDGGYGNEYD DFM