EIF3J_BOVIN
ID EIF3J_BOVIN Reviewed; 256 AA.
AC Q0VCU8; A6QPP4;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 {ECO:0000255|HAMAP-Rule:MF_03009};
GN Synonyms=EIF3S1 {ECO:0000255|HAMAP-Rule:MF_03009};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle, and Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is required for several steps in the initiation
CC of protein synthesis. The eIF-3 complex associates with the 40S
CC ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-
CC 2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex
CC (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC
CC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also
CC required for disassembly and recycling of post-termination ribosomal
CC complexes and subsequently prevents premature joining of the 40S and
CC 60S ribosomal subunits prior to initiation. The eIF-3 complex
CC specifically targets and initiates translation of a subset of mRNAs
CC involved in cell proliferation, including cell cycling, differentiation
CC and apoptosis, and uses different modes of RNA stem-loop binding to
CC exert either translational activation or repression. This subunit binds
CC directly within the mRNA entry channel of the 40S ribosome to the
CC aminoacyl (A) site. It may regulate the interaction between the 43S PIC
CC and mRNA. {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. The eIF-3 complex appears to include 3 stable modules: module A
CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. {ECO:0000255|HAMAP-
CC Rule:MF_03009}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009}.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {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; BC119989; AAI19990.1; -; mRNA.
DR EMBL; BC149417; AAI49418.1; -; mRNA.
DR RefSeq; NP_001069611.1; NM_001076143.1.
DR AlphaFoldDB; Q0VCU8; -.
DR SMR; Q0VCU8; -.
DR STRING; 9913.ENSBTAP00000000465; -.
DR PaxDb; Q0VCU8; -.
DR PRIDE; Q0VCU8; -.
DR Ensembl; ENSBTAT00000000465; ENSBTAP00000000465; ENSBTAG00000000359.
DR GeneID; 539052; -.
DR KEGG; bta:539052; -.
DR CTD; 8669; -.
DR VEuPathDB; HostDB:ENSBTAG00000000359; -.
DR VGNC; VGNC:28400; EIF3J.
DR eggNOG; KOG4813; Eukaryota.
DR GeneTree; ENSGT00390000018400; -.
DR HOGENOM; CLU_085806_2_1_1; -.
DR InParanoid; Q0VCU8; -.
DR OMA; HYGLFLE; -.
DR OrthoDB; 1565510at2759; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000000359; Expressed in longissimus thoracis muscle and 105 other tissues.
DR ExpressionAtlas; Q0VCU8; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0042802; F:identical protein binding; IEA:Ensembl.
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; Isopeptide bond; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Ubl conjugation.
FT CHAIN 1..256
FT /note="Eukaryotic translation initiation factor 3 subunit
FT J"
FT /id="PRO_0000284060"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..67
FT /note="Sufficient for interaction with EIF3B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT REGION 213..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..256
FT /note="Promotes stable association with the 40S ribosome"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT COILED 68..133
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT COMPBIAS 37..59
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-
FT Rule:MF_03009"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-
FT Rule:MF_03009"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-
FT Rule:MF_03009"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-
FT Rule:MF_03009"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-
FT Rule:MF_03009"
FT MOD_RES 252
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75822"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75822"
SQ SEQUENCE 256 AA; 28951 MW; 787F639B7BB49D14 CRC64;
MAAAAAGDSD SWDADTFSVE DPVRKVGGGG TAGGDRWEGE DEDEDVKDNW DDDDDEKKEE
AEVKPEVKIS EKKKIAEKIK EKERQQKKRQ EEIKKRLEEP EEPKVLTPEE QLADKLRLKK
LQEESDLELA KETFGVNNTV YGIDAMNPSS RDDFTEFGKL LKDKITQYEK SLYYANFLEA
LVRDVCISLE IDDLKKITNS LTVLCSEKQK QEKQSKAKKK KKGVVPGGGL KATMKDDLAD
YGGYDGGYAQ DYEDFM
