EI3JA_MOUSE
ID EI3JA_MOUSE Reviewed; 261 AA.
AC Q3UGC7;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit J-A {ECO:0000255|HAMAP-Rule:MF_03009};
DE Short=eIF3j-A {ECO:0000255|HAMAP-Rule:MF_03009};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 1-A {ECO:0000255|HAMAP-Rule:MF_03009};
DE AltName: Full=eIF-3-alpha-A {ECO:0000255|HAMAP-Rule:MF_03009};
DE AltName: Full=eIF3 p35 {ECO:0000255|HAMAP-Rule:MF_03009};
GN Name=Eif3j1; Synonyms=Eif3s1-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:BAE28282.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE36162.1}, and
RC NOD {ECO:0000312|EMBL:BAE32935.1};
RC TISSUE=Amnion {ECO:0000312|EMBL:BAE27721.1},
RC Dendritic cell {ECO:0000312|EMBL:BAE32935.1},
RC Embryonic liver {ECO:0000312|EMBL:BAE36162.1}, and
RC Melanocyte {ECO:0000312|EMBL:BAE28282.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000312|EMBL:CAM21780.1, ECO:0000312|Ensembl:ENSMUSP00000028668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:CAM21780.1,
RC ECO:0000312|Ensembl:ENSMUSP00000028668};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:EDL28081.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) 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:0000250|UniProtKB:O75822,
CC ECO:0000255|HAMAP-Rule:MF_03009}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75822,
CC ECO:0000255|HAMAP-Rule:MF_03009}.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-
CC 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; AK147154; BAE27721.1; -; mRNA.
DR EMBL; AK148004; BAE28282.1; -; mRNA.
DR EMBL; AK154934; BAE32935.1; -; mRNA.
DR EMBL; AK161038; BAE36162.1; -; mRNA.
DR EMBL; AL845457; CAM21780.1; -; Genomic_DNA.
DR EMBL; CH466519; EDL28081.1; -; Genomic_DNA.
DR CCDS; CCDS38219.1; -.
DR RefSeq; NP_653128.2; NM_144545.4.
DR AlphaFoldDB; Q3UGC7; -.
DR SMR; Q3UGC7; -.
DR BioGRID; 219556; 13.
DR IntAct; Q3UGC7; 2.
DR MINT; Q3UGC7; -.
DR STRING; 10090.ENSMUSP00000028668; -.
DR iPTMnet; Q3UGC7; -.
DR PhosphoSitePlus; Q3UGC7; -.
DR EPD; Q3UGC7; -.
DR jPOST; Q3UGC7; -.
DR MaxQB; Q3UGC7; -.
DR PaxDb; Q3UGC7; -.
DR PeptideAtlas; Q3UGC7; -.
DR PRIDE; Q3UGC7; -.
DR ProteomicsDB; 277579; -.
DR DNASU; 78655; -.
DR Ensembl; ENSMUST00000028668; ENSMUSP00000028668; ENSMUSG00000027236.
DR GeneID; 78655; -.
DR KEGG; mmu:78655; -.
DR CTD; 78655; -.
DR MGI; MGI:1925905; Eif3j1.
DR VEuPathDB; HostDB:ENSMUSG00000027236; -.
DR eggNOG; KOG4813; Eukaryota.
DR GeneTree; ENSGT00390000018400; -.
DR HOGENOM; CLU_085806_2_1_1; -.
DR InParanoid; Q3UGC7; -.
DR OMA; HYGLFLE; -.
DR OrthoDB; 1565510at2759; -.
DR PhylomeDB; Q3UGC7; -.
DR TreeFam; TF101514; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-72649; Translation initiation complex formation.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR BioGRID-ORCS; 78655; 14 hits in 52 CRISPR screens.
DR ChiTaRS; Eif3j1; mouse.
DR PRO; PR:Q3UGC7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3UGC7; protein.
DR Bgee; ENSMUSG00000027236; Expressed in quadriceps femoris and 62 other tissues.
DR Genevisible; Q3UGC7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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..261
FT /note="Eukaryotic translation initiation factor 3 subunit
FT J-A"
FT /id="PRO_0000419334"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4..72
FT /note="Sufficient for interaction with EIF3B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT REGION 246..261
FT /note="Promotes stable association with the 40S ribosome"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT COILED 73..138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT COMPBIAS 42..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-
FT Rule:MF_03009"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-
FT Rule:MF_03009"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-
FT Rule:MF_03009"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-
FT Rule:MF_03009"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75822, ECO:0000255|HAMAP-
FT Rule:MF_03009"
FT MOD_RES 257
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75822"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75822"
SQ SEQUENCE 261 AA; 29344 MW; 5BED22967289E651 CRC64;
MAAAAAAAAA AGDSDSWDAD TFSMEDPVRK VAGGGTAGGD RWEGEDEDED VKDNWDDDDD
ENKEEAEVKP EVKISEKKKI AEKIKEKERQ QKKRQEEIKK RLEEPEESKV LTPEEQLADK
LRLKKLQEES DLELAKETFG VNNTVYGIDA MNPSSRDDFT EFGKLLKDKI TQYEKSLYYA
SFLEALVRDV CISLEIDDLK KITNSLTVLC SEKQKQEKQS KAKKKKKGVV PGGGLKATMK
DDLADYGGYE GGYVQDYEDF M
