EIF3K_MOUSE
ID EIF3K_MOUSE Reviewed; 218 AA.
AC Q9DBZ5; Q58EU9; Q8K3A1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit K {ECO:0000255|HAMAP-Rule:MF_03010};
DE Short=eIF3k {ECO:0000255|HAMAP-Rule:MF_03010};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 12 {ECO:0000255|HAMAP-Rule:MF_03010};
DE AltName: Full=eIF-3 p25 {ECO:0000255|HAMAP-Rule:MF_03010};
GN Name=Eif3k; Synonyms=Eif3s12;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE
RP EIF-3 COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT "Reconstitution reveals the functional core of mammalian eIF3.";
RL EMBO J. 26:3373-3383(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC {ECO:0000255|HAMAP-Rule:MF_03010, ECO:0000269|PubMed:17581632}.
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. Identified in a HCV IRES-
CC mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3
CC and HCV RNA-replicon. Interacts with ALKBH4, IFIT1 and IFIT2.
CC {ECO:0000255|HAMAP-Rule:MF_03002, ECO:0000269|PubMed:17581632}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03010}.
CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03010}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DBZ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DBZ5-2; Sequence=VSP_013425;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit K family. {ECO:0000255|HAMAP-
CC Rule:MF_03010}.
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DR EMBL; AK004664; BAB23454.1; -; mRNA.
DR EMBL; BC027638; AAH27638.1; -; mRNA.
DR EMBL; BC091749; AAH91749.1; -; mRNA.
DR CCDS; CCDS21062.1; -. [Q9DBZ5-1]
DR CCDS; CCDS85254.1; -. [Q9DBZ5-2]
DR RefSeq; NP_001272871.1; NM_001285942.1. [Q9DBZ5-2]
DR RefSeq; NP_082935.1; NM_028659.3. [Q9DBZ5-1]
DR AlphaFoldDB; Q9DBZ5; -.
DR SMR; Q9DBZ5; -.
DR BioGRID; 216289; 24.
DR IntAct; Q9DBZ5; 3.
DR MINT; Q9DBZ5; -.
DR STRING; 10090.ENSMUSP00000066038; -.
DR iPTMnet; Q9DBZ5; -.
DR PhosphoSitePlus; Q9DBZ5; -.
DR SwissPalm; Q9DBZ5; -.
DR EPD; Q9DBZ5; -.
DR jPOST; Q9DBZ5; -.
DR MaxQB; Q9DBZ5; -.
DR PaxDb; Q9DBZ5; -.
DR PeptideAtlas; Q9DBZ5; -.
DR PRIDE; Q9DBZ5; -.
DR ProteomicsDB; 277847; -. [Q9DBZ5-1]
DR ProteomicsDB; 277848; -. [Q9DBZ5-2]
DR TopDownProteomics; Q9DBZ5-1; -. [Q9DBZ5-1]
DR Antibodypedia; 30132; 245 antibodies from 30 providers.
DR Ensembl; ENSMUST00000066070; ENSMUSP00000066038; ENSMUSG00000053565. [Q9DBZ5-1]
DR Ensembl; ENSMUST00000207683; ENSMUSP00000146940; ENSMUSG00000053565. [Q9DBZ5-2]
DR GeneID; 73830; -.
DR KEGG; mmu:73830; -.
DR UCSC; uc009gai.2; mouse. [Q9DBZ5-1]
DR UCSC; uc009gaj.2; mouse. [Q9DBZ5-2]
DR CTD; 27335; -.
DR MGI; MGI:1921080; Eif3k.
DR VEuPathDB; HostDB:ENSMUSG00000053565; -.
DR eggNOG; KOG3252; Eukaryota.
DR GeneTree; ENSGT00390000009409; -.
DR HOGENOM; CLU_076723_1_0_1; -.
DR InParanoid; Q9DBZ5; -.
DR OMA; WKHQGQG; -.
DR OrthoDB; 1576799at2759; -.
DR PhylomeDB; Q9DBZ5; -.
DR TreeFam; TF314893; -.
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; 73830; 18 hits in 75 CRISPR screens.
DR ChiTaRS; Eif3k; mouse.
DR PRO; PR:Q9DBZ5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DBZ5; protein.
DR Bgee; ENSMUSG00000053565; Expressed in floor plate of midbrain and 257 other tissues.
DR ExpressionAtlas; Q9DBZ5; baseline and differential.
DR Genevisible; Q9DBZ5; 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; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:MGI.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:InterPro.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.25.40.250; -; 1.
DR HAMAP; MF_03010; eIF3k; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033464; CSN8_PSD8_EIF3K.
DR InterPro; IPR009374; eIF3k.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR016020; Transl_init_fac_sub12_N_euk.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13022; PTHR13022; 1.
DR Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Initiation factor; Nucleus;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03010"
FT CHAIN 2..218
FT /note="Eukaryotic translation initiation factor 3 subunit
FT K"
FT /id="PRO_0000123547"
FT DOMAIN 42..204
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ5, ECO:0000255|HAMAP-
FT Rule:MF_03010"
FT MOD_RES 28
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ5"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBQ5"
FT VAR_SEQ 21..53
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013425"
SQ SEQUENCE 218 AA; 25087 MW; 84173F6E77F8C294 CRC64;
MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV LKLYQFNPAF
FQTTVTAQIL LKALTNLPHT DFTLCKCMID QAHQEERPIR QILYLGDLLE TCHFQAFWQA
LDENMDLLEG ITGFEDSVRK FICHVVGITY QHIDRWLLAE MLGDLTDNQL KVWMSKYGWS
ADESGQVFIC SQEESIKPKN IVEKIDFDSV SSIMASSQ
