EIF3D_MOUSE
ID EIF3D_MOUSE Reviewed; 548 AA.
AC O70194; Q8BLH0; Q8BWW1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit D {ECO:0000255|HAMAP-Rule:MF_03003};
DE Short=eIF3d {ECO:0000255|HAMAP-Rule:MF_03003};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 7 {ECO:0000255|HAMAP-Rule:MF_03003};
DE AltName: Full=eIF-3-zeta {ECO:0000255|HAMAP-Rule:MF_03003};
DE AltName: Full=eIF3 p66;
GN Name=Eif3d; Synonyms=Eif3s7;
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 [MRNA].
RC TISSUE=Embryo;
RA Muramatsu H.;
RT "Molecular cloning of mouse translation initiation factor eIF3 p66
RT subunit.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J;
RC TISSUE=Blastocyst, Embryo, and Embryonic spinal cord;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [4]
RP CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE EIF-3 COMPLEX,
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-529, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528, AND IDENTIFICATION BY
RP 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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: mRNA cap-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, a complex required for several
CC steps in the initiation of protein synthesis of a specialized
CC repertoire of mRNAs. The eIF-3 complex associates with the 40S ribosome
CC and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-
CC tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The
CC eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning
CC of the mRNA for AUG recognition. The eIF-3 complex is also required for
CC disassembly and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S ribosomal
CC subunits prior to initiation. The eIF-3 complex specifically targets
CC and initiates translation of a subset of mRNAs involved in cell
CC proliferation, including cell cycling, differentiation and apoptosis,
CC and uses different modes of RNA stem-loop binding to exert either
CC translational activation or repression. In the eIF-3 complex, EIF3D
CC specifically recognizes and binds the 7-methylguanosine cap of a subset
CC of mRNAs. {ECO:0000255|HAMAP-Rule:MF_03003}.
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 may interact with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation may lead 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_03003, ECO:0000269|PubMed:17581632}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.
CC -!- DOMAIN: The RNA gate region regulates mRNA cap recognition to prevent
CC promiscuous mRNA-binding before assembly of eif3d into the full
CC eukaryotic translation initiation factor 3 (eIF-3) complex.
CC {ECO:0000255|HAMAP-Rule:MF_03003}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit D family. {ECO:0000255|HAMAP-
CC Rule:MF_03003}.
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DR EMBL; AB012580; BAA25327.1; -; mRNA.
DR EMBL; AK045228; BAC32270.1; -; mRNA.
DR EMBL; AK049767; BAC33910.1; -; mRNA.
DR EMBL; AK145689; BAE26591.1; -; mRNA.
DR EMBL; AK168256; BAE40204.1; -; mRNA.
DR EMBL; BC089020; AAH89020.1; -; mRNA.
DR CCDS; CCDS37130.1; -.
DR RefSeq; NP_061219.2; NM_018749.2.
DR RefSeq; XP_006521255.1; XM_006521192.1.
DR AlphaFoldDB; O70194; -.
DR SMR; O70194; -.
DR BioGRID; 207740; 28.
DR IntAct; O70194; 7.
DR MINT; O70194; -.
DR STRING; 10090.ENSMUSP00000098053; -.
DR iPTMnet; O70194; -.
DR PhosphoSitePlus; O70194; -.
DR SwissPalm; O70194; -.
DR EPD; O70194; -.
DR jPOST; O70194; -.
DR MaxQB; O70194; -.
DR PaxDb; O70194; -.
DR PeptideAtlas; O70194; -.
DR PRIDE; O70194; -.
DR ProteomicsDB; 275653; -.
DR Antibodypedia; 25691; 276 antibodies from 32 providers.
DR DNASU; 55944; -.
DR Ensembl; ENSMUST00000100484; ENSMUSP00000098053; ENSMUSG00000016554.
DR GeneID; 55944; -.
DR KEGG; mmu:55944; -.
DR UCSC; uc007wom.1; mouse.
DR CTD; 8664; -.
DR MGI; MGI:1933181; Eif3d.
DR VEuPathDB; HostDB:ENSMUSG00000016554; -.
DR eggNOG; KOG2479; Eukaryota.
DR GeneTree; ENSGT00390000002667; -.
DR HOGENOM; CLU_024521_2_0_1; -.
DR InParanoid; O70194; -.
DR OMA; PDGWGPC; -.
DR OrthoDB; 1030308at2759; -.
DR PhylomeDB; O70194; -.
DR TreeFam; TF101519; -.
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; 55944; 26 hits in 73 CRISPR screens.
DR ChiTaRS; Eif3d; mouse.
DR PRO; PR:O70194; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O70194; protein.
DR Bgee; ENSMUSG00000016554; Expressed in floor plate of midbrain and 259 other tissues.
DR ExpressionAtlas; O70194; baseline and differential.
DR Genevisible; O70194; MM.
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:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IDA:MGI.
DR GO; GO:0098808; F:mRNA cap binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:MGI.
DR GO; GO:0002191; P:cap-dependent translational initiation; ISS:UniProtKB.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IDA:UniProtKB.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:MGI.
DR GO; GO:1902416; P:positive regulation of mRNA binding; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0006413; P:translational initiation; ISO:MGI.
DR GO; GO:0075525; P:viral translational termination-reinitiation; ISO:MGI.
DR HAMAP; MF_03003; eIF3d; 1.
DR InterPro; IPR007783; eIF3d.
DR PANTHER; PTHR12399; PTHR12399; 1.
DR Pfam; PF05091; eIF-3_zeta; 1.
DR PIRSF; PIRSF016281; EIF-3_zeta; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..548
FT /note="Eukaryotic translation initiation factor 3 subunit
FT D"
FT /id="PRO_0000123521"
FT REGION 285..299
FT /note="RNA gate"
FT /evidence="ECO:0000250|UniProtKB:K7IM66"
FT REGION 523..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..548
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15371"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CONFLICT 198..219
FT /note="ALEYYDKAFDRITTRSEKPLRS -> PWSTTTKPLTASPQGVRSPCD (in
FT Ref. 1; BAA25327)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="R -> G (in Ref. 2; BAC32270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 63989 MW; C23CA1743270DECD CRC64;
MAKFMTPVIQ DNPSGWGPCA VPEQFRDMPY QPFSKGDRLG KVADWTGATY QDKRYTNKYS
SQFGGGSQYA YFHEEDETSF QLVDTARTQK TAYQRNRMRF AQRNLRRDKD RRNMVQFNLQ
TLPKSAKQKE RERIRLQKKF QKQFGVRQKW DQKSQKPRDS SVEVRSDWEV KEEMDFPQLM
KMRYLEVSEP QDIECCGALE YYDKAFDRIT TRSEKPLRSI KRIFHTVTTT DDPVIRKLAK
TQGNVFATDA ILATLMSCTR SVYSWDIVVQ RVGSKLFFDK RDNSDFDLLT VSETANEPPQ
DEGNSFNSPR NLAMEATYIN HNFSQQCLRM GRERYNFPNP NPFVEDDMDK NEIASVAYRY
RRWKLGDDID LIVRCEHDGV MTGANGEVSF INIKTLNEWD SRHCNGVDWR QKLDSQRGAV
IATELKNNSY KLARWTCCAL LAGSEYLKLG YVSRYHVKDS SRHVILGTQQ FKPNEFASQI
NLSVENAWGI LRCVIDICMK LEEGKYLILK DPNKQVIRVY SLPDGTFSSE EDEEDEEEEE
EEEEEEET
