EIF3A_MOUSE
ID EIF3A_MOUSE Reviewed; 1344 AA.
AC P23116; E9QQ50; Q60697; Q62162;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 5.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Centrosomin;
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 10 {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=eIF-3-theta {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=eIF3 p167;
DE AltName: Full=eIF3 p180;
DE AltName: Full=eIF3 p185;
DE AltName: Full=p162;
GN Name=Eif3a; Synonyms=Csma, Eif3, Eif3s10;
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=Lymphoma;
RA Fisher R., Fillmore H., Reynolds A.B.;
RT "Molecular cloning and characterization of the 162 kDa component of a
RT multi-protein complex phosphorylated by Src.";
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 401-1142 (CENTROSOMIN B), SUBCELLULAR
RP LOCATION, AND RNA EDITING.
RC TISSUE=Ehrlich ascites tumor cell;
RX PubMed=9372446; DOI=10.1242/jcs.110.20.2573;
RA Petzelt C., Joswig G., Mincheva A., Lichter P., Stammer H., Werner D.;
RT "The centrosomal protein centrosomin A and the nuclear protein centrosomin
RT B derive from one gene by post-transcriptional processes involving RNA
RT editing.";
RL J. Cell Sci. 110:2573-2578(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 514-790 (CENTROSOMIN A).
RC TISSUE=Ehrlich ascites tumor cell;
RX PubMed=1829085; DOI=10.1242/jcs.98.1.37;
RA Joswig G., Petzelt C., Werner D.;
RT "Murine cDNAs coding for the centrosomal antigen centrosomin A.";
RL J. Cell Sci. 98:37-43(1991).
RN [5]
RP SEQUENCE REVISION.
RA Joswig G., Petzelt C., Werner D.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH EIF3B AND EIF4G1.
RX PubMed=16541103; DOI=10.1038/sj.emboj.7601047;
RA Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E.,
RA Lawrence J.C. Jr.;
RT "mTOR-dependent stimulation of the association of eIF4G and eIF3 by
RT insulin.";
RL EMBO J. 25:1659-1668(2006).
RN [7]
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 [8]
RP INTERACTION WITH PIWIL2.
RX PubMed=19114715; DOI=10.1074/jbc.m809104200;
RA Unhavaithaya Y., Hao Y., Beyret E., Yin H., Kuramochi-Miyagawa S.,
RA Nakano T., Lin H.;
RT "MILI, a PIWI-interacting RNA-binding protein, is required for germ Line
RT stem cell self-renewal and appears to positively regulate translation.";
RL J. Biol. Chem. 284:6507-6519(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584, 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).
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is required for several
CC steps in the initiation of protein synthesis. The eIF-3 complex
CC associates with the 40S ribosome and facilitates the recruitment of
CC eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-
CC initiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC recruitment to the 43S PIC and scanning of the mRNA for AUG
CC recognition. The eIF-3 complex is also required for disassembly and
CC recycling of post-termination ribosomal complexes and subsequently
CC prevents premature joining of the 40S and 60S ribosomal subunits prior
CC to initiation. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation,
CC including cell cycling, differentiation and apoptosis, and uses
CC different modes of RNA stem-loop binding to exert either translational
CC activation or repression. {ECO:0000255|HAMAP-Rule:MF_03000,
CC ECO:0000269|PubMed:17581632}.
CC -!- SUBUNIT: Interacts with KRT7 (By similarity). Component of the
CC eukaryotic translation initiation factor 3 (eIF-3) complex, which is
CC composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F,
CC EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex
CC appears to include 3 stable modules: module A is composed of EIF3A,
CC EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and
CC EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3L and
CC EIF3K. EIF3C of module C binds EIF3B of module A and EIF3H of module B,
CC thereby linking the three modules. EIF3J is a labile subunit that binds
CC to the eIF-3 complex via EIF3B. The eIF-3 complex may interact with
CC RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation
CC may lead to binding and activation of a complex composed of MTOR and
CC RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of
CC EIF4B to eIF-3. Interacts with EIF4G1 and PIWIL2. {ECO:0000250,
CC ECO:0000269|PubMed:16541103, ECO:0000269|PubMed:17581632,
CC ECO:0000269|PubMed:19114715}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:9372446}. Nucleus {ECO:0000269|PubMed:9372446}.
CC Note=Centrosomin-A is found in the centrosome. Centrosomin-B is found
CC in the nucleus.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- RNA EDITING: Modified_positions=Not_applicable; Note=Some positions are
CC modified by RNA editing via nucleotide deletion, up to position 787.
CC The unedited version gives rise to centrosomin-B (shown here). The
CC fully edited version gives rise to centrosomin-A, in which the C-
CC terminal sequence is replaced up to position 787 by Ser-Ile-Val-Ala-
CC STOP. A combination of alternative splicing and RNA editing resulting
CC in this template G deletion could also explain the generation of
CC centrosomin-A mRNA. {ECO:0000269|PubMed:9372446};
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC Rule:MF_03000}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35246.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA59144.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U14172; AAA90910.1; -; mRNA.
DR EMBL; AC163019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X84651; CAA59144.1; ALT_FRAME; mRNA.
DR EMBL; X17373; CAA35246.1; ALT_FRAME; mRNA.
DR CCDS; CCDS38035.1; -.
DR PIR; S13800; S13800.
DR PIR; T42637; T42637.
DR RefSeq; NP_034253.3; NM_010123.3.
DR AlphaFoldDB; P23116; -.
DR SMR; P23116; -.
DR BioGRID; 199415; 170.
DR IntAct; P23116; 139.
DR MINT; P23116; -.
DR STRING; 10090.ENSMUSP00000025955; -.
DR iPTMnet; P23116; -.
DR PhosphoSitePlus; P23116; -.
DR SwissPalm; P23116; -.
DR EPD; P23116; -.
DR jPOST; P23116; -.
DR MaxQB; P23116; -.
DR PaxDb; P23116; -.
DR PeptideAtlas; P23116; -.
DR PRIDE; P23116; -.
DR ProteomicsDB; 277774; -.
DR Antibodypedia; 32084; 294 antibodies from 33 providers.
DR DNASU; 13669; -.
DR Ensembl; ENSMUST00000025955; ENSMUSP00000025955; ENSMUSG00000024991.
DR GeneID; 13669; -.
DR KEGG; mmu:13669; -.
DR UCSC; uc008ibx.1; mouse.
DR CTD; 8661; -.
DR MGI; MGI:95301; Eif3a.
DR VEuPathDB; HostDB:ENSMUSG00000024991; -.
DR eggNOG; KOG2072; Eukaryota.
DR GeneTree; ENSGT00730000111063; -.
DR HOGENOM; CLU_002096_1_1_1; -.
DR InParanoid; P23116; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 967904at2759; -.
DR PhylomeDB; P23116; -.
DR TreeFam; TF101522; -.
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; 13669; 18 hits in 76 CRISPR screens.
DR ChiTaRS; Eif3a; mouse.
DR PRO; PR:P23116; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P23116; protein.
DR Bgee; ENSMUSG00000024991; Expressed in lacrimal gland and 256 other tissues.
DR ExpressionAtlas; P23116; baseline and differential.
DR Genevisible; P23116; 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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IBA:GO_Central.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IDA:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:MGI.
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:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR GO; GO:0075525; P:viral translational termination-reinitiation; ISO:MGI.
DR HAMAP; MF_03000; eIF3a; 1.
DR InterPro; IPR027512; EIF3A.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR14005; PTHR14005; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Initiation factor;
KW Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome; Repeat;
KW RNA editing; RNA-binding.
FT CHAIN 1..1344
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000123538"
FT DOMAIN 315..498
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REPEAT 924..931
FT /note="1; truncated"
FT REPEAT 932..941
FT /note="2"
FT REPEAT 942..951
FT /note="3; approximate"
FT REPEAT 953..962
FT /note="4"
FT REPEAT 963..972
FT /note="5"
FT REPEAT 973..982
FT /note="6"
FT REPEAT 983..992
FT /note="7"
FT REPEAT 993..1002
FT /note="8"
FT REPEAT 1003..1012
FT /note="9"
FT REPEAT 1013..1022
FT /note="10"
FT REPEAT 1023..1032
FT /note="11"
FT REPEAT 1033..1042
FT /note="12"
FT REPEAT 1043..1052
FT /note="13"
FT REPEAT 1054..1063
FT /note="14"
FT REPEAT 1064..1073
FT /note="15"
FT REPEAT 1074..1083
FT /note="16"
FT REPEAT 1084..1093
FT /note="17"
FT REPEAT 1094..1103
FT /note="18"
FT REPEAT 1104..1113
FT /note="19"
FT REPEAT 1114..1123
FT /note="20"
FT REPEAT 1124..1133
FT /note="21; approximate"
FT REGION 664..835
FT /note="Interaction with EIF3B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT REGION 807..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..1133
FT /note="21 X 10 AA approximate tandem repeats of [DA]-[DE]-
FT [ED]-R-[PLIGFSV]-[RPS]-[RW]-[RL]-[GNIHT]-[DGLPTAM]"
FT REGION 1252..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 82..120
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 866..1128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 68
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14152"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152, ECO:0000255|HAMAP-
FT Rule:MF_03000"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152"
FT MOD_RES 1159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152, ECO:0000255|HAMAP-
FT Rule:MF_03000"
FT MOD_RES 1223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152"
FT MOD_RES 1300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152, ECO:0000255|HAMAP-
FT Rule:MF_03000"
FT MOD_RES 1326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152, ECO:0000255|HAMAP-
FT Rule:MF_03000"
FT CONFLICT 534
FT /note="L -> I (in Ref. 1; AAA90910 and 3; CAA35246/
FT CAA59144)"
FT /evidence="ECO:0000305"
FT CONFLICT 683..684
FT /note="EL -> DY (in Ref. 3; CAA35246/CAA59144)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="Q -> H (in Ref. 3; CAA35246/CAA59144)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="A -> V (in Ref. 3; CAA35246/CAA59144)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="D -> E (in Ref. 1; AAA90910)"
FT /evidence="ECO:0000305"
FT CONFLICT 1007
FT /note="G -> A (in Ref. 3; CAA59144)"
FT /evidence="ECO:0000305"
FT CONFLICT 1056
FT /note="E -> D (in Ref. 3; CAA59144)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1344 AA; 161936 MW; 215F5CCB8A2C7296 CRC64;
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI MLKYLELCVD
LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKLAEEK TEAAKEESQQ MVLDIEDLDN
IQTPESVLLS AVSGEDTQDR TDRLLLTPWV KFLWESYRQC LDLLRNNSRV ERLYHDIAQQ
AFKFCLQYTR KAEFRKLCDN LRMHLSQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA
ISMELWQEAF KAVEDIHGLF SLSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHASTLHRLY
HLSREMRKNL TQEEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE KQRRLATLLG
LQAPPTRIGL INDMVRFSVL QYVVPEVKDL YNWLEVEFNP LKLCERVTKV LNWVREQPEK
EPELQQYVPQ LQNNTILRLL QQVAQIYQSI EFSRLTSLVP FVDAFQLERA IVDAARHCDL
QVRIDHTSRT LSFGSDLNYA TREDAPVGPH LQSMPSEQIR NQLTAMSSVL AKALEVIRPA
HILQEKEEQH QLAVNAYLKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE
LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA KAFKDIDIED
LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER AKRLEEIPLI KSAYEEQRVK
DMDLWEQQEE ERITTMQLER EKALEHKNRM SRMLEDRDLF VMRLKAARQS VYEEKLKQFE
ERLAEERHSR LEDRKRQRKE ERKITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE
LREYQERVKK LEEVERKKRQ RELEIEERER RREEERRLGD DPLSRKDSRW GDRDSEGTWR
KGPEADSEWR RGPPEKEWRR ETRDDERPHR RDEDRLRRLG GDDEERESSL RPDDDRIPRR
GLDDDRGPRR GPDEDRFSRR GTDDDRPSWR NADDDRPPRR IGDDDRGSWR HTDDDRPPRR
GLDDERGSWR TADEDRGPRR GMDDDRGPRR GGADDERSSW RNADDDRGPR RGMDDDRGPR
RGLDDDRGPW RNAAEDRISR RGADDDRGPW RNMDDDRVPR RGDDARPGPW RPFVKPGGWR
EKEKAREESW GPPRESRPSE EREWDRDKEK DRDNQDREEN DKDLERDRDR ERDGDREDRF
RRPRDEGGWR RGPAEESSSW RDSSRRDDRD REDRRRDRDD RRDLRDLRDR RDLRDDRDRR
GPPLRSEREE ASSWRRTDDR KDDRTEERDP PRRVPPPALS RDRERERERE GEKEKASWRA
EKDRESLRRT KNETDEDGWT TVRR
