EIF3A_RAT
ID EIF3A_RAT Reviewed; 1354 AA.
AC Q1JU68;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 110.
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=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};
GN Name=Eif3a; Synonyms=Eif3s10;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-155.
RC TISSUE=Spinal ganglion;
RG Amgen EST program;
RT "Amgen rat EST program.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 56-1354.
RC STRAIN=Wistar;
RA Zhang H., Fang Z., Guan D., Wu Z., Zhu X., Pan Z., Liang C.;
RT "Further study on the effects of different TCM treatments on liver cancer.
RT Constructing a rat liver cDNA library and screening and analyzing of some
RT differently expressed genes.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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, EIF3L and EIF3K. 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. Interacts with EIF4G1. Also
CC interacts with KRT7 and PIWIL2. {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC Rule:MF_03000}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE94261.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CB586480; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB259154; BAE94261.1; ALT_INIT; mRNA.
DR RefSeq; NP_001040552.2; NM_001047087.2.
DR AlphaFoldDB; Q1JU68; -.
DR SMR; Q1JU68; -.
DR BioGRID; 253779; 3.
DR IntAct; Q1JU68; 6.
DR MINT; Q1JU68; -.
DR STRING; 10116.ENSRNOP00000063484; -.
DR CarbonylDB; Q1JU68; -.
DR iPTMnet; Q1JU68; -.
DR PhosphoSitePlus; Q1JU68; -.
DR jPOST; Q1JU68; -.
DR PaxDb; Q1JU68; -.
DR PRIDE; Q1JU68; -.
DR Ensembl; ENSRNOT00000066947; ENSRNOP00000063484; ENSRNOG00000010117.
DR GeneID; 292148; -.
DR KEGG; rno:292148; -.
DR CTD; 8661; -.
DR RGD; 1307269; Eif3a.
DR eggNOG; KOG2072; Eukaryota.
DR GeneTree; ENSGT00730000111063; -.
DR HOGENOM; CLU_002096_1_1_1; -.
DR InParanoid; Q1JU68; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 967904at2759; -.
DR PhylomeDB; Q1JU68; -.
DR TreeFam; TF101522; -.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-72649; Translation initiation complex formation.
DR Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-RNO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-RNO-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR PRO; PR:Q1JU68; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000010117; Expressed in spleen and 19 other tissues.
DR Genevisible; Q1JU68; RN.
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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IBA:GO_Central.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IDA:RGD.
DR GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; ISS:UniProtKB.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR GO; GO:0075525; P:viral translational termination-reinitiation; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1354
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366327"
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 1053..1062
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"
FT REPEAT 1134..1143
FT /note="22; approximate"
FT REGION 664..835
FT /note="Interaction with EIF3B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT REGION 809..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..1143
FT /note="22 X 10 AA approximate tandem repeats of [DA]-[DE]-
FT [ED]-R-[PLIGFSV]-[RPS]-[RW]-[RL]-[GNIHT]-[DGLPTAM]"
FT REGION 1262..1354
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..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1249
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:0000250|UniProtKB:Q14152"
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 1038
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152"
FT MOD_RES 1159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152"
FT MOD_RES 1233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152"
FT MOD_RES 1310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152, ECO:0000255|HAMAP-
FT Rule:MF_03000"
FT MOD_RES 1336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14152, ECO:0000255|HAMAP-
FT Rule:MF_03000"
SQ SEQUENCE 1354 AA; 163196 MW; 3ED50215624CFC07 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 TQDEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE KQRRLATLLG
LQAPPTRIGL INDMVRFNVL QYVVPEVKDL YNWLEVEFNP LKLCERVTKV LNWVREQPEK
EPELQQYVPQ LQNNTILRLL QQVAQIYQSI EFSRLTSLVP FVDAFQLERA IVDAARHCDL
QVRIDHTSRT LSFGSDLNYA TREDAPIGPH LQSMPSEQIR NQLTAMSSVL AKALEVIKPA
HILQEKEEQH QLAVTAYIKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE
LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA KAFKDIDIED
LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER AKRLEEIPLI KSAYEEQRVK
DMDLWEQQEE ERITTMQLER EKALEHKNRM SRMLEDRDLF VMRLKAARQS VYEEKLKQFE
ERLAEERHNR LEERKRQRKE ERKITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE
LREYQERVKK LEEVERKKRQ RELEIEERER RREEERRLGE DPLSRKDSRW GDRDSEGTWR
KGPEADSEWR RGPPEKEWRR ETRDDERPHR RDEDRLRRLG GDDEERESSL RPDDDRIPRR
GLDDDRGPRR GPDEDRFSRR GTDDDRPSWR NADDDRPPRR IGDDDRGSWR HTDDDRPPRR
GLDDDRPPRR GLDDERGSWR TAEEDRGPRR GMDDDRGPRR GGADDERSSW RNADDDRGPR
RGMDDDRGPR RGLDDDRGPW RNAAEDRISR RGADDDRGPW RNMDDDRVPR RGDDARPGPW
RPFVKPGGWR EKEKAREESW GPPRESRPPE EREWDRDKEK DRDNQDREEN DKDLERDRDR
ERDGDREDRF RRPRDEGGWR RGPAEESSSW RDSSRRDDRD RDDRRRDRDD RRDLRDLRDR
RDLRDDRDRR GPPLRSEREE ASSWRRTDDR KDDRTEERDP PRRVPPPTLS RERERERDRE
GEKEKASWRA EKDRESLRRT KNETDEDGWT TVRR
