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Database: UniProt/SWISS-PROT
Entry: EIF3A_RAT
LinkDB: EIF3A_RAT
Original site: 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   24-JAN-2024, entry version 117.
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; 10116-ENSRNOP00000063484; -.
DR   Ensembl; ENSRNOT00000066947.4; ENSRNOP00000063484.1; ENSRNOG00000010117.8.
DR   Ensembl; ENSRNOT00055051898; ENSRNOP00055042835; ENSRNOG00055029926.
DR   Ensembl; ENSRNOT00060000041; ENSRNOP00060000008; ENSRNOG00060000037.
DR   Ensembl; ENSRNOT00065008716; ENSRNOP00065006177; ENSRNOG00065005807.
DR   GeneID; 292148; -.
DR   KEGG; rno:292148; -.
DR   AGR; RGD:1307269; -.
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; HQAFQFC; -.
DR   OrthoDB; 10990at2759; -.
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 cell types or 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: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   Gene3D; 1.25.40.860; -; 2.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
DR   HAMAP; MF_03000; eIF3a; 1.
DR   InterPro; IPR027512; EIF3A.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR14005:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT A; 1.
DR   PANTHER; PTHR14005; EUKARYOTIC TRANSLATION INITIATION FACTOR 3, THETA SUBUNIT; 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
//
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