ID A0A4W2CE37_BOBOX Unreviewed; 1376 AA.
AC A0A4W2CE37;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000256|HAMAP-Rule:MF_03000};
DE Short=eIF3a {ECO:0000256|HAMAP-Rule:MF_03000};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 10 {ECO:0000256|HAMAP-Rule:MF_03000};
DE AltName: Full=eIF-3-theta {ECO:0000256|HAMAP-Rule:MF_03000};
GN Name=EIF3A {ECO:0000256|HAMAP-Rule:MF_03000};
GN Synonyms=EIF3S10 {ECO:0000256|HAMAP-Rule:MF_03000};
OS Bos indicus x Bos taurus (Hybrid cattle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=30522 {ECO:0000313|Ensembl:ENSBIXP00000004607.1, ECO:0000313|Proteomes:UP000314981};
RN [1] {ECO:0000313|Ensembl:ENSBIXP00000004607.1, ECO:0000313|Proteomes:UP000314981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Low W.Y., Tearle R., Bickhart D.M., Rosen B.D., Koren S., Rhie A.,
RA Hiendleder S., Phillippy A.M., Smith T.P.L., Williams J.L.;
RT "Haplotype-resolved cattle genomes.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBIXP00000004607.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|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:0000256|HAMAP-Rule:MF_03000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03000}.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {ECO:0000256|HAMAP-Rule:MF_03000}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000256|HAMAP-
CC Rule:MF_03000}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03000}.
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DR SMR; A0A4W2CE37; -.
DR STRING; 30522.A0A4W2CE37; -.
DR Ensembl; ENSBIXT00000007472.1; ENSBIXP00000004607.1; ENSBIXG00000010931.1.
DR OMA; EHITNKR; -.
DR Proteomes; UP000314981; Chromosome 26.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_03000};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03000};
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03000};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03000};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW Reference proteome {ECO:0000313|Proteomes:UP000314981};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT DOMAIN 315..498
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 664..835
FT /note="Interaction with EIF3B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT REGION 810..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 558..634
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COILED 667..701
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 866..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1376 AA; 166049 MW; 244C2777F1F74A0E 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 INDMVRFNVL QYVVPEVKDL YNWLEVEFNP LKLCERVTKV LNWVREQPEK
EPELQQYVPQ LQNNTILRLL QQVAQIYQSI EFSRLTSLVP FVDAFQLERA IVDAARHCDL
QVRIDHTSRT LSFGSDLNYA TREDAPIGPH LQSMPSEQIR NQLTAMSSVL AKALEVIKPA
HILQEKEEQH QLAVTAYLKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE
LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA KAFKDIDIED
LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER AKRLEEIPLI KSAYEEQRIK
DMDLWEQQEE ERITTMQLER EKALEHKNRM SRMLEDRDLF VMRLKAARQS VYEEKLKQFE
ERLAEERHNR LEERKRQRKE ERRITYYREK EEEEQRRAEE KMLKEREERE RAERAKREEE
LREYQERVKK LEEVERKKRQ RELEIEERER RREEERRLGD DSLSRKDSRW GDRDTEGTWR
KGPETDSEWR RGPPEKEWRR GEGRDEERPH RRDDDRPRRL GDDEERESSV RPDDDRIPRR
GMDDDRGPRR GPDEDRFSRR GADDDRPSWR STDDDRPPRR IGDEDRGSWR HADDDRPPRR
GLDEDRGSWR TADEDRGPRR GLDEDRGPRR GGAEDERSSW RNADDDRPRR GMDDDRGPRR
GLDDDRGPRR GLDDDRGPWR NTDDDRFSRR GADDDRFSRR GADDDRGPWR NMDDDRISRR
ADDDRIPRRG DDSRPGPWRP FVKPGGWREK EKAREESWGP PRDSRPSEDR EWEREKERDR
DNQDRDENDR DPERERDRER ERERDRERDG DRDDRFRRPR DEGGWRRGPA EESSSWRDAS
RRDDRDRDDR RRERDDRRDL RDRRDDRDRR GPPLRSEREE VSSWRRTDDR KDDRAEERDT
PRRVPPAALS RDRDRDRDRE REGEKEKTSW RAEKDRESLR RTKNETDEDG WTTVRR
//
