ID A0A2Y9MQS8_DELLE Unreviewed; 1349 AA.
AC A0A2Y9MQS8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ECO:0000313|RefSeq:XP_022424335.1};
GN Synonyms=EIF3S10 {ECO:0000256|HAMAP-Rule:MF_03000};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022424335.1};
RN [1] {ECO:0000313|RefSeq:XP_022424335.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022424335.1};
RG RefSeq;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_022424335.1; XM_022568627.2.
DR STRING; 9749.A0A2Y9MQS8; -.
DR Ensembl; ENSDLET00000013224; ENSDLEP00000011990; ENSDLEG00000008753.
DR KEGG; dle:111172257; -.
DR InParanoid; A0A2Y9MQS8; -.
DR OrthoDB; 10990at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
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 GO; GO:0075522; P:IRES-dependent viral translational initiation; IEA:Ensembl.
DR GO; GO:0075525; P:viral translational termination-reinitiation; IEA:Ensembl.
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 ECO:0000313|RefSeq:XP_022424335.1};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03000};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
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..1349
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"
SQ SEQUENCE 1349 AA; 162920 MW; CFA83382EC924EC7 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 LKLCDRVTKV 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 KMMKEREERE RAERAKREEE
LREYQERVKK LEEVERKKRQ RELEIEERER RREEERRLGD DSLSRKDPRW GDRDAEGTWR
KVPEIDSEWR RGPPEKEWRR GEGRDEERPQ RRDEERPKRL GDDEERESSL RPDDDRVPRR
GMDDDRGPRR GPDEDRFSRR GADDDRPFWR NADEDRPLRR IGDEDRASWR QADDDRPPRR
GLDEDRGSWR TADEDRGPRR GMDEDRGLRR GAADEERPSW RNADDDRPRR GVDDDRGPRR
GLDDDRGPWR SSDDDRFSRR GVDDDRGPWR NTDDDRISRR ADDDRISRRA DDDRRPGPWR
PFVKPGGWRE KEKAREESWG PPRESRPSED REWDREKERD RDNQDRDEND RDPERERDRE
RDGDREDRFR RPRDEAGWRR GPAEESSSWR DASRRDDRER DDRRRERDER RDLRERRDDR
DRRGPPLRPE REEVSSWRRA DDRKDDRAEE RDAPRRVPPA ALSRDRERDR DRDREGEKEK
TSWRAEKDRE SLRRTKNETD EDGWTTVRR
//
