ID A0A3Q3WPH6_MOLML Unreviewed; 811 AA.
AC A0A3Q3WPH6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000010904.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000010904.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is involved in protein
CC synthesis of a specialized repertoire of mRNAs and, together with other
CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation.
CC {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. {ECO:0000256|HAMAP-Rule:MF_03000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03000}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000256|HAMAP-
CC Rule:MF_03000}.
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DR AlphaFoldDB; A0A3Q3WPH6; -.
DR STRING; 94237.ENSMMOP00000010904; -.
DR Ensembl; ENSMMOT00000011092.1; ENSMMOP00000010904.1; ENSMMOG00000008408.1.
DR OMA; DHMKNVV; -.
DR Proteomes; UP000261620; Unplaced.
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 Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03000};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620};
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 775..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 558..619
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COILED 652..686
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
SQ SEQUENCE 811 AA; 96530 MW; C4C7D347CA5E70EE CRC64;
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVIKSKKH RTWQKIHEPI MLKYLELCVD
LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKLAEDK TETAKEESQQ MVLDIEDLDN
IQTPESVLLS AVSGEDTQDR TDRLLLTPWV KFLWESYRQC LDLLRNNSKV ERLYHDIAQQ
AFKFCLQYTR KAEFRKLCDN LRMHLGQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA
ISMELWQEAF KAVEDIHGLF ALSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHASTLHRLY
HLSREMRKNL TQDEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE KHRRLATLLG
LQSPPTRQTL INDMVRFNLL QYVVPEVKEL YNWLEVDFHP LKLSGRVTKV LNWVRDQAEK
EVELQQYVPH LQNNTILRLL QQVAQIYQSI EFTRLATLVP FVDAFQLERS IVDAARHCDL
QVRIDHTSRT LSFGSDLNYS TREDAPVGPF LQNMPSEQIR NQLTAMSASL AKAIYVIKPV
SILQERDEHH QQAIAAYLKN ARKDHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE
MQKREKERIM QEHEQIKKKT VRERLEQIKK TELGAKAFKD IDIEDLEELD PDFIMAKQVE
QLEKEKKELQ ERLKNQEKKI DYFERAKRLE EIPLIKKAYE EQRVKDMELW ELQEEERISN
MKVEREKALE HKKRMSRMME DKENFLSKIT AARSFIYEEK LKAFQERLVE ERKRRLEERR
KQRTEDRRNA FYRQKEEEAQ RIHEEQLKKG D
//
