ID A0A4W5PAF7_9TELE Unreviewed; 1208 AA.
AC A0A4W5PAF7;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 Hucho hucho (huchen).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Hucho.
OX NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000059073.1, ECO:0000313|Proteomes:UP000314982};
RN [1] {ECO:0000313|Proteomes:UP000314982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Macqueen D.J., Gundappa M.K.;
RT "Genome assembly of Danube salmon.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSHHUP00000059073.1}
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 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; A0A4W5PAF7; -.
DR Ensembl; ENSHHUT00000061090.1; ENSHHUP00000059073.1; ENSHHUG00000034940.1.
DR GeneTree; ENSGT00730000111063; -.
DR Proteomes; UP000314982; Unassembled WGS sequence.
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:UP000314982};
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 794..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 565..634
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COILED 674..701
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 794..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1208 AA; 142543 MW; ED419B3FE1951ECA CRC64;
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVIKSKKH RTWQKIHEPI MLKYLELCVD
LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKLAEEK TETAKGESQQ MVLDIEDLDN
IQTPESVLLS AVSGEDTQDR TDRLLLTPWV KFLWESYRQC LDLLRNNSKV ERLYHDIAQQ
AFKFCLQYTR KAEFRKLCDN LRMHLGQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA
IAMELWQEAF KAVEDIHGLF ALSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHACTLHRLY
HLSREMRKNL TQEEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE KHRRLATLLG
LQSPPTRQSL INDMVRFNLL QYIVPEVKEL YNWLEMDFHP LKLSGRVTKV LNWVRDQSEK
EADLQQYVPH LQSNTILRLL QQVAQIYQSI EFNRLASLVP FVDPFQLERS IVDAARHCDL
QVRIDHTTRN LSFGSDLNYS TKEDSPVGPF LQNMPSAQIR NQLTAMSSSL AKAIQVIKPA
SMLKEREEQS QLAITAYLKN GRKEHQRILA RRQTIEERKE RLENLNIQRE KEELEQREAE
LQKVRKAEEE RLRQEAKERE KERIMQEHEQ IKKKTVRERL EQIKKTELGA KAFKDIDIED
LEDLDPDFIM SKQVEQLEKE KRELQDRLKN QEKKIDYFER AKRLEEIPLI KKAYEEQRVK
DMELWELQEE ERISNMKVER ERALEHKQRM SRMMEDKENF VGKITDARSF IYEEKLKQFQ
ERLVEERKKR LEERKIQRKE DRRNTFYRQK EEEAQRIHEE QLKKEREERE RIEQEAREAE
EAEYQERLRK LEEQERKQRA RQQEIEERER RREEEMRAPA RSEEKPRGEA KDWGAEKEEG
GGGGWRRRTE VESERRRPVP DNDAVPDKDW RADGGEDKDR EPPSRRGDGP RRGGADDRGP
PRRGFGDDDR PLRRGMDEDR PPRRTFGDDD RGLRRGGDED RAPRRGFDDG PRRGFDEDRG
PRRGFDDGPR RGTDESRAPR RGADDDTWGP RRGGDDERGG PRDDKPWKPA GRPVALVSAS
GGGWREREKA REESWGPPRE GGGSKEAEEG EREEKQESER FPERRPPREE GGGGGAWRRP
GADDEAPKKS WRDSARQEEP DREDRPPIRR ERPERRDDRD RPPPSREPEE GKLSLLSPLQ
PTLLATCF
//
