ID A0A673Y4N5_SALTR Unreviewed; 1226 AA.
AC A0A673Y4N5;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=LOC115193992 {ECO:0000313|Ensembl:ENSSTUP00000029412.1};
GN Synonyms=EIF3A {ECO:0000256|HAMAP-Rule:MF_03000}, EIF3S10
GN {ECO:0000256|HAMAP-Rule:MF_03000};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000029412.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000029412.1}
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}.
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 AlphaFoldDB; A0A673Y4N5; -.
DR Ensembl; ENSSTUT00000030784.1; ENSSTUP00000029412.1; ENSSTUG00000010537.1.
DR GeneTree; ENSGT00730000111063; -.
DR Proteomes; UP000472277; 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:UP000472277};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 313..496
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 787..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 563..632
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COILED 672..699
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 787..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..1226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1226 AA; 145233 MW; 7923ECCB80CF361B CRC64;
ARFGLRKPPE ALQLQFLEVG KKQPALDVLY DVIKSKKHRT WQKIHEPIMV KYLELCVDLR
KSHLAKEGLY QYKNICQQVN IKSLEDVVRA YLKLAEEKTE TAKGESQQMV LDIEDLDNIQ
TPESVLLSAV SGEDTQDRTD RLLLTPWVKF LWESYRQCLD LLRNNSKVER LYHDIAQQAF
KFCLQYIRKA EFRKLCDNLR MHLGQIQRHH NQSTAINLNN PESQSMHLET RLVQLDSAIA
MELWQEAFKA VEDIHGLFAL SKKPPKPQLM ANYYNKVSTV FWKSGNALFH ACTLHRLYHL
SREMRKNLTQ EEMQRMSTRV LLATLSIPIT PERTDIARLL DMDGIIVEKH RRLATLLGLQ
SPPTRQSLIN DMVRFNLLQY IVPEVKELYN WLEMDFHPLK LSGRVAKVLN WVRDQSEKEA
DLQQYVPHLQ SNTILRLLQQ VAQIYQSIEF SRLASLVPFV DAFQLERSIV DAARHCDLQV
RIDHTTRNLS FGSDLNYSTK EDSPVGPFLQ NMPSAQIRNQ LTAMSSSLAK AIQVIKPASM
LQEREEQSHL AITAYLKNGR KEHQRILARR QTIEERKERL ENLNIQREKE ELEQREAELQ
KVRKAEEERL RQEAKEREKE RIMQEHEQIK KKTVRERLEQ IKKTELGAKA FKYFDIENLE
DLDPDFIMSK QVEQLEKEKR ELQDRLKNQE KKIDYFERAK RLEEIPLIKK AYEEQRVKDM
ELWELQEEER ISNMKVDREK ALEHKQRMSR MMQDKENFVG KITDARSFIY EEKLKQFQER
LVEERTKRRE ERKIHRKEDR RNTFYRNKEE EAQRIHEEQL KKEREERERI EQEAREAEEA
VYQERLAKLE EQERKQRARQ QEIEERERRR EEEMKTPARS EEKPRGETKV AYYTSPPTSP
PRALSHSLTL PVEDWRAEGR EDVGEDRDRE PPFRRGGDGP RRGGDDDRGP PRRGFGDDDR
PLRRGMDEDR PPRRTFGDDD RGPRRGGDED RGPRRGFDDG PRRGFDDGPR RGMDESRGPR
RGADDDTWGP RRGGDDERGG PRDDKPWKPA VRPGGGWRER EKAREESWGP PRESGGRKED
EEGEREERED KQESERFPER RGGAWRRPGA DEAPKKSWRD SVRQEEPARE DRPPIRRERP
DRRDDRERPP PSREPEEGGS WRRAGDDKRE ERKEERPTPP RPREGEREED GEKSSWRSEK
DKENAGRSKK TTDETDDDGW TTVARR
//