ID A0A4U5QS13_POPAL Unreviewed; 1028 AA.
AC A0A4U5QS13;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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};
GN ORFNames=D5086_0000049860 {ECO:0000313|EMBL:TKS13754.1};
OS Populus alba (White poplar).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=43335 {ECO:0000313|EMBL:TKS13754.1, ECO:0000313|Proteomes:UP000309997};
RN [1] {ECO:0000313|Proteomes:UP000309997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PAL-ZL1 {ECO:0000313|Proteomes:UP000309997};
RX PubMed=30661181; DOI=10.1007/s11427-018-9455-2;
RA Liu Y.-J., Wang X.-R., Zeng Q.-Y.;
RT "De novo assembly of white poplar genome and genetic diversity of white
RT poplar population in Irtysh River basin in China.";
RL Sci. China Life Sci. 62:609-618(2019).
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. {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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TKS13754.1}.
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DR EMBL; RCHU01000132; TKS13754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U5QS13; -.
DR STRING; 43335.A0A4U5QS13; -.
DR Proteomes; UP000309997; 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:UP000309997};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03000}.
FT DOMAIN 378..569
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 863..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 149..176
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COILED 617..751
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03000"
FT COMPBIAS 863..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1028 AA; 119966 MW; 588CB521B229212C CRC64;
MQFLQGVMKD TSESGEGYLL PPLYRENQER PPFSYYLYTQ FQSLRCFFAL RDFDCNMSTF
AKPENALKRA EELINVGQKQ DALQALHDLI TSKRYRAWQK PLERIMFKYV ELCVDLRRGR
FAKDGLIQYR IVCQQVNVTS LEEVIKHFMH LSTEKAEQAR SQAQALEEAL DVDDLEADKR
PEDLMLSYVS GEKGKERSDR ELVTPWFKFL WETYRTVLEI LRNNSKLEAL YAMTAHRAFQ
FCKQYKRTTE FRRLCEIIRN HLANLNKYRD QRDRPDLSAP ESLQLYLDTR FEQLKVATEL
ELWQEAFRSI EDIHGLMCMV KKTPKASLMV VYYAKLTEIF WISSSHLYHA YAWLKLFTLQ
KSFNKNLSQK DLQMIASSVV LAALAVAPYD HTQGASHLEL ENEKERNMRM ANLIGFNLDL
KPESREALSR SSLLSELVSK GVMSCATQEV KDLYHLLEHE FLPLDLTAKV QPLLSKIFKL
GGKLTSASSV PEVHLSQYVP ALEKLATLRL LQQVSQVYQT MKIESLSQMI PFFDFSAVEK
ISVDAVKHNF IAMKLDHMKH VVLFDTQDLE SDGLRDHLTV FAESLNKTRA MIYPPTKKSS
KLGEILPGLG EIVDKEHKRL LARKSIIEKR KEEQERQLLE MEREEESRRL KQQKITEEAE
QKRLAAEYEQ RNKQRILREI EERELEEAQA LLEEHEKRSK RKGGKKPILE GEKVTKQILM
ERALSEQLRE RQEMEKKLQK LVKTMDYLER AKREEAAPLI EAAFQQRLVE EKALHEHEQQ
QEIELSRQRH DGDLREKNRL SRMLENKIIF EERVQSRRES EFNQRRAERE ERINQIVQAR
KQEREALRKK IFFVRSEEER LNRLREEEEA RKHEEAERRR KEEAEHKAKL DKIAEKQRQR
ERELEEKERI RREALLVDGP SRSSELPAGP EPGAAAAPAP GKYVPRFRRG GTEGSAQAPP
ETDRWGGGSG RPAPPDSDKW SSGSARQPPS DTDRWGSGGS RPDDRNPSSD RWGGGSKSTW
SSSRPRGR
//
