EIF3A_CAEEL
ID EIF3A_CAEEL Reviewed; 1076 AA.
AC P34339;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Egg-laying defective protein 45 {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 10 {ECO:0000255|HAMAP-Rule:MF_03000};
GN Name=egl-45 {ECO:0000255|HAMAP-Rule:MF_03000};
GN Synonyms=eif-3.A {ECO:0000255|HAMAP-Rule:MF_03000}; ORFNames=C27D11.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC Rule:MF_03000}.
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DR EMBL; FO080430; CCD63645.1; -; Genomic_DNA.
DR PIR; S44764; S44764.
DR RefSeq; NP_498698.1; NM_066297.4.
DR AlphaFoldDB; P34339; -.
DR SMR; P34339; -.
DR BioGRID; 41302; 22.
DR IntAct; P34339; 3.
DR STRING; 6239.C27D11.1; -.
DR iPTMnet; P34339; -.
DR EPD; P34339; -.
DR PaxDb; P34339; -.
DR PeptideAtlas; P34339; -.
DR PRIDE; P34339; -.
DR EnsemblMetazoa; C27D11.1.1; C27D11.1.1; WBGene00001209.
DR GeneID; 176094; -.
DR KEGG; cel:CELE_C27D11.1; -.
DR UCSC; C27D11.1; c. elegans.
DR CTD; 176094; -.
DR WormBase; C27D11.1; CE00543; WBGene00001209; egl-45.
DR eggNOG; KOG2072; Eukaryota.
DR GeneTree; ENSGT00730000111063; -.
DR HOGENOM; CLU_002096_2_2_1; -.
DR InParanoid; P34339; -.
DR OMA; WGSRDDR; -.
DR OrthoDB; 967904at2759; -.
DR PhylomeDB; P34339; -.
DR Reactome; R-CEL-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-CEL-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-CEL-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-CEL-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:P34339; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001209; Expressed in germ line (C elegans) and 4 other tissues.
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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IBA:GO_Central.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
DR GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045182; F:translation regulator activity; ISS:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR HAMAP; MF_03000; eIF3a; 1.
DR InterPro; IPR027512; EIF3A.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR14005; PTHR14005; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1076
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000123539"
FT DOMAIN 324..503
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 600..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 574..651
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 678..713
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 776..843
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 826..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..971
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 124408 MW; 54B6A961A72E5A0B CRC64;
MAPNYFQKPE AALKRAEELI QVGKESDALD TLHDTIKARR HKQWTTVHEQ IMIKHMELCV
DLKKQHLAKD ALFQYKALTQ QINVKSLETV VVHFLKLAEQ RTEDAQKQSI EKVEEIGDLD
QGDVPERLLL AVVSGAAAQD RMDRTVLAPW LRFLWDSYRN CLELLRNNAQ VEQLYHTISR
HSFTFCLRYQ RRTEFRKLCD LLRMHLNQIQ KHQYAPNVNS FRVKLTSPES LGLMQDTRLI
QLDTAIQMEL WQEAYKSAED VHGMMQLSKD KDKRTVKPAS YVNYYDKLAL VFWKAGNSLF
HAAALLQKFI IYKDMKKSFT QDEAQEQATR VLLATLSIPE GSDSPSDLSR NLDIEDQHVA
NMRLLSNLLR LPIAPTKNGI LKEAARIGVP EAAGQTAKDL YKLLESNFSP LKVAKDVQSV
LDTVTRPDHL QYVESLQAVA AVKALKQVSV IYEAISWERI RKIIPFYSDL ALERLVVEAS
KHRIVKAQLD HRADCVRFGS SDATLAGGVD ECDNNEGFTG DDTQLGVEGV RNHLEAMYTR
LRGLVEGLDA EKRRKEILKK IEGQVTSYEK NRPTEIERIH RRKKMLENYK ENWERVKAEK
TAAAATEQAK REEAARAEEM KRLDEQNKES ERKRKQAEQD EIQKKIKQDQ LYKMQQNAIY
QEIIKEKGLE QFRDMDPEQV LREQRERLDK ERAETQRRLQ QQEKNFDHHV RALHLEELNE
RRAVMNMRLS EAPKLHDLYE EARIAKEIAA HDSHVKLWGM WDQVRDATFD WVESVKIDNQ
ETLEKKLSDW QAKLEAVRNN RLAERAEDRK KKRKEDAIQA KIAEERKKRE EEERARLQVI
EGQRRQHNDG RGRREMENSV AMQDNDWRRN PPRESLPPRE TRPMRDGPTR EPREFRGDRD
REPREPFREV PSSKADTDNS WRSSAQPTRK PDDRRSDEFR RNDDVRRNDD VRRNDPPRPA
SKADTGDKWE RGVKPVVSPP KTDAPSVSEP KSEGPKRFVP PHLRNRQGGG GAGGSEEQSA
PARSGNSNVT SPPDRAQGLR GPPPTGRNSL PRRDGPPPRS NNTGNTGNAD SGSWRK
