EIF3A_DICDI
ID EIF3A_DICDI Reviewed; 1030 AA.
AC Q86B20; Q55A61;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=Eukaryotic translation initiation factor 3 subunit 10 {ECO:0000255|HAMAP-Rule:MF_03000};
GN Name=eif3A; Synonyms=eif3s10; ORFNames=DDB_G0272078;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP PROTEIN SEQUENCE OF 488-501 AND 626-632, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=AX2;
RA Bienvenut W.V., Ura S., Insall R.H.;
RL Submitted (JUL-2009) 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: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; AAFI02000007; EAL71400.1; -; Genomic_DNA.
DR RefSeq; XP_645332.1; XM_640240.1.
DR AlphaFoldDB; Q86B20; -.
DR SMR; Q86B20; -.
DR STRING; 44689.DDB0233930; -.
DR PaxDb; Q86B20; -.
DR EnsemblProtists; EAL71400; EAL71400; DDB_G0272078.
DR GeneID; 8618294; -.
DR KEGG; ddi:DDB_G0272078; -.
DR dictyBase; DDB_G0272078; eif3A.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_294480_0_0_1; -.
DR InParanoid; Q86B20; -.
DR OMA; VMYQTTA; -.
DR PhylomeDB; Q86B20; -.
DR Reactome; R-DDI-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DDI-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DDI-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DDI-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:Q86B20; -.
DR Proteomes; UP000002195; Chromosome 2.
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; ISS:dictyBase.
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:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
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 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Direct protein sequencing; Initiation factor;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..1030
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000330329"
FT DOMAIN 308..483
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 576..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 94..126
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 527..620
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 720..772
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 576..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 120076 MW; C39B1CE7EE40429E CRC64;
MSTQQALAQA NEHALSQAND LIKVGSKLRA LSVLRDLLSD RSQWHSSLEQ IMSLYVSLCA
EQLDYQSLRD GIHHFKVSIM SQKEFSIVPL ENIFKEIITP IEQKVDELKE KIEKENQENP
LVEQNEISLI DPQQTLLFSY MKYLFEAYKA MIEVLTRQNT KFEHTKFDHS KFDSTLLKIS
TQALNYCSKY QRKPDFMVLT ELFRSSIEQL FKVPSLDTVN THIEIRFHQL TVAISLGLYL
IAYKSIEDIN IMLFSLLVKP KPVVLATYYQ KLAQVYWITN AHLLHAYALY KHYVYNKNYN
MNFTQADSQL YSSVLLVAAL SSPIQEVNQN QSLLQFDSQS QRAMGLASLL SLQSIPKRET
FLVDVRKVTN EVYPELADLA SIFEKKTSPL MFAKLLEPKI KFIEGHAQLS QYLKPFLRVV
FTKIALQVSK VYEVIKIEEF IKLVPFYTKT QIELYLLESI KRKLIGARID HKNGVIRFGH
YDFDSAKISD QLSNLATGVG KALNMIEPEK KQQQHDKLKK EVYVKIINSL QDEHRRILAR
KEIIEKKKIY MEQQDRIKKQ KEHEELQKKI QEKVARDQQR LKEDMERREK EQAEEESQQN
QLDQTINAID KAKVEMKAKI AKIAKQLYIL ERAYREEELP VVESLQKTKA VEDKQYFEST
QAEFLKLHRE VHDRNVTEKA RLNRIVPEYQ KFTQAVIEER KKQLPALQKE QEKRFQEFLI
QQEQDVQERK AKREKARIAA AQEKARKEEQ ERERLEQEHL EQERLEEERK NAPYVPPSSR
RTFRDDDDER EESGRWGGRR GGDDFGRSKA DEGDRWGRRE DAPPPRRDEG GDRWGRREDA
PPPRRDEGGD RWGKREDAPP PRRDEGGWGR RDDAPPPRRD EGGDRWGRRD DAPPRRDDAP
PPRRDDAPPP RRDEGGDRWG RRDDAPPRRD GGGSGGFGGR RDDAPPRRDE GGDRWGRRED
APPPRRDEGG DRWGRRDDAP PRRDGGGGSG FGRNQGAQGD QNDSWRSDNK KEENKKDADG
WQTVGAKKRY
