EIF3A_DANRE
ID EIF3A_DANRE Reviewed; 1267 AA.
AC Q6PCR7; Q6NYB1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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};
DE AltName: Full=eIF-3-theta {ECO:0000255|HAMAP-Rule:MF_03000};
GN Name=eif3a; Synonyms=eif3s10;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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, which is composed of 13 subunits: eif3a, eif3b, eif3c,
CC eif3d, eif3e, eif3f, eif3g, eif3h, eif3i, eif3j, eif3k, eif3l and
CC eif3m. {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; BC059196; AAH59196.1; -; mRNA.
DR EMBL; BC066670; AAH66670.1; -; mRNA.
DR RefSeq; NP_956114.2; NM_199820.2.
DR AlphaFoldDB; Q6PCR7; -.
DR SMR; Q6PCR7; -.
DR STRING; 7955.ENSDARP00000102398; -.
DR PaxDb; Q6PCR7; -.
DR PRIDE; Q6PCR7; -.
DR Ensembl; ENSDART00000111462; ENSDARP00000102398; ENSDARG00000076815.
DR GeneID; 327515; -.
DR KEGG; dre:327515; -.
DR CTD; 327515; -.
DR ZFIN; ZDB-GENE-030131-5726; eif3s10.
DR eggNOG; KOG2072; Eukaryota.
DR GeneTree; ENSGT00730000111063; -.
DR HOGENOM; CLU_002096_1_1_1; -.
DR InParanoid; Q6PCR7; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 967904at2759; -.
DR PhylomeDB; Q6PCR7; -.
DR TreeFam; TF101522; -.
DR Reactome; R-DRE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DRE-72649; Translation initiation complex formation.
DR Reactome; R-DRE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DRE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DRE-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-DRE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR PRO; PR:Q6PCR7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000076815; Expressed in presomitic mesoderm and 28 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:0005852; C:eukaryotic translation initiation factor 3 complex; ISS:UniProtKB.
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; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome; Repeat; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT CHAIN 2..1267
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366328"
FT DOMAIN 315..498
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REPEAT 956..965
FT /note="1"
FT REPEAT 966..975
FT /note="2"
FT REPEAT 976..985
FT /note="3"
FT REPEAT 986..994
FT /note="4; truncated"
FT REPEAT 995..1004
FT /note="5"
FT REPEAT 1005..1014
FT /note="6"
FT REPEAT 1015..1023
FT /note="7; truncated"
FT REPEAT 1024..1033
FT /note="8"
FT REPEAT 1034..1043
FT /note="9"
FT REPEAT 1044..1053
FT /note="10; approximate"
FT REPEAT 1054..1063
FT /note="11"
FT REPEAT 1064..1073
FT /note="12; approximate"
FT REGION 792..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1073
FT /note="12 X 10 AA approximate tandem repeats of D-[DE]-
FT [DE]-R-[GP]-[GPQT]-R-R-[GPS]-[ADFGIM]"
FT COILED 82..118
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 792..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 852
FT /note="E -> D (in Ref. 1; AAH66670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1267 AA; 151292 MW; C0781194D2E9DE4C CRC64;
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVIKSKKH RTWQKIHEPI MLKYLELCVD
LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKLAEEK TETAKEESQQ MVLDIEDLDN
IQTPESVLLS AVSGEDTQDR TDRLLLTPWV KFLWESYRQC LDLLRNNSKV ERLYHDIAQQ
AFKFCLQYTR KAEFRKLCDN LRMHLGQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA
ISMELWQEAF KAVEDIHGLF ALSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHSCTLHRLY
HLSREMRKNL TQEEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE KHRRLATLLG
LQSPPTRQSL INDMVRFNLL QYVVPEVKEL YNWLEVDFHP LKLCGRVTKV LNWVRDQAEK
ESDLQQYVPH LQNNTILRLL QQVAQIYQSI EFSRLASLVP FVDAFQLERS IVDAARHCDL
QVRIDHSSRT LSFGSDLNYS TKEDSPVGPF LQNMPSEQIR NQLTAMSSSL AKAIQVIKPA
SILQDHEEQR QQAITAYLKN ARKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE
LQKVRKAEEE RLRQEAKERE KERIMQEHEQ IKKKTVRERL EQIKKTELGA KAFKDIDIED
LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER AKRLEEIPLI KKAYEEQRIK
DMELWELQEE ERITNMKMER EKALEHKQRM SRMMEDKENF LSKIKAARSF IYEEKLKQFQ
ERLVEERKKR LEERKKQRKE DRRKAFYHQK EEEAQRIREE QLKKEREERE RLEQEQREEE
EREYQERLRK LEEQERKQRA RQQEIEERER RKEEERRAPE EKPNKEWAER EESGWRKRGE
GESEWRRPVP DRDWRQEGRE GREEPDREDR DLPFRRGGES ARRGASDEKG LRRGCDDDRG
PRRGGDDERP PRRGFDDDRG TRRGFDDDRG QRRGDDDRGP RRGMDDDRGP RRPIDDDRGP
RRSDDDRGPR RGFDDDRGPR RGMDEPRGPR RGADDDWGPR RGGDDERGGR RGMDDSGPRR
GEDSRPWKPL GRPGAGGWRE REKAREESWG PPRDSGHDDD GGERDGDDQR EGERFRERRS
AREEGSAWRR GGGGGGGGEE QSSWRDSRRE DFDREDRRER RDMRERRDDR ERDIRGPQRD
QDEGGSWRRG GEERREERKE ERDAPPRPRE RDRDSGEKST WRSDKDKENP RRTKNETDDD
GWTTVRR
