EIF3A_XENTR
ID EIF3A_XENTR Reviewed; 1391 AA.
AC A4II09;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) 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; BC135790; AAI35791.1; -; mRNA.
DR RefSeq; NP_001096173.1; NM_001102703.1.
DR AlphaFoldDB; A4II09; -.
DR SMR; A4II09; -.
DR PRIDE; A4II09; -.
DR DNASU; 100124719; -.
DR GeneID; 100124719; -.
DR KEGG; xtr:100124719; -.
DR CTD; 8661; -.
DR Xenbase; XB-GENE-994394; eif3a.
DR eggNOG; KOG2072; Eukaryota.
DR InParanoid; A4II09; -.
DR OrthoDB; 967904at2759; -.
DR Reactome; R-XTR-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-XTR-72649; Translation initiation complex formation.
DR Reactome; R-XTR-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-XTR-72702; Ribosomal scanning and start codon recognition.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; 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; 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 Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW Repeat; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT CHAIN 2..1391
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366330"
FT DOMAIN 315..498
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REPEAT 973..982
FT /note="1"
FT REPEAT 983..992
FT /note="2"
FT REPEAT 993..1001
FT /note="3; approximate"
FT REPEAT 1002..1011
FT /note="4"
FT REPEAT 1012..1021
FT /note="5"
FT REPEAT 1022..1031
FT /note="6"
FT REPEAT 1032..1041
FT /note="7"
FT REPEAT 1042..1051
FT /note="8"
FT REPEAT 1052..1061
FT /note="9"
FT REPEAT 1062..1071
FT /note="10"
FT REPEAT 1072..1081
FT /note="11"
FT REPEAT 1082..1091
FT /note="12"
FT REPEAT 1092..1101
FT /note="13"
FT REPEAT 1102..1111
FT /note="14"
FT REPEAT 1112..1120
FT /note="15"
FT REPEAT 1122..1131
FT /note="16"
FT REPEAT 1132..1141
FT /note="17"
FT REPEAT 1142..1151
FT /note="18"
FT REPEAT 1152..1161
FT /note="19"
FT REPEAT 1162..1171
FT /note="20"
FT REPEAT 1172..1181
FT /note="21"
FT REPEAT 1182..1191
FT /note="22"
FT REPEAT 1192..1201
FT /note="23"
FT REPEAT 1202..1209
FT /note="24; approximate"
FT REPEAT 1210..1219
FT /note="25"
FT REPEAT 1220..1229
FT /note="26"
FT REGION 809..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1229
FT /note="26 X 10 AA approximate tandem repeats of [DE]-[DE]-
FT [DE]-R-[GATV]-[PS]-[KRW]-R-G-[AEFGIL]"
FT COMPBIAS 809..1236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1391 AA; 164997 MW; 550E7F3DB0C5BDBD CRC64;
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVIKSKKH RTWQKIHEPI MLKYLELCVD
LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKLAEER TEAAKESSQQ MVLDIEDLDN
IQTPESVLLS AVSGEDTQDR TDRLLLTPWV KFLWESYRQC LDLLRNNSKV ERLYHDIAQQ
AFKFCLLYTR KAEFRKLCDN LRMHLSQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA
ISMELWQEAF KAVEDIHGLF ALSKKPPKPQ LMANYYNKVS TVFWKSGNTL FHASTLHRLY
HLSREMRKNL TQEEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIILE KQRRLATLLG
LQAPPTRVGL INDMVRFNML QYVVPEVKEL YNWLEMDFHP LKLCTRVTKV LDWVKEQAEK
EPELQQYVPQ LQSNTILRLL QQVAQLYQTI EFSRLASLVP FVDAFLLERA IVDAARHCDL
QVRIDHSSRT LSFGSDLNYS TREDAPFGPF LQNMPSEQIR NQLTAMSCVL SKAVGAIKPA
HVLQEKEEQH QIAITAYQKN SRKEHQRILA RRQTIEERKE RLENLNIQRE KEEMEQKEAE
LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA KAFKDIDIEN
LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER AKRLEEIPLL KKAYEEQRIN
DMELWELQEE ERISTLLLER EKAVEHKNRM SRMVEDKELF VSKLKASRQS LYEAKLKQFQ
ERLAEEKAAR LEERKRERKE ERRVNYYRDK EEEEERLREE QLKQEREEQE KVENEKREAE
QRDYQERLKK LEEQERKKRQ RELEIEERER KREEERRGGD DTFRKDSSRW GEREESGWRR
GADPDERKQV PPERDWRRGG PDSKPVINED ASNREEDENA ALRKDEEQVS SRAFEEKVSL
PDADEEKGGS WRDEDRGPKR GLEEDRGPRR GIDDAGPRRG FEEDRGPRRG IEDDRAPRRG
FDDDRGPRRG FDDDRGPRRG FDEDRGPRRG IDDDRGPRRG FDEDRTPRRG FDDDRGPRRG
FDDDRGPRRG FDEDRGPRRG FEDDRGPRRG FEDDRGPRRG FEDDRGPRRG FEDDRGPRRG
FEDDRGPRRG FDEDRGPRRG FEDDRGPRRG FDEDRTPRRG FDDDRGPRRG LDEDRGSWRG
GDDVPRRGAD DDRGPRRGAD DDRGPRRGED RDQTPWKPMA ASRPGGWRER EKAREDSWGP
PRDSQAPEER EWSRQGEDSE KDSERDRRPV REESAWRRGG DNSETPRKPS PGDSDRKDDS
DKKRPPKTDE ANPWRRGEDK DSREEERGTP RRAPAADREK SAWRTEKKEE KDTPRRIKPE
TDEDGWTTVR R