EIF3E_PONAB
ID EIF3E_PONAB Reviewed; 445 AA.
AC Q5R8K9; Q5R6H2;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit E {ECO:0000255|HAMAP-Rule:MF_03004};
DE Short=eIF3e {ECO:0000255|HAMAP-Rule:MF_03004};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 6 {ECO:0000255|HAMAP-Rule:MF_03004};
DE AltName: Full=eIF-3 p48 {ECO:0000255|HAMAP-Rule:MF_03004};
GN Name=EIF3E {ECO:0000255|HAMAP-Rule:MF_03004};
GN Synonyms=EIF3S6 {ECO:0000255|HAMAP-Rule:MF_03004}, EIF3SE,
GN INT6 {ECO:0000255|HAMAP-Rule:MF_03004};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is required for several steps in the initiation
CC of protein synthesis. The eIF-3 complex associates with the 40S
CC ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-
CC 2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex
CC (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC
CC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also
CC required for disassembly and recycling of post-termination ribosomal
CC complexes and subsequently prevents premature joining of the 40S and
CC 60S ribosomal subunits prior to initiation. The eIF-3 complex
CC specifically targets and initiates translation of a subset of mRNAs
CC involved in cell proliferation, including cell cycling, differentiation
CC and apoptosis, and uses different modes of RNA stem-loop binding to
CC exert either translational activation or repression. Required for
CC nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to
CC divert mRNAs from translation to the NMD pathway. May interact with
CC MCM7 and EPAS1 and regulate the proteasome-mediated degradation of
CC these proteins. {ECO:0000255|HAMAP-Rule:MF_03004}.
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. The eIF-3 complex appears to include 3 stable modules: module A
CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. Interacts with COPS3, COPS6,
CC COPS7 (COPS7A or COPS7B), EIF4G1, EPAS1, MCM7, NCBP1, PSMC6, TRIM27 and
CC UPF2 (By similarity). Interacts with IFIT1 and IFIT2 (By similarity).
CC Interacts with BZW2/5MP1 (By similarity).
CC {ECO:0000250|UniProtKB:P60228, ECO:0000255|HAMAP-Rule:MF_03004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03004}.
CC Nucleus, PML body {ECO:0000255|HAMAP-Rule:MF_03004}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit E family. {ECO:0000255|HAMAP-
CC Rule:MF_03004}.
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DR EMBL; CR859743; CAH91901.1; -; mRNA.
DR EMBL; CR860517; CAH92644.1; -; mRNA.
DR RefSeq; NP_001126100.1; NM_001132628.1.
DR AlphaFoldDB; Q5R8K9; -.
DR SMR; Q5R8K9; -.
DR STRING; 9601.ENSPPYP00000021115; -.
DR PRIDE; Q5R8K9; -.
DR GeneID; 100173055; -.
DR KEGG; pon:100173055; -.
DR CTD; 3646; -.
DR eggNOG; KOG2758; Eukaryota.
DR HOGENOM; CLU_031132_0_1_1; -.
DR InParanoid; Q5R8K9; -.
DR OMA; TWGKLAC; -.
DR OrthoDB; 1151808at2759; -.
DR TreeFam; TF101518; -.
DR Proteomes; UP000001595; Chromosome 8.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
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 GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR HAMAP; MF_03004; eIF3e; 1.
DR InterPro; IPR016650; eIF3e.
DR InterPro; IPR019010; eIF3e_N.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10317; PTHR10317; 1.
DR Pfam; PF09440; eIF3_N; 1.
DR Pfam; PF01399; PCI; 1.
DR PIRSF; PIRSF016255; eIF3e_su6; 1.
DR SMART; SM01186; eIF3_N; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Initiation factor; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03004"
FT CHAIN 2..445
FT /note="Eukaryotic translation initiation factor 3 subunit
FT E"
FT /id="PRO_0000289997"
FT DOMAIN 221..398
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 4..128
FT /note="Sufficient for interaction with EPAS1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03004"
FT REGION 9..195
FT /note="Sufficient for interaction with TRIM27"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03004"
FT REGION 351..445
FT /note="Sufficient for interaction with MCM7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03004"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P60228, ECO:0000255|HAMAP-
FT Rule:MF_03004"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60228"
FT MOD_RES 439
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P60229"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60228"
FT MOD_RES 445
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P60229"
FT CONFLICT 322
FT /note="D -> G (in Ref. 1; CAH91901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 52221 MW; A5368651DD0DDD0C CRC64;
MAEYDLTTRI AHFLDRHLVF PLLEFLSVKE IYNEKELLQG KLDLLSDTNM VDFAMDVYKN
LYSDDIPHAL REKRTTVVAQ LKQLQAETEP IVKMFEDPET TRQMQSTRDG RMLFDYLADK
HGFRQEYLDT LYRYAKFQYE CGNYSGAAEY LYFFRVLVPA TDRNALSSLW GKLASEILMQ
NWDAAMEDLT RLKETIDNNS VSSPLQSLQQ RTWLIHWSLF VFFNHPKGRD NIIDLFLYQP
QYLNAIQTMC PHILRYLTTA VITNKDVRKR RQVLKDLVKV IQQESYTYKD PITEFVECLY
VNFDFDGAQK KLRECESVLV NDFFLVACLE DFIENARLFI FETFCRIHQC ISINMLADKL
NMTPEEAERW IVNLIRNARL DAKIDSKLGH VVMGNNAVSP YQQVIEKTKS LSFRSQMLAM
NIEKKLNQNS RSEAPNWATQ DSGFY
