| Description | This domain is formed by HEAT repeats, and it is found in the two human paralogs eIF5-mimic protein 1 and 2 (5MP1 and 5MP2) and related proteins. It is located at the N-terminal, and it likely contributes to the role of these proteins in translation regulation. It shares some sequence, structural, and functional similarities with the corresponding region of eIF4G.eIF5-mimic proteins 1 and 2 5MP1 and 5MP2 (also known as basic leucine zipper and W2 domain-containing proteins 1 and 2 (BZW1 and BZW2)) act as competitors of eIF5 and can inhibit general translation by interaction with eIF2 and inhibiting the tertiary complex binding to the ribosome [ , ]. These translation regulatory proteins exist in nearly all eukaryotes except in nematodes, yeasts, and some protozoans. 5MP1/2 contain MA3- and W2-type () C-terminal HEAT domains that resemble the HEAT domain of eIF5 [ ]. They enable cadherin binding activity []. The orthologue in Drosophila melanogaster, known as protein krasavietz (kra), is involved in several processes, including behavioural response to ethanol, long-term memory, and positive regulation of filopodium assembly. Kra is located in several cellular components, including the axonal growth cone, filopodium, and neuronal cell body [, ].The elf5-mimic protein family functions as translation initiation regulators. They are known to repress non-AUG-initiated translation and repeat-associated non-AUG (RAN)-initiated translation, acting as competitive inhibitors of eukaryotic translation initiation factor 5 (EIF5). These proteins increase the accuracy of translation initiation by competing with EIF5 for interaction with EIF2S2 within the 43S pre-initiation complex, in a manner dependent on binding to EIF3C. Additionally, some members of this family are involved in enhancing histone H4 gene transcription, although they do not directly bind to DNA [ , , ]. | Name | 5MP1/2-like, HEAT domain |
| Short Name | HEAT_5MP1_2 | Type | Domain |
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