Protein: Elongator complex protein 1 (Q9VGK7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the elongator complex, which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. ELP1 binds to tRNA, mediating interaction of the elongator complex with tRNA (By similarity). Binding by the elongator complex stabilizes microtubules and promotes their growth. This induces central spindle asymmetry, promoting polarized signaling endosome trafficking during asymmetric cell division and cell fate assignation of sensory organ precursor cells. Involved in protein synthesis-dependent long- term memory formation, probably as part of the elongator complex
Subcellular location: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. Note=During asymmetric cell division of sensory organ precursor cells the elongator complex preferentially binds and stabilizes microtubules on the anterior side (pIIb daughter cell) of the spindle
Sequence: MRNLKLRYCKELNAVAHPQHLLLQPELNGGASDIYFVVADNKIYAVQESGDVRLKVIADLPDIVGVEFLQLDNAICVASGAGEVILVDPQTGATSEGTFCDVGIESMAWSPNQEVVAFVTRTHNVVLMTSTFDVIAEQPLDAELDPDQQFVNVGWGKKETQFHGSEGKQAAKQKESDSTFIRDEQELNQDVSISWRGDGEFFVVSYVAAQLGRTFKVYDSEGKLNHTAEKSANLKDSVVWRPTGNWIAVPQQFPNKSTIALFEKNGLRHRELVLPFDLQEEPVVQLRWSEDSDILAIRTCAKEEQRVYLYTIGNYHWYLKQVLIFEQADPLALLHWDTRCGAEHTLHVLKESGKHLVYRWAFAVDRNNSIVGVIDGKRLLLTDFDEAIVPPPMSKIVLKFETYINAFISHGTSLWVYTCDRKIYLNEHIHTLGKELQKPIMLMPDAELSGLHLANLTHFSPHYLLATHSSAGSTRLLLLSYKDNDNKPGEWFYRVHSSVRINGLVNAVAVAPYAMNEFYVQTVNNGHTYEVSLKADKTLKVERSYVQLHEPADQIDWVIVKGCIWDGYTGALVTLRNQHLLHIDGYRIGEDVTSFCVVTNYLVYTQLNAMHFVQLDDRRQVASRNIERGAKIVTAVARKARVVLQLPRGNLEAICPRVLVLELVGDLLERGKYQKAIEMSRKQRINLNIIFDHDVKRFVSSVGAFLNDINEPQWLCLFLSELQNEDFTKGMYSSNYDASKQTYPSDYRVDQKVEYVCRLLEQQMNRFVSRFRLPLITAYVKLGCLEMALQVIWKEQQEDASLADQLLQHLLYLVDVNDLYNVALGTYDFGLVLFVAQKSQKDPKEFLPYLNDLKALPIDYRKFRIDDHLKRYTSALSHLAACGEQHYEEALEYIRKHGLYTDGLAFYREHIEFQKNIYVAYADHLRAIAKLDNASLMYERGGQLQQALLSAKHTLDWQRVLVLAKKLSEPLDQVAQSLVGPLQQQGRHMEAYELVKEHCQDRKRQFDVLLEGHLYSRAIYEAGLEDDDVSEKIAPALLAYGVQLESSLQADLQLFLDYKQRLLDIRRNQAKSGEGYIDTDVNLKEVDLLSDTTSLHSSQYSGTSRRTGKTFRSSKNRRKHERKLFSLKPGNPFEDIALIDALHNHVTKIAQQQQPVRDTCKALLQLANAADADPLAAALQREFKTLLQAVDAALDEIWTPELRGNGLMADHLTGPNVDYLALQKEQRYALLSPLKRFKPQLIMMDWQHEILQ
InterPro domains: - IPR056165: ELP1, N-terminal second beta-propeller (domain) [373-633]
- IPR056169: ELP1, three-helical bundle (domain) [1031-1197]
- IPR006849: Elongator complex protein 1 (family) [1-1251]
- IPR056166: ELP1, TPR domain (domain) [860-1018]
- IPR015943: WD40/YVTN repeat-like-containing domain superfamily (homologous_superfamily) [31-315]
- IPR056164: ELP1, first N-terminal beta-propeller (domain) [1-338]
- IPR056167: ELP1, alpha-solenoid (domain) [657-853]
Interaction partners: - Elongator complex protein 3
- Elongator complex protein 2
- Elongator complex protein 5
- Protein KTI12 homolog
- Elongator complex protein 4
- Tetraspanin 68C, isoform A
- EG:8D8.4 protein
- Diphthamide biosynthesis protein 3
- Elongator complex protein 6
- Translin
Gene Ontology annotations:
Molecular Function (MF): GO:0003674 (molecular function), GO:0005488 (binding), GO:0005515 (protein binding), GO:0043621 (protein self-association)
Biological Process (BP): GO:0008150 (biological process), GO:0050789 (regulation of biological process), GO:0009987 (cellular process), GO:0065007 (biological regulation), GO:0019222 (regulation of metabolic process), GO:0071840 (cellular component organization or biogenesis), GO:0060255 (regulation of macromolecule metabolic process), GO:0016043 (cellular component organization), GO:0006325 (chromatin organization), GO:0010468 (regulation of gene expression), GO:0040029 (epigenetic regulation of gene expression), GO:0007549 (dosage compensation), GO:0009047 (dosage compensation by hyperactivation of X chromosome)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005737 (cytoplasm), GO:0005622 (intracellular anatomical structure)