Protein: Dynactin subunit 1 (150 kDa dynein-associated polypeptide) (DAP-150) (DP-150) (Dynactin 1 subunit p150) (Protein glued) (P13496)
Organism: Drosophila melanogaster (Fruit fly)
Function: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14203}.
Interaction partners:
- Dynactin subunit 2
- CG9893 protein
- Actin-related protein 10, isoform A
- Actin-related protein 1
- Dynactin subunit 4
- Cytoplasmic dynein 1 intermediate chain
- Dynactin subunit 6
- Dynein heavy chain, cytoplasmic
- Dynactin subunit 5
- F-actin-capping protein subunit beta
Sequence:
MSEKNLKVGARVELTGKDLLGTVAYVGMTSFAVGKWVGVVLDEPKGKNSGSIKGQQYFQCDENCGMFVRPTQLRLLEAAPGSRRSIEDVSGATPTAAQPTKARLSSSRTSLSSSRQSLLGSRTQLTTSLSERTASSSSIGPRKSLAPQNSKDKESPSTSLAEGAPAASGGNGAASHASSKRASFVETGFLEILKPQFTPSQPLRSPSFTMPSNSGAEDKVALLEAQKTSAELQAQLADLTEKLETLKQRRNEDKERLREFDKMKIQFEQLQEFRTKIMGAQASLQKELLRAKQEAKDAIEAKEQHAQEMADLADNVEMITLDKEMAEEKADTLQLELESSKERIEELEVDLELLRSEMQNKAESAIGNISGGGDSPGLSTYEFKQLEQQNIRLKETLVRLRDLSAHDKHDIQKLSKELEMKRSEVTELERTKEKLSAKIDELEAIVADLQEQVDAALGAEEMVEQLAEKKMELEDKVKLLEEEIAQLEALEEVHEQLVESNHELELDLREELDLANGAKKEVLRERDAAIETIYDRDQTIVKFRELVQKLNDQLTELRDRNSSNEKESLQDPSLKMVTETIDYKQMFAESKAYTRAIDVQLRQIELSQANEHVQMLTAFMPESFMSRGGDHDSILVILLISRIVFKCDIVVSQTRERFPPVDAITREAVTQGHAVQQYAFKCRLLHYVHSLQCALHQILYGLNSCQPDTLLRAGSSLPEMVAQEKIVDGIIELLKSNQLDENSTTDNIEKCVAFFNAMNSVLLAGEQLLNEIQMIRDCVASLGAACESILSDTAIAKVIIQEAGATSDSVLLIQFLNENMESVRQQVKLIKRRLPSDQHVIKSGLSQHKVEAMRGLAQNISRIMSAMHQATKQSLAAIVSTIESDNAAEHTLPQEKYWALLTASCERIYEQDDRGPTQNFKTLLAQANSDLQLIAQHLLDKEYDIISAANNASNQQKSGAHSTPITQRAQLIKKQLEQKNVLAATLENREADVKQLKVAAKMKQNELSEMQIRKDLAEKKLSVLQNEYEHAVDKWKQKYEETSLQLQLKEKEFEETMDHLQSDIDALESEKSDLRDKLKLNSTTGKVQPGSESHSPHNISLSGNTSTAPGISNVSYSAPAGTAPVVAEEVELLKNAFNQERNQRLRLQAQDMRAKLSQFEPLHVPQPQDQRITALESELTRMKHAWVLSLLQVRSQDSVNSGTRIDAVALQRRNQPVPLKGEISSKASQLASDILTEYLQRKPHRATHGQFASFPTVDVKRVLQI