Protein: DRP1A_ARATH
Sequence: MENLISLVNKIQRACTALGDHGDSSALPTLWDSLPAIAVVGGQSSGKSSVLESIVGKDFLPRGSGIVTRRPLVLQLQKIDDGTREYAEFLHLPRKKFTDFAAVRKEIQDETDRETGRSKAISSVPIHLSIYSPNVVNLTLIDLPGLTKVAVDGQSDSIVKDIENMVRSYIEKPNCIILAISPANQDLATSDAIKISREVDPSGDRTFGVLTKIDLMDKGTDAVEILEGRSFKLKYPWVGVVNRSQADINKNVDMIAARKREREYFSNTTEYRHLANKMGSEHLAKMLSKHLERVIKSRIPGIQSLINKTVLELETELSRLGKPIAADAGGKLYSIMEICRLFDQIFKEHLDGVRAGGEKVYNVFDNQLPAALKRLQFDKQLAMDNIRKLVTEADGYQPHLIAPEQGYRRLIESSIVSIRGPAEASVDTVHAILKDLVHKSVNETVELKQYPALRVEVTNAAIESLDKMREGSKKATLQLVDMECSYLTVDFFRKLPQDVEKGGNPTHSIFDRYNDSYLRRIGSNVLSYVNMVCAGLRNSIPKSIVYCQVREAKRSLLDHFFAELGTMDMKRLSSLLNEDPAIMERRSAISKRLELYRAAQSEIDAVAWSK
What is the function of this protein?
Microtubule-associated force-producing protein that is targeted to at the leading edges of the forming cell plate during cytokinesis (PubMed:18612642).  Also plays a major role in plasma membrane maintenance and cell wall integrity with implications in vesicular trafficking, polar cell expansion, vascular formation, and other aspects of plant growth and development, including stigmatic papillae expansion (PubMed:18256049, PubMed:18344418).  Collaboratively with DRP2B, participates in clathrin-coated vesicle formation during endocytosis (PubMed:20231465).  Necessary for BOR1 polar localization in low-boron (B) conditions as well as for BOR1 endocytosis and subsequent degradation under high-concentration of boron (PubMed:27449211).  Has a GTPase activity (PubMed:20171176).  Required for the sterols-dependent dynamic high lipid order observed at the cell plate of dividing cells (PubMed:25234576).  Together with SH3P2, converts the fused vesicles to tubular structures at the cell plate and phragmoplasts during cytokinesis (PubMed:28584166, PubMed:18256049).  With DRP2B and PIP5K3, required for the precise coordination of polar ARAC3/ROP6 and ARAC4/ROP2 placement and subsequent root hair positioning during planar polarity formation in root hair-forming cells, probably by mediating the correct basal-to-planar polarity switching of D6PK into the polar, lipid-enriched domain (PubMed:27251533).  Involved in endocytosis required for cellulose deposition during cell wall formation and elongation (PubMed:18256049).  Interacts with plasma membrane-mimetic liposomes and induces their clustering (PubMed:20171176).
What are the official names of this protein?
Phragmoplastin DRP1A, Dynamin-like protein 1, Dynamin-like protein 1A, Dynamin-related protein 1A, AtDRP1A, Protein RADIAL SWELLING 9.
What is the protein family that this protein belongs to?
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.
What are the subcellular locations of this protein?
Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, phragmoplast. Cytoplasm, cell cortex. Cytoplasmic vesicle, clathrin-coated vesicle. Cell membrane. Note=Microtubule-associated and localized in the forming cell plate, at the vicinity of sterols, during cytokinesis, especially at the leading edges (PubMed:14750520, PubMed:28584166, PubMed:18612642, PubMed:25234576). Accumulates in a sterol-enriched, polar membrane domain during root hair initiation (PubMed:27251533). Forms discreet dynamic foci in the epidermal cell cortex, which colocalize with part of the clathrin endocytic machinery (PubMed:18344418). Co-localizes with BOR1 in the cell plate and the plasma membrane (PubMed:27449211).