P30009
uniprot
P30009
canonical
amino_acid_sequence
MGAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPASGGAATPAAADKDEAAAAPEPGAATADKEAAEAEPAEPGSPSAETEGASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKEAGEGAEAEGATADGAKDEAAAAAGGDAAAAPGEQAGGAGAEGAEGGESREAEAAEPEQPEQPEQPAAEEPRAEEPSEAVGEKAEEPAPGATADDAPSAAGPEQEAPAATDEPAASAAPSASPEPQPECSPEAPPAPVAE
uniprot
proteins
function
FUNCTION: Membrane-associated protein that plays a role in the structural modulation of the actin cytoskeleton, chemotaxis, motility, cell adhesion, phagocytosis, and exocytosis through lipid sequestering and/or protein docking to membranes (PubMed:24662485). Thus, exerts an influence on a plethora of physiological processes, such as embryonic development, tissue regeneration, neuronal plasticity, and inflammation. Sequesters phosphatidylinositol 4,5-bisphosphate (PIP2) at lipid rafts in the plasma membrane of quiescent cells, an action reversed by protein kinase C, ultimately inhibiting exocytosis. During inflammation, promotes the migration and adhesion of inflammatory cells and the secretion of cytokines such as tumor necrosis factor (TNF), particularly in macrophages. Plays an essential role in bacteria-induced intracellular reactive oxygen species (ROS) formation in the monocytic cell type. Participates in the regulation of neurite initiation and outgrowth by interacting with components of cellular machinery including CDC42 that regulates cell shape and process extension through modulation of the cytoskeleton (By similarity). Plays also a role in axon development by mediating docking and fusion of RAB10-positive vesicles with the plasma membrane (PubMed:24662485). {ECO:0000250|UniProtKB:P26645, ECO:0000250|UniProtKB:P29966, ECO:0000269|PubMed:24662485}.
uniprot
proteins
mass_dalton
29795
uniprot
proteins
post_translational_modification
PTM: Acetylated at Lys-165 by KAT5; acetylation is required for its subsequent phosphorylation. Deacetylated by SIRT2. {ECO:0000250|UniProtKB:P26645}.; PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity. {ECO:0000269|PubMed:8422248}.; PTM: Myristoylated. A proper myristoylation is essential for the proper distribution to the plasma membrane. {ECO:0000250|UniProtKB:P29966}.
uniprot
proteins
protein_family
MARCKS family
uniprot
proteins
pubmed
1396720
uniprot
proteins
pubmed
1707878
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
24662485
uniprot
proteins
pubmed
2676596
uniprot
proteins
pubmed
8422248
uniprot
proteins
sequence_length
309
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24662485}; Lipid-anchor {ECO:0000269|PubMed:24662485}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P29966}. Cytoplasm {ECO:0000250|UniProtKB:P29966}. Note=PKC-dependent phosphorylation displaces MARCKS from the cell membrane and subsequent dephosphorylation is accompanied by its reassociation with the membrane. {ECO:0000250|UniProtKB:P29966}.
uniprot
proteins