| Post Translational Modifications | N-glycosylated. The four subunits in a tetramer probably differ in the extent of glycosylation.simultaneous glycosylation of all experimentally validated sites would probably create steric hindrance. Sumoylated by SUMO1.sumoylation regulates PKD2 membrane recycling and is necessary for intravascular pressure-induced arterial contractility. Phosphorylated. Phosphorylation is important for protein function.a mutant that lacks the N-terminal phosphorylation sites cannot complement a zebrafish pkd2-deficient mutant. PKD-mediated phosphorylation at the C-terminus regulates its function in the release of Ca(2+) stores from the endoplasmic reticulum. Phosphorylation at Ser-810 regulates PKD2 trafficking. Phosphorylation at Ser-72 is required for PKD2 trafficking to or retention at the lateral plasma membrane. Phosphorylation at Ser-799, Ser-810 and Ser-827 regulates PKD2 channel activity. |
| Function | Forms a nonselective cation channel. Can function as a homotetrameric ion channel or can form heteromer with PKD1. Displays distinct function depending on its subcellular localization and regulation by its binding partners. Functions as a cation channel, with a preference for monovalent cations over divalent cations that allows K(+), Na(+) and Ca(2+) influx, with low selectivity for Ca(2+). Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. In the endoplasmic reticulum, likely functions as a K(+) channel to facilitate Ca(2+) release. The heterotetrameric PKD1/PKD2 channel has higher Ca(2+) permeability than homomeric PKD2 channel and acts as a primarily Ca(2+)-permeable channel. PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells. Interacts with and acts as a regulator of a number of other channels, such as TRPV4, TRPC1, IP3R, RYR2, ultimately further affecting intracellular signaling, to modulate intracellular Ca(2+) signaling. Together with TRPV4, forms mechano- and thermosensitive channels in cilium. In cardiomyocytes, PKD2 modulates Ca(2+) release from stimulated RYR2 receptors through direct association. Also involved in left-right axis specification via its role in sensing nodal flow.forms a complex with PKD1L1 in cilia to facilitate flow detection in left-right patterning. Acts as a regulator of cilium length together with PKD1. Mediates systemic blood pressure and contributes to the myogenic response in cerebral arteries though vasoconstriction. |
| Protein Name | Polycystin-2Polycystic Kidney Disease 2 Protein HomologTransient Receptor Potential Cation Channel Subfamily P Member 2 |
| Database Links | Reactome: R-MMU-5620916 |
| Cellular Localisation | Cell ProjectionCilium MembraneMulti-Pass Membrane ProteinCell MembraneBasolateral Cell MembraneCytoplasmic Vesicle MembraneEndoplasmic Reticulum MembraneGolgi ApparatusVesicleSecretedExtracellular ExosomePkd2 Localization To The Plasma And Ciliary Membranes Requires Pkd1Pkd1:Pkd2 Interaction Is Required To Reach The Golgi Apparatus Form Endoplasmic Reticulum And Then Traffic To The CiliaDetected On Kidney Tubule Basolateral Membranes And Basal Cytoplasmic VesiclesRetained In The Endoplasmic Reticulum By Interaction With Pacs1 And Pacs2Cilium Localization Requires GanabDetected On Migrasomes And On Extracellular Exosomes In UrinePreferentially Localized To The Dorsal Side Of Immotile Cilia |
| Alternative Antibody Names | Anti-Polycystin-2 antibodyAnti-Polycystic Kidney Disease 2 Protein Homolog antibodyAnti-Transient Receptor Potential Cation Channel Subfamily P Member 2 antibodyAnti-Pkd2 antibodyAnti-TRPP2 antibody |
Information sourced from Uniprot.org
