| Post Translational Modifications | 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-812 regulates PKD2 trafficking. Phosphorylation at Ser-76 is required for PKD2 trafficking to or retention at the lateral plasma membrane. Phosphorylation at Ser-801, Ser-812 and Ser-829 regulates PKD2 channel activity. 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. Thus, glycosylation at Asn-305 is not compatible with glycosylation at Asn-328.only one of these two residues is glycosylated at a given time. Sumoylated by SUMO1.sumoylation regulates PKD2 membrane recycling and is necessary for intravascular pressure-induced arterial contractility. |
| 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. In primary cilium 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. 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-2Pc2Autosomal Dominant Polycystic Kidney Disease Type Ii ProteinPolycystic Kidney Disease 2 ProteinPolycystwinR48321Transient Receptor Potential Cation Channel Subfamily P Member 2 |
| Database Links | Reactome: R-HSA-5620916 |
| Cellular Localisation | Cell ProjectionCilium MembraneMulti-Pass Membrane ProteinEndoplasmic Reticulum MembraneCell MembraneBasolateral Cell MembraneCytoplasmic Vesicle 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 CiliaRetained In The Endoplasmic Reticulum By Interaction With Pacs1 And Pacs2Detected On Kidney Tubule Basolateral Membranes And Basal Cytoplasmic VesiclesCell Surface And Cilium Localization Requires GanabDetected On Migrasomes And On Extracellular Exosomes In UrinePreferentially Localized To The Dorsal Side Of Immotile Cilia |
| Alternative Protein Names | Polycystin-2 proteinPc2 proteinAutosomal Dominant Polycystic Kidney Disease Type Ii Protein proteinPolycystic Kidney Disease 2 Protein proteinPolycystwin proteinR48321 proteinTransient Receptor Potential Cation Channel Subfamily P Member 2 proteinPKD2 proteinTRPP1 proteinTRPP2 protein |
Information sourced from Uniprot.org
