| 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. PKA-mediated phosphorylation at a C-terminal site strongly increases the open probability of the channel, but does not increase single channel conductance. 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. |
| Function | Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Can also form a functional, homotetrameric ion channel. Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. Functions as outward-rectifying K(+) channel, but is also permeable to Ca(2+), and to a much lesser degree also to Na(+). May contribute to the release of Ca(2+) stores from the endoplasmic reticulum. Together with TRPV4, forms mechano- and thermosensitive channels in cilium. PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells. Acts as a regulator of cilium length, together with PKD1. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. 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. Detection of asymmetric nodal flow gives rise to a Ca(2+) signal that is required for normal, asymmetric expression of genes involved in the specification of body left-right laterality. |
| 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 Urine |
| 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 proteinTRPP2 protein |
Information sourced from Uniprot.org
