Pkd2
entrez
18764
canonical
uniprot
O35245
canonical
ensembl
ENSMUSG00000034462
resolver
ensp
ENSMUSP00000084041
resolver
ensp
ENSMUSP00000236288
resolver
genesymbol
Pkd2
resolver
genesymbol_syn
TRPP2
resolver
uniprot
C0KJK2
resolver
uniprot
E9Q4F6
resolver
uniprot
E9QQA3
resolver
uniprot
Q8BPR6
resolver
uniprot
Q9ES37
resolver
uniprot
Q9QWP0
resolver
uniprot
Q9Z193
resolver
uniprot
Q9Z194
resolver
uniprot_entry
PKD2_MOUSE
resolver
uniprot_sec
C0KJK2
resolver
uniprot_sec
E9Q4F6
resolver
uniprot_sec
E9QQA3
resolver
uniprot_sec
Q8BPR6
resolver
uniprot_sec
Q9ES37
resolver
uniprot_sec
Q9QWP0
resolver
uniprot_sec
Q9Z193
resolver
uniprot_sec
Q9Z194
resolver
activity_regulation
ACTIVITY REGULATION: Channel activity is regulated by phosphorylation (By similarity). The channel is activated by increased cytoplasmic Ca(2+) (in the uM range) and by membrane depolarization (PubMed:27760766, PubMed:29443690). TMEM120A inhibits the channel activity of PKD2, and mediates mechanosensitivity of the PKD2-TMEM120A channel complex (By similarity). At the endoplasmic reticulum membrane (ER), TMEM33 enhances its channel activity (PubMed:31048699). PKD1/ PKD2 complex on the plasma membrane is activated by PKD1 N-terminus (By similarity). {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:27760766, ECO:0000269|PubMed:29443690, ECO:0000269|PubMed:31048699}.
uniprot
proteins
amino_acid_sequence
MVNSRRVQPQPPGDAGRSPAPRASGPGRLVAGGAGLAVPGGLGEQRGLEIEMERIRQAAARDPPAGASASPSPPLSSCSRQAWSRDNPGFEAEEDDDDDEVEGEEGGMVVEMDVEWRPGSRRSASSSAVSSVGARGRGLGSYRGAAHLSGRRRRLEDQGAQCPSPAGGGDPLHRHLPLEGQPPRVAWAERLVRGLRGLWGTRLMEESNANREKYLKSVLRELVTYLFFLVVLCILTYGMMSSNVYYYTRTLSQLFIDTPVSKTEKTNFKTLSSMEDFWKFTEGSFLDGLYWKAQTSNHTQADNRSFIFYENLLLGVPRLRQLRVRNGSCSIPQDLRDEIKECYDVYSVSSEDRAPFGPRNGTAWMYTSEKELNGSSHWGIIASYSGAGYYLDLSRTREETAAQLAGLRRNFWLDRGTRAAFIDFSVYNANINLFCVVRLLAEFPATGGVVPSWQFQPVKLIRYVTAFDFFLAACEIIFCFFIIYYVVEEILEIRIHRLSYFRSFWNCLDVVIVVLSVVAMVINIYRMSNAEGLLQFLEDQNSFPNFEHVAYWQIQFNNISAVMVFLVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFTIMFSIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPLYFTTFVFFMFFILLNMFLAIINDSYSEVKSDLAQQKAEMELSDLIRKGCQKALVKLKLKRNTVDAISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEREHQQMRDDLEKEREDLDLEHSSLPRPMSSRSFPRSLDDSEEEDDEDSGHSSRRRGSISSGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEIMERAKLKRREVLGRLLDGVAEDARLGRDSEIHREQMERLVREELERWESDDAASQTGHGVSTQVGLGGQPHPRNPRPPSSQSAEGLEGGGGNGSANVHA
uniprot
proteins
function
FUNCTION: Forms a nonselective cation channel. Can function as a homotetrameric ion channel or can form heteromer with PKD1 (PubMed:12640140, PubMed:25405894, PubMed:27214281, PubMed:27760766, PubMed:29443690). 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 (PubMed:12514735, PubMed:12640140, PubMed:18695040, PubMed:27760766, PubMed:29443690, PubMed:31048699). In the endoplasmic reticulum, likely functions as a K(+) channel to facilitate Ca(2+) release (PubMed:35835458). The heterotetrameric PKD1/PKD2 channel has higher Ca(2+) permeability than homomeric PKD2 channel and acts as a primarily Ca(2+)-permeable channel (By similarity). PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells (PubMed:10615132, PubMed:9568711). 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 (PubMed:18695040). In cardiomyocytes, PKD2 modulates Ca(2+) release from stimulated RYR2 receptors through direct association (PubMed:17404231). 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 (PubMed:21307093, PubMed:22983710). Acts as a regulator of cilium length together with PKD1 (PubMed:20096584). Mediates systemic blood pressure and contributes to the myogenic response in cerebral arteries though vasoconstriction (PubMed:23858011, PubMed:30511640, PubMed:31822608). {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:10615132, ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:12640140, ECO:0000269|PubMed:17404231, ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:20096584, ECO:0000269|PubMed:21307093, ECO:0000269|PubMed:22983710, ECO:0000269|PubMed:23858011, ECO:0000269|PubMed:25405894, ECO:0000269|PubMed:27214281, ECO:0000269|PubMed:27760766, ECO:0000269|PubMed:29443690, ECO:0000269|PubMed:30511640, ECO:0000269|PubMed:31048699, ECO:0000269|PubMed:31822608, ECO:0000269|PubMed:35835458, ECO:0000269|PubMed:9568711}.
uniprot
proteins
mass_dalton
108982
uniprot
proteins
mutagenesis
MUTAGEN 6; /note="R->G: No effect on location at nodal cilia and can rescue the laterality defect of null mutants. Abolishes location at nodal cilia and cannot complement the laterality defect of null mutants; when associated with DEL 819-966."; /evidence="ECO:0000269|PubMed:22983710"; MUTAGEN 442; /note="E->G: In lrm4; mice exhibit gross left-right abnormalities. Embryos do not show defects in kidney development. The nodes appear normal. Abolishes location at nodal cilia, but does not affect interaction with Pkd1l1."; /evidence="ECO:0000269|PubMed:21307093, ECO:0000269|PubMed:22983710"; MUTAGEN 509; /note="D->V: Abolishes location at nodal cilia and cannot complement the laterality defect of null mutants."; /evidence="ECO:0000269|PubMed:22983710"; MUTAGEN 819..966; /note="Missing: Abolishes location at nodal cilia and cannot complement the laterality defect of null mutants; when associated with G-6."; /evidence="ECO:0000269|PubMed:22983710
uniprot
proteins
post_translational_modification
PTM: N-glycosylated (PubMed:11854751). 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 (By similarity). {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:11854751}.; PTM: Sumoylated by SUMO1; sumoylation regulates PKD2 membrane recycling and is necessary for intravascular pressure-induced arterial contractility. {ECO:0000269|PubMed:31822608}.; PTM: Phosphorylated (PubMed:16551655). 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 (By similarity). {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:16551655}.
uniprot
proteins
protein_family
Polycystin family
uniprot
proteins
pubmed
10615132
uniprot
proteins
pubmed
10760273
uniprot
proteins
pubmed
10770959
uniprot
proteins
pubmed
10873385
uniprot
proteins
pubmed
10913159
uniprot
proteins
pubmed
11854751
uniprot
proteins
pubmed
12062060
uniprot
proteins
pubmed
12514735
uniprot
proteins
pubmed
12640140
uniprot
proteins
pubmed
15692563
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16192288
uniprot
proteins
pubmed
16551655
uniprot
proteins
pubmed
17404231
uniprot
proteins
pubmed
18235101
uniprot
proteins
pubmed
18695040
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20096584
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21307093
uniprot
proteins
pubmed
21670265
uniprot
proteins
pubmed
22983710
uniprot
proteins
pubmed
23858011
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
25405894
uniprot
proteins
pubmed
27214281
uniprot
proteins
pubmed
27760766
uniprot
proteins
pubmed
29443690
uniprot
proteins
pubmed
30511640
uniprot
proteins
pubmed
31048699
uniprot
proteins
pubmed
31822608
uniprot
proteins
pubmed
35835458
uniprot
proteins
pubmed
36603091
uniprot
proteins
pubmed
9339380
uniprot
proteins
pubmed
9568711
uniprot
proteins
pubmed
9716661
uniprot
proteins
sequence_length
966
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:15692563, ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:21307093, ECO:0000269|PubMed:22983710, ECO:0000269|PubMed:25405894, ECO:0000269|PubMed:27760766, ECO:0000269|PubMed:29443690}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Cell membrane {ECO:0000269|PubMed:12640140, ECO:0000269|PubMed:16551655, ECO:0000269|PubMed:27214281}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Basolateral cell membrane {ECO:0000269|PubMed:10770959, ECO:0000269|PubMed:9568711}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:10770959, ECO:0000269|PubMed:16551655, ECO:0000269|PubMed:9568711}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11854751, ECO:0000269|PubMed:25405894, ECO:0000305|PubMed:10913159}. Golgi apparatus {ECO:0000269|PubMed:25405894}. Vesicle {ECO:0000250|UniProtKB:Q13563}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:Q13563}. Note=PKD2 localization to the plasma and ciliary membranes requires PKD1. PKD1:PKD2 interaction is required to reach the Golgi apparatus form endoplasmic reticulum and then traffic to the cilia (PubMed:25405894). Detected on kidney tubule basolateral membranes and basal cytoplasmic vesicles (PubMed:10770959, PubMed:9568711). Retained in the endoplasmic reticulum by interaction with PACS1 and PACS2. Cilium localization requires GANAB (By similarity). Detected on migrasomes and on extracellular exosomes in urine (By similarity). Preferentially localized to the dorsal side of immotile cilia (PubMed:36603091). {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:10770959, ECO:0000269|PubMed:25405894, ECO:0000269|PubMed:36603091, ECO:0000269|PubMed:9568711}.
uniprot
proteins
transmembrane_region
TRANSMEM 218..239; /note="Helical; Name=S1"; /evidence="ECO:0000250|UniProtKB:Q13563"; TRANSMEM 467..487; /note="Helical; Name=S2"; /evidence="ECO:0000250|UniProtKB:Q13563"; TRANSMEM 504..524; /note="Helical; Name=S3"; /evidence="ECO:0000250|UniProtKB:Q13563"; TRANSMEM 551..571; /note="Helical; Name=S4"; /evidence="ECO:0000250|UniProtKB:Q13563"; TRANSMEM 596..617; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:Q13563"; TRANSMEM 653..673; /note="Helical; Name=S6"; /evidence="ECO:0000250|UniProtKB:Q13563
uniprot
proteins