Pkd2l1
entrez
329064
canonical
uniprot
A2A259
canonical
ensembl
ENSMUSG00000037578
resolver
ensp
ENSMUSP00000045675
resolver
enst
ENSMUST00000042026
resolver
genesymbol
Pkd2l1
resolver
genesymbol_syn
Trpp3
resolver
uniprot
Q14B55
resolver
uniprot
Q14B73
resolver
uniprot
Q80ZH4
resolver
uniprot_entry
PK2L1_MOUSE
resolver
uniprot_sec
Q14B55
resolver
uniprot_sec
Q14B73
resolver
uniprot_sec
Q80ZH4
resolver
activity_regulation
ACTIVITY REGULATION: The non-selective cation channel is gated following an off-response property by acid: gated open after the removal of acid stimulus, but not during acid application (PubMed:18535624, PubMed:19464260, PubMed:20406802, PubMed:22420714, PubMed:28904867, PubMed:29567962). Responses to acid stimulus are inhibited by capsaicin (PubMed:22420714). {ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260, ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:22420714, ECO:0000269|PubMed:28904867, ECO:0000269|PubMed:29567962}.
uniprot
proteins
amino_acid_sequence
MNSMESPKNQELQTLGNRAWDNPAYSDPPSPNRTLRICTVSSVALPETQPKKPEVRCQEKTQRTLVSSCCLHICRSIRGLWGTTLTENTAENRELYVKTTLRELVVYIVFLVDICLLTYGMTSSSAYYYTKVMSELFLHTPSDSGVSFQTISSMSDFWDFAQGPLLDSLYWTKWYNNQSLGRGSHSFIYYENLLLGAPRLRQLRVRNDSCVVHEDFREDILNCYDVYSPDKEDQLPFGPQNGTAWTYHSQNELGGSSHWGRLTSYSGGGYYLDLPGSRQASAEALQGLQEGLWLDRGTRVVFIDFSVYNANINLFCILRLVVEFPATGGTIPSWQIRTVKLIRYVNNWDFFIVGCEVVFCVFIFYYVVEEILEIHLHRLRYLSSVWNILDLVVILLSIVAVGFHIFRTLEVNRLMGKLLQQPDTYADFEFLAFWQTQYNNMNAVNLFFAWIKIFKYISFNKTMTQLSSTLARCAKDILGFAIMFFIVFFAYAQLGYLLFGTQVENFSTFVKCIFTQFRIILGDFDYNAIDNANRILGPVYFVTYVFFVFFVLLNMFLAIINDTYSEVKEELAGQKDQLQLSDFLKQSYNKTLLRLRLRKERVSDVQKVLKGGEPEIQFEDFTSTLRELGHEEHEITAAFTRFDQDGDHILDEEEQEQMRQGLEEERVTLNAEIENLGRSVGHSPPGELGAEAARGQSWVSGEEFDMLTRRVLQLQCVLEGVVSQIDAVGSKLKMLERKGELAPSPGMGEPAVWENLYNPS
uniprot
proteins
function
FUNCTION: Homotetrameric, non-selective cation channel that is permeable to sodium, potassium, magnesium and calcium (PubMed:15548533, PubMed:28904867). Also forms functional heteromeric channels with PKD1, PKD1L1 and PKD1L3 (PubMed:15548533, PubMed:16891422, PubMed:18535624, PubMed:20538909, PubMed:21185261, PubMed:24336289, PubMed:34381056). Pore-forming subunit of a heterotetrameric, non-selective cation channel, formed by PKD1L2 and PKD1L3, that is permeable to sodium, potassium, magnesium and calcium and which may act as a sour taste receptor in gustatory cells; however, its contribution to sour taste perception is unclear in vivo and may be indirect (PubMed:16891422, PubMed:16929298, PubMed:18535624, PubMed:19464260, PubMed:20406802, PubMed:20538909, PubMed:21098668, PubMed:21185261, PubMed:21625513, PubMed:22420714, PubMed:29567962). The homomeric and heteromeric channels formed by PKD1L2 and PKD1L3 are activated by low pH and Ca(2+), but opens only when the extracellular pH rises again and after the removal of acid stimulus (PubMed:18535624, PubMed:19464260, PubMed:20406802, PubMed:20538909, PubMed:22420714, PubMed:28904867, PubMed:29567962). Pore-forming subunit of a calcium-permeant ion channel formed by PKD1L2 and PKD1L1 in primary cilia, where it controls cilium calcium concentration, without affecting cytoplasmic calcium concentration, and regulates sonic hedgehog/SHH signaling and GLI2 transcription (PubMed:24336288, PubMed:24336289). The PKD1L1:PKD2L1 complex channel is mechanosensitive only at high pressures and is highly temperature sensitive (By similarity). Pore-forming subunit of a calcium-permeant ion channel formed by PKD1L2 and PKD1 that produces a transient increase in intracellular calcium concentration upon hypo-osmotic stimulation (200 mOsm) (PubMed:15548533). May play a role in the perception of carbonation taste (PubMed:19833970). May play a role in the sensory perception of water, via a mechanism that activates the channel in response to dilution of salivary bicarbonate and changes in salivary pH (PubMed:28553944). {ECO:0000250|UniProtKB:Q9P0L9, ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:16929298, ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260, ECO:0000269|PubMed:19833970, ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21098668, ECO:0000269|PubMed:21185261, ECO:0000269|PubMed:21625513, ECO:0000269|PubMed:22420714, ECO:0000269|PubMed:24336288, ECO:0000269|PubMed:24336289, ECO:0000269|PubMed:28553944, ECO:0000269|PubMed:28904867, ECO:0000269|PubMed:29567962, ECO:0000269|PubMed:34381056}.
uniprot
proteins
mass_dalton
87234
uniprot
proteins
mutagenesis
MUTAGEN 522; /note="G->L: Loss of channel activity."; /evidence="ECO:0000269|PubMed:29567962"; MUTAGEN 523; /note="D->E: Little or no effect on calcium channel activity."; /evidence="ECO:0000269|PubMed:21185261"; MUTAGEN 523; /note="D->N: Impaired calcium channel activity."; /evidence="ECO:0000269|PubMed:21185261"; MUTAGEN 525; /note="D->N: Little or no effect on calcium channel activity."; /evidence="ECO:0000269|PubMed:21185261"; MUTAGEN 530; /note="D->N: Little or no effect on calcium channel activity."; /evidence="ECO:0000269|PubMed:21185261"; MUTAGEN 531; /note="N->Q: No effect on activation by low pH."; /evidence="ECO:0000269|PubMed:28904867"; MUTAGEN 533; /note="N->Q: Loss of activation by low pH."; /evidence="ECO:0000269|PubMed:28904867"; MUTAGEN 560; /note="I->F: Loss of channel activity."; /evidence="ECO:0000269|PubMed:29567962"; MUTAGEN 568; /note="K->A: Increases localization at the cell surface when expressed in absence of PKD1."; /evidence="ECO:0000269|PubMed:15548533"; MUTAGEN 576; /note="D->A: Induces localization to the endoplasmic reticulum when expressed in absence of PKD1."; /evidence="ECO:0000269|PubMed:15548533
uniprot
proteins
post_translational_modification
PTM: Palmitoylation is important for expression at the cell membrane and for channel activity. {ECO:0000250|UniProtKB:Q9P0L9}.
uniprot
proteins
protein_family
Polycystin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15548533
uniprot
proteins
pubmed
16891422
uniprot
proteins
pubmed
16929298
uniprot
proteins
pubmed
18156604
uniprot
proteins
pubmed
18535624
uniprot
proteins
pubmed
19464260
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19833970
uniprot
proteins
pubmed
20406802
uniprot
proteins
pubmed
20408813
uniprot
proteins
pubmed
20538909
uniprot
proteins
pubmed
21098668
uniprot
proteins
pubmed
21185261
uniprot
proteins
pubmed
21625513
uniprot
proteins
pubmed
22420714
uniprot
proteins
pubmed
24336288
uniprot
proteins
pubmed
24336289
uniprot
proteins
pubmed
25820328
uniprot
proteins
pubmed
28553944
uniprot
proteins
pubmed
28904867
uniprot
proteins
pubmed
29567962
uniprot
proteins
pubmed
34381056
uniprot
proteins
sequence_length
760
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:24336288, ECO:0000269|PubMed:24336289}; Multi-pass membrane protein {ECO:0000269|PubMed:29567962}. Cell membrane {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260, ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21185261, ECO:0000269|PubMed:22420714}; Multi-pass membrane protein {ECO:0000269|PubMed:29567962}. Cytoplasmic vesicle {ECO:0000305|PubMed:20538909}. Note=Interaction with PKD1 or PKD1L3 is required for localization to the cell membrane. {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21185261}.
uniprot
proteins
transmembrane_region
TRANSMEM 104..124; /note="Helical"; /evidence="ECO:0000305|PubMed:29567962"; TRANSMEM 357..376; /note="Helical"; /evidence="ECO:0000305|PubMed:29567962"; TRANSMEM 385..405; /note="Helical"; /evidence="ECO:0000305|PubMed:29567962"; TRANSMEM 434..454; /note="Helical"; /evidence="ECO:0000305|PubMed:29567962"; TRANSMEM 480..499; /note="Helical"; /evidence="ECO:0000305|PubMed:29567962"; TRANSMEM 537..557; /note="Helical"; /evidence="ECO:0000305|PubMed:29567962
uniprot
proteins