PKD2L1
entrez
9033
canonical
uniprot
Q9P0L9
canonical
ensembl
ENSG00000107593
resolver
ensp
ENSP00000325296
resolver
genesymbol
PKD2L1
resolver
genesymbol_syn
PKD2L
resolver
genesymbol_syn
PKDL
resolver
genesymbol_syn
TRPP3
resolver
hgnc
HGNC:9011
resolver
uniprot
O75972
resolver
uniprot
Q1L4F0
resolver
uniprot
Q5W039
resolver
uniprot
Q9UP35
resolver
uniprot
Q9UPA2
resolver
uniprot_entry
PK2L1_HUMAN
resolver
uniprot_entry
Q1L4F0_HUMAN
resolver
uniprot_sec
O75972
resolver
uniprot_sec
Q5W039
resolver
uniprot_sec
Q9UP35
resolver
uniprot_sec
Q9UPA2
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:23212381). Channel activity is inhibited by phosphatidylinositol-4,5-bisphosphate (PIP2) (PubMed:29425510). Non-selective cation channel activity is substantially increased when either the extracellular or intracellular calcium-ion concentration is raised (PubMed:10517637). Regulation of non-selective cation channel activity by external calcium is bimodal, first sensitizing and subsequently inactivating the current (PubMed:26066678). {ECO:0000269|PubMed:10517637, ECO:0000269|PubMed:23212381, ECO:0000269|PubMed:26066678, ECO:0000269|PubMed:29425510}.
uniprot
proteins
amino_acid_sequence
MNAVGSPEGQELQKLGSGAWDNPAYSGPPSPHGTLRVCTISSTGPLQPQPKKPEDEPQETAYRTQVSSCCLHICQGIRGLWGTTLTENTAENRELYIKTTLRELLVYIVFLVDICLLTYGMTSSSAYYYTKVMSELFLHTPSDTGVSFQAISSMADFWDFAQGPLLDSLYWTKWYNNQSLGHGSHSFIYYENMLLGVPRLRQLKVRNDSCVVHEDFREDILSCYDVYSPDKEEQLPFGPFNGTAWTYHSQDELGGFSHWGRLTSYSGGGYYLDLPGSRQGSAEALRALQEGLWLDRGTRVVFIDFSVYNANINLFCVLRLVVEFPATGGAIPSWQIRTVKLIRYVSNWDFFIVGCEVIFCVFIFYYVVEEILELHIHRLRYLSSIWNILDLVVILLSIVAVGFHIFRTLEVNRLMGKLLQQPNTYADFEFLAFWQTQYNNMNAVNLFFAWIKIFKYISFNKTMTQLSSTLARCAKDILGFAVMFFIVFFAYAQLGYLLFGTQVENFSTFIKCIFTQFRIILGDFDYNAIDNANRILGPAYFVTYVFFVFFVLLNMFLAIINDTYSEVKEELAGQKDELQLSDLLKQGYNKTLLRLRLRKERVSDVQKVLQGGEQEIQFEDFTNTLRELGHAEHEITELTATFTKFDRDGNRILDEKEQEKMRQDLEEERVALNTEIEKLGRSIVSSPQGKSGPEAARAGGWVSGEEFYMLTRRVLQLETVLEGVVSQIDAVGSKLKMLERKGWLAPSPGVKEQAIWKHPQPAPAVTPDPWGVQGGQESEVPYKREEEALEERRLSRGEIPTLQRS
uniprot
proteins
function
FUNCTION: Homotetrameric, non-selective cation channel that is permeable to sodium, potassium, magnesium and calcium (PubMed:10517637, PubMed:11959145, PubMed:25820328, PubMed:27754867, PubMed:29425510, PubMed:30004384). Also forms functional heteromeric channels with PKD1, PKD1L1 and PKD1L3 (PubMed:23212381, PubMed:24336289). 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:19812697, PubMed:23212381). 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:23212381). 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:24336289). The PKD1L1:PKD2L1 complex channel is mechanosensitive only at high pressures and is highly temperature sensitive (PubMed:24336289). 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) (By similarity). May play a role in the perception of carbonation taste (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:A2A259, ECO:0000269|PubMed:10517637, ECO:0000269|PubMed:11959145, ECO:0000269|PubMed:19812697, ECO:0000269|PubMed:23212381, ECO:0000269|PubMed:24336289, ECO:0000269|PubMed:25820328, ECO:0000269|PubMed:27754867, ECO:0000269|PubMed:29425510, ECO:0000269|PubMed:30004384}.
uniprot
proteins
mass_dalton
91982
uniprot
proteins
mutagenesis
MUTAGEN 2..96; /note="Missing: Loss of channel activity. No effect on expression at the cell membrane."; /evidence="ECO:0000269|PubMed:25820328"; MUTAGEN 2..38; /note="Missing: Loss of channel activity."; /evidence="ECO:0000269|PubMed:27754867"; MUTAGEN 2..36; /note="Missing: No effect on channel activity."; /evidence="ECO:0000269|PubMed:27754867"; MUTAGEN 38; /note="C->A: Strongly decreased channel activity. No effect on expression at the cell membrane. Loss of palmitoylation."; /evidence="ECO:0000269|PubMed:27754867"; MUTAGEN 39; /note="T->D,E: Decreased channel activity."; /evidence="ECO:0000269|PubMed:27754867"; MUTAGEN 81..95; /note="Missing: Loss of channel activity."; /evidence="ECO:0000269|PubMed:29425510"; MUTAGEN 81; /note="W->A,K,L,R: Loss of channel activity. No effect on expression at the cell membrane."; /evidence="ECO:0000269|PubMed:29425510"; MUTAGEN 523..525; /note="DFD->AFA: Abolishes ion channel activity."; /evidence="ECO:0000269|PubMed:24336289"; MUTAGEN 523; /note="D->Q: Increased permeability of dimethylamine and trimethylamine and decreased permeability of magnesium."; /evidence="ECO:0000269|PubMed:23212381"; MUTAGEN 525; /note="D->K: Increased permeability of dimethylamine and trimethylamine and decreased permeability of magnesium."; /evidence="ECO:0000269|PubMed:23212381"; MUTAGEN 530; /note="D->A: Does not affect ion channel activity."; MUTAGEN 566..805; /note="Missing: Loss of channel activity. No effect on expression at the cell membrane."; /evidence="ECO:0000269|PubMed:25820328"; MUTAGEN 568; /note="K->A,D,E: Loss of channel activity."; /evidence="ECO:0000269|PubMed:29425510"; MUTAGEN 581..805; /note="Missing: Loss of channel activity. No effect on expression at the cell membrane."; /evidence="ECO:0000269|PubMed:25820328"; MUTAGEN 594..599; /note="Missing: Loss of phosphatidylinositol-4,5-bisphosphate binding."; /evidence="ECO:0000269|PubMed:29425510"; MUTAGEN 594; /note="R->Q: Increased channel activity."; /evidence="ECO:0000269|PubMed:29425510"; MUTAGEN 596; /note="R->Q: Increased channel activity."; /evidence="ECO:0000269|PubMed:29425510"; MUTAGEN 598; /note="R->Q: Mildly increased channel activity."; /evidence="ECO:0000269|PubMed:29425510"; MUTAGEN 599; /note="K->Q: Mildly increased channel activity."; /evidence="ECO:0000269|PubMed:29425510"; MUTAGEN 622..805; /note="Missing: No effect on channel activity. No effect on expression at the cell membrane."; /evidence="ECO:0000269|PubMed:25820328"; MUTAGEN 710; /note="L->A: Abolishes homooligomer formation; when associated with A-714; A-717; A-728; A-731 and A-735."; /evidence="ECO:0000269|PubMed:22193359"; MUTAGEN 714; /note="V->A: Abolishes homooligomer formation; when associated with A-710; A-717; A-728; A-731 and A-735."; /evidence="ECO:0000269|PubMed:22193359"; MUTAGEN 717; /note="L->A: Abolishes homooligomer formation; when associated with A-710; A-714; A-728; A-731 and A-735."; /evidence="ECO:0000269|PubMed:22193359"; MUTAGEN 728; /note="I->A: Abolishes homooligomer formation; when associated with A-710; A-714; A-717; A-731 and A-735."; /evidence="ECO:0000269|PubMed:22193359"; MUTAGEN 731; /note="V->A: Abolishes homooligomer formation; when associated with A-710; A-714; A-717; A-728 and A-735."; /evidence="ECO:0000269|PubMed:22193359"; MUTAGEN 735; /note="L->A: Abolishes homooligomer formation; when associated with A-710; A-714; A-717; A-728 and A-731."; /evidence="ECO:0000269|PubMed:22193359
uniprot
proteins
post_translational_modification
PTM: Palmitoylation is important for expression at the cell membrane and for channel activity. {ECO:0000269|PubMed:27754867}.
uniprot
proteins
protein_family
Polycystin family
uniprot
proteins
pubmed
10517637
uniprot
proteins
pubmed
10602361
uniprot
proteins
pubmed
10602992
uniprot
proteins
pubmed
11959145
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19812697
uniprot
proteins
pubmed
22174419
uniprot
proteins
pubmed
22193359
uniprot
proteins
pubmed
23212381
uniprot
proteins
pubmed
24336289
uniprot
proteins
pubmed
25820328
uniprot
proteins
pubmed
26066678
uniprot
proteins
pubmed
27754867
uniprot
proteins
pubmed
29425510
uniprot
proteins
pubmed
30004384
uniprot
proteins
pubmed
9748274
uniprot
proteins
pubmed
9878261
uniprot
proteins
sequence_length
805
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:24336289}; Multi-pass membrane protein {ECO:0000269|PubMed:30004384}. Cell membrane {ECO:0000269|PubMed:10517637, ECO:0000269|PubMed:11959145, ECO:0000269|PubMed:23212381, ECO:0000269|PubMed:25820328, ECO:0000269|PubMed:27754867, ECO:0000269|PubMed:29425510}; Multi-pass membrane protein {ECO:0000269|PubMed:30004384}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:A2A259}. Note=Interaction with PKD1L3 is required for localization to the cell membrane (PubMed:23212381). Interaction with PKD1 is required for localization to the cell membrane (By similarity). {ECO:0000250|UniProtKB:A2A259, ECO:0000269|PubMed:23212381}.
uniprot
proteins
transmembrane_region
TRANSMEM 104..124; /note="Helical"; /evidence="ECO:0000305|PubMed:30004384"; TRANSMEM 357..376; /note="Helical"; /evidence="ECO:0000305|PubMed:30004384"; TRANSMEM 385..405; /note="Helical"; /evidence="ECO:0000305|PubMed:30004384"; TRANSMEM 434..454; /note="Helical"; /evidence="ECO:0000305|PubMed:30004384"; TRANSMEM 480..499; /note="Helical"; /evidence="ECO:0000305|PubMed:30004384"; TRANSMEM 537..557; /note="Helical"; /evidence="ECO:0000305|PubMed:30004384
uniprot
proteins