Pkd1l3
entrez
244646
canonical
uniprot
Q2EG98
canonical
ensembl
ENSMUSG00000048827
resolver
ensp
ENSMUSP00000051512
resolver
ensp
ENSMUSP00000104865
resolver
ensp
ENSMUSP00000148592
resolver
genesymbol
Pkd1l3
resolver
genesymbol_syn
PKD1L3
resolver
uniprot
A2A258
resolver
uniprot
E9QPA5
resolver
uniprot
Q2EG93
resolver
uniprot
Q2EG94
resolver
uniprot
Q2EG95
resolver
uniprot
Q2EG96
resolver
uniprot
Q2EG97
resolver
uniprot
Q2EG99
resolver
uniprot
Q7TN87
resolver
uniprot_entry
A2A258_MOUSE
resolver
uniprot_entry
PK1L3_MOUSE
resolver
uniprot_sec
E9QPA5
resolver
uniprot_sec
Q2EG93
resolver
uniprot_sec
Q2EG94
resolver
uniprot_sec
Q2EG95
resolver
uniprot_sec
Q2EG96
resolver
uniprot_sec
Q2EG97
resolver
uniprot_sec
Q2EG99
resolver
uniprot_sec
Q7TN87
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:20406802). Non-selective cation channel activity is inhibited by capsaicin (PubMed:22420714). Regulation of non-selective cation channel activity by external Ca(2+) is bimodal, first sensitizing and subsequently inactivating the current (By similarity). The apo (closed) heterotetramer has an asymmetric selectivity filter (SF) guarded by Lys-2069 in absence of Ca(2+) (PubMed:34381056). However, Ca(2+)-entrance to the SF vestibule is accompanied by a swing motion of Lys-2069 on PKD1L3 (PubMed:34381056). {ECO:0000250|UniProtKB:Q7Z443, ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:22420714, ECO:0000269|PubMed:34381056}.
uniprot
proteins
amino_acid_sequence
MLLQRRSWLWLYIRIGVILGDILGRKPSIREQHGGNSCYQLNRLFCDFQEADNYCHAQRGRLAHTWNPKLRGFLKSFLNEETVWWVRGNLTLPGSHPGINQTGGDDVLRNQKPGECPSVVTHSNAVFSRWNLCIEKHHFICQAAAFPPQGASIWRNEFGPGPLLPMKRRGAETERHMIPGNGPPLAMCHQPAPPELFETLCFPIDPASSAPPKATHRMTITSLTGRPQVTSDTLASSSPPQGTSDTPASSSPPQVTSATSASSSPPQGTSDTPASSSPPQVTSATSASSSPPQGTSDTPASSSPPQVTSATSASSSPPQGTSDTPASSSPPQVTSATSASSSPPQGTSDTPASSSPPQGTLDTPSSSSPPQGTSDTPASSSPPQGTSETPASNSPPQGTSETPGFSSPPQVTTATLVSSSPPQVTSETPASSSPTQVTSETPASSSPTQVTSDTPASNSPPQGTSDTPGFSSPTQVTTATLVSSSPPQVTSDTPASSSPPQVTSDTPASSSPPQVTSETPASSSPPQVTSDTSASISPPQVISDTPASSSPPQVTSETPASSSPTNMTSDTPASSSPTNMTSDTPASSSPTNMTSDTPASSSPPWPVITEVTRPESTIPAGRSLANITSKAQEDSPLGVISTHPQMSFQSSTSQALDETAGERVPTIPDFQAHSEFQKACAILQRLRDFLPTSPTSAQVSVANLLIDLSEQLLVLPFQKNNSWSSQTPAVSCPFQPLGRLTTTEKSSHQMAQQDMEQVEDMLETSLMALGEIHRAFCQQSLCPQSAVTLASPSATLMLSSQNVSTLPLSTYTLGEPAPLTLGFPSAEALKELLNKHPGVNLQVTGLAFNPFKTLDDKNIVGSIGNVQLSSAYQSIRVHDLIEDIEIMLWRNASMETQPTSLNTSTDHFTISVNITSLEKTLIVTIEPESPLLMTLHLGFQDQLAHTHFYLNISLPRDQVWQKDEEYTWVLTPENLWYGTGTYYIMAVENKSTEAAQHTPVLVSVVTAVTQCYFWDRYNRTWKSDGCQVGPKSTILKTQCLCDHLTFFSSDFFIVPRTVDVENTIKLLLHVTNNPVGVSLLSSLLGFYILLAMWASRKDREDMQKVKVTVLADNDPSSASHYLIQVYTGYRRRAATTAKVVITLYGSEGHSEPHHLCDPEKTVFERGALDVFLLSTGSWLGDLHGLRLWHDNSGDSPSWYVSQVIVSDMTTRKKWHFQCNCWLAVDLGNCERDRVFTPASRSELSSFRHLFSSTIVEKFTQDYLWLSVATRHPWNQFTRVQRLSCCMALLLCDMVINIMFWKMGGTTAKRGTEQLGPLAVTLSELLVSIQTSIILFPIHLIFGRLFQLIHPPEALPQLPFIQAAWPPALVCESPSLTQVVKELKETVGFLLRRNTQLLSECEPSSCSSCDINKLAKLLSGLIYCHLEDEGCHQQTESHWEDAVSENHYHFCRYLLQLLRRLKAHLEALGATQDHQSCDFSEAVSQLQNLQELLETQTLRRGPGPCRHSTSFPILSPGEGKKPMSFCLFRWLKCSCWLLLGVISLASAFFITLYSLELDKDQATSWVISMMLSVLQDIFISQPIKVIFLTLLFSLMANHMPWLNKDKEQHARRIVALWAKCPWSAPGLRDKNNPIYTAPAMNNLAKPTRKAWKKQLSKLTGGTLVQILFLTLLMTTVYSAKDSSRFFLHRAIWKRFSHRFSEIKTVEDFYPWANGTLLPNLYGDYRGFITDGNSFLLGNVLIRQTRIPNDIFFPGSLHKQMKSPPQHQEDRENYGAGWVPPDTNITKVDSIWHYQNQESLGGYPIQGELATYSGGGYVVRLGRNHSAATRVLQHLEQRRWLDHCTKALFVEFTVFNANVNLLCAVTLILESSGVGTFLTSLQLDSLTSLQSSERGFAWIVSQVVYYLLVCYYAFIQGCRLKRQRLAFFTRKRNLLDTSIVLISFSILGLSMQSLSLLHKKMQQYHCDRDRFISFYEALRVNSAVTHLRGFLLLFATVRVWDLLRHHAQLQVINKTLSKAWDEVLGFILIIVVLLSSYAMTFNLLFGWSISDYQSFFRSIVTVVGLLMGTSKHKEVIALYPILGSLLVLSSIILMGLVIINLFVSAILIAFGKERKACEKEATLTDMLLQKLSSLLGIRLHQNPSEEHADNTGY
uniprot
proteins
function
FUNCTION: Pore-forming subunit of a heterotetrameric, non-selective cation channel that is permeable to Ca(2+) (PubMed:16891422, PubMed:18535624, PubMed:20406802, PubMed:21185261, PubMed:22420714, PubMed:34381056). Also shows permeability towards NA(1+), K(+) and Mg(2+) (PubMed:18535624, PubMed:34381056). Heterotetrameric complex channel is activated by external low pH and Ca(2+), but opens only when the extracellular pH rises again and after the removal of acid stimulus (PubMed:16891422, PubMed:16929298, PubMed:18535624, PubMed:20406802, PubMed:34381056). 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:21098668, PubMed:21625513). {ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:16929298, ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:20406802, ECO:0000269|PubMed:21098668, ECO:0000269|PubMed:21185261, ECO:0000269|PubMed:21625513, ECO:0000269|PubMed:22420714, ECO:0000269|PubMed:34381056}.
uniprot
proteins
mass_dalton
236389
uniprot
proteins
mutagenesis
MUTAGEN 2049; /note="D->N: Little or no effect on calcium channel activity."; /evidence="ECO:0000269|PubMed:21185261"; MUTAGEN 2072; /note="E->Q: Little or no effect on calcium channel activity."; /evidence="ECO:0000269|PubMed:21185261
uniprot
proteins
post_translational_modification
PTM: Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity. {ECO:0000255|PROSITE-ProRule:PRU00098}.
uniprot
proteins
protein_family
Polycystin family
uniprot
proteins
pubmed
12782129
uniprot
proteins
pubmed
16805797
uniprot
proteins
pubmed
16891422
uniprot
proteins
pubmed
16929298
uniprot
proteins
pubmed
18535624
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20406802
uniprot
proteins
pubmed
20538909
uniprot
proteins
pubmed
20605874
uniprot
proteins
pubmed
21098668
uniprot
proteins
pubmed
21185261
uniprot
proteins
pubmed
21625513
uniprot
proteins
pubmed
22420714
uniprot
proteins
pubmed
34381056
uniprot
proteins
sequence_length
2151
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21185261}; Multi-pass membrane protein {ECO:0000269|PubMed:34381056}. Note=Interaction with PKD2L1 is required for localization to the cell membrane. {ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:20538909, ECO:0000269|PubMed:21185261}.
uniprot
proteins
transmembrane_region
TRANSMEM 1074..1094; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1284..1304; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1321..1341; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1534..1554; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1576..1596; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1666..1676; /note="Helical"; /evidence="ECO:0000269|PubMed:34381056, ECO:0007744|PDB:7D7E, ECO:0007744|PDB:7D7F"; TRANSMEM 1893..1921; /note="Helical"; /evidence="ECO:0000269|PubMed:34381056, ECO:0007744|PDB:7D7E, ECO:0007744|PDB:7D7F"; TRANSMEM 1931..1949; /note="Helical"; /evidence="ECO:0000269|PubMed:34381056, ECO:0007744|PDB:7D7E, ECO:0007744|PDB:7D7F"; TRANSMEM 1981..2002; /note="Helical"; /evidence="ECO:0000269|PubMed:34381056, ECO:0007744|PDB:7D7E, ECO:0007744|PDB:7D7F"; TRANSMEM 2020..2044; /note="Helical"; /evidence="ECO:0000269|PubMed:34381056, ECO:0007744|PDB:7D7E, ECO:0007744|PDB:7D7F"; TRANSMEM 2078..2097; /note="Helical"; /evidence="ECO:0000269|PubMed:34381056, ECO:0007744|PDB:7D7E, ECO:0007744|PDB:7D7F
uniprot
proteins