Tpcn1
entrez
252972
canonical
uniprot
Q9EQJ0
canonical
ensembl
ENSMUSG00000032741
resolver
ensp
ENSMUSP00000042188
resolver
ensp
ENSMUSP00000280965
resolver
ensp
ENSMUSP00000280968
resolver
genesymbol
Tpcn1
resolver
genesymbol_syn
Kiaa1169
resolver
genesymbol_syn
Tpc1
resolver
uniprot
Q3V2Z6
resolver
uniprot
Q6ZPW5
resolver
uniprot_entry
TPC1_MOUSE
resolver
uniprot_sec
Q3V2Z6
resolver
uniprot_sec
Q6ZPW5
resolver
activity_regulation
ACTIVITY REGULATION: Na(+) current is inhibited by ATP in a MTORC-dependent manner. ATP sensitivity is independent of PI(3,5)P2 (By similarity). Probably regulated by Mg(2+) ions, cytosolic Mg(2+) selectively inhibits outward current while lysosomal Mg(2+) modestly inhibits both the outward and inward currents. In the absence of Mg(2+), NAADP readily activates TPCN2, with properties similar to PI(3,5)P2 (By similarity). Both current elicited by PI(3,5)P2 as well as NAADP are inhibited by tetrandrine (By similarity). {ECO:0000250|UniProtKB:Q8NHX9, ECO:0000250|UniProtKB:Q9ULQ1}.
uniprot
proteins
amino_acid_sequence
MAVSLDDDVPLILTLDEAESAPLPPSNSLGQEQLPSKNGGSHSIHNSQVPSLVSGADSPPSSPTGHNWEMNYQEAAIYLQEGQNNDKFFTHPKDARALAAYLFVHNHFFYMMELLTALLLLLLSLCESPAVPVLKLHTYVHATLELFALMVVVFELCMKLRWLGFHTFVRHKRTMVKTSVLVVQFIEAIVVLVRQTSHVRVTRALRCIFLVDCRYCGGVRRNLRQIFQSLPPFMDILLLLLFFMIIFAILGFYLFSTNPSDPYFSTLENSIVNLFVLLTTANFPDVMMPSYSRNPWSCVFFIVYLSIELYFIMNLLLAVVFDTFNDIEKHKFKSLLLHKRTAIQHAYGLLASQRRPAGISYRQFEGLMRFYKPRMSARERFLTFKALNQSNTPLLSLKDFYDIYEVAALQWKAKRNRQHWFDELPRTAFLIFKGINILVNSKAFQYFMYLVVAVNGVWILVETFMLKGGNFTSKHVPWSYLVFLTIYGVELFMKVAGLGPVEYLSSGWNLFDFSVTAFAFLGLLALTLNMEPFYFIVVLRPLQLLRLFKLKKRYRNVLDTMFELLPRMASLGLTLLTFYYSFAIVGMEFFNGRLTPNCCNTSTVADAYRFINHTVGNKTKVEEGYYYLNNFDNILNSFVTLFELTVVNNWYIIMEGVTSQTSHWSRLYFMTFYIVTMVVMTIIVAFILEAFVFRMNYSRKSQDSEVDSGIVIEKEMSKEELMAVLELYREERGTSSDVTRLLDTLSQMEKYQQNSMVFLGRRSRTKSDLSLKMYQEEIQEWYEEHAREQEQQKLRGSVPGPAAQQPPGSRQRSQTVT
uniprot
proteins
function
FUNCTION: Intracellular channel initially characterized as a non-selective Ca(2+)-permeable channel activated by NAADP (nicotinic acid adenine dinucleotide phosphate), it is also a voltage-gated highly-selective Na(+) channel activated directly by PI(3,5)P2 (phosphatidylinositol 3,5-bisphosphate) that senses pH changes and confers electrical excitability to organelles (PubMed:23063126, PubMed:23394946, PubMed:24776928). Localizes to the early and recycling endosomes membranes where it plays a role in the uptake and processing of proteins and regulates organellar membrane excitability, membrane trafficking and pH homeostasis (PubMed:28855648). Ion selectivity is not fixed but rather agonist-dependent and under defined ionic conditions, can be readily activated by both NAADP and PI(3,5)P2 (By similarity). Required for mTOR-dependent nutrient sensing (PubMed:23394946). {ECO:0000250|UniProtKB:Q8NHX9, ECO:0000269|PubMed:23063126, ECO:0000269|PubMed:23394946, ECO:0000269|PubMed:24776928, ECO:0000269|PubMed:28855648}.
uniprot
proteins
mass_dalton
94496
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:28855648}.
uniprot
proteins
protein_family
Calcium channel alpha-1 subunit (TC 1.A.1.11) family
uniprot
proteins
protein_family
Two pore calcium channel subfamily
uniprot
proteins
pubmed
12080145
uniprot
proteins
pubmed
14621295
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23063126
uniprot
proteins
pubmed
23394946
uniprot
proteins
pubmed
24776928
uniprot
proteins
pubmed
25722412
uniprot
proteins
pubmed
28855648
uniprot
proteins
sequence_length
817
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9ULQ1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9ULQ1}. Endosome membrane {ECO:0000250|UniProtKB:Q9ULQ1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9ULQ1}. Early endosome membrane {ECO:0000269|PubMed:28855648}; Multi-pass membrane protein {ECO:0000269|PubMed:28855648}. Recycling endosome membrane {ECO:0000269|PubMed:28855648}; Multi-pass membrane protein {ECO:0000269|PubMed:28855648}.
uniprot
proteins
transmembrane_region
TRANSMEM 114..134; /note="Helical; Name=S1 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 138..158; /note="Helical; Name=S2 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 173..193; /note="Helical; Name=S3 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 203..221; /note="Helical; Name=S4 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 236..256; /note="Helical; Name=S5 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 299..319; /note="Helical; Name=S6 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 446..466; /note="Helical; Name=S1 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 481..501; /note="Helical; Name=S2 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 505..527; /note="Helical; Name=S3 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 536..550; /note="Helical; Name=S4 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 570..590; /note="Helical; Name=S5 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 672..692; /note="Helical; Name=S6 of repeat II"; /evidence="ECO:0000255
uniprot
proteins