Tpcn1
entrez
246215
canonical
uniprot
Q9WTN5
canonical
ensembl
ENSRNOG00000059344
resolver
ensp
ENSRNOP00000072420
resolver
ensp
ENSRNOP00000104314
resolver
enst
ENSRNOT00000083890
resolver
enst
ENSRNOT00000166140
resolver
genesymbol
Tpcn1
resolver
genesymbol_syn
Tpc1
resolver
uniprot
A0A0G2K2X9
resolver
uniprot
A0ABK0LHM3
resolver
uniprot
Q6P6R1
resolver
uniprot_entry
A0A0G2K2X9_RAT
resolver
uniprot_entry
A0ABK0LHM3_RAT
resolver
uniprot_entry
TPC1_RAT
resolver
uniprot_sec
Q6P6R1
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
MSVILDDDVLLILTLDEELSAPLTPSNGLGQEDLPSKNGGGQSGPNSQVPSLVSGADSPPSSPPGHNWEMNYQEAAIYLQEGQNNDKFFTHPKDARALAAYLFVHNHFFYMMELLTALLLLLLSLCESPAVPALKLRTYVHATLELFALMVVVFELCMKLRWLGFHTFVRHKRTMVKTSVLVVQFIEAIVVLVRQTSHVRVTRALRCIFLVDCRYCGGVRRNLRQIFQSLPPFMDILLLLLFFMIIFAILGFYLFSTNPSDPYFNTLENSIVNLFVLLTTANFPDVMMPSYSRNPWSCVFFIVYLSIELYFIMNLLLAVVFDTFNDIEKHKFKSLLLHKRTAIQHAYHLLVSQRRPAGISYRQFEGLMRFYKPRMSARERFLTFKALNQSNTPLLSLKDFYDIYEVAALQWKAKKNRQHWFDELPRTAFLIFKGINILVNSKAFQYFMYLVVAVNGVWILVETFMLKGGNFISKHVPWSYLVFLTIYGVELFMKVAGLGPVEYLSSGWNLFDFSVTAFAFLGLLALTLNMEPFYFIVVLRPLQLLRLFKLKKRYRNVLDTMFELLPRMASLGLTLLTFYYSFAIVGMEFFSGRLSPNCCNSSTVADAYRFINHTVGNKTKVEEGYYYLNNFDNILNSFVTLFELTVVNNWYIIMEGVTSQTSHWSRLYFMTFYIVTMVVMTIIVAFILEAFVFRMNYSRKSQESEVDSGIVIEKEMSKEELLAILELHREARGTSSDVTRLLDTLSQMEKYQQNSMVFLGRRSRTKSDLSLKMYQEEIQEWYEEHAREQEQQQLRGSAPSPAAQQTPGSRQRSQTVT
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. 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. 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. Required for mTOR-dependent nutrient sensing. {ECO:0000250|UniProtKB:Q9ULQ1}.
uniprot
proteins
mass_dalton
94405
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9EQJ0}.
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
10753632
uniprot
proteins
pubmed
15489334
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:0000250|UniProtKB:Q9EQJ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9EQJ0}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q9EQJ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9EQJ0}.
uniprot
proteins
transmembrane_region
TRANSMEM 102..122; /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 575..595; /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