TPCN1
entrez
53373
canonical
uniprot
Q9ULQ1
canonical
ensembl
ENSG00000186815
resolver
ensp
ENSP00000335300
resolver
ensp
ENSP00000376350
resolver
ensp
ENSP00000448083
resolver
ensp
ENSP00000549922
resolver
ensp
ENSP00000549937
resolver
ensp
ENSP00000658722
resolver
enst
ENST00000392569
resolver
genesymbol
TPCN1
resolver
genesymbol_syn
KIAA1169
resolver
genesymbol_syn
TPC1
resolver
hgnc
HGNC:18182
resolver
uniprot
A7E258
resolver
uniprot
B3KSG7
resolver
uniprot
B7Z3R2
resolver
uniprot
J3KPN2
resolver
uniprot
Q86XS9
resolver
uniprot
Q8NC20
resolver
uniprot_entry
B3KSG7_HUMAN
resolver
uniprot_entry
B7Z3R2_HUMAN
resolver
uniprot_entry
J3KPN2_HUMAN
resolver
uniprot_entry
TPC1_HUMAN
resolver
uniprot_sec
A7E258
resolver
uniprot_sec
Q86XS9
resolver
uniprot_sec
Q8NC20
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 (PubMed:23394946). 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. {ECO:0000250|UniProtKB:Q8NHX9, ECO:0000269|PubMed:23394946, ECO:0000269|PubMed:25722412}.
uniprot
proteins
amino_acid_sequence
MAVSLDDDVPLILTLDEGGSAPLAPSNGLGQEELPSKNGGSYAIHDSQAPSLSSGGESSPSSPAHNWEMNYQEAAIYLQEGENNDKFFTHPKDAKALAAYLFAHNHLFYLMELATALLLLLLSLCEAPAVPALRLGIYVHATLELFALMVVVFELCMKLRWLGLHTFIRHKRTMVKTSVLVVQFVEAIVVLVRQMSHVRVTRALRCIFLVDCRYCGGVRRNLRQIFQSLPPFMDILLLLLFFMIIFAILGFYLFSPNPSDPYFSTLENSIVSLFVLLTTANFPDVMMPSYSRNPWSCVFFIVYLSIELYFIMNLLLAVVFDTFNDIEKRKFKSLLLHKRTAIQHAYRLLISQRRPAGISYRQFEGLMRFYKPRMSARERYLTFKALNQNNTPLLSLKDFYDIYEVAALKWKAKKNREHWFDELPRTALLIFKGINILVKSKAFQYFMYLVVAVNGVWILVETFMLKGGNFFSKHVPWSYLVFLTIYGVELFLKVAGLGPVEYLSSGWNLFDFSVTVFAFLGLLALALNMEPFYFIVVLRPLQLLRLFKLKERYRNVLDTMFELLPRMASLGLTLLIFYYSFAIVGMEFFCGIVFPNCCNTSTVADAYRWRNHTVGNRTVVEEGYYYLNNFDNILNSFVTLFELTVVNNWYIIMEGVTSQTSHWSRLYFMTFYIVTMVVMTIIVAFILEAFVFRMNYSRKNQDSEVDGGITLEKEISKEELVAVLELYREARGASSDVTRLLETLSQMERYQQHSMVFLGRRSRTKSDLSLKMYQEEIQEWYEEHAREQEQQRQLSSSAAPAAQQPPGSRQRSQTVT
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:19620632, 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 (Probable) (PubMed:23394946). 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 (Probable). Required for mTOR-dependent nutrient sensing (Probable) (PubMed:23394946). {ECO:0000269|PubMed:19620632, ECO:0000269|PubMed:23063126, ECO:0000269|PubMed:23394946, ECO:0000269|PubMed:24776928, ECO:0000305|PubMed:32679067}.; FUNCTION: (Microbial infection) During Ebola virus (EBOV) infection, controls the movement of endosomes containing virus particles and is required by EBOV to escape from the endosomal network into the cell cytoplasm. {ECO:0000269|PubMed:25722412}.
uniprot
proteins
mass_dalton
94147
uniprot
proteins
mutagenesis
MUTAGEN 219..223; /note="RRNLR->QQNLQ: Loss of voltage sensitivity."; /evidence="ECO:0000269|PubMed:24776928"; MUTAGEN 273; /note="L->P: Loss of NAADP-mediated cytoplasmic calcium release."; /evidence="ECO:0000269|PubMed:19620632"; MUTAGEN 539; /note="R->I: Loss of voltage sensitivity."; /evidence="ECO:0000269|PubMed:24776928"; MUTAGEN 740..741; /note="LL->AA: No effect on subcellular location."; /evidence="ECO:0000269|PubMed:20880839
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
10574461
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
19387438
uniprot
proteins
pubmed
19620632
uniprot
proteins
pubmed
20880839
uniprot
proteins
pubmed
23063126
uniprot
proteins
pubmed
23394946
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24776928
uniprot
proteins
pubmed
25722412
uniprot
proteins
pubmed
32679067
uniprot
proteins
pubmed
33758061
uniprot
proteins
pubmed
34362892
uniprot
proteins
sequence_length
816
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:19620632, ECO:0000269|PubMed:23063126, ECO:0000269|PubMed:25722412}; Multi-pass membrane protein {ECO:0000269|PubMed:19620632}. Endosome membrane {ECO:0000269|PubMed:19620632, ECO:0000269|PubMed:20880839, ECO:0000269|PubMed:23063126, ECO:0000269|PubMed:25722412}; Multi-pass membrane protein {ECO:0000269|PubMed:19620632}. 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 113..133; /note="Helical; Name=S1 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 135..155; /note="Helical; Name=S2 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 178..198; /note="Helical; Name=S3 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 201..220; /note="Helical; Name=S4 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 235..255; /note="Helical; Name=S5 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 295..315; /note="Helical; Name=S6 of repeat I"; /evidence="ECO:0000255"; TRANSMEM 445..465; /note="Helical; Name=S1 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 480..500; /note="Helical; Name=S2 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 504..526; /note="Helical; Name=S3 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 535..549; /note="Helical; Name=S4 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 574..594; /note="Helical; Name=S5 of repeat II"; /evidence="ECO:0000255"; TRANSMEM 671..691; /note="Helical; Name=S6 of repeat II"; /evidence="ECO:0000255
uniprot
proteins