Calhm1
entrez
546729
canonical
uniprot
D3Z291
canonical
ensembl
ENSMUSG00000079258
resolver
ensp
ENSMUSP00000107444
resolver
enst
ENSMUST00000111813
resolver
genesymbol
Calhm1
resolver
uniprot
A0A1Y1C8H8
resolver
uniprot_entry
A0A1Y1C8H8_MOUSE
resolver
uniprot_entry
CAHM1_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by membrane voltage and extracellular Ca(2+). Inhibited by Gd(3+), ruthenium red, and Zn(2+) and partially inhibited by 2-aminoethoxydiphenyl borate. {ECO:0000250|UniProtKB:Q8IU99}.
uniprot
proteins
amino_acid_sequence
MDKFRMIFQFLQSNQESFMNGICGIMALASAQMYSAFDFNCPCLPGYNVVYSLGILLTPPLVLFLLGLVMNNNISMLAEEWKRPAGRRAKDPAVLRYMFCSMAQRALIAPVVWVAVTLLDGKCFLCAFCTAVPVATLGNGSLVPGLPAPELARLLARVPCPEIYDGNWLLAREVAVRYLRCISQALGWSFVLLTTLLAFVVRSVRPCFTQVAFLKSKYWSHYIDIERKLFDETCTEHAKAFAKVCIQQFFEAMNHDLELGHTHGVLATATATATATEAVQSPSDRTEEEREKLRGITDQGTMNRLLTSWHKCKPPLRLGQEAPLMSNGWAGGEPRPPRKEVATYFSKV
uniprot
proteins
function
FUNCTION: Pore-forming subunit of gustatory voltage-gated ion channels required for sensory perception of sweet, bitter and umami tastes (PubMed:23467090). With CALHM3 forms a fast-activating voltage-gated ATP-release channel in type II taste bud cells, ATP acting as a neurotransmitter to activate afferent neural gustatory pathways (PubMed:23467090, PubMed:29681531). Acts both as a voltage-gated and calcium-activated ion channel: mediates neuronal excitability in response to membrane depolarization and low extracellular Ca(2+) concentration. Has poor ion selectivity and forms a wide pore (around 14 Angstroms) that mediates permeation of small ions including Ca(2+), Na(+), K(+) and Cl(-), as well as larger ions such as ATP(4-) (PubMed:22711817, PubMed:28734079, PubMed:29681531, PubMed:33788965). Mediates Ca(2+) influx and downstream activation of the ERK1 and ERK2 cascade in neurons (By similarity). Triggers endoplasmic reticulum stress by reducing the calcium content of the endoplasmic reticulum (By similarity). May indirectly control amyloid precursor protein (APP) proteolysis and aggregated amyloid-beta (Abeta) peptides levels in a Ca(2+) dependent manner (By similarity). {ECO:0000250|UniProtKB:Q8IU99, ECO:0000269|PubMed:22711817, ECO:0000269|PubMed:23467090, ECO:0000269|PubMed:29681531, ECO:0000269|PubMed:33788965}.
uniprot
proteins
mass_dalton
38827
uniprot
proteins
mutagenesis
MUTAGEN 23; /note="C->S: Increases channel trafficking to the plasma membrane and ATP release."; /evidence="ECO:0000269|PubMed:28734079"; MUTAGEN 76..77; /note="ML->AA: Affects basolateral membrane sorting in vitro but not in vivo; when associated with A-222 and A-225."; /evidence="ECO:0000269|PubMed:30804437"; MUTAGEN 100; /note="C->S: Decreases palmitoylation and only slightly increases channel activity. Has no significant effect on channel trafficking to the plasma membrane. Loss of palmitoylation, gain-of-function and high cytotoxicity; when associated with S-207."; /evidence="ECO:0000269|PubMed:28734079"; MUTAGEN 123; /note="C->S: Decreases channel trafficking to the plasma membrane. Abolishes ATP release."; /evidence="ECO:0000269|PubMed:28734079"; MUTAGEN 126; /note="C->S: Decreases channel trafficking to the plasma membrane. Abolishes ATP release."; /evidence="ECO:0000269|PubMed:28734079"; MUTAGEN 139; /note="N->Q: Loss of N-glycosylation associated with enhanced proteosomal degradation and impaired channel trafficking to plasma membrane."; /evidence="ECO:0000269|PubMed:33788965"; MUTAGEN 207; /note="C->S: Has no significant effect on ATP release or channel trafficking to the plasma membrane. Loss of palmitoylation, gain-of-function and high cytotoxicity; when associated with S-100."; /evidence="ECO:0000269|PubMed:28734079"; MUTAGEN 222; /note="Y->A: Affects basolateral membrane sorting in vitro but not in vivo; when associated with 76-A-A-77 and A-225."; /evidence="ECO:0000269|PubMed:30804437"; MUTAGEN 225; /note="I->A: Affects basolateral membrane sorting in vitro but not in vivo; when associated with 76-A-A-77 and A-222."; /evidence="ECO:0000269|PubMed:30804437"; MUTAGEN 234; /note="C->S: Decreases ATP release. Does not affect channel trafficking to the plasma membrane."; /evidence="ECO:0000269|PubMed:28734079"; MUTAGEN 245; /note="C->S: Increases channel trafficking to the plasma membrane. Decreases ATP release."; /evidence="ECO:0000269|PubMed:28734079"; MUTAGEN 312; /note="C->S: Decreases ATP release. Does not affect channel trafficking to the plasma membrane."; /evidence="ECO:0000269|PubMed:28734079
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. Assembly with CALHM3 is associated with N-glycan remodeling and formation of hybrid complex- and high mannose-type glycochains. This N-glycan processing regulates channel trafficking and gating kinetics. {ECO:0000269|PubMed:33788965}.; PTM: Palmitoylated by ZDHHC3, ZDHHC20 and possibly ZDHHC7. Palmitoylation regulates voltage-dependent gating of the channel by shifting it toward more depolarized potentials. {ECO:0000269|PubMed:28734079}.
uniprot
proteins
protein_family
CALHM family
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
22711817
uniprot
proteins
pubmed
22723178
uniprot
proteins
pubmed
23467090
uniprot
proteins
pubmed
28734079
uniprot
proteins
pubmed
29681531
uniprot
proteins
pubmed
30804437
uniprot
proteins
pubmed
33788965
uniprot
proteins
sequence_length
348
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IU99}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IU99}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IU99}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IU99}. Basolateral cell membrane {ECO:0000269|PubMed:30804437}; Multi-pass membrane protein. Note=Localizes to the basolateral membrane of epithelial cells including taste cells (PubMed:30804437). Colocalizes with HSPA5 at the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q8IU99, ECO:0000269|PubMed:30804437}.
uniprot
proteins
transmembrane_region
TRANSMEM 21..36; /note="Helical; Name=S1"; /evidence="ECO:0000250|UniProtKB:H2MCM1, ECO:0000250|UniProtKB:Q8IU99"; TRANSMEM 49..71; /note="Helical; Name=S2"; /evidence="ECO:0000250|UniProtKB:H2MCM1, ECO:0000250|UniProtKB:Q8IU99"; TRANSMEM 99..124; /note="Helical; Name=S3"; /evidence="ECO:0000250|UniProtKB:H2MCM1, ECO:0000250|UniProtKB:Q8IU99"; TRANSMEM 180..205; /note="Helical; Name=S4"; /evidence="ECO:0000250|UniProtKB:H2MCM1, ECO:0000250|UniProtKB:Q8IU99
uniprot
proteins