CALHM1
entrez
255022
canonical
uniprot
Q8IU99
canonical
ensembl
ENSG00000185933
resolver
ensp
ENSP00000329926
resolver
enst
ENST00000329905
resolver
genesymbol
CALHM1
resolver
genesymbol_syn
FAM26C
resolver
hgnc
HGNC:23494
resolver
uniprot
Q5W091
resolver
uniprot_entry
CAHM1_HUMAN
resolver
uniprot_sec
Q5W091
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:0000269|PubMed:22711817}.
uniprot
proteins
amino_acid_sequence
MMDKFRMIFQFLQSNQESFMNGICGIMALASAQMYSAFDFNCPCLPGYNAAYSAGILLAPPLVLFLLGLVMNNNVSMLAEEWKRPLGRRAKDPAVLRYMFCSMAQRALIAPVVWVAVTLLDGKCFLCAFCTAVPVSALGNGSLAPGLPAPELARLLARVPCPEIYDGDWLLAREVAVRYLRCISQALGWSFVLLTTLLAFVVRSVRPCFTQAAFLKSKYWSHYIDIERKLFDETCTEHAKAFAKVCIQQFFEAMNHDLELGHTHGTLATAPASAAAPTTPDGAEEEREKLRGITDQGTMNRLLTSWHKCKPPLRLGQEEPPLMGNGWAGGGPRPPRKEVATYFSKV
uniprot
proteins
function
FUNCTION: Pore-forming subunit of gustatory voltage-gated ion channels required for sensory perception of sweet, bitter and umami tastes (By similarity). 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 (By similarity) (PubMed:23467090). 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 (PubMed:22711817, PubMed:23300080). 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:23300080, PubMed:32832629, PubMed:37380652). Mediates Ca(2+) influx and downstream activation of the ERK1 and ERK2 cascade in neurons (PubMed:23345406). Triggers endoplasmic reticulum stress by reducing the Ca(2+) content of the endoplasmic reticulum (PubMed:21574960). May indirectly control amyloid precursor protein (APP) proteolysis and aggregated amyloid-beta (Abeta) peptides levels in a Ca(2+)-dependent manner (PubMed:18585350). {ECO:0000250|UniProtKB:D3Z291, ECO:0000269|PubMed:18585350, ECO:0000269|PubMed:21574960, ECO:0000269|PubMed:22711817, ECO:0000269|PubMed:23300080, ECO:0000269|PubMed:23345406, ECO:0000269|PubMed:23467090, ECO:0000269|PubMed:32832629, ECO:0000269|PubMed:37380652}.
uniprot
proteins
mass_dalton
38264
uniprot
proteins
mutagenesis
MUTAGEN 10; /note="Q->R: Decreases channel conductance. Decreases the inhibition of channel activity by ruthenium red."; /evidence="ECO:0000269|PubMed:37380652"; MUTAGEN 13; /note="Q->R: Decreases channel conductance. Decreases the inhibition of channel activity by ruthenium red."; /evidence="ECO:0000269|PubMed:37380652"; MUTAGEN 16; /note="Q->R: Markedly decreases channel conductance and confers resistance to inhibition by ruthenium red."; /evidence="ECO:0000269|PubMed:37380652"; MUTAGEN 67; /note="L->W: Decreases channel expression at the plasma membrane."; /evidence="ECO:0000269|PubMed:37380652"; MUTAGEN 72; /note="N->G: Significant inhibition on the control of cytosolic Ca(2+) levels. Does not affect ion channel activity."; /evidence="ECO:0000269|PubMed:18585350, ECO:0000269|PubMed:22711817"; MUTAGEN 74; /note="N->A: Has no effect on glycosylation."; /evidence="ECO:0000269|PubMed:18585350"; MUTAGEN 109; /note="I->W: Results in approximately five-fold increase in channel current density. Does not affect channel expression at the plasma membrane."; /evidence="ECO:0000269|PubMed:37380652"; MUTAGEN 112; /note="V->W: Decreases channel expression at the plasma membrane. Does not affect channel conductance."; /evidence="ECO:0000269|PubMed:37380652"; MUTAGEN 114; /note="W->A: Impairs the ability to activate the ERK1 and ERK2 cascade."; /evidence="ECO:0000269|PubMed:23345406"; MUTAGEN 116; /note="A->W: Decreases channel expression at the plasma membrane. Does not affect channel conductance."; /evidence="ECO:0000269|PubMed:37380652"; MUTAGEN 121; /note="D->C: Impaired ion channel activity in response to change in extracellular Ca(2+) concentration."; /evidence="ECO:0000269|PubMed:22711817"; MUTAGEN 121; /note="D->E: No effect."; /evidence="ECO:0000269|PubMed:22711817"; MUTAGEN 140; /note="N->A: Prevents glycosylation and impairs ability to activate the ERK1 and ERK2 cascade."; /evidence="ECO:0000269|PubMed:18585350, ECO:0000269|PubMed:23345406"; MUTAGEN 163; /note="E->A: No effect."; /evidence="ECO:0000269|PubMed:22711817"; MUTAGEN 166; /note="D->R: No effect."; /evidence="ECO:0000269|PubMed:22711817"; MUTAGEN 192; /note="V->W: Impairs channel expression at the plasma membrane."; /evidence="ECO:0000269|PubMed:37380652"; MUTAGEN 196; /note="T->W: Decreases channel expression at the plasma membrane. Does not affect channel conductance."; /evidence="ECO:0000269|PubMed:37380652"; MUTAGEN 199; /note="A->W: Increases channel expression at the plasma membrane. Does not affect channel conductance."; /evidence="ECO:0000269|PubMed:37380652
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:0000250|UniProtKB:D3Z291}.; PTM: Palmitoylated by ZDHHC3, ZDHHC20 and possibly ZDHHC7. Palmitoylation regulates voltage-dependent gating of the channel by shifting it toward more depolarized potentials. {ECO:0000250|UniProtKB:D3Z291}.
uniprot
proteins
protein_family
CALHM family
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18585350
uniprot
proteins
pubmed
19070563
uniprot
proteins
pubmed
19191331
uniprot
proteins
pubmed
19191332
uniprot
proteins
pubmed
19472444
uniprot
proteins
pubmed
19545933
uniprot
proteins
pubmed
19655363
uniprot
proteins
pubmed
19997627
uniprot
proteins
pubmed
20061624
uniprot
proteins
pubmed
20164592
uniprot
proteins
pubmed
20847397
uniprot
proteins
pubmed
21378601
uniprot
proteins
pubmed
21574960
uniprot
proteins
pubmed
22711817
uniprot
proteins
pubmed
23300080
uniprot
proteins
pubmed
23345406
uniprot
proteins
pubmed
23467090
uniprot
proteins
pubmed
32832629
uniprot
proteins
pubmed
37380652
uniprot
proteins
sequence_length
346
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein {ECO:0000269|PubMed:18585350, ECO:0000269|PubMed:22711817, ECO:0000269|PubMed:23300080}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18585350}; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:D3Z291}. Note=Colocalizes with HSPA5 at the endoplasmic reticulum (PubMed:18585350). Localizes to the basolateral membrane of epithelial cells including taste cells (By similarity). {ECO:0000250|UniProtKB:D3Z291, ECO:0000269|PubMed:18585350}.
uniprot
proteins
transmembrane_region
TRANSMEM 22..37; /note="Helical; Name=S1"; /evidence="ECO:0000250|UniProtKB:H2MCM1, ECO:0000269|PubMed:37380652, ECO:0007744|PDB:8GMP"; TRANSMEM 50..72; /note="Helical; Name=S2"; /evidence="ECO:0000250|UniProtKB:H2MCM1, ECO:0000269|PubMed:37380652, ECO:0007744|PDB:8GMP"; TRANSMEM 100..125; /note="Helical; Name=S3"; /evidence="ECO:0000250|UniProtKB:H2MCM1, ECO:0000269|PubMed:37380652, ECO:0007744|PDB:8GMP"; TRANSMEM 181..206; /note="Helical; Name=S4"; /evidence="ECO:0000250|UniProtKB:H2MCM1, ECO:0000269|PubMed:37380652, ECO:0007744|PDB:8GMP
uniprot
proteins