J3QMI4
uniprot
J3QMI4
canonical
amino_acid_sequence
MDRFRMLFQHLQSSSESVMNGICLLLAAVTVKIYSSLDFNCPCLERYNALYGLGLLLTPPLALFLCGLLVNRQSVLMVEEWRRPAGHRRKDLGIIRYMCSSVLQRALAAPLVWILLALLDGKCFVCAFSNSVDPEKFLDFANMTPRQVQLFLAKVPCKEDELVKNSPARKAVSRYLRCLSQAIGWSITLLVIVVAFLARCLRPCFDQTVFLQRRYWSNYMDLEQKLFDETCCEHARDFAHRCVLHFFANMQSELRALGLRRDPAGGIPESQESSEPPELREDRDSGNGKAHLRAISSREQVDQLLSTWYSSKPPLDLAASPRRWGPGLNHRAPIAAPGTKLCHQLNV
uniprot
proteins
function
FUNCTION: Pore-forming subunit of gustatory voltage-gated ion channels required for sensory perception of sweet, bitter and umami tastes. With CALHM1 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. 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-). {ECO:0000269|PubMed:29681531, ECO:0000269|PubMed:33788965}.
uniprot
proteins
mass_dalton
39328
uniprot
proteins
mutagenesis
MUTAGEN 76..77; /note="LM->AA: Affects basolateral membrane sorting in vitro but not in vivo; when associated with A-219 and A-222."; /evidence="ECO:0000269|PubMed:30804437"; MUTAGEN 99; /note="C->S: Loss of palmitoylation; when associated with S-200 and S-204. Markedly decreases ATP transport via CALHM1:CALHM3 channel. Does not affect channel assembly or trafficking to plasma membrane."; /evidence="ECO:0000269|PubMed:33788965"; MUTAGEN 142; /note="N->Q: Loss of N-glycosylation. Reduces channel conductance. Does not affect channel trafficking to plasma membrane."; /evidence="ECO:0000269|PubMed:33788965"; MUTAGEN 200; /note="C->S: Loss of palmitoylation; when associated with S-99 and S-204. Decreases ATP transport via CALHM1:CALHM3 channel. Does not affect channel assembly or trafficking to plasma membrane."; /evidence="ECO:0000269|PubMed:33788965"; MUTAGEN 204; /note="C->S: Loss of palmitoylation; when associated with S-99 and S-200. Decreases ATP transport via CALHM1:CALHM3 channel. Does not affect channel assembly or trafficking to plasma membrane."; /evidence="ECO:0000269|PubMed:33788965"; MUTAGEN 219; /note="Y->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 222; /note="L->A: Affects basolateral membrane sorting in vitro but not in vivo; when associated with 76-A-A-77 and A-219."; /evidence="ECO:0000269|PubMed:30804437
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:33788965}.; PTM: Palmitoylated by ZDHHC3 and ZDHHC15. Palmitoylation positively regulates CALHM1:CALHM3 channel conductance. {ECO:0000269|PubMed:33788965}.
uniprot
proteins
protein_family
CALHM family
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
29681531
uniprot
proteins
pubmed
30804437
uniprot
proteins
pubmed
33788965
uniprot
proteins
sequence_length
347
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:30804437, ECO:0000305|PubMed:29681531}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the basolateral membrane of epithelial cells including taste cells. {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 177..202; /note="Helical; Name=S4"; /evidence="ECO:0000250|UniProtKB:H2MCM1, ECO:0000250|UniProtKB:Q8IU99
uniprot
proteins