ANO6
entrez
196527
canonical
uniprot
Q4KMQ2
canonical
ensembl
ENSG00000177119
resolver
ensp
ENSP00000320087
resolver
ensp
ENSP00000391417
resolver
ensp
ENSP00000409126
resolver
ensp
ENSP00000413137
resolver
ensp
ENSP00000506600
resolver
ensp
ENSP00000506683
resolver
enst
ENST00000679426
resolver
genesymbol
ANO6
resolver
genesymbol_syn
TMEM16F
resolver
hgnc
HGNC:25240
resolver
uniprot
A0A7P0TBC5
resolver
uniprot
A6NNM6
resolver
uniprot
B3KX12
resolver
uniprot
B9EGG0
resolver
uniprot
E7ENK4
resolver
uniprot
E9PB30
resolver
uniprot
E9PCT2
resolver
uniprot
Q8N3Q2
resolver
uniprot_entry
A0A7P0TBC5_HUMAN
resolver
uniprot_entry
ANO6_HUMAN
resolver
uniprot_entry
B3KX12_HUMAN
resolver
uniprot_sec
A6NNM6
resolver
uniprot_sec
B9EGG0
resolver
uniprot_sec
E7ENK4
resolver
uniprot_sec
E9PB30
resolver
uniprot_sec
E9PCT2
resolver
uniprot_sec
Q8N3Q2
resolver
activity_regulation
ACTIVITY REGULATION: Exhibits synergistic gating by Ca(2+) and voltage (By similarity). Inhibited by some non-specific cation channel blockers such as: ruthenium red, 2-aminoethyl diphenylborinate (2APB), gadolinium and cadmium ions (By similarity). {ECO:0000250|UniProtKB:Q6P9J9}.; ACTIVITY REGULATION: (Microbial infection) Activated by SARS coronavirus-2/SARS-CoV-2 spike protein. {ECO:0000269|PubMed:33827113}.
uniprot
proteins
amino_acid_sequence
MKKMSRNVLLQMEEEEDDDDGDIVLENLGQTIVPDLGSLESQHDFRTPEFEEFNGKPDSLFFNDGQRRIDFVLVYEDESRKETNKKGTNEKQRRKRQAYESNLICHGLQLEATRSVLDDKLVFVKVHAPWEVLCTYAEIMHIKLPLKPNDLKNRSSAFGTLNWFTKVLSVDESIIKPEQEFFTAPFEKNRMNDFYIVDRDAFFNPATRSRIVYFILSRVKYQVINNVSKFGINRLVNSGIYKAAFPLHDCKFRRQSEDPSCPNERYLLYREWAHPRSIYKKQPLDLIRKYYGEKIGIYFAWLGYYTQMLLLAAVVGVACFLYGYLNQDNCTWSKEVCHPDIGGKIIMCPQCDRLCPFWKLNITCESSKKLCIFDSFGTLVFAVFMGVWVTLFLEFWKRRQAELEYEWDTVELQQEEQARPEYEARCTHVVINEITQEEERIPFTAWGKCIRITLCASAVFFWILLIIASVIGIIVYRLSVFIVFSAKLPKNINGTDPIQKYLTPQTATSITASIISFIIIMILNTIYEKVAIMITNFELPRTQTDYENSLTMKMFLFQFVNYYSSCFYIAFFKGKFVGYPGDPVYWLGKYRNEECDPGGCLLELTTQLTIIMGGKAIWNNIQEVLLPWIMNLIGRFHRVSGSEKITPRWEQDYHLQPMGKLGLFYEYLEMIIQFGFVTLFVASFPLAPLLALVNNILEIRVDAWKLTTQFRRLVPEKAQDIGAWQPIMQGIAILAVVTNAMIIAFTSDMIPRLVYYWSFSVPPYGDHTSYTMEGYINNTLSIFKVADFKNKSKGNPYSDLGNHTTCRYRDFRYPPGHPQEYKHNIYYWHVIAAKLAFIIVMEHVIYSVKFFISYAIPDVSKRTKSKIQREKYLTQKLLHENHLKDMTKNMGVIAERMIEAVDNNLRPKSE
uniprot
proteins
disease_involvement
DISEASE: Scott syndrome (SCTS) [MIM:262890]: A mild bleeding disorder due to impaired surface exposure of procoagulant phosphatidylserine (PS) on platelets and other blood cells, following activation with Ca(2+)-elevating agents. {ECO:0000269|PubMed:21107324}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Small-conductance calcium-activated nonselective cation (SCAN) channel which acts as a regulator of phospholipid scrambling in platelets and osteoblasts (PubMed:20056604, PubMed:21107324, PubMed:21908539, PubMed:22006324, PubMed:22946059). Phospholipid scrambling results in surface exposure of phosphatidylserine which in platelets is essential to trigger the clotting system whereas in osteoblasts is essential for the deposition of hydroxyapatite during bone mineralization (By similarity). Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Can generate outwardly rectifying chloride channel currents in airway epithelial cells and Jurkat T lymphocytes (By similarity). {ECO:0000250|UniProtKB:Q6P9J9, ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:21107324, ECO:0000269|PubMed:21908539, ECO:0000269|PubMed:22006324, ECO:0000269|PubMed:22946059}.; FUNCTION: (Microbial infection) Upon SARS coronavirus-2/SARS-CoV-2 infection, is activated by spike protein which increases the amplitude of spontaneous Ca(2+) signals and is required for spike-mediated syncytia. {ECO:0000269|PubMed:33827113}.
uniprot
proteins
mass_dalton
106165
uniprot
proteins
protein_family
Anoctamin family
uniprot
proteins
pubmed
15067359
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
20056604
uniprot
proteins
pubmed
21107324
uniprot
proteins
pubmed
21607626
uniprot
proteins
pubmed
21642943
uniprot
proteins
pubmed
21908539
uniprot
proteins
pubmed
21984732
uniprot
proteins
pubmed
22006324
uniprot
proteins
pubmed
22075693
uniprot
proteins
pubmed
22302790
uniprot
proteins
pubmed
22946059
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
33827113
uniprot
proteins
sequence_length
910
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:21107324, ECO:0000269|PubMed:22075693, ECO:0000269|PubMed:22946059}; Multi-pass membrane protein {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:21107324, ECO:0000269|PubMed:22075693, ECO:0000269|PubMed:22946059}. Note=Shows an intracellular localization according to PubMed:22075693.
uniprot
proteins
transmembrane_region
TRANSMEM 301..321; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q6P9J9"; TRANSMEM 376..396; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q6P9J9"; TRANSMEM 456..476; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q6P9J9"; TRANSMEM 510..530; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q6P9J9"; TRANSMEM 552..572; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q6P9J9"; TRANSMEM 602..621; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q6P9J9"; TRANSMEM 664..684; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q6P9J9"; TRANSMEM 685..705; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q6P9J9"; TRANSMEM 723..743; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q6P9J9"; TRANSMEM 837..857; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q6P9J9
uniprot
proteins