CLCN6
entrez
1185
canonical
uniprot
P51797
canonical
ensembl
ENSG00000011021
resolver
ensp
ENSP00000234488
resolver
ensp
ENSP00000308367
resolver
genesymbol
CLCN6
resolver
genesymbol_syn
KIAA0046
resolver
hgnc
HGNC:2024
resolver
uniprot
A8K1T4
resolver
uniprot
B4DGT7
resolver
uniprot
F8W9R3
resolver
uniprot
O60818
resolver
uniprot
O60819
resolver
uniprot
O60820
resolver
uniprot
O60821
resolver
uniprot
P78520
resolver
uniprot
P78521
resolver
uniprot
Q17R81
resolver
uniprot
Q5SNW2
resolver
uniprot
Q5SNW3
resolver
uniprot
Q5SNX1
resolver
uniprot
Q5SNX2
resolver
uniprot
Q5SNX3
resolver
uniprot
Q99427
resolver
uniprot
Q99428
resolver
uniprot
Q99429
resolver
uniprot_entry
CLCN6_HUMAN
resolver
uniprot_sec
A8K1T4
resolver
uniprot_sec
B4DGT7
resolver
uniprot_sec
F8W9R3
resolver
uniprot_sec
O60818
resolver
uniprot_sec
O60819
resolver
uniprot_sec
O60820
resolver
uniprot_sec
O60821
resolver
uniprot_sec
P78520
resolver
uniprot_sec
P78521
resolver
uniprot_sec
Q17R81
resolver
uniprot_sec
Q5SNW2
resolver
uniprot_sec
Q5SNW3
resolver
uniprot_sec
Q5SNX1
resolver
uniprot_sec
Q5SNX2
resolver
uniprot_sec
Q5SNX3
resolver
uniprot_sec
Q99427
resolver
uniprot_sec
Q99428
resolver
uniprot_sec
Q99429
resolver
amino_acid_sequence
MAGCRGSLCCCCRWCCCCGERETRTPEELTILGETQEEEDEILPRKDYESLDYDRCINDPYLEVLETMDNKKGRRYEAVKWMVVFAIGVCTGLVGLFVDFFVRLFTQLKFGVVQTSVEECSQKGCLALSLLELLGFNLTFVFLASLLVLIEPVAAGSGIPEVKCYLNGVKVPGIVRLRTLLCKVLGVLFSVAGGLFVEKEGPMIHSGSVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFRSGIQFGSWGSFQLPGLLNFGEFKCSDSDKKCHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVHPKPKLVRVLESLLVSLVTTVVVFVASMVLGECRQMSSSSQIGNDSFQLQVTEDVNSSIKTFFCPNDTYNDMATLFFNPQESAILQLFHQDGTFSPVTLALFFVLYFLLACWTYGISVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHIYSGTFALIGAAAFLGGVVRMTISLTVILIESTNEITYGLPIMVTLMVAKWTGDFFNKGIYDIHVGLRGVPLLEWETEVEMDKLRASDIMEPNLTYVYPHTRIQSLVSILRTTVHHAFPVVTENRGNEKEFMKGNQLISNNIKFKKSSILTRAGEQRKRSQSMKSYPSSELRNMCDEHIASEEPAEKEDLLQQMLERRYTPYPNLYPDQSPSEDWTMEERFRPLTFHGLILRSQLVTLLVRGVCYSESQSSASQPRLSYAEMAEDYPRYPDIHDLDLTLLNPRMIVDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTYEFLQARLRQHYQTI
uniprot
proteins
disease_involvement
DISEASE: Ceroid lipofuscinosis, neuronal, 15 (CLN15) [MIM:619173]: An autosomal dominant, progressive, neurodegenerative disorder characterized by severe global developmental delay, impaired intellectual development, poor or absent speech, hypotonia, impaired motor development, respiratory insufficiency, and feeding difficulties. Most patients have visual defects, including cortical visual blindness, nystagmus, and esotropia. Brain imaging shows abnormalities affecting the brainstem, cerebellum, and corticospinal tracts. Disease onset is in infancy or early childhood. {ECO:0000269|PubMed:33217309}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the late endosome lumen. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The presence of conserved gating glutamate residues is typical for family members that function as antiporters. {ECO:0000269|PubMed:20466723}.
uniprot
proteins
mass_dalton
97289
uniprot
proteins
mutagenesis
MUTAGEN 157; /note="S->P: Increases the nitrate/chloride conductance ratio."; /evidence="ECO:0000269|PubMed:20466723"; MUTAGEN 200; /note="E->A: Abolishes proton transport, but not chloride transport. Strongly increases anion current; when associated with S-576."; /evidence="ECO:0000269|PubMed:20466723"; MUTAGEN 267; /note="E->A: Loss of proton and chloride transport."; /evidence="ECO:0000269|PubMed:20466723"; MUTAGEN 410; /note="N->A: Abolishes N-glycosylation; when associated with A-422 and A-432."; /evidence="ECO:0000269|PubMed:17534424"; MUTAGEN 422; /note="N->A: Abolishes N-glycosylation; when associated with A-410 and A-432."; /evidence="ECO:0000269|PubMed:17534424"; MUTAGEN 432; /note="N->A: Abolishes N-glycosylation; when associated with A-410 and A-422."; /evidence="ECO:0000269|PubMed:17534424"; MUTAGEN 576; /note="Y->S: Strongly increases anion current; when associated with A-200."; /evidence="ECO:0000269|PubMed:20466723
uniprot
proteins
post_translational_modification
PTM: N-glycosylated on several asparagine residues. {ECO:0000269|PubMed:17534424}.
uniprot
proteins
protein_family
Chloride channel (TC 2.A.49) family
uniprot
proteins
protein_family
ClC-6/CLCN6 subfamily
uniprot
proteins
pubmed
10198195
uniprot
proteins
pubmed
10500249
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17534424
uniprot
proteins
pubmed
20466723
uniprot
proteins
pubmed
33217309
uniprot
proteins
pubmed
7584044
uniprot
proteins
pubmed
8543009
uniprot
proteins
pubmed
9224655
uniprot
proteins
sequence_length
869
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:17534424, ECO:0000269|PubMed:33217309}; Multi-pass membrane protein {ECO:0000269|PubMed:17534424}.
uniprot
proteins
transmembrane_region
TRANSMEM 81..113; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 128..150; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 176..194; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 200..217; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 277..294; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 335..364; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 371..392; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 462..481; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 487..511; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 553..571; /note="Helical"; /evidence="ECO:0000250
uniprot
proteins