Clcn2
entrez
29232
canonical
uniprot
P35525
canonical
ensembl
ENSRNOG00000001742
resolver
ensembl
ENSRNOG00055004767
resolver
ensembl
ENSRNOG00060011694
resolver
ensembl
ENSRNOG00065003893
resolver
ensp
ENSRNOP00000002376
resolver
ensp
ENSRNOP00000050925
resolver
ensp
ENSRNOP00055005750
resolver
ensp
ENSRNOP00060015719
resolver
ensp
ENSRNOP00065004216
resolver
enst
ENSRNOT00000002376
resolver
enst
ENSRNOT00000050927
resolver
enst
ENSRNOT00055007631
resolver
enst
ENSRNOT00060020042
resolver
enst
ENSRNOT00065005866
resolver
genesymbol
Clcn2
resolver
uniprot
A0A0A0MXT6
resolver
uniprot_entry
A0A0A0MXT6_RAT
resolver
uniprot_entry
CLCN2_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Common gate kinetics are down-regulated by intracellular ATP. Inhibited by AK-42, a derivative of meclofenamate (By similarity). Inhibited by Cd(2+) (By similarity). Inhibited by Zn(2+) and PKC activation (PubMed:8816717). Inhibited at acidic pH (By similarity). CCLN2:HEPACAM channel conductance is up-regulated upon hypo-osmolarity (By similarity). {ECO:0000250|UniProtKB:P51788, ECO:0000250|UniProtKB:Q9R0A1, ECO:0000250|UniProtKB:Q9WU45, ECO:0000269|PubMed:8816717}.
uniprot
proteins
amino_acid_sequence
MAAATAAAATVAGEGMEPRALQYEQTLMYGRYTQELGAFAKEEAARIRLGGPEPWKGSPSARATPELLEYGQSRCARCRICSVRCHKFLVSRVGEDWIFLVLLGLLMALVSWAMDYAIAVCLQAQQWMSRGLNTNILLQYLAWVTYPVVLITFSAGFTQILAPQAVGSGIPEMKTILRGVVLKEYLTLKTFVAKVIGLTCALGSGMPLGKEGPFVHIASMCAALLSKFLSLFGGIYENESRNTEMLAAACAVGVGCCFAAPIGGVLFSIEVTSTFFAVRNYWRGFFAATFSAFIFRVLAVWNRDEETITALFKTRFRLDFPFDLQELPAFAVIGIASGFGGALFVYLNRKIVQVMRKQKTINRFLMKKRLLFPALVTLLISTLTFPPGFGQFMAGQLSQKETLVTLFDNRTWVRQGLVEDLGAPSTSQAWSPPRANVFLTLVIFILMKFWMSALATTIPVPCGAFMPVFVIGAAFGRLVGESMAAWFPDGIHTDSSTYRIVPGGYAVVGAAALAGAVTHTVSTAVIVFELTGQIAHILPVMIAVILANAVAQSLQPSLYDSIIRIKKLPYLPELGWGRHQQYRVRVEDIMVRDVPHVALSCTFRDLRLALHRTKGRMLALVESPESMILLGSIERSQVVALLGAQLSPARRRQHMQKLRKAQMSPPSDQESPPSSETSIRFQVNTEDSGFPGAHGQTHKPLKPALKRGPSNATSLQEGTTGNMESAGIALRSLFCGSPPLESTTSELEKSESCDKRKLKRVRISLASDSDLEGKMSPEEILEWEEQQLDEPVNFSDCKIDPAPFQLVERTSLHKTHTIFSLLGVDHAYVTSIGRLIGIVTLKELRKAIEGSVTAQGVKVRPPLASFRDSATSSSDTETTEVHALWGPRSRHGLPREGTPSDSDDKCQ
uniprot
proteins
function
FUNCTION: Voltage-gated and osmosensitive chloride channel. Forms a homodimeric channel where each subunit has its own ion conduction pathway. Conducts double-barreled currents controlled by two types of gates, two fast glutamate gates that control each subunit independently and a slow common gate that opens and shuts off both subunits simultaneously. Displays inward rectification currents activated upon membrane hyperpolarization and extracellular hypotonicity (PubMed:12163466, PubMed:1311421, PubMed:1334533, PubMed:22405205). Contributes to chloride conductance involved in neuron excitability. In hippocampal neurons, generates a significant part of resting membrane conductance and provides an additional chloride efflux pathway to prevent chloride accumulation in dendrites upon GABA receptor activation. In glia, associates with the auxiliary subunit HEPACAM/GlialCAM at astrocytic processes and myelinated fiber tracts where it may regulate transcellular chloride flux buffering extracellular chloride and potassium concentrations (By similarity) (PubMed:8816717). Regulates aldosterone production in adrenal glands. The opening of CLCN2 channels at hyperpolarized membrane potentials in the glomerulosa causes cell membrane depolarization, activation of voltage-gated calcium channels and increased expression of aldosterone synthase, the rate-limiting enzyme for aldosterone biosynthesis (By similarity). Contributes to chloride conductance in retinal pigment epithelium involved in phagocytosis of shed photoreceptor outer segments and photoreceptor renewal (By similarity). Conducts chloride currents at the basolateral membrane of epithelial cells with a role in chloride reabsorption rather than secretion (By similarity). Permeable to small monovalent anions with chloride > thiocyanate > bromide > nitrate > iodide ion selectivity (By similarity) (PubMed:1311421, PubMed:22405205, PubMed:8816717). {ECO:0000250|UniProtKB:P51788, ECO:0000250|UniProtKB:Q9R0A1, ECO:0000269|PubMed:12163466, ECO:0000269|PubMed:1311421, ECO:0000269|PubMed:1334533, ECO:0000269|PubMed:22405205, ECO:0000269|PubMed:8816717}.
uniprot
proteins
mass_dalton
99328
uniprot
proteins
mutagenesis
MUTAGEN 25; /note="Q->L: Constitutively open channel; when associated with L-26."; /evidence="ECO:0000269|PubMed:1334533"; MUTAGEN 26; /note="T->E: Constitutively open channel; when associated with E-27."; /evidence="ECO:0000269|PubMed:1334533"; MUTAGEN 26; /note="T->L: Constitutively open channel; when associated with L-25."; /evidence="ECO:0000269|PubMed:1334533"; MUTAGEN 27; /note="L->E: Constitutively open channel; when associated with E-26."; /evidence="ECO:0000269|PubMed:1334533
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Activated by dephosphorylation. {ECO:0000269|PubMed:12163466}.
uniprot
proteins
protein_family
Chloride channel (TC 2.A.49) family
uniprot
proteins
protein_family
ClC-2/CLCN2 subfamily
uniprot
proteins
pubmed
11068136
uniprot
proteins
pubmed
12163466
uniprot
proteins
pubmed
1311421
uniprot
proteins
pubmed
1334533
uniprot
proteins
pubmed
22405205
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
8816717
uniprot
proteins
sequence_length
907
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12163466, ECO:0000269|PubMed:22405205}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51788}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendritic spine membrane {ECO:0000269|PubMed:11068136}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:11068136}. Note=Sorting to the basolateral membrane is mediated by AP-1 clathrin adapter (By similarity). Localizes at axon initial segments and dendritic shaft and spikes. Colocalizes with HEPACAM and GFAP at astrocyte end-foot in contact with brain capillaries and other glial cells (PubMed:11068136, PubMed:22405205). {ECO:0000250|UniProtKB:P51788, ECO:0000269|PubMed:11068136, ECO:0000269|PubMed:22405205}.
uniprot
proteins
transmembrane_region
TRANSMEM 94..127; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 136..161; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 186..204; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 211..229; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 281..301; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 327..355; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 364..383; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 435..455; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 463..486; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 537..554; /note="Helical"; /evidence="ECO:0000250
uniprot
proteins