Slc26a6
entrez
171429
canonical
uniprot
Q8CIW6
canonical
ensembl
ENSMUSG00000023259
resolver
ensp
ENSMUSP00000140849
resolver
ensp
ENSMUSP00000159445
resolver
ensp
ENSMUSP00000251673
resolver
genesymbol
Slc26a6
resolver
genesymbol_syn
Cfex
resolver
genesymbol_syn
Pat1
resolver
uniprot
E9Q4D3
resolver
uniprot
Q3TQD3
resolver
uniprot
Q812E2
resolver
uniprot
Q8CJD0
resolver
uniprot
Q8K142
resolver
uniprot
Q923J3
resolver
uniprot_entry
S26A6_MOUSE
resolver
uniprot_sec
E9Q4D3
resolver
uniprot_sec
Q3TQD3
resolver
uniprot_sec
Q812E2
resolver
uniprot_sec
Q8CJD0
resolver
uniprot_sec
Q8K142
resolver
uniprot_sec
Q923J3
resolver
activity_regulation
ACTIVITY REGULATION: Apical membrane chloride-bicarbonate exchange activity of the pancreatic duct is inhibited by 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS). Oxalate secretion in the duodenum and chloride-formate exchange activity is inhibited by DIDS. {ECO:0000269|PubMed:12119287, ECO:0000269|PubMed:22021714, ECO:0000269|PubMed:22895259}.; ACTIVITY REGULATION: [Isoform 2]: Chloride-formate exchange activity and transcellular sulfate absorption is inhibited by 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS). {ECO:0000269|PubMed:11459928, ECO:0000269|PubMed:12217875, ECO:0000269|PubMed:15203903}.
uniprot
proteins
amino_acid_sequence
MGLPDGSDQGTHQTQALLSAAQEMELQRRDYHVERPLLNQEQLEDLGHWGPAAKTHQWRTWFRCSRARAHSLLLQHVPVLGWLPRYPVREWLLGDLLSGLSVAIMQLPQGLAYALLAGLPPMFGLYSSFYPVFIYFLFGTSRHISVGTFAVMSVMVGSVTESLTADKAFVQGLNATADDARVQVAYTLSFLVGLFQVGLGLVHFGFVVTYLSEPLVRSYTTAASVQVLVSQLKYVFGIKLSSHSGPLSVIYTVLEVCAQLPETVPGTVVTAIVAGVALVLVKLLNEKLHRRLPLPIPGELLTLIGATGISYGVKLNDRFKVDVVGNITTGLIPPVAPKTELFATLVGNAFAIAVVGFAIAISLGKIFALRHGYRVDSNQELVALGLSNLIGGFFQCFPVSCSMSRSLVQESTGGNTQVAGAVSSLFILLIIVKLGELFRDLPKAVLAAVIIVNLKGMMKQFSDICSLWKANRVDLLIWLVTFVATILLNLDIGLAVSIVFSLLLVVVRMQLPHYSVLGQVPDTDIYRDVAEYSGAKEVPGVKVFRSSATLYFANAELYSDSLKEKCGVDVDRLITQKKKRIKKQEMKLKRMKKAKKSQKQDASSKISSVSVNVNTNLEDVKSNDVEGSEAKVHQGEELQDVVSSNQEDAKAPTMTSLKSLGLPQPGFHSLILDLSTLSFVDTVCIKSLKNIFRDFREIEVEVYIAACYSPVVAQLEAGHFFDESITKQHVFASVHDAVTFALSHRKSVPKSPVLATKL
uniprot
proteins
function
FUNCTION: Apical membrane anion-exchanger with wide epithelial distribution that plays a role as a component of the pH buffering system for maintaining acid-base homeostasis. Acts as a versatile DIDS-sensitive inorganic and organic anion transporter that mediates the uptake of monovalent anions like chloride, bicarbonate, formate and hydroxyl ion and divalent anions like sulfate and oxalate. Functions in multiple exchange modes involving pairs of these anions, which include chloride-bicarbonate, chloride-oxalate, oxalate-formate, oxalate-sulfate and chloride-formate exchange. Apical membrane chloride-bicarbonate exchanger that mediates luminal chloride absorption and bicarbonate secretion by the small intestinal brush border membrane and contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption, possibly by providing a bicarbonate import pathway. Its association with carbonic anhydrase CA2 forms a bicarbonate transport metabolon; hence maximizes the local concentration of bicarbonate at the transporter site. Also mediates intestinal chloride absorption and oxalate secretion, thereby preventing hyperoxaluria and calcium oxalate urolithiasis. Transepithelial oxalate secretion, chloride-formate, chloride-oxalate and chloride-bicarbonate transport activities in the duodenum are inhibited by PKC activation in a calcium-independent manner. The apical membrane chloride-bicarbonate exchanger also provides a major route for fluid and bicarbonate secretion into the proximal tubules of the kidney as well as into the proximal part of the interlobular pancreatic ductal tree, where it mediates electrogenic chloride-bicarbonate exchange with a chloride-bicarbonate stoichiometry of 1:2, and hence will dilute and alkalinize protein-rich acinar secretion. Also mediates the transcellular sulfate absorption and oxalate secretion across the apical membrane in the duodenum and the formate ion efflux at the apical brush border of cells in the proximal tubules of kidney. Plays a role in sperm capacitation by increasing intracellular pH. {ECO:0000269|PubMed:11842009, ECO:0000269|PubMed:12119287, ECO:0000269|PubMed:16141316, ECO:0000269|PubMed:16532010, ECO:0000269|PubMed:16606687, ECO:0000269|PubMed:17053783, ECO:0000269|PubMed:17170027, ECO:0000269|PubMed:18046080, ECO:0000269|PubMed:18496516, ECO:0000269|PubMed:20150244, ECO:0000269|PubMed:20969732, ECO:0000269|PubMed:21976599, ECO:0000269|PubMed:22021714, ECO:0000269|PubMed:22895259, ECO:0000269|PubMed:23933580, ECO:0000269|PubMed:29530983}.; FUNCTION: [Isoform 2]: Mediates electrogenic chloride-bicarbonate exchange with a chloride-bicarbonate stoichiometry of 1:2 (PubMed:12217875, PubMed:23933580). Also mediates exchange of chloride-formate and chloride-oxalate ions (PubMed:11459928, PubMed:12217875, PubMed:15203903, PubMed:17151144, PubMed:23933580). Mediates transcellular sulfate absorption (PubMed:12217875). {ECO:0000269|PubMed:11459928, ECO:0000269|PubMed:12217875, ECO:0000269|PubMed:15203903, ECO:0000269|PubMed:17151144, ECO:0000269|PubMed:23933580}.
uniprot
proteins
mass_dalton
82834
uniprot
proteins
mutagenesis
MUTAGEN Q8CIW6-2:552; /note="T->A: Does not inhibit formate transport in PMA-induced cells."; /evidence="ECO:0000269|PubMed:17151144
uniprot
proteins
post_translational_modification
PTM: N-glycosylated (PubMed:27681177). Glycosylation at Asn-174 positively regulates its chloride oxalate exchanger activity (By similarity). {ECO:0000250|UniProtKB:Q9BXS9, ECO:0000269|PubMed:27681177}.
uniprot
proteins
pubmed
11459928
uniprot
proteins
pubmed
11842009
uniprot
proteins
pubmed
12119287
uniprot
proteins
pubmed
12217875
uniprot
proteins
pubmed
15203903
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16141316
uniprot
proteins
pubmed
16532010
uniprot
proteins
pubmed
16606687
uniprot
proteins
pubmed
17053783
uniprot
proteins
pubmed
17151144
uniprot
proteins
pubmed
17170027
uniprot
proteins
pubmed
18046080
uniprot
proteins
pubmed
18496516
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20150244
uniprot
proteins
pubmed
20969732
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21976599
uniprot
proteins
pubmed
22021714
uniprot
proteins
pubmed
22895259
uniprot
proteins
pubmed
23542070
uniprot
proteins
pubmed
23933580
uniprot
proteins
pubmed
27681177
uniprot
proteins
pubmed
29530983
uniprot
proteins
sequence_length
758
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21976599}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:11842009, ECO:0000269|PubMed:16141316, ECO:0000269|PubMed:17170027, ECO:0000269|PubMed:18496516, ECO:0000269|PubMed:23933580, ECO:0000269|PubMed:29530983}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:16532010}; Multi-pass membrane protein {ECO:0000255}. Microsome {ECO:0000269|PubMed:16141316}. Note=Localized in sperm membranes. Colocalizes with CFTR at the midpiece of sperm tail. Localizes to the apical membrane brush border of epithelial cells in the proximal tubules of kidney, of enterocytes of the small intestine and of gastric parietal cells in the stomach. {ECO:0000269|PubMed:11459928, ECO:0000269|PubMed:11842009, ECO:0000269|PubMed:16141316, ECO:0000269|PubMed:21976599}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:17151144, ECO:0000269|PubMed:23933580}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:11459928}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000269|PubMed:23933580}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane {ECO:0000269|PubMed:23933580}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 118..138; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 188..208; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 264..284; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 293..313; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 341..361; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 381..401; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 418..438; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 486..506; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins