SLC26A6
entrez
65010
canonical
uniprot
Q9BXS9
canonical
ensembl
ENSG00000225697
resolver
ensp
ENSP00000337648
resolver
ensp
ENSP00000351597
resolver
ensp
ENSP00000373239
resolver
ensp
ENSP00000378920
resolver
ensp
ENSP00000401066
resolver
ensp
ENSP00000404684
resolver
enst
ENST00000337000
resolver
enst
ENST00000358747
resolver
genesymbol
SLC26A6
resolver
hgnc
HGNC:14472
resolver
uniprot
A0A0C4DFT5
resolver
uniprot
B4DMZ1
resolver
uniprot
G3XAC1
resolver
uniprot
Q548A7
resolver
uniprot
Q96MZ1
resolver
uniprot
Q96Q90
resolver
uniprot
Q9NQU1
resolver
uniprot_entry
A0A0C4DFT5_HUMAN
resolver
uniprot_entry
G3XAC1_HUMAN
resolver
uniprot_entry
Q96MZ1_HUMAN
resolver
uniprot_entry
S26A6_HUMAN
resolver
uniprot_sec
B4DMZ1
resolver
uniprot_sec
Q548A7
resolver
uniprot_sec
Q96Q90
resolver
uniprot_sec
Q9NQU1
resolver
activity_regulation
ACTIVITY REGULATION: Oxalate transport activity is inhibited by 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS). {ECO:0000269|PubMed:20501439}.; ACTIVITY REGULATION: [Isoform 4]: Chloride, bicarbonate and sulfate transport activities are inhibited by 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS). {ECO:0000269|PubMed:12444019, ECO:0000269|PubMed:15990874}.; ACTIVITY REGULATION: [Isoform 5]: Chloride, bicarbonate and sulfate transport activities are inhibited by 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS). {ECO:0000269|PubMed:12444019}.; ACTIVITY REGULATION: [Isoform 6]: Chloride, bicarbonate and sulfate transport activities are inhibited by 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS). {ECO:0000269|PubMed:12444019}.
uniprot
proteins
amino_acid_sequence
MGLADASGPRDTQALLSATQAMDLRRRDYHMERPLLNQEHLEELGRWGSAPRTHQWRTWLQCSRARAYALLLQHLPVLVWLPRYPVRDWLLGDLLSGLSVAIMQLPQGLAYALLAGLPPVFGLYSSFYPVFIYFLFGTSRHISVGTFAVMSVMVGSVTESLAPQALNDSMINETARDAARVQVASTLSVLVGLFQVGLGLIHFGFVVTYLSEPLVRGYTTAAAVQVFVSQLKYVFGLHLSSHSGPLSLIYTVLEVCWKLPQSKVGTVVTAAVAGVVLVVVKLLNDKLQQQLPMPIPGELLTLIGATGISYGMGLKHRFEVDVVGNIPAGLVPPVAPNTQLFSKLVGSAFTIAVVGFAIAISLGKIFALRHGYRVDSNQELVALGLSNLIGGIFQCFPVSCSMSRSLVQESTGGNSQVAGAISSLFILLIIVKLGELFHDLPKAVLAAIIIVNLKGMLRQLSDMRSLWKANRADLLIWLVTFTATILLNLDLGLVVAVIFSLLLVVVRTQMPHYSVLGQVPDTDIYRDVAEYSEAKEVRGVKVFRSSATVYFANAEFYSDALKQRCGVDVDFLISQKKKLLKKQEQLKLKQLQKEEKLRKQAASPKGASVSINVNTSLEDMRSNNVEDCKMMQVSSGDKMEDATANGQEDSKAPDGSTLKALGLPQPDFHSLILDLGALSFVDTVCLKSLKNIFHDFREIEVEVYMAACHSPVVSQLEAGHFFDASITKKHLFASVHDAVTFALQHPRPVPDSPVSVTRL
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. 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:0000250|UniProtKB:Q8CIW6, ECO:0000269|PubMed:20501439, ECO:0000269|PubMed:27681177}.; FUNCTION: [Isoform 4]: Apical membrane chloride-bicarbonate exchanger. Its association with carbonic anhydrase CA2 forms a bicarbonate transport metabolon; hence maximizes the local concentration of bicarbonate at the transporter site. {ECO:0000269|PubMed:15990874}.
uniprot
proteins
mass_dalton
82967
uniprot
proteins
mutagenesis
MUTAGEN 167; /note="N->Q: Reduced chloride oxalate exchanger activity."; /evidence="ECO:0000269|PubMed:27681177"; MUTAGEN 172; /note="N->Q: Reduced chloride oxalate exchanger activity."; /evidence="ECO:0000269|PubMed:27681177"; MUTAGEN Q9BXS9-4:547..549; /note="DVD->NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport."; /evidence="ECO:0000269|PubMed:15990874"; MUTAGEN Q9BXS9-4:553; /note="S->A: Does not inhibit interaction with CA2. Inhibits interaction with CA2 and bicarbonate transport in PMA-induced cells."; /evidence="ECO:0000269|PubMed:15990874"; MUTAGEN Q9BXS9-4:582; /note="S->A: Does not inhibit interaction with CA2. Does not inhibit interaction with CA2 and bicarbonate transport in PMA-induced cells."; /evidence="ECO:0000269|PubMed:15990874
uniprot
proteins
post_translational_modification
PTM: [Isoform 4]: Phosphorylated on serine residues by PKC; the phosphorylation disrupts interaction with carbonic anhydrase CA2 and reduces bicarbonate transport activity in a phorbol myristate acetate (PMA)-induced manner. {ECO:0000269|PubMed:15990874}.; PTM: Glycosylation at Asn-167 and Asn-172 positively regulates its chloride oxalate exchanger activity. {ECO:0000269|PubMed:27681177}.
uniprot
proteins
protein_family
SLC26A/SulP transporter (TC 2.A.53) family
uniprot
proteins
pubmed
11087667
uniprot
proteins
pubmed
11247665
uniprot
proteins
pubmed
12217875
uniprot
proteins
pubmed
12444019
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15990874
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18655181
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20501439
uniprot
proteins
pubmed
27681177
uniprot
proteins
sequence_length
759
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11247665, ECO:0000269|PubMed:27681177}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:20501439}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8CIW6}; Multi-pass membrane protein {ECO:0000255}. Microsome {ECO:0000250|UniProtKB:Q8CIW6}. 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:0000250|UniProtKB:Q8CIW6}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000269|PubMed:12444019, ECO:0000269|PubMed:15990874}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:11087667}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:11087667}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the apical and basolateral surfaces of tubular wall cells in kidney and in the brush border of pancreatic duct cells (PubMed:11087667). Colocalized with CA2 at the surface of the cell membrane in order to form a bicarbonate transport metabolon; colocalization is reduced in phorbol myristate acetate (PMA)-induced cells (PubMed:15990874). May be translocated from the cytosolic surface of the cell membrane to the intracellular space by PKC in phorbol myristate acetate (PMA)-induced cells (PubMed:15990874). {ECO:0000269|PubMed:11087667, ECO:0000269|PubMed:15990874}.; SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane {ECO:0000269|PubMed:12444019}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 6]: Cell membrane {ECO:0000269|PubMed:12444019}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 116..136; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 187..207; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 264..284; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 294..314; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 348..368; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 380..400; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 417..437; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 485..505; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins