Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BXS9 (S26A6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Solute carrier family 26 member 6
Alternative name(s):
Anion exchange transporter
Pendrin-like protein 1
Short name=Pendrin-L1
Gene names
Name:SLC26A6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length759 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Function 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. Mediates also 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 provides also 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. Mediates also 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. Ref.9 Ref.10 Ref.13

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. Ref.9 Ref.10 Ref.13

Enzyme regulation

Apical membrane chloride-formate exchange activity in the proximal tubules of the kidney and oxalate secretion in the duodenum are inhibited by 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of several anion channels and transporters) By similarity. Apical membrane chloride-bicarbonate exchange activity of the pancreatic duct is inhibited by 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of several anion channels and transporters). Isoform 4, isoform 5 and isoform 6 chloride, bicarbonate and sulfate transport activities are inhibited by DIDS. Ref.9 Ref.10 Ref.13

Subunit structure

Interacts (via C-terminal domain) with PDZK1 (via C-terminal PDZ domain); the interaction induces chloride and oxalate exchange transport. Interacts with CFTR, SLC26A3 and SLC9A3R1 By similarity. Isoform 4 interacts (via C-terminal cytoplasmic domain) with CA2; the interaction stimulates chloride-bicarbonate exchange activity. Isoform 4 and isoform 5 interact with SLC9A3R1 (via the PDZ domains). Isoform 4 and isoform 5 interact with SLC9A3R2 (via the PDZ domains). Ref.9 Ref.10

Subcellular location

Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein By similarity. Cytoplasmic vesicle membrane; Multi-pass membrane protein By similarity. Microsome By similarity. 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. May be translocated from the cytosolic surface of the cell membrane to the intracellular space by PKC in phorbol myristate acetate (PMA)-induced cells By similarity. 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. Ref.1 Ref.2 Ref.9 Ref.10

Isoform 4: Cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Note: Localizes to the apical and basolateral surfaces of tubular wall cells in kidney and in the brush border of pancreatic duct cells. Ref.1 Ref.2 Ref.9 Ref.10

Isoform 5: Cell membrane; Multi-pass membrane protein Ref.1 Ref.2 Ref.9 Ref.10.

Isoform 6: Cell membrane; Multi-pass membrane protein Ref.1 Ref.2 Ref.9 Ref.10.

Tissue specificity

Ubiquitous. Highest levels in kidney and pancreas. Lower expression in heart, skeletal muscle, liver and placenta. Also found in lung and brain. Isoform 4 is ubiquitously expressed. Isoform 6 is expressed in heart, brain, placenta, lung, liver, kidney, pancreas, spleen, thymus, prostate, testis and ovary. Isoform 5 is expressed weakly in placenta, lung, liver and pancreas. Ref.1 Ref.2

Induction

Down-regulated by pro-inflammatory cytokine IFN gamma. Ref.9 Ref.10 Ref.12 Ref.13

Post-translational modification

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. Ref.10

Sequence similarities

Belongs to the SLC26A/SulP transporter (TC 2.A.53) family. [View classification]

Contains 1 STAS domain.

Ontologies

Keywords
   Biological processAnion exchange
Antiport
Ion transport
Transport
   Cellular componentCell membrane
Cytoplasmic vesicle
Endoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   LigandChloride
   Molecular functionChloride channel
Ion channel
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiotensin-activated signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

anion transport

Inferred from direct assay Ref.9. Source: GOC

bicarbonate transport

Inferred from direct assay Ref.9. Source: GOC

cellular response to cAMP

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to fructose stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to interferon-gamma

Inferred from direct assay Ref.12. Source: UniProtKB

chloride transmembrane transport

Inferred from direct assay Ref.9Ref.10. Source: GOC

chloride transport

Inferred from direct assay Ref.9. Source: GOC

epithelial fluid transport

Inferred from sequence or structural similarity. Source: UniProtKB

formate transport

Inferred from sequence or structural similarity. Source: UniProtKB

intestinal absorption

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular pH elevation

Inferred from sequence or structural similarity. Source: UniProtKB

ion transport

Traceable author statement. Source: Reactome

mannitol transport

Inferred from sequence or structural similarity. Source: UniProtKB

oxalate transport

Inferred from mutant phenotype Ref.13. Source: UniProtKB

oxalic acid secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of dipeptide transmembrane transport

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase C signaling

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of intracellular pH

Inferred from direct assay Ref.10. Source: UniProtKB

sperm capacitation

Inferred from sequence or structural similarity. Source: UniProtKB

sulfate transmembrane transport

Inferred from direct assay Ref.9. Source: GOC

sulfate transport

Inferred from mutant phenotype Ref.13. Source: UniProtKB

transepithelial chloride transport

Inferred from mutant phenotype Ref.13. Source: UniProtKB

transepithelial transport

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

Inferred from direct assay Ref.1Ref.13. Source: UniProtKB

basolateral plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

brush border membrane

Inferred from direct assay Ref.1. Source: UniProtKB

chloride channel complex

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

integral component of membrane

Inferred from direct assay Ref.1Ref.9. Source: UniProtKB

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

membrane-bounded vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.9Ref.10. Source: UniProtKB

sperm midpiece

Inferred from sequence or structural similarity. Source: UniProtKB

vesicle membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionPDZ domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

anion:anion antiporter activity

Inferred from direct assay Ref.9Ref.10. Source: UniProtKB

bicarbonate transmembrane transporter activity

Inferred from direct assay Ref.9Ref.10. Source: UniProtKB

chloride channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

chloride transmembrane transporter activity

Inferred from direct assay Ref.9Ref.10. Source: UniProtKB

efflux transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

formate efflux transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

formate transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

formate uptake transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

oxalate transmembrane transporter activity

Inferred from mutant phenotype Ref.13. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9Ref.10. Source: UniProtKB

secondary active sulfate transmembrane transporter activity

Inferred from electronic annotation. Source: InterPro

sulfate transmembrane transporter activity

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BXS9-1)

Also known as: SLC26A6b;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BXS9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     602-631: ASPKGASVSINVNTSLEDMRSNNVEDCKMM → GPLLSACLAPQ
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9BXS9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     632-632: Missing.
Isoform 4 (identifier: Q9BXS9-4)

Also known as: SLC26A6a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     632-632: Missing.
Isoform 5 (identifier: Q9BXS9-5)

Also known as: SLC26A6c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     264-301: Missing.
     632-632: Missing.
Isoform 6 (identifier: Q9BXS9-6)

Also known as: SLC26A6d;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     632-759: QVSSGDKMED...PDSPVSVTRL → VRLEVGKEVT...SGSVVICHRI
Isoform 7 (identifier: Q9BXS9-7)

The sequence of this isoform differs from the canonical sequence as follows:
     145-216: GTFAVMSVMV...VTYLSEPLVR → ATPGPLPLLT...PLWATVPHLL
     217-252: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 759759Solute carrier family 26 member 6
PRO_0000080171

Regions

Topological domain1 – 115115Cytoplasmic Potential
Transmembrane116 – 13621Helical; Potential
Topological domain137 – 18650Extracellular Potential
Transmembrane187 – 20721Helical; Potential
Topological domain208 – 26356Cytoplasmic Potential
Transmembrane264 – 28421Helical; Potential
Topological domain285 – 2939Extracellular Potential
Transmembrane294 – 31421Helical; Potential
Topological domain315 – 34733Cytoplasmic Potential
Transmembrane348 – 36821Helical; Potential
Topological domain369 – 37911Extracellular Potential
Transmembrane380 – 40021Helical; Potential
Topological domain401 – 41616Cytoplasmic Potential
Transmembrane417 – 43721Helical; Potential
Topological domain438 – 48447Extracellular Potential
Transmembrane485 – 50521Helical; Potential
Topological domain506 – 759254Cytoplasmic Potential
Domain530 – 742213STAS

Amino acid modifications

Modified residue5741Phosphoserine; by PKC Probable
Modified residue6031Phosphoserine; by PKC Probable
Modified residue6161Phosphoserine Ref.15
Modified residue7521Phosphoserine Ref.11 Ref.15
Modified residue7551Phosphoserine Ref.15

Natural variations

Alternative sequence1 – 2121Missing in isoform 4, isoform 5 and isoform 6.
VSP_046807
Alternative sequence145 – 21672GTFAV…EPLVR → ATPGPLPLLTAPGRPTGGAG PDPLRLRGHLPVRTSCPRLY HSCSCAGLRLTAQVCVWPPS EQPLWATVPHLL in isoform 7.
VSP_055273
Alternative sequence217 – 25236Missing in isoform 7.
VSP_055274
Alternative sequence264 – 30138Missing in isoform 5.
VSP_047851
Alternative sequence602 – 63130ASPKG…DCKMM → GPLLSACLAPQ in isoform 2.
VSP_006169
Alternative sequence632 – 759128QVSSG…SVTRL → VRLEVGKEVTAVSCRDAGST CLMRNAMDPAAVGSRVLRRW QEEWGGWVRYSSGSVVICHR I in isoform 6.
VSP_047852
Alternative sequence6321Missing in isoform 3, isoform 4 and isoform 5.
VSP_040127
Natural variant2061V → M. Ref.2
Corresponds to variant rs13324142 [ dbSNP | Ensembl ].
VAR_012776

Experimental info

Mutagenesis568 – 5703DVD → NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport. Ref.10
Mutagenesis5741S → A: Does not inhibit interaction with CA2. Inhibits interaction with CA2 and bicarbonate transport in PMA-induced cells. Ref.10
Mutagenesis6031S → A: Does not inhibit interaction with CA2. Does not inhibit interaction with CA2 and bicarbonate transport in PMA-induced cells. Ref.10

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SLC26A6b) [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 63CB0B756C9675C6

FASTA75982,967
        10         20         30         40         50         60 
MGLADASGPR DTQALLSATQ AMDLRRRDYH MERPLLNQEH LEELGRWGSA PRTHQWRTWL 

        70         80         90        100        110        120 
QCSRARAYAL LLQHLPVLVW LPRYPVRDWL LGDLLSGLSV AIMQLPQGLA YALLAGLPPV 

       130        140        150        160        170        180 
FGLYSSFYPV FIYFLFGTSR HISVGTFAVM SVMVGSVTES LAPQALNDSM INETARDAAR 

       190        200        210        220        230        240 
VQVASTLSVL VGLFQVGLGL IHFGFVVTYL SEPLVRGYTT AAAVQVFVSQ LKYVFGLHLS 

       250        260        270        280        290        300 
SHSGPLSLIY TVLEVCWKLP QSKVGTVVTA AVAGVVLVVV KLLNDKLQQQ LPMPIPGELL 

       310        320        330        340        350        360 
TLIGATGISY GMGLKHRFEV DVVGNIPAGL VPPVAPNTQL FSKLVGSAFT IAVVGFAIAI 

       370        380        390        400        410        420 
SLGKIFALRH GYRVDSNQEL VALGLSNLIG GIFQCFPVSC SMSRSLVQES TGGNSQVAGA 

       430        440        450        460        470        480 
ISSLFILLII VKLGELFHDL PKAVLAAIII VNLKGMLRQL SDMRSLWKAN RADLLIWLVT 

       490        500        510        520        530        540 
FTATILLNLD LGLVVAVIFS LLLVVVRTQM PHYSVLGQVP DTDIYRDVAE YSEAKEVRGV 

       550        560        570        580        590        600 
KVFRSSATVY FANAEFYSDA LKQRCGVDVD FLISQKKKLL KKQEQLKLKQ LQKEEKLRKQ 

       610        620        630        640        650        660 
AASPKGASVS INVNTSLEDM RSNNVEDCKM MQVSSGDKME DATANGQEDS KAPDGSTLKA 

       670        680        690        700        710        720 
LGLPQPDFHS LILDLGALSF VDTVCLKSLK NIFHDFREIE VEVYMAACHS PVVSQLEAGH 

       730        740        750 
FFDASITKKH LFASVHDAVT FALQHPRPVP DSPVSVTRL 

« Hide

Isoform 2 [UniParc].

Checksum: 9BBFAB68E0D8B2C5
Show »

FASTA74080,807
Isoform 3 [UniParc].

Checksum: 6CC16170D6F9F01C
Show »

FASTA75882,839
Isoform 4 (SLC26A6a) [UniParc].

Checksum: 1AFAFB8DEDB69E6E
Show »

FASTA73780,782
Isoform 5 (SLC26A6c) [UniParc].

Checksum: 8E03EA6F5DE56EFC
Show »

FASTA69976,876
Isoform 6 (SLC26A6d) [UniParc].

Checksum: B2C9AD808C256713
Show »

FASTA67173,817
Isoform 7 [UniParc].

Checksum: A3D9F408FD3DD9F3
Show »

FASTA72379,159

References

« Hide 'large scale' references
[1]"Mapping of five new putative anion transporter genes in human and characterization of SLC26A6, a candidate gene for pancreatic anion exchanger."
Lohi H., Kujala M., Kerkelae E., Saarialho-Kere U., Kestilae M., Kere J.
Genomics 70:102-112(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Cloning and characterization of SLC26A6, a novel member of the solute carrier 26 gene family."
Waldegger S., Moschen I., Ramirez A., Smith R.J.H., Ayadi H., Lang F., Kubisch C.
Genomics 72:43-50(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT MET-206.
[3]"Molecular characterization of the murine Slc26a6 anion exchanger: functional comparison with Slc26a1."
Xie Q., Welch R., Mercado A., Romero M.F., Mount D.B.
Am. J. Physiol. 283:F826-F838(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]"Molecular cloning of a new putative sulfate anion transporter."
Ishibashi K.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Kidney.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
Tissue: Lung.
[6]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Duodenum.
[9]"Isoforms of SLC26A6 mediate anion transport and have functional PDZ interaction domains."
Lohi H., Lamprecht G., Markovich D., Heil A., Kujala M., Seidler U., Kere J.
Am. J. Physiol. 284:C769-C779(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 4; 5 AND 6), FUNCTION, ENZYME REGULATION, INTERACTION WITH SLC9A3R1 AND SLC9A3R2, SUBCELLULAR LOCATION, TOPOLOGY.
[10]"Metabolon disruption: a mechanism that regulates bicarbonate transport."
Alvarez B.V., Vilas G.L., Casey J.R.
EMBO J. 24:2499-2511(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM 4), ENZYME REGULATION, INTERACTION WITH CA2, PHOSPHORYLATION AT SER-574 AND SER-603 BY PKC, SUBCELLULAR LOCATION, MUTAGENESIS OF 568-ASP--ASP-570; SER-574 AND SER-603.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Characterization of the 5'-flanking region and regulation of expression of human anion exchanger SLC26A6."
Saksena S., Dwivedi A., Singla A., Gill R.K., Tyagi S., Borthakur A., Alrefai W.A., Ramaswamy K., Dudeja P.K.
J. Cell. Biochem. 105:454-466(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[13]"Parsing apical oxalate exchange in Caco-2BBe1 monolayers: siRNA knockdown of SLC26A6 reveals the role and properties of PAT-1."
Freel R.W., Morozumi M., Hatch M.
Am. J. Physiol. 297:G918-G929(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616; SER-752 AND SER-755, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF279265 mRNA. Translation: AAF81911.1.
AF288410 mRNA. Translation: AAK19153.1.
AF416721 mRNA. Translation: AAN07094.1.
AB033288 mRNA. Translation: BAB69041.1.
AK297695 mRNA. Translation: BAG60053.1.
AC121252 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64901.1.
CH471055 Genomic DNA. Translation: EAW64903.1.
BC017697 mRNA. Translation: AAH17697.1.
CCDSCCDS43087.1. [Q9BXS9-1]
CCDS46824.1. [Q9BXS9-2]
CCDS46825.1. [Q9BXS9-3]
RefSeqNP_001035544.1. NM_001040454.1.
NP_075062.2. NM_022911.2. [Q9BXS9-1]
NP_599025.2. NM_134263.2. [Q9BXS9-3]
NP_602298.2. NM_134426.2. [Q9BXS9-2]
UniGeneHs.631925.
Hs.663208.

3D structure databases

ProteinModelPortalQ9BXS9.
SMRQ9BXS9. Positions 511-560, 667-739.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122373. 1 interaction.
STRING9606.ENSP00000378920.

Protein family/group databases

TCDB2.A.53.2.7. the sulfate permease (sulp) family.

PTM databases

PhosphoSiteQ9BXS9.

Polymorphism databases

DMDM20140224.

Proteomic databases

MaxQBQ9BXS9.
PaxDbQ9BXS9.
PRIDEQ9BXS9.

Protocols and materials databases

DNASU65010.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358747; ENSP00000351597; ENSG00000225697.
ENST00000383733; ENSP00000373239; ENSG00000225697. [Q9BXS9-2]
ENST00000395550; ENSP00000378920; ENSG00000225697. [Q9BXS9-1]
ENST00000420764; ENSP00000404684; ENSG00000225697. [Q9BXS9-3]
ENST00000455886; ENSP00000401066; ENSG00000225697.
GeneID65010.
KEGGhsa:65010.
UCSCuc003cug.3. human. [Q9BXS9-1]
uc003cui.3. human.
uc003cuj.3. human. [Q9BXS9-2]

Organism-specific databases

CTD65010.
GeneCardsGC03M048664.
HGNCHGNC:14472. SLC26A6.
HPAHPA048363.
MIM610068. gene.
neXtProtNX_Q9BXS9.
PharmGKBPA37889.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0659.
HOGENOMHOG000006546.
HOVERGENHBG000639.
KOK14704.
OMANNVEDCK.
OrthoDBEOG76T9QT.
PhylomeDBQ9BXS9.
TreeFamTF313784.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ9BXS9.
BgeeQ9BXS9.
CleanExHS_SLC26A6.
GenevestigatorQ9BXS9.

Family and domain databases

Gene3D3.30.750.24. 2 hits.
InterProIPR018045. S04_transporter_CS.
IPR002645. STAS_dom.
IPR001902. SulP_transpt.
IPR011547. Sulph_transpt.
[Graphical view]
PfamPF01740. STAS. 1 hit.
PF00916. Sulfate_transp. 1 hit.
[Graphical view]
SUPFAMSSF52091. SSF52091. 2 hits.
TIGRFAMsTIGR00815. sulP. 1 hit.
PROSITEPS01130. SLC26A. 1 hit.
PS50801. STAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSLC26A6.
GenomeRNAi65010.
NextBio67202.
PROQ9BXS9.
SOURCESearch...

Entry information

Entry nameS26A6_HUMAN
AccessionPrimary (citable) accession number: Q9BXS9
Secondary accession number(s): B4DMZ1 expand/collapse secondary AC list , Q548A7, Q96Q90, Q9NQU1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM