ID S26A6_HUMAN Reviewed; 759 AA. AC Q9BXS9; B4DMZ1; Q548A7; Q96Q90; Q9NQU1; DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 179. DE RecName: Full=Solute carrier family 26 member 6; DE AltName: Full=Anion exchange transporter; DE AltName: Full=Pendrin-like protein 1; DE Short=Pendrin-L1; GN Name=SLC26A6; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=11087667; DOI=10.1006/geno.2000.6355; RA Lohi H., Kujala M., Kerkelae E., Saarialho-Kere U., Kestilae M., Kere J.; RT "Mapping of five new putative anion transporter genes in human and RT characterization of SLC26A6, a candidate gene for pancreatic anion RT exchanger."; RL Genomics 70:102-112(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR RP LOCATION, AND VARIANT MET-206. RX PubMed=11247665; DOI=10.1006/geno.2000.6445; RA Waldegger S., Moschen I., Ramirez A., Smith R.J.H., Ayadi H., Lang F., RA Kubisch C.; RT "Cloning and characterization of SLC26A6, a novel member of the solute RT carrier 26 gene family."; RL Genomics 72:43-50(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX PubMed=12217875; DOI=10.1152/ajprenal.00079.2002; RA Xie Q., Welch R., Mercado A., Romero M.F., Mount D.B.; RT "Molecular characterization of the murine Slc26a6 anion exchanger: RT functional comparison with Slc26a1."; RL Am. J. Physiol. 283:F826-F838(2002). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Kidney; RA Ishibashi K.; RT "Molecular cloning of a new putative sulfate anion transporter."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). RC TISSUE=Lung; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Duodenum; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP ALTERNATIVE SPLICING (ISOFORMS 4; 5 AND 6), FUNCTION, ACTIVITY REGULATION, RP INTERACTION WITH NHERF1 AND NHERF2, SUBCELLULAR LOCATION, TOPOLOGY, RP TRANSPORTER ACTIVITY, AND TISSUE SPECIFICITY. RX PubMed=12444019; DOI=10.1152/ajpcell.00270.2002; RA Lohi H., Lamprecht G., Markovich D., Heil A., Kujala M., Seidler U., RA Kere J.; RT "Isoforms of SLC26A6 mediate anion transport and have functional PDZ RT interaction domains."; RL Am. J. Physiol. 284:C769-C779(2003). RN [10] RP FUNCTION (ISOFORM 4), ACTIVITY REGULATION, INTERACTION WITH CA2, RP PHOSPHORYLATION AT SER-553 AND SER-582 BY PKC (ISOFORM 4), SUBCELLULAR RP LOCATION, MUTAGENESIS OF 547-ASP--ASP-549; SER-553 AND SER-582 (ISOFORM 4), RP AND TRANSPORTER ACTIVITY. RX PubMed=15990874; DOI=10.1038/sj.emboj.7600736; RA Alvarez B.V., Vilas G.L., Casey J.R.; RT "Metabolon disruption: a mechanism that regulates bicarbonate transport."; RL EMBO J. 24:2499-2511(2005). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [12] RP INDUCTION. RX PubMed=18655181; DOI=10.1002/jcb.21842; RA Saksena S., Dwivedi A., Singla A., Gill R.K., Tyagi S., Borthakur A., RA Alrefai W.A., Ramaswamy K., Dudeja P.K.; RT "Characterization of the 5'-flanking region and regulation of expression of RT human anion exchanger SLC26A6."; RL J. Cell. Biochem. 105:454-466(2008). RN [13] RP FUNCTION, ACTIVITY REGULATION, TRANSPORTER ACTIVITY, AND SUBCELLULAR RP LOCATION. RX PubMed=20501439; DOI=10.1152/ajpgi.00251.2009; RA Freel R.W., Morozumi M., Hatch M.; RT "Parsing apical oxalate exchange in Caco-2BBe1 monolayers: siRNA knockdown RT of SLC26A6 reveals the role and properties of PAT-1."; RL Am. J. Physiol. 297:G918-G929(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616; SER-752 AND SER-755, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] RP FUNCTION, TRANSPORTER ACTIVITY, GLYCOSYLATION AT ASN-167 AND ASN-172, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-167 AND ASN-172. RX PubMed=27681177; DOI=10.1152/ajpcell.00171.2016; RA Thomson R.B., Thomson C.L., Aronson P.S.; RT "N-glycosylation critically regulates function of oxalate transporter RT SLC26A6."; RL Am. J. Physiol. 311:C866-C873(2016). CC -!- FUNCTION: Apical membrane anion-exchanger with wide epithelial CC distribution that plays a role as a component of the pH buffering CC system for maintaining acid-base homeostasis. Acts as a versatile DIDS- CC sensitive inorganic and organic anion transporter that mediates the CC uptake of monovalent anions like chloride, bicarbonate, formate and CC hydroxyl ion and divalent anions like sulfate and oxalate. Functions in CC multiple exchange modes involving pairs of these anions, which include CC chloride-bicarbonate, chloride-oxalate, oxalate-formate, oxalate- CC sulfate and chloride-formate exchange. Apical membrane chloride- CC bicarbonate exchanger that mediates luminal chloride absorption and CC bicarbonate secretion by the small intestinal brush border membrane and CC contributes to intracellular pH regulation in the duodenal upper CC villous epithelium during proton-coupled peptide absorption, possibly CC by providing a bicarbonate import pathway. Mediates also intestinal CC chloride absorption and oxalate secretion, thereby preventing CC hyperoxaluria and calcium oxalate urolithiasis. Transepithelial oxalate CC secretion, chloride-formate, chloride-oxalate and chloride-bicarbonate CC transport activities in the duodenum are inhibited by PKC activation in CC a calcium-independent manner. The apical membrane chloride-bicarbonate CC exchanger provides also a major route for fluid and bicarbonate CC secretion into the proximal tubules of the kidney as well as into the CC proximal part of the interlobular pancreatic ductal tree, where it CC mediates electrogenic chloride-bicarbonate exchange with a chloride- CC bicarbonate stoichiometry of 1:2, and hence will dilute and alkalinize CC protein-rich acinar secretion. Mediates also the transcellular sulfate CC absorption and oxalate secretion across the apical membrane in the CC duodenum and the formate ion efflux at the apical brush border of cells CC in the proximal tubules of kidney. Plays a role in sperm capacitation CC by increasing intracellular pH. {ECO:0000250|UniProtKB:Q8CIW6, CC ECO:0000269|PubMed:20501439, ECO:0000269|PubMed:27681177}. CC -!- FUNCTION: [Isoform 4]: Apical membrane chloride-bicarbonate exchanger. CC Its association with carbonic anhydrase CA2 forms a bicarbonate CC transport metabolon; hence maximizes the local concentration of CC bicarbonate at the transporter site. {ECO:0000269|PubMed:15990874}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(out) + 2 hydrogencarbonate(in) = chloride(in) + 2 CC hydrogencarbonate(out); Xref=Rhea:RHEA:72207, ChEBI:CHEBI:17544, CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:20501439}; CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(out) + oxalate(in) = chloride(in) + oxalate(out); CC Xref=Rhea:RHEA:72263, ChEBI:CHEBI:17996, ChEBI:CHEBI:30623; CC Evidence={ECO:0000269|PubMed:20501439, ECO:0000269|PubMed:27681177}; CC -!- CATALYTIC ACTIVITY: CC Reaction=formate(out) + oxalate(in) = formate(in) + oxalate(out); CC Xref=Rhea:RHEA:72271, ChEBI:CHEBI:15740, ChEBI:CHEBI:30623; CC Evidence={ECO:0000250|UniProtKB:Q8CIW6}; CC -!- CATALYTIC ACTIVITY: CC Reaction=oxalate(in) + sulfate(out) = oxalate(out) + sulfate(in); CC Xref=Rhea:RHEA:72275, ChEBI:CHEBI:16189, ChEBI:CHEBI:30623; CC Evidence={ECO:0000250|UniProtKB:Q8CIW6}; CC -!- CATALYTIC ACTIVITY: [Isoform 4]: CC Reaction=chloride(out) + 2 hydrogencarbonate(in) = chloride(in) + 2 CC hydrogencarbonate(out); Xref=Rhea:RHEA:72207, ChEBI:CHEBI:17544, CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:12444019, CC ECO:0000269|PubMed:15990874}; CC -!- CATALYTIC ACTIVITY: [Isoform 4]: CC Reaction=2 hydrogencarbonate(out) + sulfate(in) = 2 CC hydrogencarbonate(in) + sulfate(out); Xref=Rhea:RHEA:72387, CC ChEBI:CHEBI:16189, ChEBI:CHEBI:17544; CC Evidence={ECO:0000269|PubMed:12444019}; CC -!- CATALYTIC ACTIVITY: [Isoform 5]: CC Reaction=chloride(out) + 2 hydrogencarbonate(in) = chloride(in) + 2 CC hydrogencarbonate(out); Xref=Rhea:RHEA:72207, ChEBI:CHEBI:17544, CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:12444019}; CC -!- CATALYTIC ACTIVITY: [Isoform 5]: CC Reaction=2 hydrogencarbonate(out) + sulfate(in) = 2 CC hydrogencarbonate(in) + sulfate(out); Xref=Rhea:RHEA:72387, CC ChEBI:CHEBI:16189, ChEBI:CHEBI:17544; CC Evidence={ECO:0000269|PubMed:12444019}; CC -!- CATALYTIC ACTIVITY: [Isoform 6]: CC Reaction=chloride(out) + 2 hydrogencarbonate(in) = chloride(in) + 2 CC hydrogencarbonate(out); Xref=Rhea:RHEA:72207, ChEBI:CHEBI:17544, CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:12444019}; CC -!- CATALYTIC ACTIVITY: [Isoform 6]: CC Reaction=2 hydrogencarbonate(out) + sulfate(in) = 2 CC hydrogencarbonate(in) + sulfate(out); Xref=Rhea:RHEA:72387, CC ChEBI:CHEBI:16189, ChEBI:CHEBI:17544; CC Evidence={ECO:0000269|PubMed:12444019}; CC -!- ACTIVITY REGULATION: Oxalate transport activity is inhibited by 4,4'- CC diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS). CC {ECO:0000269|PubMed:20501439}. CC -!- ACTIVITY REGULATION: [Isoform 4]: Chloride, bicarbonate and sulfate CC transport activities are inhibited by 4,4'- CC diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS). CC {ECO:0000269|PubMed:12444019, ECO:0000269|PubMed:15990874}. CC -!- ACTIVITY REGULATION: [Isoform 5]: Chloride, bicarbonate and sulfate CC transport activities are inhibited by 4,4'- CC diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS). CC {ECO:0000269|PubMed:12444019}. CC -!- ACTIVITY REGULATION: [Isoform 6]: Chloride, bicarbonate and sulfate CC transport activities are inhibited by 4,4'- CC diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS). CC {ECO:0000269|PubMed:12444019}. CC -!- SUBUNIT: Interacts (via C-terminal domain) with PDZK1 (via C-terminal CC PDZ domain); the interaction induces chloride and oxalate exchange CC transport. Interacts with CFTR and SLC26A3 (By similarity). Interacts CC with AHCYL1; the interaction increases SLC26A6 activity (By CC similarity). {ECO:0000250|UniProtKB:Q8CIW6}. CC -!- SUBUNIT: [Isoform 4]: Interacts with NHERF1 (via the PDZ domains) and CC NHERF2 (via the PDZ domains) (PubMed:12444019). Interacts (via C- CC terminal cytoplasmic domain) with CA2; the interaction stimulates CC chloride-bicarbonate exchange activity (PubMed:15990874). CC {ECO:0000269|PubMed:12444019, ECO:0000269|PubMed:15990874}. CC -!- SUBUNIT: [Isoform 5]: Interacts with NHERF1 (via the PDZ domains) and CC NHERF2 (via the PDZ domains). {ECO:0000269|PubMed:12444019}. CC -!- INTERACTION: CC Q9BXS9-3; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-12814225, EBI-4290634; CC Q9BXS9-3; P41181: AQP2; NbExp=3; IntAct=EBI-12814225, EBI-12701138; CC Q9BXS9-3; O15155: BET1; NbExp=3; IntAct=EBI-12814225, EBI-749204; CC Q9BXS9-3; P60033: CD81; NbExp=3; IntAct=EBI-12814225, EBI-712921; CC Q9BXS9-3; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-12814225, EBI-711490; CC Q9BXS9-3; O43561-2: LAT; NbExp=3; IntAct=EBI-12814225, EBI-8070286; CC Q9BXS9-3; P60201-2: PLP1; NbExp=3; IntAct=EBI-12814225, EBI-12188331; CC Q9BXS9-3; Q9BXS9-3: SLC26A6; NbExp=3; IntAct=EBI-12814225, EBI-12814225; CC Q9BXS9-3; Q6UX34: SNORC; NbExp=3; IntAct=EBI-12814225, EBI-11957067; CC Q9BXS9-3; P02787: TF; NbExp=3; IntAct=EBI-12814225, EBI-714319; CC Q9BXS9-3; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-12814225, EBI-10694905; CC Q9BXS9-3; Q5SNT2-2: TMEM201; NbExp=3; IntAct=EBI-12814225, EBI-11994282; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11247665, CC ECO:0000269|PubMed:27681177}; Multi-pass membrane protein CC {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:20501439}; CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane CC {ECO:0000250|UniProtKB:Q8CIW6}; Multi-pass membrane protein CC {ECO:0000255}. Microsome {ECO:0000250|UniProtKB:Q8CIW6}. Note=Localized CC in sperm membranes. Colocalizes with CFTR at the midpiece of sperm CC tail. Localizes to the apical membrane brush border of epithelial cells CC in the proximal tubules of kidney, of enterocytes of the small CC intestine and of gastric parietal cells in the stomach. CC {ECO:0000250|UniProtKB:Q8CIW6}. CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane CC {ECO:0000269|PubMed:12444019, ECO:0000269|PubMed:15990874}; Multi-pass CC membrane protein {ECO:0000255}. Apical cell membrane CC {ECO:0000269|PubMed:11087667}; Multi-pass membrane protein CC {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:11087667}; CC Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the apical CC and basolateral surfaces of tubular wall cells in kidney and in the CC brush border of pancreatic duct cells (PubMed:11087667). Colocalized CC with CA2 at the surface of the cell membrane in order to form a CC bicarbonate transport metabolon; colocalization is reduced in phorbol CC myristate acetate (PMA)-induced cells (PubMed:15990874). May be CC translocated from the cytosolic surface of the cell membrane to the CC intracellular space by PKC in phorbol myristate acetate (PMA)-induced CC cells (PubMed:15990874). {ECO:0000269|PubMed:11087667, CC ECO:0000269|PubMed:15990874}. CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane CC {ECO:0000269|PubMed:12444019}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cell membrane CC {ECO:0000269|PubMed:12444019}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=SLC26A6b; CC IsoId=Q9BXS9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BXS9-2; Sequence=VSP_006169; CC Name=3; CC IsoId=Q9BXS9-3; Sequence=VSP_040127; CC Name=4; Synonyms=SLC26A6a {ECO:0000303|PubMed:12444019}; CC IsoId=Q9BXS9-4; Sequence=VSP_046807, VSP_040127; CC Name=5; Synonyms=SLC26A6c {ECO:0000303|PubMed:12444019}; CC IsoId=Q9BXS9-5; Sequence=VSP_046807, VSP_047851, VSP_040127; CC Name=6; Synonyms=SLC26A6d {ECO:0000303|PubMed:12444019}; CC IsoId=Q9BXS9-6; Sequence=VSP_046807, VSP_047852; CC Name=7; CC IsoId=Q9BXS9-7; Sequence=VSP_055273, VSP_055274; CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels in kidney and pancreas. CC Lower expression in heart, skeletal muscle, liver and placenta. Also CC found in lung and brain. {ECO:0000269|PubMed:11087667, CC ECO:0000269|PubMed:11247665}. CC -!- TISSUE SPECIFICITY: [Isoform 4]: Ubiquitously expressed. Highest levels CC expressed in the kidney and pancreas. {ECO:0000269|PubMed:11087667, CC ECO:0000269|PubMed:12444019}. CC -!- TISSUE SPECIFICITY: [Isoform 5]: Expressed weakly in placenta, lung, CC liver and pancreas. {ECO:0000269|PubMed:12444019}. CC -!- TISSUE SPECIFICITY: [Isoform 6]: Expressed in heart, brain, placenta, CC lung, liver, kidney, pancreas, spleen, thymus, prostate, testis and CC ovary. {ECO:0000269|PubMed:12444019}. CC -!- INDUCTION: Down-regulated by pro-inflammatory cytokine IFN gamma. CC {ECO:0000269|PubMed:18655181}. CC -!- PTM: [Isoform 4]: Phosphorylated on serine residues by PKC; the CC phosphorylation disrupts interaction with carbonic anhydrase CA2 and CC reduces bicarbonate transport activity in a phorbol myristate acetate CC (PMA)-induced manner. {ECO:0000269|PubMed:15990874}. CC -!- PTM: Glycosylation at Asn-167 and Asn-172 positively regulates its CC chloride oxalate exchanger activity. {ECO:0000269|PubMed:27681177}. CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF279265; AAF81911.1; -; mRNA. DR EMBL; AF288410; AAK19153.1; -; mRNA. DR EMBL; AF416721; AAN07094.1; -; mRNA. DR EMBL; AB033288; BAB69041.1; -; mRNA. DR EMBL; AK297695; BAG60053.1; -; mRNA. DR EMBL; AC121252; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64901.1; -; Genomic_DNA. DR EMBL; CH471055; EAW64903.1; -; Genomic_DNA. DR EMBL; BC017697; AAH17697.1; -; mRNA. DR CCDS; CCDS43087.1; -. [Q9BXS9-1] DR CCDS; CCDS46824.1; -. [Q9BXS9-2] DR CCDS; CCDS46825.1; -. [Q9BXS9-3] DR CCDS; CCDS63628.1; -. [Q9BXS9-7] DR RefSeq; NP_001035544.1; NM_001040454.1. DR RefSeq; NP_001268661.1; NM_001281732.1. [Q9BXS9-7] DR RefSeq; NP_001268662.1; NM_001281733.1. DR RefSeq; NP_075062.2; NM_022911.2. [Q9BXS9-1] DR RefSeq; NP_599025.2; NM_134263.2. [Q9BXS9-3] DR RefSeq; NP_602298.2; NM_134426.2. [Q9BXS9-2] DR PDB; 8OPQ; EM; 3.28 A; A/B=2-759. DR PDBsum; 8OPQ; -. DR AlphaFoldDB; Q9BXS9; -. DR SMR; Q9BXS9; -. DR BioGRID; 122373; 84. DR IntAct; Q9BXS9; 33. DR STRING; 9606.ENSP00000378920; -. DR TCDB; 2.A.53.2.7; the sulfate permease (sulp) family. DR GlyGen; Q9BXS9; 2 sites. DR iPTMnet; Q9BXS9; -. DR PhosphoSitePlus; Q9BXS9; -. DR SwissPalm; Q9BXS9; -. DR BioMuta; SLC26A6; -. DR DMDM; 20140224; -. DR EPD; Q9BXS9; -. DR jPOST; Q9BXS9; -. DR MassIVE; Q9BXS9; -. DR MaxQB; Q9BXS9; -. DR PaxDb; 9606-ENSP00000378920; -. DR PeptideAtlas; Q9BXS9; -. DR ProteomicsDB; 4656; -. DR ProteomicsDB; 79499; -. [Q9BXS9-1] DR ProteomicsDB; 79500; -. [Q9BXS9-2] DR ProteomicsDB; 79501; -. [Q9BXS9-3] DR ProteomicsDB; 82188; -. DR Pumba; Q9BXS9; -. DR Antibodypedia; 30187; 242 antibodies from 27 providers. DR DNASU; 65010; -. DR Ensembl; ENST00000383733.7; ENSP00000373239.3; ENSG00000225697.13. [Q9BXS9-2] DR Ensembl; ENST00000395550.7; ENSP00000378920.2; ENSG00000225697.13. [Q9BXS9-1] DR Ensembl; ENST00000420764.6; ENSP00000404684.2; ENSG00000225697.13. [Q9BXS9-3] DR Ensembl; ENST00000455886.6; ENSP00000401066.2; ENSG00000225697.13. [Q9BXS9-7] DR GeneID; 65010; -. DR KEGG; hsa:65010; -. DR MANE-Select; ENST00000395550.7; ENSP00000378920.2; NM_022911.3; NP_075062.2. DR UCSC; uc003cug.4; human. [Q9BXS9-1] DR AGR; HGNC:14472; -. DR CTD; 65010; -. DR DisGeNET; 65010; -. DR GeneCards; SLC26A6; -. DR HGNC; HGNC:14472; SLC26A6. DR HPA; ENSG00000225697; Low tissue specificity. DR MIM; 610068; gene. DR neXtProt; NX_Q9BXS9; -. DR OpenTargets; ENSG00000225697; -. DR PharmGKB; PA37889; -. DR VEuPathDB; HostDB:ENSG00000225697; -. DR eggNOG; KOG0236; Eukaryota. DR GeneTree; ENSGT01070000253775; -. DR HOGENOM; CLU_003182_9_4_1; -. DR InParanoid; Q9BXS9; -. DR OMA; SKRCRFP; -. DR OrthoDB; 1067648at2759; -. DR PhylomeDB; Q9BXS9; -. DR TreeFam; TF313784; -. DR PathwayCommons; Q9BXS9; -. DR Reactome; R-HSA-427601; Multifunctional anion exchangers. DR SignaLink; Q9BXS9; -. DR BioGRID-ORCS; 65010; 15 hits in 1155 CRISPR screens. DR ChiTaRS; SLC26A6; human. DR GeneWiki; SLC26A6; -. DR GenomeRNAi; 65010; -. DR Pharos; Q9BXS9; Tbio. DR PRO; PR:Q9BXS9; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9BXS9; Protein. DR Bgee; ENSG00000225697; Expressed in mucosa of transverse colon and 107 other cell types or tissues. DR ExpressionAtlas; Q9BXS9; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB. DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB. DR GO; GO:0031982; C:vesicle; ISS:UniProtKB. DR GO; GO:0012506; C:vesicle membrane; ISS:UniProtKB. DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW. DR GO; GO:0015108; F:chloride transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0140900; F:chloride:bicarbonate antiporter activity; IDA:UniProtKB. DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0015499; F:formate transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB. DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; IDA:UniProtKB. DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015383; F:sulfate:bicarbonate antiporter activity; IDA:UniProtKB. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0038166; P:angiotensin-activated signaling pathway; IDA:UniProtKB. DR GO; GO:0015701; P:bicarbonate transport; IDA:UniProtKB. DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB. DR GO; GO:0071332; P:cellular response to fructose stimulus; ISS:UniProtKB. DR GO; GO:0071346; P:cellular response to type II interferon; IDA:UniProtKB. DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB. DR GO; GO:0042045; P:epithelial fluid transport; ISS:UniProtKB. DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl. DR GO; GO:0044849; P:estrous cycle; IEA:Ensembl. DR GO; GO:0015724; P:formate transport; ISS:UniProtKB. DR GO; GO:0050892; P:intestinal absorption; ISS:UniProtKB. DR GO; GO:0051454; P:intracellular pH elevation; ISS:UniProtKB. DR GO; GO:0015797; P:mannitol transmembrane transport; ISS:UniProtKB. DR GO; GO:0006811; P:monoatomic ion transport; TAS:Reactome. DR GO; GO:0019532; P:oxalate transport; IMP:UniProtKB. DR GO; GO:0046724; P:oxalic acid secretion; ISS:UniProtKB. DR GO; GO:2001150; P:positive regulation of dipeptide transmembrane transport; ISS:UniProtKB. DR GO; GO:0070528; P:protein kinase C signaling; IDA:UniProtKB. DR GO; GO:0051453; P:regulation of intracellular pH; IDA:UniProtKB. DR GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB. DR GO; GO:0008272; P:sulfate transport; IMP:UniProtKB. DR GO; GO:0030321; P:transepithelial chloride transport; IMP:UniProtKB. DR GO; GO:0070633; P:transepithelial transport; ISS:UniProtKB. DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1. DR Gene3D; 3.30.750.24; STAS domain; 1. DR InterPro; IPR018045; S04_transporter_CS. DR InterPro; IPR011547; SLC26A/SulP_dom. DR InterPro; IPR001902; SLC26A/SulP_fam. DR InterPro; IPR002645; STAS_dom. DR InterPro; IPR036513; STAS_dom_sf. DR NCBIfam; TIGR00815; sulP; 1. DR PANTHER; PTHR11814:SF113; SOLUTE CARRIER FAMILY 26 MEMBER 6; 1. DR PANTHER; PTHR11814; SULFATE TRANSPORTER; 1. DR Pfam; PF01740; STAS; 1. DR Pfam; PF00916; Sulfate_transp; 1. DR SUPFAM; SSF52091; SpoIIaa-like; 1. DR PROSITE; PS01130; SLC26A; 1. DR PROSITE; PS50801; STAS; 1. DR Genevisible; Q9BXS9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Anion exchange; Antiport; KW Cell membrane; Chloride; Chloride channel; Cytoplasmic vesicle; KW Endoplasmic reticulum; Glycoprotein; Ion channel; Ion transport; Membrane; KW Microsome; Phosphoprotein; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..759 FT /note="Solute carrier family 26 member 6" FT /id="PRO_0000080171" FT TOPO_DOM 1..115 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 116..136 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 137..186 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 187..207 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 208..263 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 264..284 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 285..293 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 294..314 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 315..347 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 348..368 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 369..379 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 380..400 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 401..416 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 417..437 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 438..484 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 485..505 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 506..759 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 530..742 FT /note="STAS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198" FT REGION 636..657 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 616 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 752 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT MOD_RES 755 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT CARBOHYD 167 FT /note="N-linked (GlcNAc) asparagine" FT /evidence="ECO:0000269|PubMed:27681177" FT CARBOHYD 172 FT /note="N-linked (GlcNAc) asparagine" FT /evidence="ECO:0000269|PubMed:27681177" FT VAR_SEQ 1..21 FT /note="Missing (in isoform 4, isoform 5 and isoform 6)" FT /evidence="ECO:0000303|PubMed:11087667" FT /id="VSP_046807" FT VAR_SEQ 145..216 FT /note="GTFAVMSVMVGSVTESLAPQALNDSMINETARDAARVQVASTLSVLVGLFQV FT GLGLIHFGFVVTYLSEPLVR -> ATPGPLPLLTAPGRPTGGAGPDPLRLRGHLPVRTS FT CPRLYHSCSCAGLRLTAQVCVWPPSEQPLWATVPHLL (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055273" FT VAR_SEQ 217..252 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055274" FT VAR_SEQ 264..301 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_047851" FT VAR_SEQ 602..631 FT /note="ASPKGASVSINVNTSLEDMRSNNVEDCKMM -> GPLLSACLAPQ (in FT isoform 2)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_006169" FT VAR_SEQ 632..759 FT /note="QVSSGDKMEDATANGQEDSKAPDGSTLKALGLPQPDFHSLILDLGALSFVDT FT VCLKSLKNIFHDFREIEVEVYMAACHSPVVSQLEAGHFFDASITKKHLFASVHDAVTFA FT LQHPRPVPDSPVSVTRL -> VRLEVGKEVTAVSCRDAGSTCLMRNAMDPAAVGSRVLR FT RWQEEWGGWVRYSSGSVVICHRI (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_047852" FT VAR_SEQ 632 FT /note="Missing (in isoform 3, isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:11087667, FT ECO:0000303|PubMed:12217875, ECO:0000303|PubMed:15489334" FT /id="VSP_040127" FT VARIANT 206 FT /note="V -> M (in dbSNP:rs13324142)" FT /evidence="ECO:0000269|PubMed:11247665" FT /id="VAR_012776" FT MUTAGEN 167 FT /note="N->Q: Reduced chloride oxalate exchanger activity." FT /evidence="ECO:0000269|PubMed:27681177" FT MUTAGEN 172 FT /note="N->Q: Reduced chloride oxalate exchanger activity." FT /evidence="ECO:0000269|PubMed:27681177" FT HELIX 38..45 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 64..74 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 77..80 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 86..115 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 119..125 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 128..136 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 148..161 FT /evidence="ECO:0007829|PDB:8OPQ" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 171..200 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 206..209 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 212..235 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 247..257 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 259..261 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 264..286 FT /evidence="ECO:0007829|PDB:8OPQ" FT TURN 287..290 FT /evidence="ECO:0007829|PDB:8OPQ" FT STRAND 291..293 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 297..312 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 314..318 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 341..370 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 376..392 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 402..411 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 416..431 FT /evidence="ECO:0007829|PDB:8OPQ" FT TURN 432..434 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 435..437 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 442..451 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 454..469 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 471..486 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 488..508 FT /evidence="ECO:0007829|PDB:8OPQ" FT STRAND 514..518 FT /evidence="ECO:0007829|PDB:8OPQ" FT STRAND 525..527 FT /evidence="ECO:0007829|PDB:8OPQ" FT TURN 528..530 FT /evidence="ECO:0007829|PDB:8OPQ" FT STRAND 531..533 FT /evidence="ECO:0007829|PDB:8OPQ" FT STRAND 540..544 FT /evidence="ECO:0007829|PDB:8OPQ" FT TURN 551..553 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 554..564 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 569..593 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 658..661 FT /evidence="ECO:0007829|PDB:8OPQ" FT STRAND 669..674 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 683..698 FT /evidence="ECO:0007829|PDB:8OPQ" FT STRAND 702..706 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 710..718 FT /evidence="ECO:0007829|PDB:8OPQ" FT STRAND 724..726 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 728..730 FT /evidence="ECO:0007829|PDB:8OPQ" FT STRAND 731..734 FT /evidence="ECO:0007829|PDB:8OPQ" FT HELIX 735..744 FT /evidence="ECO:0007829|PDB:8OPQ" FT MOD_RES Q9BXS9-4:553 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000305|PubMed:15990874" FT MOD_RES Q9BXS9-4:582 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000305|PubMed:15990874" FT MUTAGEN Q9BXS9-4:547..549 FT /note="DVD->NVN: Does not inhibit cell membrane FT localization. Inhibits interaction with CA2 and bicarbonate FT transport." FT /evidence="ECO:0000269|PubMed:15990874" FT MUTAGEN Q9BXS9-4:553 FT /note="S->A: Does not inhibit interaction with CA2. FT Inhibits interaction with CA2 and bicarbonate transport in FT PMA-induced cells." FT /evidence="ECO:0000269|PubMed:15990874" FT MUTAGEN Q9BXS9-4:582 FT /note="S->A: Does not inhibit interaction with CA2. Does FT not inhibit interaction with CA2 and bicarbonate transport FT in PMA-induced cells." FT /evidence="ECO:0000269|PubMed:15990874" SQ SEQUENCE 759 AA; 82967 MW; 63CB0B756C9675C6 CRC64; MGLADASGPR DTQALLSATQ AMDLRRRDYH MERPLLNQEH LEELGRWGSA PRTHQWRTWL QCSRARAYAL LLQHLPVLVW LPRYPVRDWL LGDLLSGLSV AIMQLPQGLA YALLAGLPPV FGLYSSFYPV FIYFLFGTSR HISVGTFAVM SVMVGSVTES LAPQALNDSM INETARDAAR VQVASTLSVL VGLFQVGLGL IHFGFVVTYL SEPLVRGYTT AAAVQVFVSQ LKYVFGLHLS SHSGPLSLIY TVLEVCWKLP QSKVGTVVTA AVAGVVLVVV KLLNDKLQQQ LPMPIPGELL TLIGATGISY GMGLKHRFEV DVVGNIPAGL VPPVAPNTQL FSKLVGSAFT IAVVGFAIAI SLGKIFALRH GYRVDSNQEL VALGLSNLIG GIFQCFPVSC SMSRSLVQES TGGNSQVAGA ISSLFILLII VKLGELFHDL PKAVLAAIII VNLKGMLRQL SDMRSLWKAN RADLLIWLVT FTATILLNLD LGLVVAVIFS LLLVVVRTQM PHYSVLGQVP DTDIYRDVAE YSEAKEVRGV KVFRSSATVY FANAEFYSDA LKQRCGVDVD FLISQKKKLL KKQEQLKLKQ LQKEEKLRKQ AASPKGASVS INVNTSLEDM RSNNVEDCKM MQVSSGDKME DATANGQEDS KAPDGSTLKA LGLPQPDFHS LILDLGALSF VDTVCLKSLK NIFHDFREIE VEVYMAACHS PVVSQLEAGH FFDASITKKH LFASVHDAVT FALQHPRPVP DSPVSVTRL //