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'-diisothiocyanatostilbene-
CC 2,2'-disulfonic acid (DIDS). {ECO:0000269|PubMed:12444019,
CC ECO:0000269|PubMed:15990874}.
CC -!- ACTIVITY REGULATION: [Isoform 5]: Chloride, bicarbonate and sulfate
CC transport activities are inhibited by 4,4'-diisothiocyanatostilbene-
CC 2,2'-disulfonic acid (DIDS). {ECO:0000269|PubMed:12444019}.
CC -!- ACTIVITY REGULATION: [Isoform 6]: Chloride, bicarbonate and sulfate
CC transport activities are inhibited by 4,4'-diisothiocyanatostilbene-
CC 2,2'-disulfonic acid (DIDS). {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}.
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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 Genevisible; Q9BXS9; HS.
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.
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
//
