S26A7_MOUSE
ID S26A7_MOUSE Reviewed; 656 AA.
AC Q8R2Z3; A2AJZ4; B1AWS0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Anion exchange transporter;
DE AltName: Full=Solute carrier family 26 member 7;
GN Name=Slc26a7 {ECO:0000312|EMBL:AAH26928.1, ECO:0000312|MGI:MGI:2384791};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:AAO49172.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO49172.1};
RA Mount D.B.;
RT "Characterization of Mus musculus Slc26a7, a novel putative anion
RT exchanger.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:AAO49172.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAH26928.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH26928.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH26928.1};
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 [5] {ECO:0000305}
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12736153; DOI=10.1152/ajpgi.00454.2002;
RA Petrovic S., Ju X., Barone S., Seidler U., Alper S.L., Lohi H., Kere J.,
RA Soleimani M.;
RT "Identification of a basolateral Cl-/HCO3- exchanger specific to gastric
RT parietal cells.";
RL Am. J. Physiol. 284:G1093-G1103(2003).
RN [6] {ECO:0000305}
RP FUNCTION, AND INHIBITION.
RX PubMed=15591059; DOI=10.1074/jbc.m409162200;
RA Kim K.H., Shcheynikov N., Wang Y., Muallem S.;
RT "SLC26A7 is a Cl- channel regulated by intracellular pH.";
RL J. Biol. Chem. 280:6463-6470(2005).
RN [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16263805; DOI=10.1152/ajprenal.00197.2004;
RA Dudas P.L., Mentone S., Greineder C.F., Biemesderfer D., Aronson P.S.;
RT "Immunolocalization of anion transporter Slc26a7 in mouse kidney.";
RL Am. J. Physiol. 290:F937-F945(2006).
RN [8] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16524946; DOI=10.1681/asn.2005111174;
RA Xu J., Worrell R.T., Li H.C., Barone S.L., Petrovic S., Amlal H.,
RA Soleimani M.;
RT "Chloride/bicarbonate exchanger SLC26A7 is localized in endosomes in
RT medullary collecting duct cells and is targeted to the basolateral membrane
RT in hypertonicity and potassium depletion.";
RL J. Am. Soc. Nephrol. 17:956-967(2006).
CC -!- FUNCTION: Acts as a sodium-independent DIDS-sensitive anion exchanger
CC mediating bicarbonate, chloride, sulfate and oxalate transport. May
CC play a role in the maintenance of the electrolyte and acid-base
CC homeostasis in the kidney, by acting as a distal excretory segment-
CC specific anion exchanger, specifically chloride. Plays a major role in
CC gastric acid secretion. {ECO:0000250|UniProtKB:Q8TE54,
CC ECO:0000269|PubMed:12736153, ECO:0000269|PubMed:15591059,
CC ECO:0000269|PubMed:16263805}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane
CC protein {ECO:0000269|PubMed:12736153, ECO:0000269|PubMed:16263805,
CC ECO:0000269|PubMed:16524946}. Recycling endosome membrane; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12736153,
CC ECO:0000269|PubMed:16263805, ECO:0000269|PubMed:16524946}.
CC Note=Expressed on the basolateral membrane of acid-secreting gastric
CC parietal cells, distal nephron segments and apical domains of proximal
CC tubules and in the glomerulus. Expressed in the cytoplasm in recycling
CC endosomes of kidney outer medullary collecting duct cells and in acid-
CC secreting gastric parietal cells. Targeted to the basolateral membrane
CC in hypertonicity and potassium depletion.
CC {ECO:0000250|UniProtKB:Q8TE54, ECO:0000269|PubMed:12736153,
CC ECO:0000269|PubMed:16263805, ECO:0000269|PubMed:16524946}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in parietal cells on the
CC glandular portion of the stomach. Lower levels are observed in the
CC kidney, with expression in the proximal tubule and thick ascending limb
CC of the loop of Henle. Also expressed in distal segments of nephron, in
CC extraglomerular mesagial cells and a subpopulation of intercalated
CC cells of outer medullary collecting ducts.
CC {ECO:0000269|PubMed:12736153, ECO:0000269|PubMed:16263805,
CC ECO:0000269|PubMed:16524946}.
CC -!- MISCELLANEOUS: Regulated by pH. Activity inhibited by all inhibitors of
CC several anion channels and transporters, including 4,4'-Di-
CC isothiocyanatostilbene-2,2'-disulfonic acid (DIDS), diphenylamine-2-
CC carboxylic acid and glybenclamide.
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000255}.
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DR EMBL; AF345194; AAO49172.1; -; mRNA.
DR EMBL; AL772236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL772270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466538; EDL05611.1; -; Genomic_DNA.
DR EMBL; BC026928; AAH26928.1; -; mRNA.
DR CCDS; CCDS17979.1; -.
DR RefSeq; NP_666059.2; NM_145947.2.
DR AlphaFoldDB; Q8R2Z3; -.
DR SMR; Q8R2Z3; -.
DR BioGRID; 229021; 12.
DR STRING; 10090.ENSMUSP00000041789; -.
DR PhosphoSitePlus; Q8R2Z3; -.
DR jPOST; Q8R2Z3; -.
DR PaxDb; Q8R2Z3; -.
DR PeptideAtlas; Q8R2Z3; -.
DR PRIDE; Q8R2Z3; -.
DR ProteomicsDB; 253375; -.
DR Antibodypedia; 25657; 68 antibodies from 8 providers.
DR DNASU; 208890; -.
DR Ensembl; ENSMUST00000042221; ENSMUSP00000041789; ENSMUSG00000040569.
DR GeneID; 208890; -.
DR KEGG; mmu:208890; -.
DR UCSC; uc008saz.2; mouse.
DR CTD; 115111; -.
DR MGI; MGI:2384791; Slc26a7.
DR VEuPathDB; HostDB:ENSMUSG00000040569; -.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244807; -.
DR HOGENOM; CLU_003182_9_5_1; -.
DR InParanoid; Q8R2Z3; -.
DR OMA; SLVHCTA; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; Q8R2Z3; -.
DR TreeFam; TF313784; -.
DR Reactome; R-MMU-427601; Multifunctional anion exchangers.
DR BioGRID-ORCS; 208890; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q8R2Z3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8R2Z3; protein.
DR Bgee; ENSMUSG00000040569; Expressed in vestibular membrane of cochlear duct and 171 other tissues.
DR ExpressionAtlas; Q8R2Z3; baseline and differential.
DR Genevisible; Q8R2Z3; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IC:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005253; F:anion channel activity; IMP:MGI.
DR GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; IDA:MGI.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0019531; F:oxalate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0006820; P:anion transport; IMP:MGI.
DR GO; GO:0015701; P:bicarbonate transport; IMP:UniProtKB.
DR GO; GO:0006821; P:chloride transport; IDA:MGI.
DR GO; GO:0001696; P:gastric acid secretion; IDA:UniProtKB.
DR GO; GO:0019532; P:oxalate transport; ISO:MGI.
DR GO; GO:0008272; P:sulfate transport; ISO:MGI.
DR Gene3D; 3.30.750.24; -; 1.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR030329; SLC26A7.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR PANTHER; PTHR11814; PTHR11814; 1.
DR PANTHER; PTHR11814:SF75; PTHR11814:SF75; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR PROSITE; PS50801; STAS; 1.
PE 2: Evidence at transcript level;
KW Anion exchange; Cell membrane; Endosome; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..656
FT /note="Anion exchange transporter"
FT /id="PRO_0000320682"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..144
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..343
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..448
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..656
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 492..641
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 641..656
FT /note="Membrane targeting"
FT /evidence="ECO:0000250|UniProtKB:Q8TE54"
FT CONFLICT 233
FT /note="F -> L (in Ref. 1; AAO49172 and 4; AAH26928)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="S -> T (in Ref. 1; AAO49172 and 4; AAH26928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 71829 MW; 321924A9BE7A1D0A CRC64;
MTGAKRKKRS VLWGKMHTPH REDIKQWCKR RLPILEWAPQ YNLKENLLPD TVSGIMLAVQ
QVAQGLSFAM LSSVHPVFGL YGSLFPAIIY AIFGMGRHVA TGTFALTSLI SANAVERLVP
QSSRNLTTQS NSSVLGLSEF ELQRIGVAAA VSFLGGVIQL VMFVLQLGSA TFLLTEPVIS
AMTTGAATHV VTSQVKYLLG IKMPYISGPL GFFYIYAYVF ENIKSVQLEA LLFSLLSIIV
LVLVKELNEQ FKRKIKVVLP VDLVLIIAAS FACYCTNMEN TYGLEVVGHI PNGIPPPRAP
PMNILSAVLT EAFGVALVGY VASLALAQGS AKKFKYSVDD NQEFLAHGLS NVIPSFLFCI
PSAAAMGRTA GLYSTGAKTQ VACLISCIFV LIVIYAIGPL LYWLPMCVLA SIIVVGLKGM
LIQFRDLKKY WNVDKIDWGI WISTYIFTIC FAANVGLLFG VICTIAIVLG RFPRAKTLSI
TDMKEMELKV KTEMHDETSQ QIKIISINNP LVFLNAKKFS ADLMKIILKE SDSNQPLDDV
SKCEQNTLLS SLSNGNCNEE ASQPCSSEKC SLVLNCSGLT FFDYTGVSTL VELYLDCKSR
SVDVFLANCT ASLIKAMTYY GDLDTEKPIF FDSVPAAISI IQSNKNLSKA SDHSEV
