Anion exchange transporter - Mus musculus (Mouse)

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Q8R2Z3 (S26A7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Anion exchange transporter

Alternative name(s):
Solute carrier family 26 member 7

Gene names

Name:

Slc26a7

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	656 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Acts as a sodium-independent DIDS-sensitive anion exchanger mediating bicarbonate, chloride, sulfate and oxalate transport. May play a role in the maintenance of the electrolyte and acid-base homeostasis in the kidney, by acting as a distal excretory segment-specific anion exchanger, specifically chloride. Plays a major role in gastric acid secretion. Ref.5 Ref.6 Ref.7 UniProtKB Q8TE54
Subcellular location	Basolateral cell membrane; Multi-pass membrane protein. Recycling endosome membrane; Multi-pass membrane protein. Note: Expressed on the basolateral membrane of acid-secreting gastric parietal cells, distal nephron segments and apical domains of proximal tubules and in the glomerulus. Expressed in the cytoplasm in recycling endosomes of kidney outer medullary collecting duct cells and in acid-secreting gastric parietal cells. Targeted to the basolateral membrane in hypertonicity and potassium depletion. Ref.5 Ref.7 Ref.8
Tissue specificity	Abundantly expressed in parietal cells on the glandular portion of the stomach. Lower levels are observed in the kidney, with expression in the proximal tubule and thick ascending limb of the loop of Henle. Also expressed in distal segments of nephron, in extraglomerular mesagial cells and a subpopulation of intercalated cells of outer medullary collecting ducts. Ref.5 Ref.7 Ref.8
Miscellaneous	Regulated by pH. Activity inhibited by all inhibitors of several anion channels and transporters, including 4,4'-Di-isothiocyanatostilbene-2,2'-disulfonic acid (DIDS), diphenylamine-2-carboxylic acid and glybenclamide. Ref.6
Sequence similarities	Belongs to the SLC26A/SulP transporter (TC 2.A.53) family. [View classification] Contains 1 STAS domain.

Ontologies

Keywords
Biological process	Anion exchange Ion transport Transport
Cellular component	Cell membrane Endosome Membrane
Domain	Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gastric acid secretion Inferred from direct assay Ref.5. Source: UniProtKB sulfate transport Inferred from electronic annotation. Source: Compara
Cellular_component	basolateral plasma membrane Inferred from direct assay Ref.5. Source: UniProtKB integral to membrane Inferred by curator Ref.6. Source: MGI recycling endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	anion:anion antiporter activity Inferred from electronic annotation. Source: UniProtKB-KW bicarbonate transmembrane transporter activity Inferred from mutant phenotype Ref.5. Source: UniProtKB chloride channel activity Inferred from direct assay Ref.6. Source: MGI oxalate transmembrane transporter activity Inferred from electronic annotation. Source: Compara sulfate transmembrane transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 656

656

Anion exchange transporter

PRO_0000320682

Regions

Topological domain

1 – 75

Cytoplasmic Potential

Transmembrane

76 – 96

Helical; Potential

Topological domain

97 – 144

Extracellular Potential

Transmembrane

145 – 165

Helical; Potential

Topological domain

166

Cytoplasmic Potential

Transmembrane

167 – 187

Helical; Potential

Topological domain

188 – 199

Extracellular Potential

Transmembrane

200 – 220

Helical; Potential

Topological domain

221 – 222

Cytoplasmic Potential

Transmembrane

223 – 243

Helical; Potential

Topological domain

244 – 254

Extracellular Potential

Transmembrane

255 – 275

Helical; Potential

Topological domain

276 – 306

Cytoplasmic Potential

Transmembrane

307 – 327

Helical; Potential

Topological domain

328 – 343

Extracellular Potential

Transmembrane

344 – 364

Helical; Potential

Topological domain

365 – 383

Cytoplasmic Potential

Transmembrane

384 – 404

Helical; Potential

Transmembrane

405 – 425

Helical; Potential

Topological domain

426 – 448

Extracellular Potential

Transmembrane

449 – 469

Helical; Potential

Topological domain

470 – 656

187

Cytoplasmic Potential

Domain

492 – 641

150

STAS

Region

641 – 656

Membrane targeting By similarity UniProtKB Q8TE54

Experimental info

Sequence conflict

233

F → L in AAO49172. Ref.1

Sequence conflict

233

F → L in AAH26928. Ref.4

Sequence conflict

639

S → T in AAO49172. Ref.1

Sequence conflict

639

S → T in AAH26928. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

Q8R2Z3 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 321924A9BE7A1D0A
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FASTA

656

71,829

        10         20         30         40         50         60 
MTGAKRKKRS VLWGKMHTPH REDIKQWCKR RLPILEWAPQ YNLKENLLPD TVSGIMLAVQ 

        70         80         90        100        110        120 
QVAQGLSFAM LSSVHPVFGL YGSLFPAIIY AIFGMGRHVA TGTFALTSLI SANAVERLVP 

       130        140        150        160        170        180 
QSSRNLTTQS NSSVLGLSEF ELQRIGVAAA VSFLGGVIQL VMFVLQLGSA TFLLTEPVIS 

       190        200        210        220        230        240 
AMTTGAATHV VTSQVKYLLG IKMPYISGPL GFFYIYAYVF ENIKSVQLEA LLFSLLSIIV 

       250        260        270        280        290        300 
LVLVKELNEQ FKRKIKVVLP VDLVLIIAAS FACYCTNMEN TYGLEVVGHI PNGIPPPRAP 

       310        320        330        340        350        360 
PMNILSAVLT EAFGVALVGY VASLALAQGS AKKFKYSVDD NQEFLAHGLS NVIPSFLFCI 

       370        380        390        400        410        420 
PSAAAMGRTA GLYSTGAKTQ VACLISCIFV LIVIYAIGPL LYWLPMCVLA SIIVVGLKGM 

       430        440        450        460        470        480 
LIQFRDLKKY WNVDKIDWGI WISTYIFTIC FAANVGLLFG VICTIAIVLG RFPRAKTLSI 

       490        500        510        520        530        540 
TDMKEMELKV KTEMHDETSQ QIKIISINNP LVFLNAKKFS ADLMKIILKE SDSNQPLDDV 

       550        560        570        580        590        600 
SKCEQNTLLS SLSNGNCNEE ASQPCSSEKC SLVLNCSGLT FFDYTGVSTL VELYLDCKSR 

       610        620        630        640        650 
SVDVFLANCT ASLIKAMTYY GDLDTEKPIF FDSVPAAISI IQSNKNLSKA SDHSEV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of Mus musculus Slc26a7, a novel putative anion exchanger." Mount D.B. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Strain: Czech II. Tissue: Mammary tumor.
[5]	"Identification of a basolateral Cl-/HCO3- exchanger specific to gastric parietal cells." Petrovic S., Ju X., Barone S., Seidler U., Alper S.L., Lohi H., Kere J., Soleimani M. Am. J. Physiol. 284:G1093-G1103(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]	"SLC26A7 is a Cl- channel regulated by intracellular pH." Kim K.H., Shcheynikov N., Wang Y., Muallem S. J. Biol. Chem. 280:6463-6470(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INHIBITION.
[7]	"Immunolocalization of anion transporter Slc26a7 in mouse kidney." Dudas P.L., Mentone S., Greineder C.F., Biemesderfer D., Aronson P.S. Am. J. Physiol. 290:F937-F945(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]	"Chloride/bicarbonate exchanger SLC26A7 is localized in endosomes in medullary collecting duct cells and is targeted to the basolateral membrane in hypertonicity and potassium depletion." Xu J., Worrell R.T., Li H.C., Barone S.L., Petrovic S., Amlal H., Soleimani M. J. Am. Soc. Nephrol. 17:956-967(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF345194 mRNA. Translation: AAO49172.1. AL772270, AL772236 Genomic DNA. Translation: CAM19223.1. AL772236, AL772270 Genomic DNA. Translation: CAM27494.1. CH466538 Genomic DNA. Translation: EDL05611.1. BC026928 mRNA. Translation: AAH26928.1.
IPI	IPI00153705.
RefSeq	NP_666059.2. NM_145947.2.
UniGene	Mm.483839.
3D structure databases
ProteinModelPortal	Q8R2Z3.
ModBase	Search...
PTM databases
PhosphoSite	Q8R2Z3.
Proteomic databases
PaxDb	Q8R2Z3.
PRIDE	Q8R2Z3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000042221; ENSMUSP00000041789; ENSMUSG00000040569.
GeneID	208890.
KEGG	mmu:208890.
Organism-specific databases
CTD	115111.
MGI	MGI:2384791. Slc26a7.
Phylogenomic databases
eggNOG	COG0659.
GeneTree	ENSGT00650000092895.
HOGENOM	HOG000049231.
HOVERGEN	HBG108442.
InParanoid	B1AWS0.
KO	K13962.
OMA	NAKKFYT.
OrthoDB	EOG45HRWX.
Gene expression databases
ArrayExpress	Q8R2Z3.
Bgee	Q8R2Z3.
CleanEx	MM_SLC26A7.
Genevestigator	Q8R2Z3.
Family and domain databases
Gene3D	3.30.750.24. 2 hits.
InterPro	IPR002645. STAS_dom. IPR011547. Sulph_transpt. [Graphical view]
Pfam	PF01740. STAS. 1 hit. PF00916. Sulfate_transp. 1 hit. [Graphical view]
SUPFAM	SSF52091. STAS. 1 hit.
PROSITE	PS01130. SLC26A. False negative. PS50801. STAS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	372447.
SOURCE	Search...

Entry information

Entry name

S26A7_MOUSE

Accession

Primary (citable) accession number: Q8R2Z3
Secondary accession number(s): A2AJZ4, B1AWS0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 77 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents