S26A7_HUMAN
ID S26A7_HUMAN Reviewed; 656 AA.
AC Q8TE54; Q24JS8; Q8TE53; Q96RN2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Anion exchange transporter;
DE AltName: Full=Solute carrier family 26 member 7;
GN Name=SLC26A7 {ECO:0000312|HGNC:HGNC:14467};
GN Synonyms=SUT2 {ECO:0000312|EMBL:CAC88372.1};
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] {ECO:0000305, ECO:0000312|EMBL:CAC88372.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Endothelial cell {ECO:0000312|EMBL:CAC88371.1}, and
RC Kidney {ECO:0000312|EMBL:CAC88372.1};
RX PubMed=11829495; DOI=10.1006/geno.2002.6689;
RA Vincourt J.-B., Jullien D., Kossida S., Amalric F., Girard J.-P.;
RT "Molecular cloning of SLC26A7, a novel member of the SLC26 sulfate/anion
RT transporter family, from high endothelial venules and kidney.";
RL Genomics 79:249-256(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK95665.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11834742; DOI=10.1074/jbc.m111802200;
RA Lohi H., Kujala M., Maekelae S., Lehtonen E., Kestilae M.,
RA Saarialho-Kere U., Markovich D., Kere J.;
RT "Functional characterization of three novel tissue-specific anion
RT exchangers SLC26A7, -A8, and -A9.";
RL J. Biol. Chem. 277:14246-14254(2002).
RN [3] {ECO:0000312|EMBL:EAW91679.1}
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAI13867.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta {ECO:0000312|EMBL:AAH94730.1};
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, AND INHIBITION.
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 TISSUE SPECIFICITY.
RX PubMed=15956810; DOI=10.1159/000086345;
RA Kujala M., Tienari J., Lohi H., Elomaa O., Sariola H., Lehtonen E.,
RA Kere J.;
RT "SLC26A6 and SLC26A7 anion exchangers have a distinct distribution in human
RT kidney.";
RL Nephron Exp. Nephrol. 101:E50-E58(2005).
RN [7] {ECO:0000305}
RP SUBCELLULAR LOCATION.
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).
RN [8] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=17504921; DOI=10.1530/rep.1.00964;
RA Kujala M., Hihnala S., Tienari J., Kaunisto K., Hastbacka J., Holmberg C.,
RA Kere J., Hoglund P.;
RT "Expression of ion transport-associated proteins in human efferent and
RT epididymal ducts.";
RL Reproduction 133:775-784(2007).
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. Plays a major role in gastric acid secretion.
CC {ECO:0000250|UniProtKB:Q8R2Z3, ECO:0000269|PubMed:11834742,
CC ECO:0000269|PubMed:12736153}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000269|PubMed:16524946}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16524946}. Note=Expressed in the cytoplasm in
CC recycling endosomes of 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:0000269|PubMed:16524946}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:11829495}; Synonyms=1A
CC {ECO:0000269|PubMed:11829495}, 1B {ECO:0000269|PubMed:11829495};
CC IsoId=Q8TE54-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11829495, ECO:0000269|PubMed:15489334};
CC Synonyms=B {ECO:0000269|PubMed:15489334};
CC IsoId=Q8TE54-2; Sequence=VSP_052689;
CC -!- TISSUE SPECIFICITY: Expressed in tonsillar high endothelial venule
CC endothelial cells (HEVEC), placenta and in testis, expressed in a
CC subgroup of basal cells in the epididymal ducts.
CC {ECO:0000269|PubMed:11829495, ECO:0000269|PubMed:11834742,
CC ECO:0000269|PubMed:15956810, ECO:0000269|PubMed:17504921}.
CC -!- MISCELLANEOUS: Is active at both alkaline and acidic pH. Activity is
CC inhibited by 4,4'-Di-isothiocyanatostilbene-2,2'-disulfonic acid (DIDS
CC - an inhibitor of several anion channels and transporters).
CC -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC {ECO:0000255}.
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DR EMBL; AJ413228; CAC88370.1; -; mRNA.
DR EMBL; AJ413229; CAC88371.1; -; mRNA.
DR EMBL; AJ413230; CAC88372.1; -; mRNA.
DR EMBL; AF331521; AAK95665.1; -; mRNA.
DR EMBL; CH471060; EAW91680.1; -; Genomic_DNA.
DR EMBL; CH471060; EAW91679.1; -; Genomic_DNA.
DR EMBL; BC094730; AAH94730.1; -; mRNA.
DR EMBL; BC113866; AAI13867.1; -; mRNA.
DR EMBL; BC114474; AAI14475.1; -; mRNA.
DR CCDS; CCDS6254.1; -. [Q8TE54-1]
DR CCDS; CCDS6255.1; -. [Q8TE54-2]
DR RefSeq; NP_001269285.1; NM_001282356.1. [Q8TE54-1]
DR RefSeq; NP_001269286.1; NM_001282357.1.
DR RefSeq; NP_439897.1; NM_052832.3. [Q8TE54-1]
DR RefSeq; NP_599028.1; NM_134266.1. [Q8TE54-2]
DR AlphaFoldDB; Q8TE54; -.
DR SMR; Q8TE54; -.
DR BioGRID; 125414; 1.
DR STRING; 9606.ENSP00000309504; -.
DR TCDB; 2.A.53.2.6; the sulfate permease (sulp) family.
DR GlyConnect; 2019; 1 N-Linked glycan (1 site).
DR GlyGen; Q8TE54; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q8TE54; -.
DR PhosphoSitePlus; Q8TE54; -.
DR BioMuta; SLC26A7; -.
DR DMDM; 172045817; -.
DR MassIVE; Q8TE54; -.
DR PaxDb; Q8TE54; -.
DR PeptideAtlas; Q8TE54; -.
DR PRIDE; Q8TE54; -.
DR ProteomicsDB; 74394; -. [Q8TE54-1]
DR ProteomicsDB; 74395; -. [Q8TE54-2]
DR Antibodypedia; 25657; 68 antibodies from 8 providers.
DR DNASU; 115111; -.
DR Ensembl; ENST00000276609.8; ENSP00000276609.3; ENSG00000147606.9. [Q8TE54-1]
DR Ensembl; ENST00000309536.6; ENSP00000309504.2; ENSG00000147606.9. [Q8TE54-2]
DR Ensembl; ENST00000523719.5; ENSP00000428849.1; ENSG00000147606.9. [Q8TE54-1]
DR Ensembl; ENST00000617233.2; ENSP00000482549.1; ENSG00000147606.9. [Q8TE54-1]
DR GeneID; 115111; -.
DR KEGG; hsa:115111; -.
DR MANE-Select; ENST00000276609.8; ENSP00000276609.3; NM_052832.4; NP_439897.1.
DR UCSC; uc003yex.5; human. [Q8TE54-1]
DR CTD; 115111; -.
DR DisGeNET; 115111; -.
DR GeneCards; SLC26A7; -.
DR HGNC; HGNC:14467; SLC26A7.
DR HPA; ENSG00000147606; Tissue enriched (thyroid).
DR MIM; 608479; gene.
DR neXtProt; NX_Q8TE54; -.
DR OpenTargets; ENSG00000147606; -.
DR PharmGKB; PA37884; -.
DR VEuPathDB; HostDB:ENSG00000147606; -.
DR eggNOG; KOG0236; Eukaryota.
DR GeneTree; ENSGT01050000244807; -.
DR HOGENOM; CLU_003182_9_5_1; -.
DR InParanoid; Q8TE54; -.
DR OMA; SLVHCTA; -.
DR OrthoDB; 690428at2759; -.
DR PhylomeDB; Q8TE54; -.
DR TreeFam; TF313784; -.
DR PathwayCommons; Q8TE54; -.
DR Reactome; R-HSA-427601; Multifunctional anion exchangers.
DR SignaLink; Q8TE54; -.
DR BioGRID-ORCS; 115111; 10 hits in 1070 CRISPR screens.
DR ChiTaRS; SLC26A7; human.
DR GeneWiki; SLC26A7; -.
DR GenomeRNAi; 115111; -.
DR Pharos; Q8TE54; Tbio.
DR PRO; PR:Q8TE54; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8TE54; protein.
DR Bgee; ENSG00000147606; Expressed in thyroid gland and 119 other tissues.
DR ExpressionAtlas; Q8TE54; baseline and differential.
DR Genevisible; Q8TE54; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IMP:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; IDA:UniProtKB.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0019531; F:oxalate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015116; F:sulfate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0006820; P:anion transport; IDA:UniProtKB.
DR GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR GO; GO:0001696; P:gastric acid secretion; IEA:Ensembl.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
DR GO; GO:0019532; P:oxalate transport; IDA:UniProtKB.
DR GO; GO:0008272; P:sulfate transport; IDA:UniProtKB.
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 Alternative splicing; Anion exchange; Endosome; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..656
FT /note="Anion exchange transporter"
FT /id="PRO_0000320681"
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..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..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:0000269|PubMed:16524946"
FT VAR_SEQ 646..656
FT /note="NLSKLSDHSEV -> ASYKLLFDNLDLPTMPPL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11829495,
FT ECO:0000303|PubMed:11834742, ECO:0000303|PubMed:15489334"
FT /id="VSP_052689"
FT VARIANT 215
FT /note="I -> V (in dbSNP:rs16912250)"
FT /id="VAR_053666"
FT VARIANT 381
FT /note="V -> G (in dbSNP:rs34921316)"
FT /id="VAR_053667"
FT CONFLICT 132
FT /note="T -> A (in Ref. 1; CAC88371)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="T -> A (in Ref. 4; AAI14475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 72213 MW; 9F8D2E140E5C00CB CRC64;
MTGAKRKKKS MLWSKMHTPQ CEDIIQWCRR RLPILDWAPH YNLKENLLPD TVSGIMLAVQ
QVTQGLAFAV LSSVHPVFGL YGSLFPAIIY AIFGMGHHVA TGTFALTSLI SANAVERIVP
QNMQNLTTQS NTSVLGLSDF EMQRIHVAAA VSFLGGVIQV AMFVLQLGSA TFVVTEPVIS
AMTTGAATHV VTSQVKYLLG MKMPYISGPL GFFYIYAYVF ENIKSVRLEA LLLSLLSIVV
LVLVKELNEQ FKRKIKVVLP VDLVLIIAAS FACYCTNMEN TYGLEVVGHI PQGIPSPRAP
PMNILSAVIT EAFGVALVGY VASLALAQGS AKKFKYSIDD NQEFLAHGLS NIVSSFFFCI
PSAAAMGRTA GLYSTGAKTQ VACLISCIFV LIVIYAIGPL LYWLPMCVLA SIIVVGLKGM
LIQFRDLKKY WNVDKIDWGI WVSTYVFTIC FAANVGLLFG VVCTIAIVIG RFPRAMTVSI
KNMKEMEFKV KTEMDSETLQ QVKIISINNP LVFLNAKKFY TDLMNMIQKE NACNQPLDDI
SKCEQNTLLN SLSNGNCNEE ASQSCPNEKC YLILDCSGFT FFDYSGVSML VEVYMDCKGR
SVDVLLAHCT ASLIKAMTYY GNLDSEKPIF FESVSAAISH IHSNKNLSKL SDHSEV
