ID   S26A3_HUMAN             Reviewed;         764 AA.
AC   P40879;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 207.
DE   RecName: Full=Chloride anion exchanger;
DE   AltName: Full=Down-regulated in adenoma;
DE            Short=Protein DRA;
DE   AltName: Full=Solute carrier family 26 member 3;
GN   Name=SLC26A3; Synonyms=DRA;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Colon;
RX   PubMed=7683425; DOI=10.1073/pnas.90.9.4166;
RA   Schweinfest C.W., Henderson K.W., Suster S., Kondoh N., Papas T.S.;
RT   "Identification of a colon mucosa gene that is down-regulated in colon
RT   adenomas and adenocarcinomas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:4166-4170(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [3]
RP   SIMILARITY TO SULFATE PERMEASES.
RX   PubMed=8140616; DOI=10.1016/0968-0004(94)90168-6;
RA   Sandal N.N., Marcker K.A.;
RT   "Similarities between a soybean nodulin, Neurospora crassa sulphate
RT   permease II and a putative human tumour suppressor.";
RL   Trends Biochem. Sci. 19:19-19(1994).
RN   [4]
RP   INTERACTION WITH PDZK1.
RX   PubMed=15766278; DOI=10.1021/bi048828b;
RA   Rossmann H., Jacob P., Baisch S., Hassoun R., Meier J., Natour D.,
RA   Yahya K., Yun C., Biber J., Lackner K.J., Fiehn W., Gregor M., Seidler U.,
RA   Lamprecht G.;
RT   "The CFTR associated protein CAP70 interacts with the apical Cl-/HCO3-
RT   exchanger DRA in rabbit small intestinal mucosa.";
RL   Biochemistry 44:4477-4487(2005).
RN   [5]
RP   FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=16606687; DOI=10.1085/jgp.200509392;
RA   Shcheynikov N., Wang Y., Park M., Ko S.B., Dorwart M., Naruse S.,
RA   Thomas P.J., Muallem S.;
RT   "Coupling modes and stoichiometry of Cl-/HCO3- exchange by slc26a3 and
RT   slc26a6.";
RL   J. Gen. Physiol. 127:511-524(2006).
RN   [6]
RP   FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=19321737; DOI=10.1152/ajpcell.00638.2008;
RA   Hayashi H., Suruga K., Yamashita Y.;
RT   "Regulation of intestinal Cl-/HCO3- exchanger SLC26A3 by intracellular
RT   pH.";
RL   Am. J. Physiol. 296:C1279-C1290(2009).
RN   [7]
RP   GLYCOSYLATION AT ASN-153; ASN-161 AND ASN-165, SUBCELLULAR LOCATION,
RP   FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=22159084; DOI=10.1152/ajpcell.00165.2011;
RA   Hayashi H., Yamashita Y.;
RT   "Role of N-glycosylation in cell surface expression and protection against
RT   proteolysis of the intestinal anion exchanger SLC26A3.";
RL   Am. J. Physiol. 302:C781-C795(2012).
RN   [8]
RP   FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH
RP   NHERF4, MUTAGENESIS OF 761-GLU--PHE-764, AND PDZ-BINDING MOTIF.
RX   PubMed=22627094; DOI=10.1016/j.cellsig.2012.05.010;
RA   Lee J.H., Nam J.H., Park J., Kang D.W., Kim J.Y., Lee M.G., Yoon J.S.;
RT   "Regulation of SLC26A3 activity by NHERF4 PDZ-mediated interaction.";
RL   Cell. Signal. 24:1821-1830(2012).
RN   [9]
RP   VARIANTS DIAR1 LEU-124 AND VAL-318 DEL, AND VARIANT TRP-307.
RX   PubMed=8896562; DOI=10.1038/ng1196-316;
RA   Hoeglund P., Haila S., Socha J., Tomaszewski L., Saarialho-Kere U.,
RA   Karjalainen-Lindsberg M.-L., Airola K., Holmberg C., de la Chapelle A.,
RA   Kere J.;
RT   "Mutations of the Down-regulated in adenoma (DRA) gene cause congenital
RT   chloride diarrhoea.";
RL   Nat. Genet. 14:316-319(1996).
RN   [10]
RP   VARIANTS DIAR1 SER-120; LEU-124; ARG-131 AND ARG-496.
RX   PubMed=9718329; DOI=10.1086/301998;
RA   Hoglund P., Auranen M., Socha J., Popinska K., Nazer H., Rajaram U.,
RA   Al Sanie A., Al-Ghanim M., Holmberg C., de la Chapelle A., Kere J.;
RT   "Genetic background of congenital chloride diarrhea in high-incidence
RT   populations: Finland, Poland, and Saudi Arabia and Kuwait.";
RL   Am. J. Hum. Genet. 63:760-768(1998).
RN   [11]
RP   VARIANTS DIAR1 SER-120; ARG-131; VAL-318 DEL AND TYR-527 DEL.
RX   PubMed=9554749;
RX   DOI=10.1002/(sici)1098-1004(1998)11:4<321::aid-humu10>3.0.co;2-a;
RA   Hoeglund P., Haila S., Gustavson K.-H., Taipale M., Hannula K.,
RA   Popinska K., Holmberg C., Socha J., de la Chapelle A., Kere J.;
RT   "Clustering of private mutations in the congenital chloride diarrhea/down-
RT   regulated in adenoma gene.";
RL   Hum. Mutat. 11:321-327(1998).
RN   [12]
RP   VARIANTS DIAR1 PRO-206 AND VAL-468.
RX   PubMed=11524734; DOI=10.1002/humu.1179;
RA   Hoeglund P., Sormaala M., Haila S., Socha J., Rajaram U., Scheurlen W.,
RA   Sinaasappel M., de Jonge H., Holmberg C., Yoshikawa H., Kere J.;
RT   "Identification of seven novel mutations including the first two genomic
RT   rearrangements in SLC26A3 mutated in congenital chloride diarrhea.";
RL   Hum. Mutat. 18:233-242(2001).
RN   [13]
RP   VARIANTS DIAR1 CYS-520 AND ASN-652.
RX   PubMed=19861545; DOI=10.1073/pnas.0910672106;
RA   Choi M., Scholl U.I., Ji W., Liu T., Tikhonova I.R., Zumbo P., Nayir A.,
RA   Bakkaloglu A., Ozen S., Sanjad S., Nelson-Williams C., Farhi A., Mane S.,
RA   Lifton R.P.;
RT   "Genetic diagnosis by whole exome capture and massively parallel DNA
RT   sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:19096-19101(2009).
RN   [14]
RP   VARIANTS DIAR1 LEU-129; LEU-131; ILE-136; ASP-204; PRO-220; TYR-343;
RP   344-PHE--VAL-349 DELINS ASP-ALA; ALA-379; PHE-398; ASN-521 AND ASN-544.
RX   PubMed=21394828; DOI=10.1002/humu.21498;
RA   Wedenoja S., Pekansaari E., Hoglund P., Makela S., Holmberg C., Kere J.;
RT   "Update on SLC26A3 mutations in congenital chloride diarrhea.";
RL   Hum. Mutat. 32:715-722(2011).
RN   [15]
RP   VARIANT DIAR1 PRO-220.
RX   PubMed=21150650; DOI=10.1097/mpg.0b013e3181f28d1a;
RA   Rodriguez-Herrera A., Navas-Lopez V.M., Redondo-Nevado J., Gutierrez G.;
RT   "Compound heterozygous mutations in the SLC26A3 gene in 2 Spanish siblings
RT   with congenital chloride diarrhea.";
RL   J. Pediatr. Gastroenterol. Nutr. 52:106-110(2011).
RN   [16]
RP   VARIANT DIAR1 SER-175.
RX   PubMed=22779076; DOI=10.3343/alm.2012.32.4.312;
RA   Lee E.S., Cho A.R., Ki C.S.;
RT   "Identification of SLC26A3 mutations in a Korean patient with congenital
RT   chloride diarrhea.";
RL   Ann. Lab. Med. 32:312-315(2012).
RN   [17]
RP   VARIANTS DIAR1 LEU-131 AND ASN-134.
RX   PubMed=23274434; DOI=10.1007/s00431-012-1905-3;
RA   Hong J., Seo J.K., Ko J.S., Cheong H.I., Choi J.H., Lee J.H., Seo J.W.;
RT   "Congenital chloride diarrhea in Korean children: novel mutations and
RT   genetic characteristics.";
RL   Eur. J. Pediatr. 172:545-550(2013).
RN   [18]
RP   VARIANTS DIAR1 SER-120; LEU-129; ARG-131; VAL-318 DEL; ILE-394; PRO-438;
RP   PRO-495; ARG-508; GLU-547; PRO-654 AND ILE-675 INS.
RX   PubMed=28644346; DOI=10.1097/mpg.0000000000001418;
RA   Amato F., Cardillo G., Liguori R., Scorza M., Comegna M., Elce A.,
RA   Giordano S., Lucaccioni L., Lugli L., Cardile S., Romano C., Pezzella V.,
RA   Castaldo G., Canani R.B.;
RT   "Twelve novel mutations in the SLC26A3 gene in 17 sporadic cases of
RT   congenital chloride diarrhea.";
RL   J. Pediatr. Gastroenterol. Nutr. 65:26-30(2017).
CC   -!- FUNCTION: Mediates chloride-bicarbonate exchange with a chloride
CC       bicarbonate stoichiometry of 2:1 in the intestinal epithelia
CC       (PubMed:16606687, PubMed:19321737, PubMed:22159084, PubMed:22627094).
CC       Plays a role in the chloride and bicarbonate homeostasis during sperm
CC       epididymal maturation and capacitation (By similarity).
CC       {ECO:0000250|UniProtKB:Q9WVC8, ECO:0000269|PubMed:16606687,
CC       ECO:0000269|PubMed:19321737, ECO:0000269|PubMed:22159084,
CC       ECO:0000269|PubMed:22627094}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 chloride(out) + hydrogencarbonate(in) = 2 chloride(in) +
CC         hydrogencarbonate(out); Xref=Rhea:RHEA:72203, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:16606687,
CC         ECO:0000269|PubMed:19321737, ECO:0000269|PubMed:22159084,
CC         ECO:0000269|PubMed:22627094};
CC   -!- ACTIVITY REGULATION: Inhibited by acidic pH.
CC       {ECO:0000269|PubMed:19321737}.
CC   -!- SUBUNIT: Interacts with CFTR, SLC26A6 and NHERF1 (By similarity).
CC       Interacts with PDZK1 (PubMed:15766278). Interacts (via PDZ-binding
CC       motif) with NHERF4 (via the third PDZ domain); interaction leads to
CC       decreased expression of SLC26A3 on the cell membrane resulting in its
CC       reduced exchanger activity (PubMed:22627094).
CC       {ECO:0000250|UniProtKB:Q9WVC8, ECO:0000269|PubMed:15766278,
CC       ECO:0000269|PubMed:22627094}.
CC   -!- INTERACTION:
CC       P40879; Q15599: NHERF2; NbExp=5; IntAct=EBI-8542350, EBI-1149760;
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:22159084}; Multi-pass membrane protein
CC       {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:Q9WVC8}; Multi-pass
CC       membrane protein {ECO:0000255}. Cell membrane
CC       {ECO:0000269|PubMed:19321737, ECO:0000269|PubMed:22627094}; Multi-pass
CC       membrane protein {ECO:0000255}. Note=Localized in sperm membranes.
CC       Midpiece of sperm tail. Colocalizes with CFTR at the midpiece of sperm
CC       tail (By similarity). {ECO:0000250|UniProtKB:Q9WVC8}.
CC   -!- TISSUE SPECIFICITY: Expressed in the colon. Expression is significantly
CC       decreased in adenomas (polyps) and adenocarcinomas of the colon.
CC       {ECO:0000269|PubMed:7683425}.
CC   -!- PTM: N-glycosylation is required for efficient cell surface expression,
CC       and protection from proteolytic degradation.
CC       {ECO:0000269|PubMed:22159084}.
CC   -!- DISEASE: Diarrhea 1, secretory chloride, congenital (DIAR1)
CC       [MIM:214700]: A disease characterized by voluminous watery stools
CC       containing an excess of chloride. The children with this disease are
CC       often premature. {ECO:0000269|PubMed:11524734,
CC       ECO:0000269|PubMed:19861545, ECO:0000269|PubMed:21150650,
CC       ECO:0000269|PubMed:21394828, ECO:0000269|PubMed:22779076,
CC       ECO:0000269|PubMed:23274434, ECO:0000269|PubMed:28644346,
CC       ECO:0000269|PubMed:8896562, ECO:0000269|PubMed:9554749,
CC       ECO:0000269|PubMed:9718329}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC       {ECO:0000305}.
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DR   EMBL; L02785; AAA58443.1; -; mRNA.
DR   EMBL; BC025671; AAH25671.1; -; mRNA.
DR   CCDS; CCDS5748.1; -.
DR   PIR; A47456; A47456.
DR   RefSeq; NP_000102.1; NM_000111.2.
DR   RefSeq; XP_011514169.1; XM_011515867.2.
DR   PDB; 7XUH; EM; 2.76 A; A/B=1-764.
DR   PDB; 7XUJ; EM; 2.80 A; A/B=8-725.
DR   PDB; 7XUL; EM; 3.16 A; A/B=8-725.
DR   PDBsum; 7XUH; -.
DR   PDBsum; 7XUJ; -.
DR   PDBsum; 7XUL; -.
DR   AlphaFoldDB; P40879; -.
DR   EMDB; EMD-33469; -.
DR   EMDB; EMD-33471; -.
DR   EMDB; EMD-33473; -.
DR   SMR; P40879; -.
DR   BioGRID; 108145; 1.
DR   IntAct; P40879; 2.
DR   MINT; P40879; -.
DR   STRING; 9606.ENSP00000345873; -.
DR   ChEMBL; CHEMBL4523223; -.
DR   TCDB; 2.A.53.2.18; the sulfate permease (sulp) family.
DR   GlyCosmos; P40879; 3 sites, No reported glycans.
DR   GlyGen; P40879; 3 sites.
DR   iPTMnet; P40879; -.
DR   PhosphoSitePlus; P40879; -.
DR   BioMuta; SLC26A3; -.
DR   DMDM; 729367; -.
DR   jPOST; P40879; -.
DR   MassIVE; P40879; -.
DR   PaxDb; 9606-ENSP00000345873; -.
DR   PeptideAtlas; P40879; -.
DR   ProteomicsDB; 55383; -.
DR   Antibodypedia; 31383; 121 antibodies from 26 providers.
DR   DNASU; 1811; -.
DR   Ensembl; ENST00000340010.10; ENSP00000345873.5; ENSG00000091138.13.
DR   GeneID; 1811; -.
DR   KEGG; hsa:1811; -.
DR   MANE-Select; ENST00000340010.10; ENSP00000345873.5; NM_000111.3; NP_000102.1.
DR   UCSC; uc003ver.3; human.
DR   AGR; HGNC:3018; -.
DR   CTD; 1811; -.
DR   DisGeNET; 1811; -.
DR   GeneCards; SLC26A3; -.
DR   HGNC; HGNC:3018; SLC26A3.
DR   HPA; ENSG00000091138; Tissue enriched (intestine).
DR   MalaCards; SLC26A3; -.
DR   MIM; 126650; gene.
DR   MIM; 214700; phenotype.
DR   neXtProt; NX_P40879; -.
DR   OpenTargets; ENSG00000091138; -.
DR   Orphanet; 53689; Congenital chloride diarrhea.
DR   PharmGKB; PA35044; -.
DR   VEuPathDB; HostDB:ENSG00000091138; -.
DR   eggNOG; KOG0236; Eukaryota.
DR   GeneTree; ENSGT01070000253775; -.
DR   HOGENOM; CLU_003182_9_4_1; -.
DR   InParanoid; P40879; -.
DR   OMA; WVMTFIF; -.
DR   OrthoDB; 1067648at2759; -.
DR   PhylomeDB; P40879; -.
DR   TreeFam; TF313784; -.
DR   PathwayCommons; P40879; -.
DR   Reactome; R-HSA-427601; Multifunctional anion exchangers.
DR   Reactome; R-HSA-5619085; Defective SLC26A3 causes congenital secretory chloride diarrhea 1 (DIAR1).
DR   SignaLink; P40879; -.
DR   SIGNOR; P40879; -.
DR   BioGRID-ORCS; 1811; 10 hits in 1145 CRISPR screens.
DR   ChiTaRS; SLC26A3; human.
DR   GeneWiki; SLC26A3; -.
DR   GenomeRNAi; 1811; -.
DR   Pharos; P40879; Tbio.
DR   PRO; PR:P40879; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P40879; Protein.
DR   Bgee; ENSG00000091138; Expressed in colonic mucosa and 111 other cell types or tissues.
DR   ExpressionAtlas; P40879; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR   GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0140900; F:chloride:bicarbonate antiporter activity; IDA:UniProtKB.
DR   GO; GO:0019531; F:oxalate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0005452; F:solute:inorganic anion antiporter activity; TAS:Reactome.
DR   GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR   GO; GO:0051454; P:intracellular pH elevation; ISS:UniProtKB.
DR   GO; GO:0060081; P:membrane hyperpolarization; ISS:UniProtKB.
DR   GO; GO:0006820; P:monoatomic anion transport; TAS:ProtInc.
DR   GO; GO:0006811; P:monoatomic ion transport; TAS:Reactome.
DR   GO; GO:0048240; P:sperm capacitation; 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:SF19; CHLORIDE ANION EXCHANGER; 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; P40879; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Antiport; Cell membrane; Chloride; Disease variant;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..764
FT                   /note="Chloride anion exchanger"
FT                   /id="PRO_0000080161"
FT   TOPO_DOM        1..76
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..99
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        146..175
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        219..257
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        279..342
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        364..374
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        396..411
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        433..469
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        470..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        491..701
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          525..720
FT                   /note="STAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT   MOTIF           761..764
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000269|PubMed:22627094"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22159084"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22159084"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22159084"
FT   VARIANT         68
FT                   /note="R -> Q (in dbSNP:rs10280704)"
FT                   /id="VAR_053660"
FT   VARIANT         120
FT                   /note="G -> S (in DIAR1; dbSNP:rs386833479)"
FT                   /evidence="ECO:0000269|PubMed:28644346,
FT                   ECO:0000269|PubMed:9554749, ECO:0000269|PubMed:9718329"
FT                   /id="VAR_007428"
FT   VARIANT         124
FT                   /note="H -> L (in DIAR1; dbSNP:rs121913030)"
FT                   /evidence="ECO:0000269|PubMed:8896562,
FT                   ECO:0000269|PubMed:9718329"
FT                   /id="VAR_007429"
FT   VARIANT         129
FT                   /note="P -> L (in DIAR1; dbSNP:rs386833480)"
FT                   /evidence="ECO:0000269|PubMed:21394828,
FT                   ECO:0000269|PubMed:28644346"
FT                   /id="VAR_066062"
FT   VARIANT         131
FT                   /note="P -> L (in DIAR1; dbSNP:rs386833481)"
FT                   /evidence="ECO:0000269|PubMed:21394828,
FT                   ECO:0000269|PubMed:23274434"
FT                   /id="VAR_066063"
FT   VARIANT         131
FT                   /note="P -> R (in DIAR1; dbSNP:rs386833481)"
FT                   /evidence="ECO:0000269|PubMed:28644346,
FT                   ECO:0000269|PubMed:9554749, ECO:0000269|PubMed:9718329"
FT                   /id="VAR_007430"
FT   VARIANT         134
FT                   /note="S -> N (in DIAR1)"
FT                   /evidence="ECO:0000269|PubMed:23274434"
FT                   /id="VAR_077354"
FT   VARIANT         136
FT                   /note="M -> I (in DIAR1; dbSNP:rs386833483)"
FT                   /evidence="ECO:0000269|PubMed:21394828"
FT                   /id="VAR_066064"
FT   VARIANT         175
FT                   /note="R -> S (in DIAR1; dbSNP:rs386833484)"
FT                   /evidence="ECO:0000269|PubMed:22779076"
FT                   /id="VAR_077355"
FT   VARIANT         204
FT                   /note="Y -> D (in DIAR1; dbSNP:rs386833487)"
FT                   /evidence="ECO:0000269|PubMed:21394828"
FT                   /id="VAR_066065"
FT   VARIANT         206
FT                   /note="S -> P (in DIAR1; dbSNP:rs386833488)"
FT                   /evidence="ECO:0000269|PubMed:11524734"
FT                   /id="VAR_012777"
FT   VARIANT         220
FT                   /note="H -> P (in DIAR1; dbSNP:rs386833489)"
FT                   /evidence="ECO:0000269|PubMed:21150650,
FT                   ECO:0000269|PubMed:21394828"
FT                   /id="VAR_066066"
FT   VARIANT         307
FT                   /note="C -> W (in dbSNP:rs34407351)"
FT                   /evidence="ECO:0000269|PubMed:8896562"
FT                   /id="VAR_007431"
FT   VARIANT         318
FT                   /note="Missing (in DIAR1; dbSNP:rs386833491)"
FT                   /evidence="ECO:0000269|PubMed:28644346,
FT                   ECO:0000269|PubMed:8896562, ECO:0000269|PubMed:9554749"
FT                   /id="VAR_007432"
FT   VARIANT         343
FT                   /note="C -> Y (in DIAR1; dbSNP:rs386833444)"
FT                   /evidence="ECO:0000269|PubMed:21394828"
FT                   /id="VAR_066067"
FT   VARIANT         344..349
FT                   /note="FGIAMV -> DA (in DIAR1)"
FT                   /evidence="ECO:0000269|PubMed:21394828"
FT                   /id="VAR_066068"
FT   VARIANT         379
FT                   /note="G -> A (in DIAR1; dbSNP:rs386833446)"
FT                   /evidence="ECO:0000269|PubMed:21394828"
FT                   /id="VAR_066069"
FT   VARIANT         394
FT                   /note="S -> I (in DIAR1; dbSNP:rs1228273365)"
FT                   /evidence="ECO:0000269|PubMed:28644346"
FT                   /id="VAR_077356"
FT   VARIANT         398
FT                   /note="S -> F (in DIAR1; dbSNP:rs143839547)"
FT                   /evidence="ECO:0000269|PubMed:21394828"
FT                   /id="VAR_066070"
FT   VARIANT         438
FT                   /note="S -> P (in DIAR1; dbSNP:rs763669046)"
FT                   /evidence="ECO:0000269|PubMed:28644346"
FT                   /id="VAR_077357"
FT   VARIANT         468
FT                   /note="D -> V (in DIAR1; dbSNP:rs386833454)"
FT                   /evidence="ECO:0000269|PubMed:11524734"
FT                   /id="VAR_012778"
FT   VARIANT         495
FT                   /note="Q -> P (in DIAR1)"
FT                   /evidence="ECO:0000269|PubMed:28644346"
FT                   /id="VAR_077358"
FT   VARIANT         496
FT                   /note="L -> R (in DIAR1; dbSNP:rs386833457)"
FT                   /evidence="ECO:0000269|PubMed:9718329"
FT                   /id="VAR_066071"
FT   VARIANT         508
FT                   /note="C -> R (in DIAR1)"
FT                   /evidence="ECO:0000269|PubMed:28644346"
FT                   /id="VAR_077359"
FT   VARIANT         520
FT                   /note="Y -> C (in DIAR1; dbSNP:rs386833462)"
FT                   /evidence="ECO:0000269|PubMed:19861545"
FT                   /id="VAR_066072"
FT   VARIANT         521
FT                   /note="K -> N (in DIAR1; dbSNP:rs386833463)"
FT                   /evidence="ECO:0000269|PubMed:21394828"
FT                   /id="VAR_066073"
FT   VARIANT         527
FT                   /note="Missing (in DIAR1; dbSNP:rs386833464)"
FT                   /evidence="ECO:0000269|PubMed:9554749"
FT                   /id="VAR_007433"
FT   VARIANT         544
FT                   /note="I -> N (in DIAR1; dbSNP:rs386833467)"
FT                   /evidence="ECO:0000269|PubMed:21394828"
FT                   /id="VAR_066074"
FT   VARIANT         547
FT                   /note="A -> E (in DIAR1)"
FT                   /evidence="ECO:0000269|PubMed:28644346"
FT                   /id="VAR_077360"
FT   VARIANT         554
FT                   /note="R -> Q (in dbSNP:rs2301635)"
FT                   /id="VAR_053661"
FT   VARIANT         652
FT                   /note="D -> N (in DIAR1; dbSNP:rs140426439)"
FT                   /evidence="ECO:0000269|PubMed:19861545"
FT                   /id="VAR_066075"
FT   VARIANT         654
FT                   /note="S -> P (in DIAR1)"
FT                   /evidence="ECO:0000269|PubMed:28644346"
FT                   /id="VAR_077361"
FT   VARIANT         675
FT                   /note="I -> II (in DIAR1; dbSNP:rs121913031)"
FT                   /evidence="ECO:0000269|PubMed:28644346"
FT                   /id="VAR_077362"
FT   VARIANT         753
FT                   /note="N -> S (in dbSNP:rs35342296)"
FT                   /id="VAR_053662"
FT   MUTAGEN         761..764
FT                   /note="Missing: Loss of interaction with NHERF4. No effect
FT                   on localization to cell membrane or its exchanger
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:22627094"
SQ   SEQUENCE   764 AA;  84505 MW;  694C5BC2D4121F6D CRC64;
     MIEPFGNQYI VARPVYSTNA FEENHKKTGR HHKTFLDHLK VCCSCSPQKA KRIVLSLFPI
     ASWLPAYRLK EWLLSDIVSG ISTGIVAVLQ GLAFALLVDI PPVYGLYASF FPAIIYLFFG
     TSRHISVGPF PILSMMVGLA VSGAVSKAVP DRNATTLGLP NNSNNSSLLD DERVRVAAAA
     SVTVLSGIIQ LAFGILRIGF VVIYLSESLI SGFTTAAAVH VLVSQLKFIF QLTVPSHTDP
     VSIFKVLYSV FSQIEKTNIA DLVTALIVLL VVSIVKEINQ RFKDKLPVPI PIEFIMTVIA
     AGVSYGCDFK NRFKVAVVGD MNPGFQPPIT PDVETFQNTV GDCFGIAMVA FAVAFSVASV
     YSLKYDYPLD GNQELIALGL GNIVCGVFRG FAGSTALSRS AVQESTGGKT QIAGLIGAII
     VLIVVLAIGF LLAPLQKSVL AALALGNLKG MLMQFAEIGR LWRKDKYDCL IWIMTFIFTI
     VLGLGLGLAA SVAFQLLTIV FRTQFPKCST LANIGRTNIY KNKKDYYDMY EPEGVKIFRC
     PSPIYFANIG FFRRKLIDAV GFSPLRILRK RNKALRKIRK LQKQGLLQVT PKGFICTVDT
     IKDSDEELDN NQIEVLDQPI NTTDLPFHID WNDDLPLNIE VPKISLHSLI LDFSAVSFLD
     VSSVRGLKSI LQEFIRIKVD VYIVGTDDDF IEKLNRYEFF DGEVKSSIFF LTIHDAVLHI
     LMKKDYSTSK FNPSQEKDGK IDFTINTNGG LRNRVYEVPV ETKF
//