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 29-MAY-2024, entry version 208. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 DrugBank; DB01586; Ursodeoxycholic acid. 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. 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 //