ID S4A11_HUMAN Reviewed; 891 AA. AC Q8NBS3; B4DKC8; B4DKX9; G3V1M3; Q2TB62; Q2TB63; Q9BXF4; Q9NTW9; DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2003, sequence version 2. DT 22-APR-2020, entry version 160. DE RecName: Full=Sodium bicarbonate transporter-like protein 11; DE AltName: Full=Bicarbonate transporter-related protein 1; DE AltName: Full=Sodium borate cotransporter 1; DE Short=NaBC1; DE AltName: Full=Solute carrier family 4 member 11; GN Name=SLC4A11; Synonyms=BTR1; 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] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS RP HIS-408; ASN-409; THR-483 AND ALA-708. RC TISSUE=Kidney; RX PubMed=11302728; DOI=10.1006/bbrc.2001.4692; RA Parker M.D., Ourmozdi E.P., Tanner M.J.A.; RT "Human BTR1, a new bicarbonate transporter superfamily member and human AE4 RT from kidney."; RL Biochem. Biophys. Res. Commun. 282:1103-1109(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 227-891 (ISOFORM 1). RC TISSUE=Retinoblastoma, Thalamus, and Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 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 [6] RP FUNCTION. RX PubMed=15525507; DOI=10.1016/j.molcel.2004.09.030; RA Park M., Li Q., Shcheynikov N., Zeng W., Muallem S.; RT "NaBC1 is a ubiquitous electrogenic Na+-coupled borate transporter RT essential for cellular boron homeostasis and cell growth and RT proliferation."; RL Mol. Cell 16:331-341(2004). RN [7] RP SUBCELLULAR LOCATION, GLYCOSYLATION, VARIANTS FECD4 LYS-399; GLU-709 AND RP MET-754, VARIANTS THR-72; VAL-91; VAL-327; MET-561 AND LEU-565, AND RP CHARACTERIZATION OF VARIANTS FECD4 LYS-399; GLU-709 AND MET-754. RX PubMed=18024964; DOI=10.1093/hmg/ddm337; RA Vithana E.N., Morgan P.E., Ramprasad V., Tan D.T.H., Yong V.H.K., RA Venkataraman D., Venkatraman A., Yam G.H.F., Nagasamy S., Law R.W.K., RA Rajagopal R., Pang C.P., Kumaramanickevel G., Casey J.R., Aung T.; RT "SLC4A11 mutations in Fuchs endothelial corneal dystrophy."; RL Hum. Mol. Genet. 17:656-666(2008). RN [8] RP HOMODIMERIZATION, CHARACTERIZATION OF VARIANTS CHED LYS-143; ARG-386 AND RP TRP-755, AND CHARACTERIZATION OF VARIANTS FECD4 LYS-399; GLU-709 AND RP MET-754. RX PubMed=22072594; DOI=10.1002/humu.21655; RA Vilas G.L., Loganathan S.K., Quon A., Sundaresan P., Vithana E.N., RA Casey J.; RT "Oligomerization of SLC4A11 protein and the severity of FECD and CHED2 RT corneal dystrophies caused by SLC4A11 mutations."; RL Hum. Mutat. 33:419-428(2012). RN [9] RP VARIANTS CHED ASP-464; LEU-489; GLN-755 AND CYS-869, CHARACTERIZATION OF RP VARIANTS CHED ASP-464; LEU-489; GLN-755 AND CYS-869, AND TISSUE RP SPECIFICITY. RX PubMed=16767101; DOI=10.1038/ng1824; RA Vithana E.N., Morgan P., Sundaresan P., Ebenezer N.D., Tan D.T.H., RA Mohamed M.D., Anand S., Khine K.O., Venkataraman D., Yong V.H.K., RA Salto-Tellez M., Venkatraman A., Guo K., Hemadevi B., Srinivasan M., RA Prajna V., Khine M., Casey J.R., Inglehearn C.F., Aung T.; RT "Mutations in sodium-borate cotransporter SLC4A11 cause recessive RT congenital hereditary endothelial dystrophy (CHED2)."; RL Nat. Genet. 38:755-757(2006). RN [10] RP VARIANTS CHED LYS-143; ARG-386; TRP-755; GLN-755 AND CYS-869. RX PubMed=17397048; DOI=10.1002/humu.9487; RA Ramprasad V.L., Ebenezer N.D., Aung T., Rajagopal R., Yong V.H., Tuft S.J., RA Viswanathan D., El-Ashry M.F., Liskova P., Tan D.T., Bhattacharya S.S., RA Kumaramanickavel G., Vithana E.N.; RT "Novel SLC4A11 mutations in patients with recessive congenital hereditary RT endothelial dystrophy (CHED2). Mutation in brief #958. Online."; RL Hum. Mutat. 28:522-523(2007). RN [11] RP VARIANTS CHED GLN-755; HIS-804; MET-833 AND HIS-869, AND VARIANT THR-160. RX PubMed=16825429; DOI=10.1136/jmg.2006.044644; RA Jiao X., Sultana A., Garg P., Ramamurthy B., Vemuganti G.K., RA Gangopadhyay N., Hejtmancik J.F., Kannabiran C.; RT "Autosomal recessive corneal endothelial dystrophy (CHED2) is associated RT with mutations in SLC4A11."; RL J. Med. Genet. 44:64-68(2007). RN [12] RP VARIANTS CDPD PRO-213; LYS-488; PRO-843 AND VAL-856, AND VARIANT CHED RP MET-824. RX PubMed=17220209; DOI=10.1136/jmg.2006.046904; RA Desir J., Moya G., Reish O., Van Regemorter N., Deconinck H., David K.L., RA Meire F.M., Abramowicz M.J.; RT "Borate transporter SLC4A11 mutations cause both Harboyan syndrome and non- RT syndromic corneal endothelial dystrophy."; RL J. Med. Genet. 44:322-326(2007). RN [13] RP VARIANTS CHED TRP-209; LEU-213; CYS-233; LYS-401; ASP-418; ARG-473; RP LEU-489; LYS-584; TRP-755; GLN-755; LEU-773; MET-824 AND CYS-869. RX PubMed=17679935; RA Sultana A., Garg P., Ramamurthy B., Vemuganti G.K., Kannabiran C.; RT "Mutational spectrum of the SLC4A11 gene in autosomal recessive congenital RT hereditary endothelial dystrophy."; RL Mol. Vis. 13:1327-1332(2007). RN [14] RP VARIANTS CHED HIS-125; THR-160; VAL-269; ARG-386; TRP-755; LEU-773 AND RP PRO-873. RX PubMed=18474783; DOI=10.1001/archopht.126.5.700; RA Hemadevi B., Veitia R.A., Srinivasan M., Arunkumar J., Prajna N.V., RA Lesaffre C., Sundaresan P.; RT "Identification of mutations in the SLC4A11 gene in patients with recessive RT congenital hereditary endothelial dystrophy."; RL Arch. Ophthalmol. 126:700-708(2008). RN [15] RP VARIANTS CHED ARG-394 AND ASP-418. RX PubMed=19369245; DOI=10.1167/iovs.08-3006; RA Aldahmesh M.A., Khan A.O., Meyer B.F., Alkuraya F.S.; RT "Mutational spectrum of SLC4A11 in autosomal recessive CHED in Saudi RT Arabia."; RL Invest. Ophthalmol. Vis. Sci. 50:4142-4145(2009). RN [16] RP VARIANT CHED ARG-394. RX PubMed=20108384; RA Chai S.M., Vithana E.N., Venkataraman D., Saleh H., RA Chekkalichintavida N.P., al-Sayyed F., Aung T.; RT "Novel human pathological mutations. Gene symbol: SLC4A11. Disease: Corneal RT endothelial dystrophy 2."; RL Hum. Genet. 127:110-110(2010). RN [17] RP VARIANTS FECD4 ASP-167; PRO-282; CYS-526; MET-575; ASP-583; ARG-742 AND RP SER-834, AND CHARACTERIZATION OF VARIANTS FECD4 ASP-167; PRO-282; CYS-526; RP MET-575; ASP-583; ARG-742 AND SER-834. RX PubMed=20848555; DOI=10.1002/humu.21356; RA Riazuddin S.A., Vithana E.N., Seet L.F., Liu Y., Al-Saif A., Koh L.W., RA Heng Y.M., Aung T., Meadows D.N., Eghrari A.O., Gottsch J.D., Katsanis N.; RT "Missense mutations in the sodium borate cotransporter SLC4A11 cause late- RT onset Fuchs corneal dystrophya."; RL Hum. Mutat. 31:1261-1268(2010). RN [18] RP CHARACTERIZATION OF VARIANT CHED VAL-269. RX PubMed=20185830; DOI=10.1074/jbc.m109.094680; RA Groger N., Frohlich H., Maier H., Olbrich A., Kostin S., Braun T., RA Boettger T.; RT "SLC4A11 prevents osmotic imbalance leading to corneal endothelial RT dystrophy, deafness, and polyuria."; RL J. Biol. Chem. 285:14467-14474(2010). RN [19] RP VARIANTS CHED ARG-386 AND MET-824. RX PubMed=21203343; RA Paliwal P., Sharma A., Tandon R., Sharma N., Titiyal J.S., Sen S., RA Nag T.C., Vajpayee R.B.; RT "Congenital hereditary endothelial dystrophy - mutation analysis of SLC4A11 RT and genotype-phenotype correlation in a North Indian patient cohort."; RL Mol. Vis. 16:2955-2963(2010). RN [20] RP VARIANTS FECD4 SER-240; LYS-399; ILE-434 AND ILE-507, CHARACTERIZATION OF RP VARIANTS FECD4 SER-240; ILE-434 AND ILE-507, FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=25007886; DOI=10.1038/jhg.2014.55; RA Soumittra N., Loganathan S.K., Madhavan D., Ramprasad V.L., Arokiasamy T., RA Sumathi S., Karthiyayini T., Rachapalli S.R., Kumaramanickavel G., RA Casey J.R., Rajagopal R.; RT "Biosynthetic and functional defects in newly identified SLC4A11 mutants RT and absence of COL8A2 mutations in Fuchs endothelial corneal dystrophy."; RL J. Hum. Genet. 59:444-453(2014). RN [21] RP VARIANT CHED ALA-675. RX PubMed=26286922; DOI=10.1111/cxo.12276; RA Kaul H., Suman M., Khan Z., Ullah M.I., Ashfaq U.A., Idrees S.; RT "Missense mutation in SLC4A11 in two Pakistani families affected with RT congenital hereditary endothelial dystrophy (CHED2)."; RL Clin. Exp. Optom. 99:73-77(2016). CC -!- FUNCTION: Transporter which plays an important role in sodium-mediated CC fluid transport in different organs. Prevents severe morphological CC changes of the cornea caused by increased sodium chloride CC concentrations in the stroma. In the inner ear, is involved in CC transport of potassium through the fibrocyte layer to the stria CC vascularis and is essential for the generation of the endocochlear CC potential but not for regulation of potassium concentrations in the CC endolymph. In the kidney, is essential for urinary concentration, CC mediates a sodium flux into the thin descending limb of Henle loop to CC allow countercurrent multiplication by osmotic equilibration (By CC similarity). Involved in borate homeostasis. In the absence of borate, CC it functions as a Na(+) and OH(-)(H(+)) channel. In the presence of CC borate functions as an electrogenic Na(+) coupled borate cotransporter. CC {ECO:0000250|UniProtKB:A2AJN7, ECO:0000269|PubMed:15525507, CC ECO:0000269|PubMed:25007886}. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18024964, CC ECO:0000269|PubMed:25007886}. Membrane {ECO:0000269|PubMed:18024964}; CC Multi-pass membrane protein {ECO:0000269|PubMed:18024964}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8NBS3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NBS3-2; Sequence=VSP_035891; CC Name=3; CC IsoId=Q8NBS3-3; Sequence=VSP_044846; CC Name=4; CC IsoId=Q8NBS3-4; Sequence=VSP_054049; CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney, CC testis, salivary gland, thyroid, trachea and corneal endothelium. Not CC detected in retina and lymphocytes. {ECO:0000269|PubMed:11302728, CC ECO:0000269|PubMed:16767101}. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:18024964}. CC -!- DISEASE: Corneal dystrophy and perceptive deafness (CDPD) [MIM:217400]: CC An ocular disease characterized by the association of corneal clouding CC with progressive perceptive hearing loss. CC {ECO:0000269|PubMed:17220209}. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- DISEASE: Corneal endothelial dystrophy (CHED) [MIM:217700]: A CC congenital corneal dystrophy characterized by thickening and CC opacification of the cornea, altered morphology of the endothelium, and CC secretion of an abnormal collagenous layer at the Descemet membrane. CC {ECO:0000269|PubMed:16767101, ECO:0000269|PubMed:16825429, CC ECO:0000269|PubMed:17220209, ECO:0000269|PubMed:17397048, CC ECO:0000269|PubMed:17679935, ECO:0000269|PubMed:18474783, CC ECO:0000269|PubMed:19369245, ECO:0000269|PubMed:20108384, CC ECO:0000269|PubMed:20185830, ECO:0000269|PubMed:21203343, CC ECO:0000269|PubMed:22072594, ECO:0000269|PubMed:26286922}. Note=The CC disease is caused by mutations affecting the gene represented in this CC entry. CC -!- DISEASE: Corneal dystrophy, Fuchs endothelial, 4 (FECD4) [MIM:613268]: CC A corneal disease caused by loss of endothelium of the central cornea. CC It is characterized by focal wart-like guttata that arise from Descemet CC membrane and develop in the central cornea, epithelial blisters, CC reduced vision and pain. Descemet membrane is thickened by abnormal CC collagenous deposition. {ECO:0000269|PubMed:18024964, CC ECO:0000269|PubMed:20848555, ECO:0000269|PubMed:22072594, CC ECO:0000269|PubMed:25007886}. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC11536.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AF336127; AAK16734.1; -; mRNA. DR EMBL; AK075303; BAC11536.1; ALT_INIT; mRNA. DR EMBL; AK296508; BAG59140.1; -; mRNA. DR EMBL; AK296760; BAG59341.1; -; mRNA. DR EMBL; AL109976; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10536.1; -; Genomic_DNA. DR EMBL; BC110540; AAI10541.1; -; mRNA. DR EMBL; BC110541; AAI10542.1; -; mRNA. DR CCDS; CCDS13052.1; -. [Q8NBS3-1] DR CCDS; CCDS54445.1; -. [Q8NBS3-4] DR CCDS; CCDS54446.1; -. [Q8NBS3-3] DR RefSeq; NP_001167560.1; NM_001174089.1. [Q8NBS3-3] DR RefSeq; NP_001167561.1; NM_001174090.1. [Q8NBS3-4] DR RefSeq; NP_114423.1; NM_032034.3. [Q8NBS3-1] DR IntAct; Q8NBS3; 1. DR STRING; 9606.ENSP00000369399; -. DR TCDB; 2.A.31.4.1; the anion exchanger (ae) family. DR iPTMnet; Q8NBS3; -. DR PhosphoSitePlus; Q8NBS3; -. DR BioMuta; SLC4A11; -. DR DMDM; 29611858; -. DR MassIVE; Q8NBS3; -. DR MaxQB; Q8NBS3; -. DR PaxDb; Q8NBS3; -. DR PeptideAtlas; Q8NBS3; -. DR PRIDE; Q8NBS3; -. DR ProteomicsDB; 32378; -. DR ProteomicsDB; 72815; -. [Q8NBS3-1] DR ProteomicsDB; 72816; -. [Q8NBS3-2] DR Antibodypedia; 7351; 102 antibodies. DR Ensembl; ENST00000380056; ENSP00000369396; ENSG00000088836. [Q8NBS3-1] DR Ensembl; ENST00000380059; ENSP00000369399; ENSG00000088836. [Q8NBS3-4] DR Ensembl; ENST00000642402; ENSP00000493503; ENSG00000088836. [Q8NBS3-3] DR GeneID; 83959; -. DR KEGG; hsa:83959; -. DR UCSC; uc002wig.3; human. [Q8NBS3-1] DR CTD; 83959; -. DR DisGeNET; 83959; -. DR GeneCards; SLC4A11; -. DR HGNC; HGNC:16438; SLC4A11. DR HPA; ENSG00000088836; Tissue enhanced (salivary gland, thyroid gland). DR MalaCards; SLC4A11; -. DR MIM; 217400; phenotype. DR MIM; 217700; phenotype. DR MIM; 610206; gene. DR MIM; 613268; phenotype. DR neXtProt; NX_Q8NBS3; -. DR OpenTargets; ENSG00000088836; -. DR Orphanet; 293603; Congenital hereditary endothelial dystrophy type II. DR Orphanet; 1490; Corneal dystrophy-perceptive deafness syndrome. DR Orphanet; 98974; Fuchs endothelial corneal dystrophy. DR PharmGKB; PA38139; -. DR eggNOG; KOG1172; Eukaryota. DR eggNOG; ENOG410XPHD; LUCA. DR GeneTree; ENSGT00940000154894; -. DR HOGENOM; CLU_002289_6_0_1; -. DR InParanoid; Q8NBS3; -. DR KO; K13862; -. DR OMA; YDHNVSS; -. DR OrthoDB; 265068at2759; -. DR PhylomeDB; Q8NBS3; -. DR TreeFam; TF313630; -. DR ChiTaRS; SLC4A11; human. DR GeneWiki; SLC4A11; -. DR GenomeRNAi; 83959; -. DR Pharos; Q8NBS3; Tbio. DR PRO; PR:Q8NBS3; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q8NBS3; protein. DR Bgee; ENSG00000088836; Expressed in nasal cavity epithelium and 138 other tissues. DR ExpressionAtlas; Q8NBS3; baseline and differential. DR Genevisible; Q8NBS3; HS. DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; ISS:ARUK-UCL. DR GO; GO:0012506; C:vesicle membrane; ISS:ARUK-UCL. DR GO; GO:0046715; F:active borate transmembrane transporter activity; IDA:HGNC-UCL. DR GO; GO:0015301; F:anion:anion antiporter activity; IEA:UniProtKB-KW. DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IDA:HGNC-UCL. DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro. DR GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB. DR GO; GO:0015252; F:proton channel activity; IDA:HGNC-UCL. DR GO; GO:0005272; F:sodium channel activity; IDA:HGNC-UCL. DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW. DR GO; GO:0015701; P:bicarbonate transport; IDA:HGNC-UCL. DR GO; GO:0046713; P:borate transport; IDA:HGNC-UCL. DR GO; GO:0030003; P:cellular cation homeostasis; IDA:HGNC-UCL. DR GO; GO:0042044; P:fluid transport; ISS:UniProtKB. DR GO; GO:1902600; P:proton transmembrane transport; IDA:HGNC-UCL. DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central. DR GO; GO:0006814; P:sodium ion transport; IDA:HGNC-UCL. DR Gene3D; 3.40.930.10; -; 1. DR InterPro; IPR011531; HCO3_transpt_C. DR InterPro; IPR003020; HCO3_transpt_euk. DR InterPro; IPR016152; PTrfase/Anion_transptr. DR PANTHER; PTHR11453; PTHR11453; 1. DR Pfam; PF00955; HCO3_cotransp; 1. DR PRINTS; PR01231; HCO3TRNSPORT. DR SUPFAM; SSF55804; SSF55804; 1. PE 1: Evidence at protein level; KW Alternative splicing; Anion exchange; Cell membrane; Corneal dystrophy; KW Deafness; Disease mutation; Glycoprotein; Ion transport; Membrane; KW Polymorphism; Reference proteome; Symport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..891 FT /note="Sodium bicarbonate transporter-like protein 11" FT /id="PRO_0000079236" FT TOPO_DOM 1..375 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 376..396 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 416..436 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 466..486 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 493..513 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 514..571 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 572..592 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 593..653 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 654..674 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 700..720 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 759..779 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 782..802 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 831..851 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 853..873 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 376..891 FT /note="Membrane (bicarbonate transporter)" FT CARBOHYD 545 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 553 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..482 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_035891" FT VAR_SEQ 1..30 FT /note="MSQVGGRGDRCTQEVQGLVHGAGDLSASLA -> MAAATRRVFHLQPC (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044846" FT VAR_SEQ 1..30 FT /note="MSQVGGRGDRCTQEVQGLVHGAGDLSASLA -> MGVYGPQDRSESEKRDVQ FT RDPPPWHPRREGERPARARSLPLAAAGQGFLRKTWISEH (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054049" FT VARIANT 72 FT /note="N -> T (in dbSNP:rs778688114)" FT /evidence="ECO:0000269|PubMed:18024964" FT /id="VAR_047806" FT VARIANT 91 FT /note="M -> V (in dbSNP:rs200940928)" FT /evidence="ECO:0000269|PubMed:18024964" FT /id="VAR_047807" FT VARIANT 125 FT /note="R -> H (in CHED; dbSNP:rs1276051624)" FT /evidence="ECO:0000269|PubMed:18474783" FT /id="VAR_063713" FT VARIANT 143 FT /note="E -> K (in CHED; the mutant protein is retained FT intracellularly; coexpression with wild-type protein FT partially rescues the cell surface trafficking of CHED2 FT mutant; dbSNP:rs1482631297)" FT /evidence="ECO:0000269|PubMed:17397048, FT ECO:0000269|PubMed:22072594" FT /id="VAR_067272" FT VARIANT 150 FT /note="N -> S (in dbSNP:rs34520315)" FT /id="VAR_034944" FT VARIANT 160 FT /note="A -> T (in CHED; dbSNP:rs752287261)" FT /evidence="ECO:0000269|PubMed:16825429, FT ECO:0000269|PubMed:18474783" FT /id="VAR_034945" FT VARIANT 167 FT /note="E -> D (in FECD4; interferes with post-translational FT processing; the mutant protein localizes to the cytoplasm; FT dbSNP:rs141836046)" FT /evidence="ECO:0000269|PubMed:20848555" FT /id="VAR_064422" FT VARIANT 209 FT /note="R -> W (in CHED; dbSNP:rs566507872)" FT /evidence="ECO:0000269|PubMed:17679935" FT /id="VAR_064978" FT VARIANT 213 FT /note="S -> L (in CHED; dbSNP:rs759667344)" FT /evidence="ECO:0000269|PubMed:17679935" FT /id="VAR_064979" FT VARIANT 213 FT /note="S -> P (in CDPD; dbSNP:rs121909395)" FT /evidence="ECO:0000269|PubMed:17220209" FT /id="VAR_034946" FT VARIANT 233 FT /note="R -> C (in CHED; dbSNP:rs762942751)" FT /evidence="ECO:0000269|PubMed:17679935" FT /id="VAR_064980" FT VARIANT 240 FT /note="W -> S (in FECD4; decreases cell surface expression; FT abolishes functional activity; dbSNP:rs746532062)" FT /evidence="ECO:0000269|PubMed:25007886" FT /id="VAR_075537" FT VARIANT 269 FT /note="A -> V (in CHED; affects transport to the cell FT surface; dbSNP:rs1298347142)" FT /evidence="ECO:0000269|PubMed:18474783, FT ECO:0000269|PubMed:20185830" FT /id="VAR_063714" FT VARIANT 282 FT /note="R -> P (in FECD4; interferes with post-translational FT processing; the mutant protein localizes to the cytoplasm)" FT /evidence="ECO:0000269|PubMed:20848555" FT /id="VAR_064423" FT VARIANT 327 FT /note="A -> V (in dbSNP:rs760889152)" FT /evidence="ECO:0000269|PubMed:18024964" FT /id="VAR_047808" FT VARIANT 386 FT /note="C -> R (in CHED; the mutant protein is retained FT intracellularly; coexpression with wild-type protein FT partially rescues the cell surface trafficking of CHED2 FT mutant)" FT /evidence="ECO:0000269|PubMed:17397048, FT ECO:0000269|PubMed:18474783, ECO:0000269|PubMed:21203343, FT ECO:0000269|PubMed:22072594" FT /id="VAR_063715" FT VARIANT 394 FT /note="G -> R (in CHED; dbSNP:rs780171125)" FT /evidence="ECO:0000269|PubMed:19369245, FT ECO:0000269|PubMed:20108384" FT /id="VAR_064981" FT VARIANT 399 FT /note="E -> K (in FECD4; affects protein processing and FT transport to the cell surface; the mutant protein is FT retained intracellularly; coexpression with wild-type FT protein does not rescue the cell surface trafficking of FT FECD4 mutant; dbSNP:rs267607065)" FT /evidence="ECO:0000269|PubMed:18024964, FT ECO:0000269|PubMed:22072594, ECO:0000269|PubMed:25007886" FT /id="VAR_047809" FT VARIANT 401 FT /note="T -> K (in CHED)" FT /evidence="ECO:0000269|PubMed:17679935" FT /id="VAR_064982" FT VARIANT 408 FT /note="Q -> H" FT /evidence="ECO:0000269|PubMed:11302728" FT /id="VAR_015521" FT VARIANT 409 FT /note="K -> N" FT /evidence="ECO:0000269|PubMed:11302728" FT /id="VAR_015522" FT VARIANT 418 FT /note="G -> D (in CHED)" FT /evidence="ECO:0000269|PubMed:17679935, FT ECO:0000269|PubMed:19369245" FT /id="VAR_064983" FT VARIANT 434 FT /note="T -> I (in FECD4; decreases cell surface expression; FT highly reduces functional activity)" FT /evidence="ECO:0000269|PubMed:25007886" FT /id="VAR_075538" FT VARIANT 464 FT /note="G -> D (in CHED; affects protein processing and FT transport to the cell surface; dbSNP:rs121909389)" FT /evidence="ECO:0000269|PubMed:16767101" FT /id="VAR_030662" FT VARIANT 473 FT /note="L -> R (in CHED)" FT /evidence="ECO:0000269|PubMed:17679935" FT /id="VAR_064984" FT VARIANT 483 FT /note="M -> T" FT /evidence="ECO:0000269|PubMed:11302728" FT /id="VAR_015523" FT VARIANT 488 FT /note="R -> K (in CDPD; dbSNP:rs121909393)" FT /evidence="ECO:0000269|PubMed:17220209" FT /id="VAR_034947" FT VARIANT 489 FT /note="S -> L (in CHED; affects protein processing and FT transport to the cell surface; dbSNP:rs121909388)" FT /evidence="ECO:0000269|PubMed:16767101, FT ECO:0000269|PubMed:17679935" FT /id="VAR_030663" FT VARIANT 507 FT /note="V -> I (in FECD4; slightly decreases cell surface FT expression; reduces; dbSNP:rs532728316)" FT /evidence="ECO:0000269|PubMed:25007886" FT /id="VAR_075539" FT VARIANT 526 FT /note="Y -> C (in FECD4; does not interferes with post- FT translational processing; the mutant protein partially FT localizes to the cytoplasm; dbSNP:rs150571742)" FT /evidence="ECO:0000269|PubMed:20848555" FT /id="VAR_064424" FT VARIANT 561 FT /note="T -> M (in dbSNP:rs755379986)" FT /evidence="ECO:0000269|PubMed:18024964" FT /id="VAR_047810" FT VARIANT 565 FT /note="S -> L (in dbSNP:rs754745672)" FT /evidence="ECO:0000269|PubMed:18024964" FT /id="VAR_047811" FT VARIANT 575 FT /note="V -> M (in FECD4; does not interferes with post- FT translational processing; the mutant protein partially FT localizes to the cytoplasm; dbSNP:rs144734280)" FT /evidence="ECO:0000269|PubMed:20848555" FT /id="VAR_064425" FT VARIANT 583 FT /note="G -> D (in FECD4; interferes with post-translational FT processing; the mutant protein localizes to the cytoplasm; FT dbSNP:rs139078082)" FT /evidence="ECO:0000269|PubMed:20848555" FT /id="VAR_064426" FT VARIANT 584 FT /note="T -> K (in CHED)" FT /evidence="ECO:0000269|PubMed:17679935" FT /id="VAR_064985" FT VARIANT 675 FT /note="E -> A (in CHED; dbSNP:rs749826950)" FT /evidence="ECO:0000269|PubMed:26286922" FT /id="VAR_074015" FT VARIANT 708 FT /note="T -> A (in dbSNP:rs1180556979)" FT /evidence="ECO:0000269|PubMed:11302728" FT /id="VAR_015524" FT VARIANT 709 FT /note="G -> E (in FECD4; affects protein processing and FT transport to the cell surface; the mutant protein is FT retained intracellularly; coexpression with wild-type FT protein does not rescue the cell surface trafficking of FT FECD4 mutant; dbSNP:rs267607064)" FT /evidence="ECO:0000269|PubMed:18024964, FT ECO:0000269|PubMed:22072594" FT /id="VAR_047812" FT VARIANT 742 FT /note="G -> R (in FECD4; interferes with post-translational FT processing; the mutant protein partially localizes to the FT cytoplasm; dbSNP:rs143965185)" FT /evidence="ECO:0000269|PubMed:20848555" FT /id="VAR_064427" FT VARIANT 754 FT /note="T -> M (in FECD4; affects protein processing and FT transport to the cell surface; the mutant protein is FT retained intracellularly; coexpression with wild-type FT protein does not rescue the cell surface trafficking of FT FECD4 mutant; dbSNP:rs267607066)" FT /evidence="ECO:0000269|PubMed:18024964, FT ECO:0000269|PubMed:22072594" FT /id="VAR_047813" FT VARIANT 755 FT /note="R -> Q (in CHED; affects protein processing and FT transport to the cell surface; the mutant protein is FT retained intracellularly; coexpression with wild-type FT protein partially rescues the cell surface trafficking of FT CHED mutant; dbSNP:rs121909387)" FT /evidence="ECO:0000269|PubMed:16767101, FT ECO:0000269|PubMed:16825429, ECO:0000269|PubMed:17397048, FT ECO:0000269|PubMed:17679935" FT /id="VAR_030664" FT VARIANT 755 FT /note="R -> W (in CHED; dbSNP:rs757553189)" FT /evidence="ECO:0000269|PubMed:17397048, FT ECO:0000269|PubMed:17679935, ECO:0000269|PubMed:18474783, FT ECO:0000269|PubMed:22072594" FT /id="VAR_063716" FT VARIANT 773 FT /note="P -> L (in CHED; dbSNP:rs1465111896)" FT /evidence="ECO:0000269|PubMed:17679935, FT ECO:0000269|PubMed:18474783" FT /id="VAR_063717" FT VARIANT 804 FT /note="R -> H (in CHED; dbSNP:rs766567944)" FT /evidence="ECO:0000269|PubMed:16825429" FT /id="VAR_034948" FT VARIANT 824 FT /note="V -> M (in CHED; deafness not assessed; FT dbSNP:rs757244518)" FT /evidence="ECO:0000269|PubMed:17220209, FT ECO:0000269|PubMed:17679935, ECO:0000269|PubMed:21203343" FT /id="VAR_034949" FT VARIANT 833 FT /note="T -> M (in CHED; dbSNP:rs1422526172)" FT /evidence="ECO:0000269|PubMed:16825429" FT /id="VAR_034950" FT VARIANT 834 FT /note="G -> S (in FECD4; does not interferes with post- FT translational processing; the mutant protein partially FT localizes to the cytoplasm; dbSNP:rs144586846)" FT /evidence="ECO:0000269|PubMed:20848555" FT /id="VAR_064428" FT VARIANT 843 FT /note="L -> P (in CDPD; dbSNP:rs121909394)" FT /evidence="ECO:0000269|PubMed:17220209" FT /id="VAR_034951" FT VARIANT 848 FT /note="M -> I (in dbSNP:rs34224785)" FT /id="VAR_034952" FT VARIANT 856 FT /note="M -> V (in CDPD; dbSNP:rs121909396)" FT /evidence="ECO:0000269|PubMed:17220209" FT /id="VAR_034953" FT VARIANT 869 FT /note="R -> C (in CHED; affects protein processing and FT transport to the cell surface; dbSNP:rs121909391)" FT /evidence="ECO:0000269|PubMed:16767101, FT ECO:0000269|PubMed:17397048, ECO:0000269|PubMed:17679935" FT /id="VAR_030665" FT VARIANT 869 FT /note="R -> H (in CHED; dbSNP:rs121909392)" FT /evidence="ECO:0000269|PubMed:16825429" FT /id="VAR_034954" FT VARIANT 873 FT /note="L -> P (in CHED)" FT /evidence="ECO:0000269|PubMed:18474783" FT /id="VAR_063718" FT CONFLICT 324 FT /note="S -> P (in Ref. 2; BAC11536)" FT /evidence="ECO:0000305" FT CONFLICT 576 FT /note="L -> P (in Ref. 2; BAG59341)" FT /evidence="ECO:0000305" FT CONFLICT 684 FT /note="N -> S (in Ref. 2; BAG59140)" FT /evidence="ECO:0000305" FT CONFLICT 784 FT /note="L -> R (in Ref. 5; AAI10541)" FT /evidence="ECO:0000305" FT CONFLICT 834 FT /note="G -> D (in Ref. 2; BAG59341)" FT /evidence="ECO:0000305" SQ SEQUENCE 891 AA; 99581 MW; 06AC2FED156BF535 CRC64; MSQVGGRGDR CTQEVQGLVH GAGDLSASLA ENSPTMSQNG YFEDSSYYKC DTDDTFEARE EILGDEAFDT ANSSIVSGES IRFFVNVNLE MQATNTENEA TSGGCVLLHT SRKYLKLKNF KEEIRAHRDL DGFLAQASIV LNETATSLDN VLRTMLRRFA RDPDNNEPNC NLDLLMAMLF TDAGAPMRGK VHLLSDTIQG VTATVTGVRY QQSWLCIICT MKALQKRHVC ISRLVRPQNW GENSCEVRFV ILVLAPPKMK STKTAMEVAR TFATMFSDIA FRQKLLETRT EEEFKEALVH QRQLLTMVSH GPVAPRTKER STVSLPAHRH PEPPKCKDFV PFGKGIREDI ARRFPLYPLD FTDGIIGKNK AVGKYITTTL FLYFACLLPT IAFGSLNDEN TDGAIDVQKT IAGQSIGGLL YALFSGQPLV ILLTTAPLAL YIQVIRVICD DYDLDFNSFY AWTGLWNSFF LALYAFFNLS LVMSLFKRST EEIIALFISI TFVLDAVKGT VKIFWKYYYG HYLDDYHTKR TSSLVSLSGL GASLNASLHT ALNASFLASP TELPSATHSG QATAVLSLLI MLGTLWLGYT LYQFKKSPYL HPCVREILSD CALPIAVLAF SLISSHGFRE IEMSKFRYNP SESPFAMAQI QSLSLRAVSG AMGLGFLLSM LFFIEQNLVA ALVNAPENRL VKGTAYHWDL LLLAIINTGL SLFGLPWIHA AYPHSPLHVR ALALVEERVE NGHIYDTIVN VKETRLTSLG ASVLVGLSLL LLPVPLQWIP KPVLYGLFLY IALTSLDGNQ LVQRVALLLK EQTAYPPTHY IRRVPQRKIH YFTGLQVLQL LLLCAFGMSS LPYMKMIFPL IMIAMIPIRY ILLPRIIEAK YLDVMDAEHR P //