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 14-MAY-2014, entry version 111. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND RP VARIANTS 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 RT human AE4 from kidney."; RL Biochem. Biophys. Res. Commun. 282:1103-1109(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND RP NUCLEOTIDE 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA 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., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RP AND MET-754, VARIANTS THR-72; VAL-91; VAL-327; MET-561 AND LEU-565, RP AND 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 CHED2 LYS-143; ARG-386 RP AND TRP-755, AND CHARACTERIZATION OF VARIANTS FECD4 LYS-399; GLU-709 RP AND 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 CHED2 ASP-464; LEU-489; GLN-755 AND CYS-869, CHARACTERIZATION RP OF VARIANTS CHED2 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 CHED2 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., RA Tuft S.J., Viswanathan D., El-Ashry M.F., Liskova P., Tan D.T., RA Bhattacharya S.S., Kumaramanickavel G., Vithana E.N.; RT "Novel SLC4A11 mutations in patients with recessive congenital RT hereditary endothelial dystrophy (CHED2). Mutation in brief #958. RT Online."; RL Hum. Mutat. 28:522-523(2007). RN [11] RP VARIANTS CHED2 GLN-755; HIS-804; MET-833 AND HIS-869, AND VARIANT RP 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 RT associated 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 CHED2 RP MET-824. RX PubMed=17220209; DOI=10.1136/jmg.2006.046904; RA Desir J., Moya G., Reish O., Van Regemorter N., Deconinck H., RA David K.L., Meire F.M., Abramowicz M.J.; RT "Borate transporter SLC4A11 mutations cause both Harboyan syndrome and RT non-syndromic corneal endothelial dystrophy."; RL J. Med. Genet. 44:322-326(2007). RN [13] RP VARIANTS CHED2 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 RT congenital hereditary endothelial dystrophy."; RL Mol. Vis. 13:1327-1332(2007). RN [14] RP VARIANTS CHED2 HIS-125; THR-160; VAL-269; ARG-386; TRP-755; LEU-773 RP AND 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 RT recessive congenital hereditary endothelial dystrophy."; RL Arch. Ophthalmol. 126:700-708(2008). RN [15] RP VARIANTS CHED2 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 CHED2 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: RT Corneal 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 RP AND SER-834, AND CHARACTERIZATION OF VARIANTS FECD4 ASP-167; PRO-282; RP CYS-526; 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., RA Katsanis N.; RT "Missense mutations in the sodium borate cotransporter SLC4A11 cause RT late-onset Fuchs corneal dystrophya."; RL Hum. Mutat. 31:1261-1268(2010). RN [18] RP CHARACTERIZATION OF VARIANT CHED2 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 CHED2 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 RT SLC4A11 and genotype-phenotype correlation in a North Indian patient RT cohort."; RL Mol. Vis. 16:2955-2963(2010). CC -!- FUNCTION: Transporter which plays an important role in sodium- CC mediated fluid transport in different organs. Prevents severe CC morphological changes of the cornea caused by increased sodium CC chloride concentrations in the stroma. In the inner ear, is CC involved in transport of potassium through the fibrocyte layer to CC the stria vascularis and is essential for the generation of the CC endocochlear potential but not for regulation of potassium CC concentrations in the endolymph. In the kidney, is essential for CC urinary concentration, mediates a sodium flux into the thin CC descending limb of Henle loop to allow countercurrent CC multiplication by osmotic equilibration (By similarity). Involved CC in borate homeostasis. In the absence of borate, it functions as a CC Na(+) and OH(-)(H(+)) channel. In the presence of borate functions CC as an electrogenic Na(+) coupled borate cotransporter. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cell membrane. Membrane; Multi-pass membrane CC protein. 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 Note=No experimental confirmation available; CC Name=3; CC IsoId=Q8NBS3-3; Sequence=VSP_044846; CC Note=No experimental confirmation available; 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. CC Not detected in retina and lymphocytes. CC -!- PTM: Glycosylated. CC -!- DISEASE: Corneal dystrophy and perceptive deafness (CDPD) CC [MIM:217400]: An ocular disease characterized by the association CC of corneal clouding with progressive perceptive hearing loss. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- DISEASE: Corneal dystrophy, endothelial 2, autosomal recessive CC (CHED2) [MIM:217700]: A congenital corneal dystrophy characterized CC by thickening and opacification of the cornea, altered morphology CC of the endothelium, and secretion of an abnormal collagenous layer CC at the Descemet membrane. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- DISEASE: Corneal dystrophy, Fuchs endothelial, 4 (FECD4) CC [MIM:613268]: A corneal disease caused by loss of endothelium of CC the central cornea. It is characterized by focal wart-like guttata CC that arise from Descemet membrane and develop in the central CC cornea, epithelial blisters, reduced vision and pain. Descemet CC membrane is thickened by abnormal collagenous deposition. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family. CC -!- SEQUENCE CAUTION: CC Sequence=BAC11536.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC Sequence=CAB90170.4; Type=Erroneous gene model prediction; CC Sequence=CAD55942.1; Type=Erroneous gene model prediction; 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; CAD55941.1; -; Genomic_DNA. DR EMBL; AL109976; CAD55942.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL109976; CAB90170.4; ALT_SEQ; Genomic_DNA. DR EMBL; CH471133; EAX10536.1; -; Genomic_DNA. DR EMBL; BC110540; AAI10541.1; -; mRNA. DR EMBL; BC110541; AAI10542.1; -; mRNA. DR RefSeq; NP_001167560.1; NM_001174089.1. [Q8NBS3-3] DR RefSeq; NP_001167561.1; NM_001174090.1. DR RefSeq; NP_114423.1; NM_032034.3. [Q8NBS3-1] DR UniGene; Hs.105607; -. DR ProteinModelPortal; Q8NBS3; -. DR SMR; Q8NBS3; 353-400, 799-831. DR BioGrid; 123832; 1. DR STRING; 9606.ENSP00000369396; -. DR TCDB; 2.A.31.4.1; the anion exchanger (ae) family. DR PhosphoSite; Q8NBS3; -. DR DMDM; 29611858; -. DR MaxQB; Q8NBS3; -. DR PaxDb; Q8NBS3; -. DR PRIDE; Q8NBS3; -. DR Ensembl; ENST00000380056; ENSP00000369396; ENSG00000088836. [Q8NBS3-1] DR Ensembl; ENST00000539553; ENSP00000441370; ENSG00000088836. [Q8NBS3-3] DR GeneID; 83959; -. DR KEGG; hsa:83959; -. DR UCSC; uc002wig.3; human. [Q8NBS3-1] DR UCSC; uc010zqf.2; human. DR CTD; 83959; -. DR GeneCards; GC20M003203; -. DR HGNC; HGNC:16438; SLC4A11. DR HPA; HPA018120; -. DR MIM; 217400; phenotype. DR MIM; 217700; phenotype. DR MIM; 610206; gene. DR MIM; 613268; phenotype. DR neXtProt; NX_Q8NBS3; -. DR Orphanet; 293603; Congenital hereditary endothelial dystrophy type II. DR Orphanet; 1490; Corneal dystrophy - perceptive deafness. DR Orphanet; 98974; Fuchs endothelial corneal dystrophy. DR PharmGKB; PA38139; -. DR eggNOG; NOG268067; -. DR HOGENOM; HOG000016966; -. DR HOVERGEN; HBG079162; -. DR KO; K13862; -. DR OrthoDB; EOG7M6D7V; -. DR PhylomeDB; Q8NBS3; -. DR TreeFam; TF313630; -. DR GeneWiki; SLC4A11; -. DR GenomeRNAi; 83959; -. DR NextBio; 73102; -. DR PRO; PR:Q8NBS3; -. DR Bgee; Q8NBS3; -. DR CleanEx; HS_SLC4A11; -. DR Genevestigator; Q8NBS3; -. DR GO; GO:0016323; C:basolateral plasma membrane; TAS:HGNC. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IDA:HGNC. DR GO; GO:0046715; F:borate transmembrane transporter activity; IDA:HGNC. DR GO; GO:0015252; F:hydrogen ion channel activity; IDA:HGNC. DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro. DR GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB. DR GO; GO:0005272; F:sodium channel activity; IDA:HGNC. DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW. DR GO; GO:0015701; P:bicarbonate transport; IDA:HGNC. DR GO; GO:0035445; P:borate transmembrane transport; IDA:GOC. DR GO; GO:0046713; P:borate transport; IDA:HGNC. DR GO; GO:0030003; P:cellular cation homeostasis; IDA:HGNC. DR GO; GO:0042044; P:fluid transport; ISS:UniProtKB. DR GO; GO:0015992; P:proton transport; IDA:HGNC. DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA:GOC. DR GO; GO:0006814; P:sodium ion transport; IDA:HGNC. 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 InterPro; IPR002178; PTS_EIIA_type-2_dom. DR PANTHER; PTHR11453; PTHR11453; 1. DR Pfam; PF00955; HCO3_cotransp; 1. DR Pfam; PF00359; PTS_EIIA_2; 1. DR PRINTS; PR01231; HCO3TRNSPORT. DR SUPFAM; SSF55804; SSF55804; 1. PE 1: Evidence at protein level; KW Alternative splicing; Anion exchange; Cell membrane; KW Complete proteome; Corneal dystrophy; Disease mutation; Glycoprotein; KW Ion transport; Membrane; Polymorphism; Reference proteome; Symport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 891 Sodium bicarbonate transporter-like FT protein 11. FT /FTId=PRO_0000079236. FT TOPO_DOM 1 375 Cytoplasmic (Potential). FT TRANSMEM 376 396 Helical; (Potential). FT TRANSMEM 416 436 Helical; (Potential). FT TRANSMEM 466 486 Helical; (Potential). FT TRANSMEM 493 513 Helical; (Potential). FT TOPO_DOM 514 571 Extracellular (Potential). FT TRANSMEM 572 592 Helical; (Potential). FT TOPO_DOM 593 653 Cytoplasmic (Potential). FT TRANSMEM 654 674 Helical; (Potential). FT TRANSMEM 700 720 Helical; (Potential). FT TRANSMEM 759 779 Helical; (Potential). FT TRANSMEM 782 802 Helical; (Potential). FT TRANSMEM 831 851 Helical; (Potential). FT TRANSMEM 853 873 Helical; (Potential). FT REGION 376 891 Membrane (bicarbonate transporter). FT CARBOHYD 545 545 N-linked (GlcNAc...) (Potential). FT CARBOHYD 553 553 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 1 482 Missing (in isoform 2). FT /FTId=VSP_035891. FT VAR_SEQ 1 30 MSQVGGRGDRCTQEVQGLVHGAGDLSASLA -> MAAATRR FT VFHLQPC (in isoform 3). FT /FTId=VSP_044846. FT VAR_SEQ 1 30 MSQVGGRGDRCTQEVQGLVHGAGDLSASLA -> MGVYGPQ FT DRSESEKRDVQRDPPPWHPRREGERPARARSLPLAAAGQGF FT LRKTWISEH (in isoform 4). FT /FTId=VSP_054049. FT VARIANT 72 72 N -> T. FT /FTId=VAR_047806. FT VARIANT 91 91 M -> V (in dbSNP:rs200940928). FT /FTId=VAR_047807. FT VARIANT 125 125 R -> H (in CHED2). FT /FTId=VAR_063713. FT VARIANT 143 143 E -> K (in CHED2; the mutant protein is FT retained intracellularly; coexpression FT with wild-type protein partially rescues FT the cell surface trafficking of CHED2 FT mutant). FT /FTId=VAR_067272. FT VARIANT 150 150 N -> S (in dbSNP:rs34520315). FT /FTId=VAR_034944. FT VARIANT 160 160 A -> T (in CHED2). FT /FTId=VAR_034945. FT VARIANT 167 167 E -> D (in FECD4; interferes with post- FT translational processing; the mutant FT protein localizes to the cytoplasm). FT /FTId=VAR_064422. FT VARIANT 209 209 R -> W (in CHED2). FT /FTId=VAR_064978. FT VARIANT 213 213 S -> L (in CHED2). FT /FTId=VAR_064979. FT VARIANT 213 213 S -> P (in CDPD). FT /FTId=VAR_034946. FT VARIANT 233 233 R -> C (in CHED2). FT /FTId=VAR_064980. FT VARIANT 269 269 A -> V (in CHED2; affects transport to FT the cell surface). FT /FTId=VAR_063714. FT VARIANT 282 282 R -> P (in FECD4; interferes with post- FT translational processing; the mutant FT protein localizes to the cytoplasm). FT /FTId=VAR_064423. FT VARIANT 327 327 A -> V. FT /FTId=VAR_047808. FT VARIANT 386 386 C -> R (in CHED2; the mutant protein is FT retained intracellularly; coexpression FT with wild-type protein partially rescues FT the cell surface trafficking of CHED2 FT mutant). FT /FTId=VAR_063715. FT VARIANT 394 394 G -> R (in CHED2). FT /FTId=VAR_064981. FT VARIANT 399 399 E -> K (in FECD4; affects protein FT processing and transport to the cell FT surface; the mutant protein is retained FT intracellularly; coexpression with wild- FT type protein does not rescue the cell FT surface trafficking of FECD4 mutant). FT /FTId=VAR_047809. FT VARIANT 401 401 T -> K (in CHED2). FT /FTId=VAR_064982. FT VARIANT 408 408 Q -> H. FT /FTId=VAR_015521. FT VARIANT 409 409 K -> N. FT /FTId=VAR_015522. FT VARIANT 418 418 G -> D (in CHED2). FT /FTId=VAR_064983. FT VARIANT 464 464 G -> D (in CHED2; affects protein FT processing and transport to the cell FT surface). FT /FTId=VAR_030662. FT VARIANT 473 473 L -> R (in CHED2). FT /FTId=VAR_064984. FT VARIANT 483 483 M -> T. FT /FTId=VAR_015523. FT VARIANT 488 488 R -> K (in CDPD). FT /FTId=VAR_034947. FT VARIANT 489 489 S -> L (in CHED2; affects protein FT processing and transport to the cell FT surface). FT /FTId=VAR_030663. FT VARIANT 526 526 Y -> C (in FECD4; does not interferes FT with post-translational processing; the FT mutant protein partially localizes to the FT cytoplasm). FT /FTId=VAR_064424. FT VARIANT 561 561 T -> M. FT /FTId=VAR_047810. FT VARIANT 565 565 S -> L. FT /FTId=VAR_047811. FT VARIANT 575 575 V -> M (in FECD4; does not interferes FT with post-translational processing; the FT mutant protein partially localizes to the FT cytoplasm). FT /FTId=VAR_064425. FT VARIANT 583 583 G -> D (in FECD4; interferes with post- FT translational processing; the mutant FT protein localizes to the cytoplasm). FT /FTId=VAR_064426. FT VARIANT 584 584 T -> K (in CHED2). FT /FTId=VAR_064985. FT VARIANT 708 708 T -> A. FT /FTId=VAR_015524. FT VARIANT 709 709 G -> E (in FECD4; affects protein FT processing and transport to the cell FT surface; the mutant protein is retained FT intracellularly; coexpression with wild- FT type protein does not rescue the cell FT surface trafficking of FECD4 mutant). FT /FTId=VAR_047812. FT VARIANT 742 742 G -> R (in FECD4; interferes with post- FT translational processing; the mutant FT protein partially localizes to the FT cytoplasm; dbSNP:rs143965185). FT /FTId=VAR_064427. FT VARIANT 754 754 T -> M (in FECD4; affects protein FT processing and transport to the cell FT surface; the mutant protein is retained FT intracellularly; coexpression with wild- FT type protein does not rescue the cell FT surface trafficking of FECD4 mutant). FT /FTId=VAR_047813. FT VARIANT 755 755 R -> Q (in CHED2; affects protein FT processing and transport to the cell FT surface; the mutant protein is retained FT intracellularly; coexpression with wild- FT type protein partially rescues the cell FT surface trafficking of CHED2 mutant). FT /FTId=VAR_030664. FT VARIANT 755 755 R -> W (in CHED2). FT /FTId=VAR_063716. FT VARIANT 773 773 P -> L (in CHED2). FT /FTId=VAR_063717. FT VARIANT 804 804 R -> H (in CHED2). FT /FTId=VAR_034948. FT VARIANT 824 824 V -> M (in CHED2; deafness not assessed). FT /FTId=VAR_034949. FT VARIANT 833 833 T -> M (in CHED2). FT /FTId=VAR_034950. FT VARIANT 834 834 G -> S (in FECD4; does not interferes FT with post-translational processing; the FT mutant protein partially localizes to the FT cytoplasm). FT /FTId=VAR_064428. FT VARIANT 843 843 L -> P (in CDPD). FT /FTId=VAR_034951. FT VARIANT 848 848 M -> I (in dbSNP:rs34224785). FT /FTId=VAR_034952. FT VARIANT 856 856 M -> V (in CDPD). FT /FTId=VAR_034953. FT VARIANT 869 869 R -> C (in CHED2; affects protein FT processing and transport to the cell FT surface). FT /FTId=VAR_030665. FT VARIANT 869 869 R -> H (in CHED2). FT /FTId=VAR_034954. FT VARIANT 873 873 L -> P (in CHED2). FT /FTId=VAR_063718. FT CONFLICT 324 324 S -> P (in Ref. 2; BAC11536). FT CONFLICT 576 576 L -> P (in Ref. 2; BAG59341). FT CONFLICT 684 684 N -> S (in Ref. 2; BAG59140). FT CONFLICT 784 784 L -> R (in Ref. 5; AAI10541). FT CONFLICT 834 834 G -> D (in Ref. 2; BAG59341). 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 //