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Q8NBS3 (S4A11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium bicarbonate transporter-like protein 11
Alternative name(s):
Bicarbonate transporter-related protein 1
Sodium borate cotransporter 1
Short name=NaBC1
Solute carrier family 4 member 11
Gene names
Name:SLC4A11
Synonyms:BTR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length891 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transporter which plays an important role in sodium-mediated fluid transport in different organs. Prevents severe morphological changes of the cornea caused by increased sodium chloride concentrations in the stroma. In the inner ear, is involved in transport of potassium through the fibrocyte layer to the stria vascularis and is essential for the generation of the endocochlear potential but not for regulation of potassium concentrations in the endolymph. In the kidney, is essential for urinary concentration, mediates a sodium flux into the thin descending limb of Henle loop to allow countercurrent multiplication by osmotic equilibration By similarity. Involved in borate homeostasis. In the absence of borate, it functions as a Na+ and OH-(H+) channel. In the presence of borate functions as an electrogenic Na+ coupled borate cotransporter. Ref.6

Subunit structure

Homodimer. Ref.8

Subcellular location

Cell membrane. Membrane; Multi-pass membrane protein Ref.7.

Tissue specificity

Widely expressed. Highly expressed in kidney, testis, salivary gland, thyroid, trachea and corneal endothelium. Not detected in retina and lymphocytes. Ref.1 Ref.9

Post-translational modification

Glycosylated. Ref.7

Involvement in disease

Corneal dystrophy and perceptive deafness (CDPD) [MIM:217400]: An ocular disease characterized by the association of corneal clouding with progressive perceptive hearing loss.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Corneal dystrophy, endothelial 2, autosomal recessive (CHED2) [MIM:217700]: A congenital corneal dystrophy characterized by thickening and opacification of the cornea, altered morphology of the endothelium, and secretion of an abnormal collagenous layer at the Descemet membrane.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19

Corneal dystrophy, Fuchs endothelial, 4 (FECD4) [MIM:613268]: A corneal disease caused by loss of endothelium of the central cornea. It is characterized by focal wart-like guttata that arise from Descemet membrane and develop in the central cornea, epithelial blisters, reduced vision and pain. Descemet membrane is thickened by abnormal collagenous deposition.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.17

Sequence similarities

Belongs to the anion exchanger (TC 2.A.31) family. [View classification]

Sequence caution

The sequence BAC11536.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAB90170.4 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAD55942.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processAnion exchange
Ion transport
Symport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCorneal dystrophy
Disease mutation
   DomainTransmembrane
Transmembrane helix
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbicarbonate transport

Inferred from direct assay Ref.6. Source: HGNC

borate transmembrane transport

Inferred from direct assay Ref.6. Source: GOC

borate transport

Inferred from direct assay Ref.6. Source: HGNC

cellular cation homeostasis

Inferred from direct assay Ref.6. Source: HGNC

fluid transport

Inferred from sequence or structural similarity. Source: UniProtKB

proton transport

Inferred from direct assay Ref.6. Source: HGNC

sodium ion transmembrane transport

Inferred from direct assay Ref.6. Source: GOC

sodium ion transport

Inferred from direct assay Ref.6. Source: HGNC

   Cellular_componentbasolateral plasma membrane

Traceable author statement Ref.6. Source: HGNC

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionbicarbonate transmembrane transporter activity

Inferred from direct assay Ref.6. Source: HGNC

borate transmembrane transporter activity

Inferred from direct assay Ref.6. Source: HGNC

hydrogen ion channel activity

Inferred from direct assay Ref.6. Source: HGNC

inorganic anion exchanger activity

Inferred from electronic annotation. Source: InterPro

protein dimerization activity

Inferred from direct assay Ref.8. Source: UniProtKB

sodium channel activity

Inferred from direct assay Ref.6. Source: HGNC

symporter activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NBS3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8NBS3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-482: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8NBS3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MSQVGGRGDRCTQEVQGLVHGAGDLSASLA → MAAATRRVFHLQPC
Note: No experimental confirmation available.
Isoform 4 (identifier: Q8NBS3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MSQVGGRGDRCTQEVQGLVHGAGDLSASLA → MGVYGPQDRS...FLRKTWISEH

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 891891Sodium bicarbonate transporter-like protein 11
PRO_0000079236

Regions

Topological domain1 – 375375Cytoplasmic Potential
Transmembrane376 – 39621Helical; Potential
Transmembrane416 – 43621Helical; Potential
Transmembrane466 – 48621Helical; Potential
Transmembrane493 – 51321Helical; Potential
Topological domain514 – 57158Extracellular Potential
Transmembrane572 – 59221Helical; Potential
Topological domain593 – 65361Cytoplasmic Potential
Transmembrane654 – 67421Helical; Potential
Transmembrane700 – 72021Helical; Potential
Transmembrane759 – 77921Helical; Potential
Transmembrane782 – 80221Helical; Potential
Transmembrane831 – 85121Helical; Potential
Transmembrane853 – 87321Helical; Potential
Region376 – 891516Membrane (bicarbonate transporter)

Amino acid modifications

Glycosylation5451N-linked (GlcNAc...) Potential
Glycosylation5531N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 482482Missing in isoform 2.
VSP_035891
Alternative sequence1 – 3030MSQVG…SASLA → MAAATRRVFHLQPC in isoform 3.
VSP_044846
Alternative sequence1 – 3030MSQVG…SASLA → MGVYGPQDRSESEKRDVQRD PPPWHPRREGERPARARSLP LAAAGQGFLRKTWISEH in isoform 4.
VSP_054049
Natural variant721N → T. Ref.7
VAR_047806
Natural variant911M → V. Ref.7
Corresponds to variant rs200940928 [ dbSNP | Ensembl ].
VAR_047807
Natural variant1251R → H in CHED2. Ref.14
VAR_063713
Natural variant1431E → K in CHED2; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant. Ref.8 Ref.10
VAR_067272
Natural variant1501N → S.
Corresponds to variant rs34520315 [ dbSNP | Ensembl ].
VAR_034944
Natural variant1601A → T in CHED2. Ref.11 Ref.14
VAR_034945
Natural variant1671E → D in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. Ref.17
VAR_064422
Natural variant2091R → W in CHED2. Ref.13
VAR_064978
Natural variant2131S → L in CHED2. Ref.13
VAR_064979
Natural variant2131S → P in CDPD. Ref.12
VAR_034946
Natural variant2331R → C in CHED2. Ref.13
VAR_064980
Natural variant2691A → V in CHED2; affects transport to the cell surface. Ref.14 Ref.18
VAR_063714
Natural variant2821R → P in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. Ref.17
VAR_064423
Natural variant3271A → V. Ref.7
VAR_047808
Natural variant3861C → R in CHED2; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant. Ref.8 Ref.10 Ref.14 Ref.19
VAR_063715
Natural variant3941G → R in CHED2. Ref.15 Ref.16
VAR_064981
Natural variant3991E → K in FECD4; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein does not rescue the cell surface trafficking of FECD4 mutant. Ref.7 Ref.8
VAR_047809
Natural variant4011T → K in CHED2. Ref.13
VAR_064982
Natural variant4081Q → H. Ref.1
VAR_015521
Natural variant4091K → N. Ref.1
VAR_015522
Natural variant4181G → D in CHED2. Ref.13 Ref.15
VAR_064983
Natural variant4641G → D in CHED2; affects protein processing and transport to the cell surface. Ref.9
VAR_030662
Natural variant4731L → R in CHED2. Ref.13
VAR_064984
Natural variant4831M → T. Ref.1
VAR_015523
Natural variant4881R → K in CDPD. Ref.12
VAR_034947
Natural variant4891S → L in CHED2; affects protein processing and transport to the cell surface. Ref.9 Ref.13
VAR_030663
Natural variant5261Y → C in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. Ref.17
VAR_064424
Natural variant5611T → M. Ref.7
VAR_047810
Natural variant5651S → L. Ref.7
VAR_047811
Natural variant5751V → M in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. Ref.17
VAR_064425
Natural variant5831G → D in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. Ref.17
VAR_064426
Natural variant5841T → K in CHED2. Ref.13
VAR_064985
Natural variant7081T → A. Ref.1
VAR_015524
Natural variant7091G → E in FECD4; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein does not rescue the cell surface trafficking of FECD4 mutant. Ref.7 Ref.8
VAR_047812
Natural variant7421G → R in FECD4; interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. Ref.17
Corresponds to variant rs143965185 [ dbSNP | Ensembl ].
VAR_064427
Natural variant7541T → M in FECD4; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein does not rescue the cell surface trafficking of FECD4 mutant. Ref.7 Ref.8
VAR_047813
Natural variant7551R → Q in CHED2; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant. Ref.9 Ref.10 Ref.11 Ref.13
VAR_030664
Natural variant7551R → W in CHED2. Ref.8 Ref.10 Ref.13 Ref.14
VAR_063716
Natural variant7731P → L in CHED2. Ref.13 Ref.14
VAR_063717
Natural variant8041R → H in CHED2. Ref.11
VAR_034948
Natural variant8241V → M in CHED2; deafness not assessed. Ref.12 Ref.13 Ref.19
VAR_034949
Natural variant8331T → M in CHED2. Ref.11
VAR_034950
Natural variant8341G → S in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. Ref.17
VAR_064428
Natural variant8431L → P in CDPD. Ref.12
VAR_034951
Natural variant8481M → I.
Corresponds to variant rs34224785 [ dbSNP | Ensembl ].
VAR_034952
Natural variant8561M → V in CDPD. Ref.12
VAR_034953
Natural variant8691R → C in CHED2; affects protein processing and transport to the cell surface. Ref.9 Ref.10 Ref.13
VAR_030665
Natural variant8691R → H in CHED2. Ref.11
VAR_034954
Natural variant8731L → P in CHED2. Ref.14
VAR_063718

Experimental info

Sequence conflict3241S → P in BAC11536. Ref.2
Sequence conflict5761L → P in BAG59341. Ref.2
Sequence conflict6841N → S in BAG59140. Ref.2
Sequence conflict7841L → R in AAI10541. Ref.5
Sequence conflict8341G → D in BAG59341. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 4, 2003. Version 2.
Checksum: 06AC2FED156BF535

FASTA89199,581
        10         20         30         40         50         60 
MSQVGGRGDR CTQEVQGLVH GAGDLSASLA ENSPTMSQNG YFEDSSYYKC DTDDTFEARE 

        70         80         90        100        110        120 
EILGDEAFDT ANSSIVSGES IRFFVNVNLE MQATNTENEA TSGGCVLLHT SRKYLKLKNF 

       130        140        150        160        170        180 
KEEIRAHRDL DGFLAQASIV LNETATSLDN VLRTMLRRFA RDPDNNEPNC NLDLLMAMLF 

       190        200        210        220        230        240 
TDAGAPMRGK VHLLSDTIQG VTATVTGVRY QQSWLCIICT MKALQKRHVC ISRLVRPQNW 

       250        260        270        280        290        300 
GENSCEVRFV ILVLAPPKMK STKTAMEVAR TFATMFSDIA FRQKLLETRT EEEFKEALVH 

       310        320        330        340        350        360 
QRQLLTMVSH GPVAPRTKER STVSLPAHRH PEPPKCKDFV PFGKGIREDI ARRFPLYPLD 

       370        380        390        400        410        420 
FTDGIIGKNK AVGKYITTTL FLYFACLLPT IAFGSLNDEN TDGAIDVQKT IAGQSIGGLL 

       430        440        450        460        470        480 
YALFSGQPLV ILLTTAPLAL YIQVIRVICD DYDLDFNSFY AWTGLWNSFF LALYAFFNLS 

       490        500        510        520        530        540 
LVMSLFKRST EEIIALFISI TFVLDAVKGT VKIFWKYYYG HYLDDYHTKR TSSLVSLSGL 

       550        560        570        580        590        600 
GASLNASLHT ALNASFLASP TELPSATHSG QATAVLSLLI MLGTLWLGYT LYQFKKSPYL 

       610        620        630        640        650        660 
HPCVREILSD CALPIAVLAF SLISSHGFRE IEMSKFRYNP SESPFAMAQI QSLSLRAVSG 

       670        680        690        700        710        720 
AMGLGFLLSM LFFIEQNLVA ALVNAPENRL VKGTAYHWDL LLLAIINTGL SLFGLPWIHA 

       730        740        750        760        770        780 
AYPHSPLHVR ALALVEERVE NGHIYDTIVN VKETRLTSLG ASVLVGLSLL LLPVPLQWIP 

       790        800        810        820        830        840 
KPVLYGLFLY IALTSLDGNQ LVQRVALLLK EQTAYPPTHY IRRVPQRKIH YFTGLQVLQL 

       850        860        870        880        890 
LLLCAFGMSS LPYMKMIFPL IMIAMIPIRY ILLPRIIEAK YLDVMDAEHR P 

« Hide

Isoform 2 [UniParc].

Checksum: A3AED736B90209A7
Show »

FASTA40945,762
Isoform 3 [UniParc].

Checksum: 6BEDDC9939BADF10
Show »

FASTA87598,181
Isoform 4 [UniParc].

Checksum: BA314E50D8F6CD48
Show »

FASTA918103,145

References

« Hide 'large scale' references
[1]"Human BTR1, a new bicarbonate transporter superfamily member and human AE4 from kidney."
Parker M.D., Ourmozdi E.P., Tanner M.J.A.
Biochem. Biophys. Res. Commun. 282:1103-1109(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS HIS-408; ASN-409; THR-483 AND ALA-708.
Tissue: Kidney.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 227-891 (ISOFORM 1).
Tissue: Retinoblastoma, Thalamus and Tongue.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
[6]"NaBC1 is a ubiquitous electrogenic Na+-coupled borate transporter essential for cellular boron homeostasis and cell growth and proliferation."
Park M., Li Q., Shcheynikov N., Zeng W., Muallem S.
Mol. Cell 16:331-341(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"SLC4A11 mutations in Fuchs endothelial corneal dystrophy."
Vithana E.N., Morgan P.E., Ramprasad V., Tan D.T.H., Yong V.H.K., Venkataraman D., Venkatraman A., Yam G.H.F., Nagasamy S., Law R.W.K., Rajagopal R., Pang C.P., Kumaramanickevel G., Casey J.R., Aung T.
Hum. Mol. Genet. 17:656-666(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, VARIANTS FECD4 LYS-399; GLU-709 AND MET-754, VARIANTS THR-72; VAL-91; VAL-327; MET-561 AND LEU-565, CHARACTERIZATION OF VARIANTS FECD4 LYS-399; GLU-709 AND MET-754.
[8]"Oligomerization of SLC4A11 protein and the severity of FECD and CHED2 corneal dystrophies caused by SLC4A11 mutations."
Vilas G.L., Loganathan S.K., Quon A., Sundaresan P., Vithana E.N., Casey J.
Hum. Mutat. 33:419-428(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION, CHARACTERIZATION OF VARIANTS CHED2 LYS-143; ARG-386 AND TRP-755, CHARACTERIZATION OF VARIANTS FECD4 LYS-399; GLU-709 AND MET-754.
[9]"Mutations in sodium-borate cotransporter SLC4A11 cause recessive congenital hereditary endothelial dystrophy (CHED2)."
Vithana E.N., Morgan P., Sundaresan P., Ebenezer N.D., Tan D.T.H., Mohamed M.D., Anand S., Khine K.O., Venkataraman D., Yong V.H.K., Salto-Tellez M., Venkatraman A., Guo K., Hemadevi B., Srinivasan M., Prajna V., Khine M., Casey J.R., Inglehearn C.F., Aung T.
Nat. Genet. 38:755-757(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CHED2 ASP-464; LEU-489; GLN-755 AND CYS-869, CHARACTERIZATION OF VARIANTS CHED2 ASP-464; LEU-489; GLN-755 AND CYS-869, TISSUE SPECIFICITY.
[10]"Novel SLC4A11 mutations in patients with recessive congenital hereditary endothelial dystrophy (CHED2). Mutation in brief #958. Online."
Ramprasad V.L., Ebenezer N.D., Aung T., Rajagopal R., Yong V.H., Tuft S.J., Viswanathan D., El-Ashry M.F., Liskova P., Tan D.T., Bhattacharya S.S., Kumaramanickavel G., Vithana E.N.
Hum. Mutat. 28:522-523(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CHED2 LYS-143; ARG-386; TRP-755; GLN-755 AND CYS-869.
[11]"Autosomal recessive corneal endothelial dystrophy (CHED2) is associated with mutations in SLC4A11."
Jiao X., Sultana A., Garg P., Ramamurthy B., Vemuganti G.K., Gangopadhyay N., Hejtmancik J.F., Kannabiran C.
J. Med. Genet. 44:64-68(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CHED2 GLN-755; HIS-804; MET-833 AND HIS-869, VARIANT THR-160.
[12]"Borate transporter SLC4A11 mutations cause both Harboyan syndrome and non-syndromic corneal endothelial dystrophy."
Desir J., Moya G., Reish O., Van Regemorter N., Deconinck H., David K.L., Meire F.M., Abramowicz M.J.
J. Med. Genet. 44:322-326(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CDPD PRO-213; LYS-488; PRO-843 AND VAL-856, VARIANT CHED2 MET-824.
[13]"Mutational spectrum of the SLC4A11 gene in autosomal recessive congenital hereditary endothelial dystrophy."
Sultana A., Garg P., Ramamurthy B., Vemuganti G.K., Kannabiran C.
Mol. Vis. 13:1327-1332(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CHED2 TRP-209; LEU-213; CYS-233; LYS-401; ASP-418; ARG-473; LEU-489; LYS-584; TRP-755; GLN-755; LEU-773; MET-824 AND CYS-869.
[14]"Identification of mutations in the SLC4A11 gene in patients with recessive congenital hereditary endothelial dystrophy."
Hemadevi B., Veitia R.A., Srinivasan M., Arunkumar J., Prajna N.V., Lesaffre C., Sundaresan P.
Arch. Ophthalmol. 126:700-708(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CHED2 HIS-125; THR-160; VAL-269; ARG-386; TRP-755; LEU-773 AND PRO-873.
[15]"Mutational spectrum of SLC4A11 in autosomal recessive CHED in Saudi Arabia."
Aldahmesh M.A., Khan A.O., Meyer B.F., Alkuraya F.S.
Invest. Ophthalmol. Vis. Sci. 50:4142-4145(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CHED2 ARG-394 AND ASP-418.
[16]"Novel human pathological mutations. Gene symbol: SLC4A11. Disease: Corneal endothelial dystrophy 2."
Chai S.M., Vithana E.N., Venkataraman D., Saleh H., Chekkalichintavida N.P., al-Sayyed F., Aung T.
Hum. Genet. 127:110-110(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CHED2 ARG-394.
[17]"Missense mutations in the sodium borate cotransporter SLC4A11 cause late-onset Fuchs corneal dystrophya."
Riazuddin S.A., Vithana E.N., Seet L.F., Liu Y., Al-Saif A., Koh L.W., Heng Y.M., Aung T., Meadows D.N., Eghrari A.O., Gottsch J.D., Katsanis N.
Hum. Mutat. 31:1261-1268(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FECD4 ASP-167; PRO-282; CYS-526; MET-575; ASP-583; ARG-742 AND SER-834, CHARACTERIZATION OF VARIANTS FECD4 ASP-167; PRO-282; CYS-526; MET-575; ASP-583; ARG-742 AND SER-834.
[18]"SLC4A11 prevents osmotic imbalance leading to corneal endothelial dystrophy, deafness, and polyuria."
Groger N., Frohlich H., Maier H., Olbrich A., Kostin S., Braun T., Boettger T.
J. Biol. Chem. 285:14467-14474(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT CHED2 VAL-269.
[19]"Congenital hereditary endothelial dystrophy - mutation analysis of SLC4A11 and genotype-phenotype correlation in a North Indian patient cohort."
Paliwal P., Sharma A., Tandon R., Sharma N., Titiyal J.S., Sen S., Nag T.C., Vajpayee R.B.
Mol. Vis. 16:2955-2963(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CHED2 ARG-386 AND MET-824.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF336127 mRNA. Translation: AAK16734.1.
AK075303 mRNA. Translation: BAC11536.1. Different initiation.
AK296508 mRNA. Translation: BAG59140.1.
AK296760 mRNA. Translation: BAG59341.1.
AL109976 Genomic DNA. Translation: CAD55941.1.
AL109976 Genomic DNA. Translation: CAD55942.1. Sequence problems.
AL109976 Genomic DNA. Translation: CAB90170.4. Sequence problems.
CH471133 Genomic DNA. Translation: EAX10536.1.
BC110540 mRNA. Translation: AAI10541.1.
BC110541 mRNA. Translation: AAI10542.1.
RefSeqNP_001167560.1. NM_001174089.1.
NP_001167561.1. NM_001174090.1.
NP_114423.1. NM_032034.3.
UniGeneHs.105607.

3D structure databases

ProteinModelPortalQ8NBS3.
SMRQ8NBS3. Positions 353-400, 799-831.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123832. 1 interaction.
STRING9606.ENSP00000369396.

Protein family/group databases

TCDB2.A.31.4.1. the anion exchanger (ae) family.

PTM databases

PhosphoSiteQ8NBS3.

Polymorphism databases

DMDM29611858.

Proteomic databases

PaxDbQ8NBS3.
PRIDEQ8NBS3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380056; ENSP00000369396; ENSG00000088836. [Q8NBS3-1]
ENST00000539553; ENSP00000441370; ENSG00000088836. [Q8NBS3-3]
GeneID83959.
KEGGhsa:83959.
UCSCuc002wig.3. human. [Q8NBS3-1]
uc010zqf.2. human.

Organism-specific databases

CTD83959.
GeneCardsGC20M003203.
HGNCHGNC:16438. SLC4A11.
HPAHPA018120.
MIM217400. phenotype.
217700. phenotype.
610206. gene.
613268. phenotype.
neXtProtNX_Q8NBS3.
Orphanet293603. Congenital hereditary endothelial dystrophy type II.
1490. Corneal dystrophy - perceptive deafness.
98974. Fuchs endothelial corneal dystrophy.
PharmGKBPA38139.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG268067.
HOGENOMHOG000016966.
HOVERGENHBG079162.
KOK13862.
OrthoDBEOG7M6D7V.
PhylomeDBQ8NBS3.
TreeFamTF313630.

Gene expression databases

BgeeQ8NBS3.
CleanExHS_SLC4A11.
GenevestigatorQ8NBS3.

Family and domain databases

Gene3D3.40.930.10. 1 hit.
InterProIPR011531. HCO3_transpt_C.
IPR003020. HCO3_transpt_euk.
IPR016152. PTrfase/Anion_transptr.
IPR002178. PTS_EIIA_type-2_dom.
[Graphical view]
PANTHERPTHR11453. PTHR11453. 1 hit.
PfamPF00955. HCO3_cotransp. 1 hit.
PF00359. PTS_EIIA_2. 1 hit.
[Graphical view]
PRINTSPR01231. HCO3TRNSPORT.
SUPFAMSSF55804. SSF55804. 1 hit.
ProtoNetSearch...

Other

GeneWikiSLC4A11.
GenomeRNAi83959.
NextBio73102.
PROQ8NBS3.
SOURCESearch...

Entry information

Entry nameS4A11_HUMAN
AccessionPrimary (citable) accession number: Q8NBS3
Secondary accession number(s): B4DKC8 expand/collapse secondary AC list , B4DKX9, G3V1M3, Q2TB62, Q2TB63, Q9BXF4, Q9NTW9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2003
Last sequence update: April 4, 2003
Last modified: April 16, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM