Q8NBS3 (S4A11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	891 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Anion exchange Ion transport Symport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Corneal dystrophy Disease mutation
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular cation homeostasis Inferred from direct assay Ref.6. Source: HGNC fluid transport Inferred from sequence or structural similarity. Source: UniProtKB phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: InterPro
Cellular_component	basolateral plasma membrane Traceable author statement Ref.6. Source: HGNC integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	bicarbonate 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 sugar:hydrogen symporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 891	891	Sodium bicarbonate transporter-like protein 11		PRO_0000079236
Regions
	Topological domain	1 – 375	375	Cytoplasmic Potential
	Transmembrane	376 – 396	21	Helical; Potential
	Transmembrane	416 – 436	21	Helical; Potential
	Transmembrane	466 – 486	21	Helical; Potential
	Transmembrane	493 – 513	21	Helical; Potential
	Topological domain	514 – 571	58	Extracellular Potential
	Transmembrane	572 – 592	21	Helical; Potential
	Topological domain	593 – 653	61	Cytoplasmic Potential
	Transmembrane	654 – 674	21	Helical; Potential
	Transmembrane	700 – 720	21	Helical; Potential
	Transmembrane	759 – 779	21	Helical; Potential
	Transmembrane	782 – 802	21	Helical; Potential
	Transmembrane	831 – 851	21	Helical; Potential
	Transmembrane	853 – 873	21	Helical; Potential
	Region	376 – 891	516	Membrane (bicarbonate transporter)
Amino acid modifications
	Glycosylation	545	1	N-linked (GlcNAc...) Potential
	Glycosylation	553	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 482	482	Missing in isoform 2.		VSP_035891
	Alternative sequence	1 – 30	30	MSQVG…SASLA → MAAATRRVFHLQPC in isoform 3.		VSP_044846
	Natural variant	72	1	N → T. Ref.7		VAR_047806
	Natural variant	91	1	M → V. Ref.7		VAR_047807
	Natural variant	125	1	R → H in CHED2. Ref.14		VAR_063713
	Natural variant	143	1	E → 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 variant	150	1	N → S. Corresponds to variant rs34520315 [ dbSNP | Ensembl ].		VAR_034944
	Natural variant	160	1	A → T in CHED2. Ref.11 Ref.14		VAR_034945
	Natural variant	167	1	E → D in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. Ref.17		VAR_064422
	Natural variant	209	1	R → W in CHED2. Ref.13		VAR_064978
	Natural variant	213	1	S → L in CHED2. Ref.13		VAR_064979
	Natural variant	213	1	S → P in CDPD. Ref.12		VAR_034946
	Natural variant	233	1	R → C in CHED2. Ref.13		VAR_064980
	Natural variant	269	1	A → V in CHED2; affects transport to the cell surface. Ref.14 Ref.18		VAR_063714
	Natural variant	282	1	R → P in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. Ref.17		VAR_064423
	Natural variant	327	1	A → V. Ref.7		VAR_047808
	Natural variant	386	1	C → 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 variant	394	1	G → R in CHED2. Ref.15 Ref.16		VAR_064981
	Natural variant	399	1	E → 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 variant	401	1	T → K in CHED2. Ref.13		VAR_064982
	Natural variant	408	1	Q → H. Ref.1		VAR_015521
	Natural variant	409	1	K → N. Ref.1		VAR_015522
	Natural variant	418	1	G → D in CHED2. Ref.13 Ref.15		VAR_064983
	Natural variant	464	1	G → D in CHED2; affects protein processing and transport to the cell surface. Ref.9		VAR_030662
	Natural variant	473	1	L → R in CHED2. Ref.13		VAR_064984
	Natural variant	483	1	M → T. Ref.1		VAR_015523
	Natural variant	488	1	R → K in CDPD. Ref.12		VAR_034947
	Natural variant	489	1	S → L in CHED2; affects protein processing and transport to the cell surface. Ref.9 Ref.13		VAR_030663
	Natural variant	526	1	Y → C in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. Ref.17		VAR_064424
	Natural variant	561	1	T → M. Ref.7		VAR_047810
	Natural variant	565	1	S → L. Ref.7		VAR_047811
	Natural variant	575	1	V → M in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. Ref.17		VAR_064425
	Natural variant	583	1	G → D in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. Ref.17		VAR_064426
	Natural variant	584	1	T → K in CHED2. Ref.13		VAR_064985
	Natural variant	708	1	T → A. Ref.1		VAR_015524
	Natural variant	709	1	G → 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 variant	742	1	G → R in FECD4; interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. Ref.17		VAR_064427
	Natural variant	754	1	T → 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 variant	755	1	R → 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 variant	755	1	R → W in CHED2. Ref.8 Ref.10 Ref.13 Ref.14		VAR_063716
	Natural variant	773	1	P → L in CHED2. Ref.13 Ref.14		VAR_063717
	Natural variant	804	1	R → H in CHED2. Ref.11		VAR_034948
	Natural variant	824	1	V → M in CHED2; deafness not assessed. Ref.12 Ref.13 Ref.19		VAR_034949
	Natural variant	833	1	T → M in CHED2. Ref.11		VAR_034950
	Natural variant	834	1	G → S in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. Ref.17		VAR_064428
	Natural variant	843	1	L → P in CDPD. Ref.12		VAR_034951
	Natural variant	848	1	M → I. Corresponds to variant rs34224785 [ dbSNP | Ensembl ].		VAR_034952
	Natural variant	856	1	M → V in CDPD. Ref.12		VAR_034953
	Natural variant	869	1	R → C in CHED2; affects protein processing and transport to the cell surface. Ref.9 Ref.10 Ref.13		VAR_030665
	Natural variant	869	1	R → H in CHED2. Ref.11		VAR_034954
	Natural variant	873	1	L → P in CHED2. Ref.14		VAR_063718
Experimental info
	Sequence conflict	324	1	S → P in BAC11536. Ref.2
	Sequence conflict	576	1	L → P in BAG59341. Ref.2
	Sequence conflict	784	1	L → R in AAI10541. Ref.5
	Sequence conflict	834	1	G → D in BAG59341. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 4, 2003. Version 2. Checksum: 06AC2FED156BF535	FASTA	891	99,581
	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
	Isoform 2 [UniParc]. Checksum: A3AED736B90209A7	FASTA	409	45,762
	10 20 30 40 50 60 MSLFKRSTEE IIALFISITF VLDAVKGTVK IFWKYYYGHY LDDYHTKRTS SLVSLSGLGA 70 80 90 100 110 120 SLNASLHTAL NASFLASPTE LPSATHSGQA TAVLSLLIML GTLWLGYTLY QFKKSPYLHP 130 140 150 160 170 180 CVREILSDCA LPIAVLAFSL ISSHGFREIE MSKFRYNPSE SPFAMAQIQS LSLRAVSGAM 190 200 210 220 230 240 GLGFLLSMLF FIEQNLVAAL VNAPENRLVK GTAYHWDLLL LAIINTGLSL FGLPWIHAAY 250 260 270 280 290 300 PHSPLHVRAL ALVEERVENG HIYDTIVNVK ETRLTSLGAS VLVGLSLLLL PVPLQWIPKP 310 320 330 340 350 360 VLYGLFLYIA LTSLDGNQLV QRVALLLKEQ TAYPPTHYIR RVPQRKIHYF TGLQVLQLLL 370 380 390 400 LCAFGMSSLP YMKMIFPLIM IAMIPIRYIL LPRIIEAKYL DVMDAEHRP
	Isoform 3 [UniParc]. Checksum: 6BEDDC9939BADF10	FASTA	875	98,181
	10 20 30 40 50 60 MAAATRRVFH LQPCENSPTM SQNGYFEDSS YYKCDTDDTF EAREEILGDE AFDTANSSIV 70 80 90 100 110 120 SGESIRFFVN VNLEMQATNT ENEATSGGCV LLHTSRKYLK LKNFKEEIRA HRDLDGFLAQ 130 140 150 160 170 180 ASIVLNETAT SLDNVLRTML RRFARDPDNN EPNCNLDLLM AMLFTDAGAP MRGKVHLLSD 190 200 210 220 230 240 TIQGVTATVT GVRYQQSWLC IICTMKALQK RHVCISRLVR PQNWGENSCE VRFVILVLAP 250 260 270 280 290 300 PKMKSTKTAM EVARTFATMF SDIAFRQKLL ETRTEEEFKE ALVHQRQLLT MVSHGPVAPR 310 320 330 340 350 360 TKERSTVSLP AHRHPEPPKC KDFVPFGKGI REDIARRFPL YPLDFTDGII GKNKAVGKYI 370 380 390 400 410 420 TTTLFLYFAC LLPTIAFGSL NDENTDGAID VQKTIAGQSI GGLLYALFSG QPLVILLTTA 430 440 450 460 470 480 PLALYIQVIR VICDDYDLDF NSFYAWTGLW NSFFLALYAF FNLSLVMSLF KRSTEEIIAL 490 500 510 520 530 540 FISITFVLDA VKGTVKIFWK YYYGHYLDDY HTKRTSSLVS LSGLGASLNA SLHTALNASF 550 560 570 580 590 600 LASPTELPSA THSGQATAVL SLLIMLGTLW LGYTLYQFKK SPYLHPCVRE ILSDCALPIA 610 620 630 640 650 660 VLAFSLISSH GFREIEMSKF RYNPSESPFA MAQIQSLSLR AVSGAMGLGF LLSMLFFIEQ 670 680 690 700 710 720 NLVAALVNAP ENRLVKGTAY HWDLLLLAII NTGLSLFGLP WIHAAYPHSP LHVRALALVE 730 740 750 760 770 780 ERVENGHIYD TIVNVKETRL TSLGASVLVG LSLLLLPVPL QWIPKPVLYG LFLYIALTSL 790 800 810 820 830 840 DGNQLVQRVA LLLKEQTAYP PTHYIRRVPQ RKIHYFTGLQ VLQLLLLCAF GMSSLPYMKM 850 860 870 IFPLIMIAMI PIRYILLPRI IEAKYLDVMD AEHRP

References

	« Hide 'large scale' referencesShow '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. , 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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 227-891 (ISOFORM 1). Tissue: Retinoblastoma 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. , 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. , 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. 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.
IPI	IPI00015488. IPI00639817.
RefSeq	NP_001167560.1. NM_001174089.1. NP_001167561.1. NM_001174090.1. NP_114423.1. NM_032034.3.
UniGene	Hs.105607.
3D structure databases
ProteinModelPortal	Q8NBS3.
SMR	Q8NBS3. Positions 353-400, 799-831.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000369396.
Protein family/group databases
TCDB	2.A.31.4.1. anion exchanger (AE) family.
PTM databases
PhosphoSite	Q8NBS3.
Polymorphism databases
DMDM	29611858.
Proteomic databases
PaxDb	Q8NBS3.
PRIDE	Q8NBS3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380056; ENSP00000369396; ENSG00000088836. ENST00000380059; ENSP00000369399; ENSG00000088836. ENST00000437836; ENSP00000404271; ENSG00000088836. ENST00000539553; ENSP00000441370; ENSG00000088836.
GeneID	83959.
KEGG	hsa:83959.
UCSC	uc002wig.3. human.
Organism-specific databases
CTD	83959.
GeneCards	GC20M003203.
HGNC	HGNC:16438. SLC4A11.
HPA	HPA018120.
MIM	217400. phenotype. 217700. phenotype. 610206. gene. 613268. phenotype.
neXtProt	NX_Q8NBS3.
Orphanet	293603. Congenital hereditary endothelial dystrophy II. 1490. Corneal dystrophy - perceptive deafness. 98974. Fuchs endothelial corneal dystrophy.
PharmGKB	PA38139.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG268067.
HOGENOM	HOG000016966.
HOVERGEN	HBG079162.
KO	K13862.
PhylomeDB	Q8NBS3.
Gene expression databases
ArrayExpress	Q8NBS3.
Bgee	Q8NBS3.
CleanEx	HS_SLC4A11.
Genevestigator	Q8NBS3.
GermOnline	ENSG00000088836. Homo sapiens.
Family and domain databases
Gene3D	3.40.930.10. 1 hit.
InterPro	IPR011531. HCO3_transpt_C. IPR003020. HCO3_transpt_euk. IPR016152. PTrfase/Anion_transptr. IPR002178. PTS_EIIA_2. [Graphical view]
PANTHER	PTHR11453. PTHR11453. 1 hit.
Pfam	PF00955. HCO3_cotransp. 1 hit. PF00359. PTS_EIIA_2. 1 hit. [Graphical view]
PRINTS	PR01231. HCO3TRNSPORT.
SUPFAM	SSF55804. PTrfase/Anion_transptr. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	83959.
NextBio	73102.
SOURCE	Search...

Entry information

Entry name

S4A11_HUMAN

Accession

Primary (citable) accession number: Q8NBS3
Secondary accession number(s): B4DKX9 , G3V1M3, Q2TB62, Q2TB63, Q9BXF4, Q9NTW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2003
Last sequence update:	April 4, 2003
Last modified:	May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.