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Q8NBS3

- S4A11_HUMAN

UniProt

Q8NBS3 - S4A11_HUMAN

Protein

Sodium bicarbonate transporter-like protein 11

Gene

SLC4A11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (04 Apr 2003)
      Previous versions | rss
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    Functioni

    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.By similarity1 Publication

    GO - Molecular functioni

    1. bicarbonate transmembrane transporter activity Source: HGNC
    2. borate transmembrane transporter activity Source: HGNC
    3. hydrogen ion channel activity Source: HGNC
    4. inorganic anion exchanger activity Source: InterPro
    5. protein dimerization activity Source: UniProtKB
    6. sodium channel activity Source: HGNC
    7. symporter activity Source: UniProtKB-KW

    GO - Biological processi

    1. bicarbonate transport Source: HGNC
    2. borate transmembrane transport Source: GOC
    3. borate transport Source: HGNC
    4. cellular cation homeostasis Source: HGNC
    5. fluid transport Source: UniProtKB
    6. proton transport Source: HGNC
    7. sodium ion transmembrane transport Source: GOC
    8. sodium ion transport Source: HGNC

    Keywords - Biological processi

    Anion exchange, Ion transport, Symport, Transport

    Protein family/group databases

    TCDBi2.A.31.4.1. the anion exchanger (ae) family.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:SLC4A11
    Synonyms:BTR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:16438. SLC4A11.

    Subcellular locationi

    Cell membrane 1 Publication. Membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. basolateral plasma membrane Source: HGNC
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Corneal dystrophy and perceptive deafness (CDPD) [MIM:217400]: An ocular disease characterized by the association of corneal clouding with progressive perceptive hearing loss.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti213 – 2131S → P in CDPD. 1 Publication
    VAR_034946
    Natural varianti488 – 4881R → K in CDPD. 1 Publication
    VAR_034947
    Natural varianti843 – 8431L → P in CDPD. 1 Publication
    VAR_034951
    Natural varianti856 – 8561M → V in CDPD. 1 Publication
    VAR_034953
    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.9 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti125 – 1251R → H in CHED2. 1 Publication
    VAR_063713
    Natural varianti143 – 1431E → K in CHED2; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant. 1 Publication
    VAR_067272
    Natural varianti160 – 1601A → T in CHED2. 2 Publications
    VAR_034945
    Natural varianti209 – 2091R → W in CHED2. 1 Publication
    VAR_064978
    Natural varianti213 – 2131S → L in CHED2. 1 Publication
    VAR_064979
    Natural varianti233 – 2331R → C in CHED2. 1 Publication
    VAR_064980
    Natural varianti269 – 2691A → V in CHED2; affects transport to the cell surface. 1 Publication
    VAR_063714
    Natural varianti386 – 3861C → R in CHED2; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant. 3 Publications
    VAR_063715
    Natural varianti394 – 3941G → R in CHED2. 2 Publications
    VAR_064981
    Natural varianti401 – 4011T → K in CHED2. 1 Publication
    VAR_064982
    Natural varianti418 – 4181G → D in CHED2. 2 Publications
    VAR_064983
    Natural varianti464 – 4641G → D in CHED2; affects protein processing and transport to the cell surface. 1 Publication
    VAR_030662
    Natural varianti473 – 4731L → R in CHED2. 1 Publication
    VAR_064984
    Natural varianti489 – 4891S → L in CHED2; affects protein processing and transport to the cell surface. 2 Publications
    VAR_030663
    Natural varianti584 – 5841T → K in CHED2. 1 Publication
    VAR_064985
    Natural varianti755 – 7551R → 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. 4 Publications
    VAR_030664
    Natural varianti755 – 7551R → W in CHED2. 3 Publications
    VAR_063716
    Natural varianti773 – 7731P → L in CHED2. 2 Publications
    VAR_063717
    Natural varianti804 – 8041R → H in CHED2. 1 Publication
    VAR_034948
    Natural varianti824 – 8241V → M in CHED2; deafness not assessed. 3 Publications
    VAR_034949
    Natural varianti833 – 8331T → M in CHED2. 1 Publication
    VAR_034950
    Natural varianti869 – 8691R → C in CHED2; affects protein processing and transport to the cell surface. 3 Publications
    VAR_030665
    Natural varianti869 – 8691R → H in CHED2. 1 Publication
    VAR_034954
    Natural varianti873 – 8731L → P in CHED2. 1 Publication
    VAR_063718
    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti167 – 1671E → D in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. 1 Publication
    VAR_064422
    Natural varianti282 – 2821R → P in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. 1 Publication
    VAR_064423
    Natural varianti399 – 3991E → 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. 1 Publication
    VAR_047809
    Natural varianti526 – 5261Y → C in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
    VAR_064424
    Natural varianti575 – 5751V → M in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
    VAR_064425
    Natural varianti583 – 5831G → D in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. 1 Publication
    VAR_064426
    Natural varianti709 – 7091G → 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. 1 Publication
    VAR_047812
    Natural varianti742 – 7421G → R in FECD4; interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
    Corresponds to variant rs143965185 [ dbSNP | Ensembl ].
    VAR_064427
    Natural varianti754 – 7541T → 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. 1 Publication
    VAR_047813
    Natural varianti834 – 8341G → S in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
    VAR_064428

    Keywords - Diseasei

    Corneal dystrophy, Disease mutation

    Organism-specific databases

    MIMi217400. phenotype.
    217700. phenotype.
    613268. phenotype.
    Orphaneti293603. Congenital hereditary endothelial dystrophy type II.
    1490. Corneal dystrophy - perceptive deafness.
    98974. Fuchs endothelial corneal dystrophy.
    PharmGKBiPA38139.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 891891Sodium bicarbonate transporter-like protein 11PRO_0000079236Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi545 – 5451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi553 – 5531N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ8NBS3.
    PaxDbiQ8NBS3.
    PRIDEiQ8NBS3.

    PTM databases

    PhosphoSiteiQ8NBS3.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in kidney, testis, salivary gland, thyroid, trachea and corneal endothelium. Not detected in retina and lymphocytes.2 Publications

    Gene expression databases

    BgeeiQ8NBS3.
    CleanExiHS_SLC4A11.
    GenevestigatoriQ8NBS3.

    Organism-specific databases

    HPAiHPA018120.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi123832. 1 interaction.
    STRINGi9606.ENSP00000369396.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8NBS3.
    SMRiQ8NBS3. Positions 353-400, 799-831.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 375375CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini514 – 57158ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini593 – 65361CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei376 – 39621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei416 – 43621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei466 – 48621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei493 – 51321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei572 – 59221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei654 – 67421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei700 – 72021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei759 – 77921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei782 – 80221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei831 – 85121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei853 – 87321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni376 – 891516Membrane (bicarbonate transporter)Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG268067.
    HOGENOMiHOG000016966.
    HOVERGENiHBG079162.
    KOiK13862.
    OrthoDBiEOG7M6D7V.
    PhylomeDBiQ8NBS3.
    TreeFamiTF313630.

    Family and domain databases

    Gene3Di3.40.930.10. 1 hit.
    InterProiIPR011531. HCO3_transpt_C.
    IPR003020. HCO3_transpt_euk.
    IPR016152. PTrfase/Anion_transptr.
    IPR002178. PTS_EIIA_type-2_dom.
    [Graphical view]
    PANTHERiPTHR11453. PTHR11453. 1 hit.
    PfamiPF00955. HCO3_cotransp. 1 hit.
    PF00359. PTS_EIIA_2. 1 hit.
    [Graphical view]
    PRINTSiPR01231. HCO3TRNSPORT.
    SUPFAMiSSF55804. SSF55804. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8NBS3-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSQVGGRGDR CTQEVQGLVH GAGDLSASLA ENSPTMSQNG YFEDSSYYKC    50
    DTDDTFEARE EILGDEAFDT ANSSIVSGES IRFFVNVNLE MQATNTENEA 100
    TSGGCVLLHT SRKYLKLKNF KEEIRAHRDL DGFLAQASIV LNETATSLDN 150
    VLRTMLRRFA RDPDNNEPNC NLDLLMAMLF TDAGAPMRGK VHLLSDTIQG 200
    VTATVTGVRY QQSWLCIICT MKALQKRHVC ISRLVRPQNW GENSCEVRFV 250
    ILVLAPPKMK STKTAMEVAR TFATMFSDIA FRQKLLETRT EEEFKEALVH 300
    QRQLLTMVSH GPVAPRTKER STVSLPAHRH PEPPKCKDFV PFGKGIREDI 350
    ARRFPLYPLD FTDGIIGKNK AVGKYITTTL FLYFACLLPT IAFGSLNDEN 400
    TDGAIDVQKT IAGQSIGGLL YALFSGQPLV ILLTTAPLAL YIQVIRVICD 450
    DYDLDFNSFY AWTGLWNSFF LALYAFFNLS LVMSLFKRST EEIIALFISI 500
    TFVLDAVKGT VKIFWKYYYG HYLDDYHTKR TSSLVSLSGL GASLNASLHT 550
    ALNASFLASP TELPSATHSG QATAVLSLLI MLGTLWLGYT LYQFKKSPYL 600
    HPCVREILSD CALPIAVLAF SLISSHGFRE IEMSKFRYNP SESPFAMAQI 650
    QSLSLRAVSG AMGLGFLLSM LFFIEQNLVA ALVNAPENRL VKGTAYHWDL 700
    LLLAIINTGL SLFGLPWIHA AYPHSPLHVR ALALVEERVE NGHIYDTIVN 750
    VKETRLTSLG ASVLVGLSLL LLPVPLQWIP KPVLYGLFLY IALTSLDGNQ 800
    LVQRVALLLK EQTAYPPTHY IRRVPQRKIH YFTGLQVLQL LLLCAFGMSS 850
    LPYMKMIFPL IMIAMIPIRY ILLPRIIEAK YLDVMDAEHR P 891
    Length:891
    Mass (Da):99,581
    Last modified:April 4, 2003 - v2
    Checksum:i06AC2FED156BF535
    GO
    Isoform 2 (identifier: Q8NBS3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-482: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:409
    Mass (Da):45,762
    Checksum:iA3AED736B90209A7
    GO
    Isoform 3 (identifier: Q8NBS3-3) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:875
    Mass (Da):98,181
    Checksum:i6BEDDC9939BADF10
    GO
    Isoform 4 (identifier: Q8NBS3-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:918
    Mass (Da):103,145
    Checksum:iBA314E50D8F6CD48
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti324 – 3241S → P in BAC11536. (PubMed:14702039)Curated
    Sequence conflicti576 – 5761L → P in BAG59341. (PubMed:14702039)Curated
    Sequence conflicti684 – 6841N → S in BAG59140. (PubMed:14702039)Curated
    Sequence conflicti784 – 7841L → R in AAI10541. (PubMed:15489334)Curated
    Sequence conflicti834 – 8341G → D in BAG59341. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721N → T.1 Publication
    VAR_047806
    Natural varianti91 – 911M → V.1 Publication
    Corresponds to variant rs200940928 [ dbSNP | Ensembl ].
    VAR_047807
    Natural varianti125 – 1251R → H in CHED2. 1 Publication
    VAR_063713
    Natural varianti143 – 1431E → K in CHED2; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant. 1 Publication
    VAR_067272
    Natural varianti150 – 1501N → S.
    Corresponds to variant rs34520315 [ dbSNP | Ensembl ].
    VAR_034944
    Natural varianti160 – 1601A → T in CHED2. 2 Publications
    VAR_034945
    Natural varianti167 – 1671E → D in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. 1 Publication
    VAR_064422
    Natural varianti209 – 2091R → W in CHED2. 1 Publication
    VAR_064978
    Natural varianti213 – 2131S → L in CHED2. 1 Publication
    VAR_064979
    Natural varianti213 – 2131S → P in CDPD. 1 Publication
    VAR_034946
    Natural varianti233 – 2331R → C in CHED2. 1 Publication
    VAR_064980
    Natural varianti269 – 2691A → V in CHED2; affects transport to the cell surface. 1 Publication
    VAR_063714
    Natural varianti282 – 2821R → P in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. 1 Publication
    VAR_064423
    Natural varianti327 – 3271A → V.1 Publication
    VAR_047808
    Natural varianti386 – 3861C → R in CHED2; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant. 3 Publications
    VAR_063715
    Natural varianti394 – 3941G → R in CHED2. 2 Publications
    VAR_064981
    Natural varianti399 – 3991E → 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. 1 Publication
    VAR_047809
    Natural varianti401 – 4011T → K in CHED2. 1 Publication
    VAR_064982
    Natural varianti408 – 4081Q → H.1 Publication
    VAR_015521
    Natural varianti409 – 4091K → N.1 Publication
    VAR_015522
    Natural varianti418 – 4181G → D in CHED2. 2 Publications
    VAR_064983
    Natural varianti464 – 4641G → D in CHED2; affects protein processing and transport to the cell surface. 1 Publication
    VAR_030662
    Natural varianti473 – 4731L → R in CHED2. 1 Publication
    VAR_064984
    Natural varianti483 – 4831M → T.1 Publication
    VAR_015523
    Natural varianti488 – 4881R → K in CDPD. 1 Publication
    VAR_034947
    Natural varianti489 – 4891S → L in CHED2; affects protein processing and transport to the cell surface. 2 Publications
    VAR_030663
    Natural varianti526 – 5261Y → C in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
    VAR_064424
    Natural varianti561 – 5611T → M.1 Publication
    VAR_047810
    Natural varianti565 – 5651S → L.1 Publication
    VAR_047811
    Natural varianti575 – 5751V → M in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
    VAR_064425
    Natural varianti583 – 5831G → D in FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm. 1 Publication
    VAR_064426
    Natural varianti584 – 5841T → K in CHED2. 1 Publication
    VAR_064985
    Natural varianti708 – 7081T → A.1 Publication
    VAR_015524
    Natural varianti709 – 7091G → 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. 1 Publication
    VAR_047812
    Natural varianti742 – 7421G → R in FECD4; interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
    Corresponds to variant rs143965185 [ dbSNP | Ensembl ].
    VAR_064427
    Natural varianti754 – 7541T → 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. 1 Publication
    VAR_047813
    Natural varianti755 – 7551R → 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. 4 Publications
    VAR_030664
    Natural varianti755 – 7551R → W in CHED2. 3 Publications
    VAR_063716
    Natural varianti773 – 7731P → L in CHED2. 2 Publications
    VAR_063717
    Natural varianti804 – 8041R → H in CHED2. 1 Publication
    VAR_034948
    Natural varianti824 – 8241V → M in CHED2; deafness not assessed. 3 Publications
    VAR_034949
    Natural varianti833 – 8331T → M in CHED2. 1 Publication
    VAR_034950
    Natural varianti834 – 8341G → S in FECD4; does not interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm. 1 Publication
    VAR_064428
    Natural varianti843 – 8431L → P in CDPD. 1 Publication
    VAR_034951
    Natural varianti848 – 8481M → I.
    Corresponds to variant rs34224785 [ dbSNP | Ensembl ].
    VAR_034952
    Natural varianti856 – 8561M → V in CDPD. 1 Publication
    VAR_034953
    Natural varianti869 – 8691R → C in CHED2; affects protein processing and transport to the cell surface. 3 Publications
    VAR_030665
    Natural varianti869 – 8691R → H in CHED2. 1 Publication
    VAR_034954
    Natural varianti873 – 8731L → P in CHED2. 1 Publication
    VAR_063718

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 482482Missing in isoform 2. 1 PublicationVSP_035891Add
    BLAST
    Alternative sequencei1 – 3030MSQVG…SASLA → MAAATRRVFHLQPC in isoform 3. 1 PublicationVSP_044846Add
    BLAST
    Alternative sequencei1 – 3030MSQVG…SASLA → MGVYGPQDRSESEKRDVQRD PPPWHPRREGERPARARSLP LAAAGQGFLRKTWISEH in isoform 4. 1 PublicationVSP_054049Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13052.1. [Q8NBS3-1]
    CCDS54445.1. [Q8NBS3-4]
    CCDS54446.1. [Q8NBS3-3]
    RefSeqiNP_001167560.1. NM_001174089.1. [Q8NBS3-3]
    NP_001167561.1. NM_001174090.1. [Q8NBS3-4]
    NP_114423.1. NM_032034.3. [Q8NBS3-1]
    UniGeneiHs.105607.

    Genome annotation databases

    EnsembliENST00000380056; ENSP00000369396; ENSG00000088836. [Q8NBS3-1]
    ENST00000380059; ENSP00000369399; ENSG00000088836. [Q8NBS3-4]
    ENST00000539553; ENSP00000441370; ENSG00000088836. [Q8NBS3-3]
    GeneIDi83959.
    KEGGihsa:83959.
    UCSCiuc002wig.3. human. [Q8NBS3-1]
    uc010zqf.2. human.

    Polymorphism databases

    DMDMi29611858.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS13052.1. [Q8NBS3-1 ]
    CCDS54445.1. [Q8NBS3-4 ]
    CCDS54446.1. [Q8NBS3-3 ]
    RefSeqi NP_001167560.1. NM_001174089.1. [Q8NBS3-3 ]
    NP_001167561.1. NM_001174090.1. [Q8NBS3-4 ]
    NP_114423.1. NM_032034.3. [Q8NBS3-1 ]
    UniGenei Hs.105607.

    3D structure databases

    ProteinModelPortali Q8NBS3.
    SMRi Q8NBS3. Positions 353-400, 799-831.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123832. 1 interaction.
    STRINGi 9606.ENSP00000369396.

    Protein family/group databases

    TCDBi 2.A.31.4.1. the anion exchanger (ae) family.

    PTM databases

    PhosphoSitei Q8NBS3.

    Polymorphism databases

    DMDMi 29611858.

    Proteomic databases

    MaxQBi Q8NBS3.
    PaxDbi Q8NBS3.
    PRIDEi Q8NBS3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380056 ; ENSP00000369396 ; ENSG00000088836 . [Q8NBS3-1 ]
    ENST00000380059 ; ENSP00000369399 ; ENSG00000088836 . [Q8NBS3-4 ]
    ENST00000539553 ; ENSP00000441370 ; ENSG00000088836 . [Q8NBS3-3 ]
    GeneIDi 83959.
    KEGGi hsa:83959.
    UCSCi uc002wig.3. human. [Q8NBS3-1 ]
    uc010zqf.2. human.

    Organism-specific databases

    CTDi 83959.
    GeneCardsi GC20M003203.
    HGNCi HGNC:16438. SLC4A11.
    HPAi HPA018120.
    MIMi 217400. phenotype.
    217700. phenotype.
    610206. gene.
    613268. phenotype.
    neXtProti NX_Q8NBS3.
    Orphaneti 293603. Congenital hereditary endothelial dystrophy type II.
    1490. Corneal dystrophy - perceptive deafness.
    98974. Fuchs endothelial corneal dystrophy.
    PharmGKBi PA38139.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG268067.
    HOGENOMi HOG000016966.
    HOVERGENi HBG079162.
    KOi K13862.
    OrthoDBi EOG7M6D7V.
    PhylomeDBi Q8NBS3.
    TreeFami TF313630.

    Miscellaneous databases

    GeneWikii SLC4A11.
    GenomeRNAii 83959.
    NextBioi 73102.
    PROi Q8NBS3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8NBS3.
    CleanExi HS_SLC4A11.
    Genevestigatori Q8NBS3.

    Family and domain databases

    Gene3Di 3.40.930.10. 1 hit.
    InterProi IPR011531. HCO3_transpt_C.
    IPR003020. HCO3_transpt_euk.
    IPR016152. PTrfase/Anion_transptr.
    IPR002178. PTS_EIIA_type-2_dom.
    [Graphical view ]
    PANTHERi PTHR11453. PTHR11453. 1 hit.
    Pfami PF00955. HCO3_cotransp. 1 hit.
    PF00359. PTS_EIIA_2. 1 hit.
    [Graphical view ]
    PRINTSi PR01231. HCO3TRNSPORT.
    SUPFAMi SSF55804. SSF55804. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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] (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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiS4A11_HUMAN
    AccessioniPrimary (citable) accession number: Q8NBS3
    Secondary accession number(s): B4DKC8
    , B4DKX9, G3V1M3, Q2TB62, Q2TB63, Q9BXF4, Q9NTW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2003
    Last sequence update: April 4, 2003
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3