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Q8BTY2 (S4A7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 cotransporter 3
Alternative name(s):
Solute carrier family 4 member 7
Gene names
Name:Slc4a7
Synonyms:Nbc3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1034 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Electroneutral sodium- and bicarbonate-dependent cotransporter with a Na+:HCO3- 1:1 stoichiometry. Regulates intracellular pH and may play a role in bicarbonate salvage in secretory epithelia. May also have an associated sodium channel activity. Ref.4

Enzyme regulation

Transporter activity is regulated by CA2/carbonic anhydrase 2, cAMP and PKA. Insensitive to stilbene derivatives. May be inhibited by 5-(N-ethyl-N-isopropyl)-amiloride (EIPA) By similarity.

Subunit structure

Forms a complex with ATP6V1B1 and SLC9A3R1/EBP50. Interacts in a pH dependent-manner with CA2/carbonic anhydrase 2 By similarity. Interacts with CFTR through SLC9A3R1/EBP50. Interacts with USH1C. Ref.3 Ref.5

Subcellular location

Basolateral cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein By similarity. Cell projectionstereocilium By similarity. Note: Also described at the apical cell membrane. Localizes to the stereocilia of cochlear outer hair cells and to the lateral membrane of cochlear inner hair cells By similarity.

Tissue specificity

Expressed in the spiral ligament throughout the cochlea and in photoreceptors of the outer plexiform layer of the retina (at protein level). Ref.4 Ref.5

Domain

The PDZ-binding motif mediates interaction with the CFTR, SLC9A3R1/EBP50 complex and probably with USH1C By similarity.

Disruption phenotype

Deafness and blindness due to degeneration of sensory receptors in internal ear and retina. Ref.4

Sequence similarities

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BTY2-1)

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: Q8BTY2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     243-243: G → GKKHSDPHLLERNG
     815-815: F → KGAGYHLDLL...FILSCKEIKH
     816-1034: Missing.
Note: Contains a phosphoserine at position 263.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10341034Sodium bicarbonate cotransporter 3
PRO_0000079234

Regions

Topological domain1 – 476476Extracellular Potential
Transmembrane477 – 49721Helical; Potential
Topological domain498 – 5058Cytoplasmic Potential
Transmembrane506 – 52621Helical; Potential
Topological domain527 – 56337Extracellular Potential
Transmembrane564 – 58421Helical; Potential
Topological domain585 – 5939Cytoplasmic Potential
Transmembrane594 – 61421Helical; Potential
Topological domain615 – 68571Extracellular Potential
Transmembrane686 – 70621Helical; Potential
Topological domain707 – 72923Cytoplasmic Potential
Transmembrane730 – 75021Helical; Potential
Topological domain751 – 77626Extracellular Potential
Transmembrane777 – 79721Helical; Potential
Topological domain798 – 81215Cytoplasmic Potential
Transmembrane813 – 83321Helical; Potential
Topological domain834 – 87643Extracellular Potential
Transmembrane877 – 89721Helical; Potential
Topological domain898 – 1034137Cytoplasmic Potential
Region918 – 9203CA2-binding By similarity
Motif1031 – 10344PDZ-binding By similarity

Amino acid modifications

Modified residue571Phosphoserine Ref.7
Modified residue2381Phosphoserine Ref.7
Modified residue2711Phosphoserine By similarity
Modified residue2751Phosphoserine Ref.6
Modified residue9511Phosphothreonine By similarity
Modified residue9601Phosphoserine Ref.7 Ref.8
Modified residue10331Phosphoserine By similarity
Glycosylation1761N-linked (GlcNAc...) Potential
Glycosylation2741N-linked (GlcNAc...) Potential
Glycosylation6441N-linked (GlcNAc...) Potential
Glycosylation6541N-linked (GlcNAc...) Ref.9
Glycosylation6641N-linked (GlcNAc...) Ref.9

Natural variations

Alternative sequence2431G → GKKHSDPHLLERNG in isoform 2.
VSP_017166
Alternative sequence8151F → KGAGYHLDLLMVGVMLGVCS IMGLPWFVAATVLSISHVNS LKVESECSAPGEQPKFLGIR EQRVTGLMIFILMGLSVFMT SVLKVKPLWQCSTILFTLTF ILSCKEIKH in isoform 2.
VSP_017167
Alternative sequence816 – 1034219Missing in isoform 2.
VSP_017168

Experimental info

Sequence conflict4301G → D in BAC40330. Ref.1
Sequence conflict7171G → R in BAC40330. Ref.1

Sequences

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

Last modified February 7, 2006. Version 2.
Checksum: 92B080274D206097

FASTA1,034116,514
        10         20         30         40         50         60 
MEADGAGEQM RPLLTRGPDE EAVVDLGKTS STVNTKFEKE ELESHRAVYV GVHVPFSKES 

        70         80         90        100        110        120 
RRRHKHRGHK HHHRRRKDKD SDKEDGRESP SYDTPSQRVQ FILGTEDDDE EHIPHDLFTE 

       130        140        150        160        170        180 
MDELCYRDGE EYEWKETARW LKFEEDVEDG GDRWSKPYVA TLSLHSLFEL RSCILNGTVM 

       190        200        210        220        230        240 
LDMRASTLDE IADMVLDNMI ASGQLDDSIR ENVREALLKR HHHQNEKRFT SRIPLVRSFA 

       250        260        270        280        290        300 
DIGILASPQS APGNLDNSKS GEMKGNGSGG SRENSTVDFS KVDMNFMRKI PTGAEASNVL 

       310        320        330        340        350        360 
VGEVDFLERP IIAFVRLAPA VLLSGLTEVP VPTRFLFLLL GPAGKAPQYH EIGRSIATLM 

       370        380        390        400        410        420 
TDEIFHDVAY KAKDRNDLLS GIDEFLDQVT VLPPGEWDPS IRIEPPKSVP SQEKRKIPVF 

       430        440        450        460        470        480 
PNGSAAMSVG PPKEDDHHAG PELQRTGRLF GGLILDIKRK APFFLSDFKD ALSLQCLASI 

       490        500        510        520        530        540 
LFLYCACMSP VITFGGLLGE ATEGRISAIE SLFGASLTGI AYSLFAGQPL TILGSTGPVL 

       550        560        570        580        590        600 
VFEKILFKFC RDYHLSYLSL RTSIGLWTSF LCIVLVATDA SSLVCYITRF TEEAFAALIC 

       610        620        630        640        650        660 
IIFIYEALEK LFHLGEIYAF NMHNNLDELT SYTCVCAEPS NPSNETLELW KRKNITAYSV 

       670        680        690        700        710        720 
SWGNLTVSEC KTFHGMFVGS ACGPHGPYVP DVLFWCVVLF FTTFFLSSFL KQFKTKGYFP 

       730        740        750        760        770        780 
TKVRSTISDF AVFLTIVIMV AIDYLVGIPS PKLHVPEKFE PTDPSRGWII SPLGDNPWWT 

       790        800        810        820        830        840 
LLIAAVPALL CTILIFMDQQ ITAVIINRKE HKLKFIPMPV LYGVFLYMGV SSLKGIQFFD 

       850        860        870        880        890        900 
RIKLFGMPAK HQPDLIYLRY VPLWKVHVFT VVQLTCLVLL WVIKASAAAV VFPMMVLALV 

       910        920        930        940        950        960 
FVRKLMDLCF TKRELSWLDD LMPESKKKKE DDKKKKEKEE AERMLQDDED TVHLPFERGS 

       970        980        990       1000       1010       1020 
LLQIPVKTLK YSIDPSVVNI SDEMAKTAQW KALSMNTENA KVTRPNTSPE KPVSVTINFE 

      1030 
DEPSKKYMDA ETSL 

« Hide

Isoform 2 [UniParc].

Checksum: 03664D0534FD2EBC
Show »

FASTA936104,678

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-932 (ISOFORM 1).
Strain: C57BL/6J and NOD.
Tissue: Bone marrow and Thymus.
[2]"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] OF 826-1034 (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain.
[3]"The cystic fibrosis transmembrane conductance regulator interacts with and regulates the activity of the HCO3- salvage transporter human Na+-HCO3-cotransport isoform 3."
Park M., Ko S.B.H., Choi J.Y., Muallem G., Thomas P.J., Pushkin A., Lee M.-S., Kim J.Y., Lee M.G., Muallem S., Kurtz I.
J. Biol. Chem. 277:50503-50509(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CFTR AND SLC9A3R1.
[4]"Blindness and auditory impairment caused by loss of the sodium bicarbonate cotransporter NBC3."
Bok D., Galbraith G., Lopez I., Woodruff M., Nusinowitz S., BeltrandelRio H., Huang W., Zhao S., Geske R., Montgomery C., van Sligtenhorst I., Friddle C., Platt K., Sparks M.J., Pushkin A., Abuladze N., Ishiyama A., Dukkipati R., Liu W., Kurtz I.
Nat. Genet. 34:313-319(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[5]"Scaffold protein harmonin (USH1C) provides molecular links between Usher syndrome type 1 and type 2."
Reiners J., van Wijk E., Maerker T., Zimmermann U., Juergens K., te Brinke H., Overlack N., Roepman R., Knipper M., Kremer H., Wolfrum U.
Hum. Mol. Genet. 14:3933-3943(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH USH1C, TISSUE SPECIFICITY.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-238 AND SER-960, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-960, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[9]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-654 AND ASN-664.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK088400 mRNA. Translation: BAC40330.1.
AK152233 mRNA. Translation: BAE31059.1.
AK153567 mRNA. Translation: BAE32101.1.
CN532915 mRNA. No translation available.
UniGeneMm.258893.

3D structure databases

ProteinModelPortalQ8BTY2.
SMRQ8BTY2. Positions 115-394, 460-500.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8BTY2.

Proteomic databases

MaxQBQ8BTY2.
PaxDbQ8BTY2.
PRIDEQ8BTY2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:2443878. Slc4a7.

Phylogenomic databases

eggNOGNOG268067.
HOGENOMHOG000280684.
HOVERGENHBG004326.
PhylomeDBQ8BTY2.

Gene expression databases

GenevestigatorQ8BTY2.

Family and domain databases

Gene3D3.40.1100.10. 1 hit.
InterProIPR013769. Band3_cytoplasmic_dom.
IPR011531. HCO3_transpt_C.
IPR003020. HCO3_transpt_euk.
IPR003024. Na/HCO3_transpt.
IPR016152. PTrfase/Anion_transptr.
[Graphical view]
PANTHERPTHR11453. PTHR11453. 1 hit.
PfamPF07565. Band_3_cyto. 1 hit.
PF00955. HCO3_cotransp. 1 hit.
[Graphical view]
PRINTSPR01231. HCO3TRNSPORT.
PR01232. NAHCO3TRSPRT.
SUPFAMSSF55804. SSF55804. 1 hit.
TIGRFAMsTIGR00834. ae. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSLC4A7. mouse.
PROQ8BTY2.
SOURCESearch...

Entry information

Entry nameS4A7_MOUSE
AccessionPrimary (citable) accession number: Q8BTY2
Secondary accession number(s): Q3U5H7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 7, 2006
Last modified: June 11, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot