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Q8BTY2

- S4A7_MOUSE

UniProt

Q8BTY2 - S4A7_MOUSE

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Protein

Sodium bicarbonate cotransporter 3

Gene

Slc4a7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Enzyme regulationi

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).By similarity

GO - Molecular functioni

  1. inorganic anion exchanger activity Source: InterPro
  2. symporter activity Source: UniProtKB-KW

GO - Biological processi

  1. auditory receptor cell development Source: MGI
  2. cochlear nucleus development Source: MGI
  3. retinal cell programmed cell death Source: MGI
  4. retina vasculature morphogenesis in camera-type eye Source: MGI
  5. sodium ion transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Ion transport, Sodium transport, Symport, Transport

Keywords - Ligandi

Sodium

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium bicarbonate cotransporter 3
Alternative name(s):
Solute carrier family 4 member 7
Gene namesi
Name:Slc4a7
Synonyms:Nbc3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:2443878. Slc4a7.

Subcellular locationi

Basolateral cell membrane; Multi-pass membrane protein. Apical cell membrane By similarity; 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).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 476476ExtracellularSequence AnalysisAdd
BLAST
Transmembranei477 – 49721HelicalSequence AnalysisAdd
BLAST
Topological domaini498 – 5058CytoplasmicSequence Analysis
Transmembranei506 – 52621HelicalSequence AnalysisAdd
BLAST
Topological domaini527 – 56337ExtracellularSequence AnalysisAdd
BLAST
Transmembranei564 – 58421HelicalSequence AnalysisAdd
BLAST
Topological domaini585 – 5939CytoplasmicSequence Analysis
Transmembranei594 – 61421HelicalSequence AnalysisAdd
BLAST
Topological domaini615 – 68571ExtracellularSequence AnalysisAdd
BLAST
Transmembranei686 – 70621HelicalSequence AnalysisAdd
BLAST
Topological domaini707 – 72923CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei730 – 75021HelicalSequence AnalysisAdd
BLAST
Topological domaini751 – 77626ExtracellularSequence AnalysisAdd
BLAST
Transmembranei777 – 79721HelicalSequence AnalysisAdd
BLAST
Topological domaini798 – 81215CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei813 – 83321HelicalSequence AnalysisAdd
BLAST
Topological domaini834 – 87643ExtracellularSequence AnalysisAdd
BLAST
Transmembranei877 – 89721HelicalSequence AnalysisAdd
BLAST
Topological domaini898 – 1034137CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. basolateral plasma membrane Source: UniProtKB
  3. cell projection Source: UniProtKB-KW
  4. cytoplasm Source: UniProtKB
  5. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Disruption phenotypei

Deafness and blindness due to degeneration of sensory receptors in internal ear and retina.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10341034Sodium bicarbonate cotransporter 3PRO_0000079234Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571Phosphoserine1 Publication
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis
Modified residuei238 – 2381Phosphoserine1 Publication
Modified residuei271 – 2711PhosphoserineBy similarity
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence Analysis
Modified residuei275 – 2751Phosphoserine1 Publication
Glycosylationi644 – 6441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi654 – 6541N-linked (GlcNAc...)1 Publication
Glycosylationi664 – 6641N-linked (GlcNAc...)1 Publication
Modified residuei951 – 9511PhosphothreonineBy similarity
Modified residuei960 – 9601Phosphoserine2 Publications
Modified residuei1033 – 10331PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8BTY2.
PaxDbiQ8BTY2.
PRIDEiQ8BTY2.

PTM databases

PhosphoSiteiQ8BTY2.

Expressioni

Tissue specificityi

Expressed in the spiral ligament throughout the cochlea and in photoreceptors of the outer plexiform layer of the retina (at protein level).2 Publications

Gene expression databases

GenevestigatoriQ8BTY2.

Interactioni

Subunit structurei

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.By similarity2 Publications

Structurei

3D structure databases

ProteinModelPortaliQ8BTY2.
SMRiQ8BTY2. Positions 115-394, 460-500.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni918 – 9203CA2-bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1031 – 10344PDZ-bindingBy similarity

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG268067.
HOGENOMiHOG000280684.
HOVERGENiHBG004326.
InParanoidiQ8BTY2.
PhylomeDBiQ8BTY2.

Family and domain databases

Gene3Di3.40.1100.10. 1 hit.
InterProiIPR013769. Band3_cytoplasmic_dom.
IPR011531. HCO3_transpt_C.
IPR003020. HCO3_transpt_euk.
IPR003024. Na/HCO3_transpt.
IPR016152. PTrfase/Anion_transptr.
[Graphical view]
PANTHERiPTHR11453. PTHR11453. 1 hit.
PfamiPF07565. Band_3_cyto. 1 hit.
PF00955. HCO3_cotransp. 1 hit.
[Graphical view]
PRINTSiPR01231. HCO3TRNSPORT.
PR01232. NAHCO3TRSPRT.
SUPFAMiSSF55804. SSF55804. 1 hit.
TIGRFAMsiTIGR00834. ae. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BTY2-1) [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

        10         20         30         40         50
MEADGAGEQM RPLLTRGPDE EAVVDLGKTS STVNTKFEKE ELESHRAVYV
60 70 80 90 100
GVHVPFSKES RRRHKHRGHK HHHRRRKDKD SDKEDGRESP SYDTPSQRVQ
110 120 130 140 150
FILGTEDDDE EHIPHDLFTE MDELCYRDGE EYEWKETARW LKFEEDVEDG
160 170 180 190 200
GDRWSKPYVA TLSLHSLFEL RSCILNGTVM LDMRASTLDE IADMVLDNMI
210 220 230 240 250
ASGQLDDSIR ENVREALLKR HHHQNEKRFT SRIPLVRSFA DIGILASPQS
260 270 280 290 300
APGNLDNSKS GEMKGNGSGG SRENSTVDFS KVDMNFMRKI PTGAEASNVL
310 320 330 340 350
VGEVDFLERP IIAFVRLAPA VLLSGLTEVP VPTRFLFLLL GPAGKAPQYH
360 370 380 390 400
EIGRSIATLM TDEIFHDVAY KAKDRNDLLS GIDEFLDQVT VLPPGEWDPS
410 420 430 440 450
IRIEPPKSVP SQEKRKIPVF PNGSAAMSVG PPKEDDHHAG PELQRTGRLF
460 470 480 490 500
GGLILDIKRK APFFLSDFKD ALSLQCLASI LFLYCACMSP VITFGGLLGE
510 520 530 540 550
ATEGRISAIE SLFGASLTGI AYSLFAGQPL TILGSTGPVL VFEKILFKFC
560 570 580 590 600
RDYHLSYLSL RTSIGLWTSF LCIVLVATDA SSLVCYITRF TEEAFAALIC
610 620 630 640 650
IIFIYEALEK LFHLGEIYAF NMHNNLDELT SYTCVCAEPS NPSNETLELW
660 670 680 690 700
KRKNITAYSV SWGNLTVSEC KTFHGMFVGS ACGPHGPYVP DVLFWCVVLF
710 720 730 740 750
FTTFFLSSFL KQFKTKGYFP TKVRSTISDF AVFLTIVIMV AIDYLVGIPS
760 770 780 790 800
PKLHVPEKFE PTDPSRGWII SPLGDNPWWT LLIAAVPALL CTILIFMDQQ
810 820 830 840 850
ITAVIINRKE HKLKFIPMPV LYGVFLYMGV SSLKGIQFFD RIKLFGMPAK
860 870 880 890 900
HQPDLIYLRY VPLWKVHVFT VVQLTCLVLL WVIKASAAAV VFPMMVLALV
910 920 930 940 950
FVRKLMDLCF TKRELSWLDD LMPESKKKKE DDKKKKEKEE AERMLQDDED
960 970 980 990 1000
TVHLPFERGS LLQIPVKTLK YSIDPSVVNI SDEMAKTAQW KALSMNTENA
1010 1020 1030
KVTRPNTSPE KPVSVTINFE DEPSKKYMDA ETSL
Length:1,034
Mass (Da):116,514
Last modified:February 7, 2006 - v2
Checksum:i92B080274D206097
GO
Isoform 2 (identifier: Q8BTY2-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:936
Mass (Da):104,678
Checksum:i03664D0534FD2EBC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti430 – 4301G → D in BAC40330. (PubMed:16141072)Curated
Sequence conflicti717 – 7171G → R in BAC40330. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei243 – 2431G → GKKHSDPHLLERNG in isoform 2. 1 PublicationVSP_017166
Alternative sequencei815 – 8151F → KGAGYHLDLLMVGVMLGVCS IMGLPWFVAATVLSISHVNS LKVESECSAPGEQPKFLGIR EQRVTGLMIFILMGLSVFMT SVLKVKPLWQCSTILFTLTF ILSCKEIKH in isoform 2. 1 PublicationVSP_017167
Alternative sequencei816 – 1034219Missing in isoform 2. 1 PublicationVSP_017168Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK088400 mRNA. Translation: BAC40330.1.
AK152233 mRNA. Translation: BAE31059.1.
AK153567 mRNA. Translation: BAE32101.1.
CN532915 mRNA. No translation available.
UniGeneiMm.258893.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK088400 mRNA. Translation: BAC40330.1 .
AK152233 mRNA. Translation: BAE31059.1 .
AK153567 mRNA. Translation: BAE32101.1 .
CN532915 mRNA. No translation available.
UniGenei Mm.258893.

3D structure databases

ProteinModelPortali Q8BTY2.
SMRi Q8BTY2. Positions 115-394, 460-500.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8BTY2.

Proteomic databases

MaxQBi Q8BTY2.
PaxDbi Q8BTY2.
PRIDEi Q8BTY2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:2443878. Slc4a7.

Phylogenomic databases

eggNOGi NOG268067.
HOGENOMi HOG000280684.
HOVERGENi HBG004326.
InParanoidi Q8BTY2.
PhylomeDBi Q8BTY2.

Miscellaneous databases

ChiTaRSi Slc4a7. mouse.
PROi Q8BTY2.
SOURCEi Search...

Gene expression databases

Genevestigatori Q8BTY2.

Family and domain databases

Gene3Di 3.40.1100.10. 1 hit.
InterProi IPR013769. Band3_cytoplasmic_dom.
IPR011531. HCO3_transpt_C.
IPR003020. HCO3_transpt_euk.
IPR003024. Na/HCO3_transpt.
IPR016152. PTrfase/Anion_transptr.
[Graphical view ]
PANTHERi PTHR11453. PTHR11453. 1 hit.
Pfami PF07565. Band_3_cyto. 1 hit.
PF00955. HCO3_cotransp. 1 hit.
[Graphical view ]
PRINTSi PR01231. HCO3TRNSPORT.
PR01232. NAHCO3TRSPRT.
SUPFAMi SSF55804. SSF55804. 1 hit.
TIGRFAMsi TIGR00834. ae. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiS4A7_MOUSE
AccessioniPrimary (citable) accession number: Q8BTY2
Secondary accession number(s): Q3U5H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 7, 2006
Last modified: November 26, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3