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Q8JZR6 (S4A8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. 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:
Electroneutral sodium bicarbonate exchanger 1
Alternative name(s):
Electroneutral Na+-driven Cl-HCO3 exchanger
Solute carrier family 4 member 8
k-NBC3
Gene names
Name:Slc4a8
Synonyms:Kiaa0739
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1089 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Mediates electroneutral sodium- and carbonate-dependent chloride-HCO3- exchange with a Na+:HCO3- stoichiometry of 2:1. Plays a major role in pH regulation in neurons. May be involved in cell pH regulation by transporting HCO3- from blood to cell. Enhanced expression in severe acid stress could be important for cell survival by mediating the influx of HCO3- into the cells. Also mediates lithium-dependent HCO3- cotransport. May be regulated by osmolarity. Ref.1 UniProtKB Q2Y0W8

Enzyme regulation

Activity is inhibited by 4,4'-Di-isothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of several anion channels and transporters).

Subcellular location

Membrane; Multi-pass membrane protein Ref.1.

Tissue specificity

Highly expressed in brain with lower levels in lung, kidney and heart. In the kidney, there is high expression in the inner medulla, localized to the inner medullary collecting duct. In the brain, there seems to be three transcripts each having a different expression pattern. The smaller 3kb transcript has highest expression levels in the thalamus and the largest 9.5kb transcript has highest levels in the substantia nigra. The middle transcript of 4.4kb, which is also the main transcript in kidney, is highly expressed in thalamus. Hence, the highest levels are observed in the thalamus, amygdala and caudate nucleus and very low expression was seen in the corpus callosum. Ref.1

Sequence similarities

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

Sequence caution

The sequence BAD32292.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.2 Ref.4 (identifier: Q8JZR6-1)

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 Ref.2 (identifier: Q8JZR6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10891089Electroneutral sodium bicarbonate exchanger 1
PRO_0000328923

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 – 82225Cytoplasmic Potential
Transmembrane823 – 84321Helical; Potential
Topological domain844 – 87936Extracellular Potential
Transmembrane880 – 90021Helical; Potential
Topological domain901 – 9022Cytoplasmic Potential
Transmembrane903 – 92321Helical; Potential
Topological domain924 – 96037Extracellular Potential
Transmembrane961 – 98121Helical; Potential
Topological domain982 – 1089108Cytoplasmic Potential
Compositional bias1021 – 10266Poly-Glu

Natural variations

Alternative sequence1 – 5252Missing in isoform 2. Ref.2
VSP_052769

Experimental info

Sequence conflict2191K → E in BAE42561. Ref.2
Sequence conflict2581V → M in AAF61705. Ref.1
Sequence conflict2911K → R in BAE42561. Ref.2
Sequence conflict6441N → S in BAC30341. Ref.2
Sequence conflict7071S → P in AAF61705. Ref.1
Sequence conflict9491K → E in BAE42561. Ref.2
Sequence conflict10151D → G in BAC30341. Ref.2

Sequences

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

Last modified October 1, 2002. Version 1.
Checksum: CFAE127D3853DDD8

FASTA1,089122,421
        10         20         30         40         50         60 
MPAGSNEPDG VLSYQRPDEE AVVDQGGTST ILNIHYEKEE LEGHRTLYVG VRMPLGRQSH 

        70         80         90        100        110        120 
RHHRTHGQKH RRRGGRGKGA SQGEEGLEAL AHDTPSQRVQ FILGTEEDEE HVPHELFTEL 

       130        140        150        160        170        180 
DEICMKEGED AEWKETARWL KFEEDVEDGG ERWSKPYVAT LSLHSLFELR SCLINGSVLL 

       190        200        210        220        230        240 
DMRASSIEEI SDLILDQQEL LRDLSDSVRV KVREALLKKH HHQNERRRNN LIPIVRSFAE 

       250        260        270        280        290        300 
VGKKQSDPHS MDRDGQTVSP QSATNLEVKN GVNCEHSPVD LSKVDLHFMK KIPTGAEASN 

       310        320        330        340        350        360 
VLVGEVDTLD RPIVAFVRLS PAVLLSGLTE VPIPTRFLFI LLGPVGKGQQ YHEIGRSMAT 

       370        380        390        400        410        420 
IMTDEIFHDV AYKAKERDDL LAGIDEFLDQ VTVLPPGEWD PSIRIEPPKN VPSQEKRKMP 

       430        440        450        460        470        480 
GVPNGNVCHI EPEPHGGHSG PELERTGRLF GGLVLDVKRK APWYWSDYRD ALSLQCLASF 

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

       550        560        570        580        590        600 
VFEKILFKFC KDYALSYLSL RALIGLWTAF LCIVLVATDA SSLVCYITRF TEEAFASLIC 

       610        620        630        640        650        660 
IIFIYEAIEK LIHLAETYPI HMHSQLDHLS LYYCRCVLPE NPNNHTLQYW KDHNILAAEV 

       670        680        690        700        710        720 
NWANLTVSEC QEMHGEFMGS ACGHHGPYTP DVLFWSCILF FATFIVSSTL KTFKTSRYFP 

       730        740        750        760        770        780 
TRVRSMVSDF AVFLTIFTMV VLDFLIGVPS PKLQVPNVFK PTRDDRGWFI NPIGPNPWWT 

       790        800        810        820        830        840 
VIAAIIPALL CTILIFMDQQ ITAVIINRKE HKLKKGCGYH LDLLMVAVML GVCSIMGLPW 

       850        860        870        880        890        900 
FVAATVLSIT HVNSLKLESE CSAPGEQPKF LGIREQRVTG LMIFVLMGCS VFMTAVLKFI 

       910        920        930        940        950        960 
PMPVLYGVFL YMGVSSLQGI QFFDRLKLFG MPAKHQPDFI YLRHVPLRKV HLFTLVQLTC 

       970        980        990       1000       1010       1020 
LVLLWVIKAS PAAIVFPMMV LALVFVRKVM DLCFSKRELS WLDDLMPESK KKKLDDAKKK 

      1030       1040       1050       1060       1070       1080 
EEEEAEKMLD IGGDKFPLES RKLLSSPGKS SSFRCDPSEI NISDEMPKTT VWKALSINSG 


NTKEKSPFN 

« Hide

Isoform 2 [UniParc].

Checksum: 81818C80B335F19B
Show »

FASTA1,037116,681

References

« Hide 'large scale' references
[1]"Mouse Na+: HCO3- cotransporter isoform NBC-3 (kNBC-3): cloning, expression, and renal distribution."
Wang Z., Conforti L., Petrovic S., Amlal H., Burnham C.E., Soleimani M.
Kidney Int. 59:1405-1414(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INHIBITION.
Tissue: Kidney inner medulla.
[2]"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] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Dendritic cell and Spinal cord.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[4]"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] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Retina.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF224508 mRNA. Translation: AAF61705.1.
AK039404 mRNA. Translation: BAC30341.1.
AK171610 mRNA. Translation: BAE42561.1.
AK173014 mRNA. Translation: BAD32292.1. Different initiation.
BC030388 mRNA. Translation: AAH30388.1.
CCDSCCDS37214.1. [Q8JZR6-1]
RefSeqNP_067505.2. NM_021530.2. [Q8JZR6-1]
XP_006521288.1. XM_006521225.1. [Q8JZR6-2]
XP_006521289.1. XM_006521226.1. [Q8JZR6-2]
UniGeneMm.209856.

3D structure databases

ProteinModelPortalQ8JZR6.
SMRQ8JZR6. Positions 115-396, 460-500.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8JZR6.

Proteomic databases

PaxDbQ8JZR6.
PRIDEQ8JZR6.

Protocols and materials databases

DNASU59033.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023776; ENSMUSP00000023776; ENSMUSG00000023032. [Q8JZR6-1]
ENSMUST00000162049; ENSMUSP00000125090; ENSMUSG00000023032. [Q8JZR6-2]
GeneID59033.
KEGGmmu:59033.
UCSCuc007xse.1. mouse. [Q8JZR6-1]

Organism-specific databases

CTD9498.
MGIMGI:1928745. Slc4a8.
RougeSearch...

Phylogenomic databases

eggNOGNOG268067.
GeneTreeENSGT00560000076851.
HOGENOMHOG000280684.
HOVERGENHBG004326.
InParanoidQ8JZR6.
KOK13859.
OMAVLNIHYE.
OrthoDBEOG7TMZR0.
PhylomeDBQ8JZR6.
TreeFamTF313630.

Gene expression databases

ArrayExpressQ8JZR6.
BgeeQ8JZR6.
GenevestigatorQ8JZR6.

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

NextBio314630.
PROQ8JZR6.
SOURCESearch...

Entry information

Entry nameS4A8_MOUSE
AccessionPrimary (citable) accession number: Q8JZR6
Secondary accession number(s): Q3TAV7 expand/collapse secondary AC list , Q6A004, Q8BYI7, Q9JKV6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 85 of the entry and version 1 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