Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y6M7 (S4A7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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):
Electroneutral Na/HCO(3) cotransporter
Sodium bicarbonate cotransporter 2
Sodium bicarbonate cotransporter 2b
Short name=Bicarbonate transporter
Solute carrier family 4 member 7
Gene names
Name:SLC4A7
Synonyms:BT, NBC2, NBC2B, NBC3, NBCn1, SBC2, SLC4A6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1214 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.2 Ref.9

Enzyme regulation

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

Subunit structure

Interacts with CFTR through SLC9A3R1/EBP50. Interacts with USH1C. Forms a complex with ATP6V1B1 and SLC9A3R1/EBP50. Interacts in a pH dependent-manner with CA2/carbonic anhydrase 2. Ref.9 Ref.10 Ref.11 Ref.13

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

Highly expressed in testis and spleen. Also expressed in retina, colon, small intestine, ovary, thymus, prostate, muscle, heart and kidney. Isoform 1 is expressed in skeletal muscle and heart muscle. Ref.1

Domain

The PDZ-binding motif mediates interaction with the CFTR, SLC9A3R1/EBP50 complex and probably with USH1C. Ref.9

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=24 mM for external sodium Ref.2

Ontologies

Keywords
   Biological processIon transport
Sodium transport
Symport
Transport
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   LigandSodium
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processauditory receptor cell development

Inferred from electronic annotation. Source: Ensembl

bicarbonate transport

Non-traceable author statement Ref.2. Source: UniProtKB

cochlear nucleus development

Inferred from electronic annotation. Source: Ensembl

ion transport

Traceable author statement. Source: Reactome

retina vasculature morphogenesis in camera-type eye

Inferred from electronic annotation. Source: Ensembl

retinal cell programmed cell death

Inferred from electronic annotation. Source: Ensembl

sodium ion transmembrane transport

Non-traceable author statement Ref.2. Source: GOC

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

basolateral plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Non-traceable author statement Ref.2. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

stereocilium

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioninorganic anion exchanger activity

Inferred from electronic annotation. Source: InterPro

sodium:bicarbonate symporter activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 14 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y6M7-1)

Also known as: mNBC3; NBCn1-A;

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: Q9Y6M7-2)

Also known as: NBCn1-F;

The sequence of this isoform differs from the canonical sequence as follows:
     251-374: Missing.
Note: Contains a phosphoserine at position 258. Contains a phosphoserine at position 255.
Isoform 3 (identifier: Q9Y6M7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.
     91-118: SQRVQFILGTEDDDEEHIPHDLFTEMDE → MAVTQFIHFREEIMGNMFFIIIFSTKDK
     251-374: Missing.
     1189-1214: PDKPVSVKISFEDEPRKKYVDAETSL → GDPSIGNISDEMAKTAQWKALSMNTENAKVTRSNMSPDKPVSVK
Note: Contains a phosphoserine at position 168. Contains a phosphoserine at position 1010. Contains a phosphoserine at position 1016. Contains a phosphoserine at position 165. Contains a phosphoserine at position 1007.
Isoform 4 (identifier: Q9Y6M7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.
     91-118: SQRVQFILGTEDDDEEHIPHDLFTEMDE → MAVTQFIHFREEIMGNMFFIIIFSTKDK
     251-374: Missing.
Note: Contains a phosphoserine at position 168. Contains a phosphoserine at position 165.
Isoform 5 (identifier: Q9Y6M7-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-450: Missing.
     451-465: PAVLLTGLTEVPVPT → MEVVEAEKIVLLTSA
     1188-1188: S → SVDPSIVNISDEMAKTAQWKALSMNTENAKVTRSNMS
Note: No experimental confirmation available. Contains a phosphoserine at position 774. Contains a phosphoserine at position 780. Contains a phosphoserine at position 742. Contains a phosphoserine at position 771.
Isoform 6 (identifier: Q9Y6M7-6)

Also known as: NBCn1-G;

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MERFRLEKKLP → MEADGAGEQMRPLLTR
     251-374: Missing.
     1188-1188: S → SVDPSIVNISDEMAKTAQWKALSMNTENAKVTRSNMS
Note: Contains a phosphoserine at position 263. Contains a phosphoserine at position 1105. Contains a phosphoserine at position 1111. Contains a phosphoserine at position 1073. Contains a phosphoserine at position 260. Contains a phosphoserine at position 1102.
Isoform 7 (identifier: Q9Y6M7-7)

Also known as: NBCn1-D;

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MERFRLEKKLP → MEADGAGEQMRPLLTRVTSR
     1188-1188: S → SVDPSIVNISDEMAKTAQWKALSMNTENAKVTRSNMS
Note: Contains a phosphoserine at position 1233. Contains a phosphoserine at position 1239. Contains a phosphoserine at position 1201. Contains a phosphoserine at position 1230.
Isoform 8 (identifier: Q9Y6M7-8)

Also known as: NBCn1-C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MERFRLEKKLP → MEADGAGEQMRPLLTRVTSR
     238-250: Missing.
     1188-1188: S → SVDPSIVNISDEMAKTAQWKALSMNTENAKVTRSNMS
Note: Contains a phosphoserine at position 1220. Contains a phosphoserine at position 1226. Contains a phosphoserine at position 1188. Contains a phosphoserine at position 1217.
Isoform 9 (identifier: Q9Y6M7-9)

Also known as: NBCn1-E;

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MERFRLEKKLP → MEADGAGEQMRPLLTR
     251-374: Missing.
Note: Contains a phosphoserine at position 263. Contains a phosphoserine at position 260.
Isoform 10 (identifier: Q9Y6M7-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MERFRLEKKLP → MEADGAGEQMRPLLTR
     238-250: Missing.
     581-582: LF → VQ
     583-1214: Missing.
Isoform 11 (identifier: Q9Y6M7-11)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MERFRLEKKLP → MEADGAGEQMRPLLTR
     251-374: Missing.
     581-582: LF → VQ
     583-1214: Missing.
Note: Contains a phosphoserine at position 263. Contains a phosphoserine at position 260.
Isoform 12 (identifier: Q9Y6M7-12)

Also known as: NBCn1-H;

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MERFRLEKKLP → MEADGAGEQMRPLLTR
     238-250: Missing.
Isoform 13 (identifier: Q9Y6M7-13)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MERFRLEKKLP → MEADGAGEQMRPLLTRVTSR
     251-374: Missing.
     1188-1188: S → SVDPSIVNISDEMAKTAQWKALSMNTENAKVTRSNMS
Note: Contains a phosphoserine at position 267. Contains a phosphoserine at position 1109. Contains a phosphoserine at position 1115. Contains a phosphoserine at position 1077. Contains a phosphoserine at position 264. Contains a phosphoserine at position 1106.
Isoform 14 (identifier: Q9Y6M7-14)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MERFRLEKKLP → MEADGAGEQMRPLLTRVTSR
     251-374: Missing.
     581-582: LF → VQ
     583-1214: Missing.
Note: Contains a phosphoserine at position 267. Contains a phosphoserine at position 264.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12141214Sodium bicarbonate cotransporter 3
PRO_0000079233

Regions

Topological domain1 – 608608Extracellular Potential
Transmembrane609 – 62921Helical; Potential
Topological domain630 – 6378Cytoplasmic Potential
Transmembrane638 – 65821Helical; Potential
Topological domain659 – 69537Extracellular Potential
Transmembrane696 – 71621Helical; Potential
Topological domain717 – 7259Cytoplasmic Potential
Transmembrane726 – 74621Helical; Potential
Topological domain747 – 81771Extracellular Potential
Transmembrane818 – 83821Helical; Potential
Topological domain839 – 86123Cytoplasmic Potential
Transmembrane862 – 88221Helical; Potential
Topological domain883 – 90826Extracellular Potential
Transmembrane909 – 92921Helical; Potential
Topological domain930 – 95425Cytoplasmic Potential
Transmembrane955 – 97521Helical; Potential
Topological domain976 – 101136Extracellular Potential
Transmembrane1012 – 103221Helical; Potential
Topological domain1033 – 10342Cytoplasmic Potential
Transmembrane1035 – 105521Helical; Potential
Topological domain1056 – 109237Extracellular Potential
Transmembrane1093 – 111321Helical; Potential
Topological domain1114 – 1214101Cytoplasmic Potential
Region1134 – 11363CA2-binding
Motif1211 – 12144PDZ-binding

Amino acid modifications

Modified residue521Phosphoserine By similarity
Modified residue2331Phosphoserine By similarity
Modified residue2421Phosphoserine Ref.21
Modified residue4031Phosphoserine Ref.16 Ref.21
Modified residue4071Phosphoserine By similarity
Modified residue11671Phosphothreonine Ref.15 Ref.19
Modified residue11761Phosphoserine Ref.15 Ref.19 Ref.20
Modified residue12131Phosphoserine Ref.16
Glycosylation1711N-linked (GlcNAc...) Potential
Glycosylation2691N-linked (GlcNAc...) Potential
Glycosylation3981N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation7761N-linked (GlcNAc...) Ref.18
Glycosylation7861N-linked (GlcNAc...) Ref.18
Glycosylation7911N-linked (GlcNAc...) Ref.18

Natural variations

Alternative sequence1 – 450450Missing in isoform 5.
VSP_047838
Alternative sequence1 – 9090Missing in isoform 3 and isoform 4.
VSP_047839
Alternative sequence1 – 1111MERFRLEKKLP → MEADGAGEQMRPLLTR in isoform 6, isoform 9, isoform 10, isoform 11 and isoform 12.
VSP_047840
Alternative sequence1 – 1111MERFRLEKKLP → MEADGAGEQMRPLLTRVTSR in isoform 7, isoform 8, isoform 13 and isoform 14.
VSP_047841
Alternative sequence91 – 11828SQRVQ…TEMDE → MAVTQFIHFREEIMGNMFFI IIFSTKDK in isoform 3 and isoform 4.
VSP_047842
Alternative sequence238 – 25013Missing in isoform 8, isoform 10 and isoform 12.
VSP_047843
Alternative sequence251 – 374124Missing in isoform 2, isoform 3, isoform 4, isoform 6, isoform 9, isoform 11, isoform 13 and isoform 14.
VSP_047844
Alternative sequence451 – 46515PAVLL…VPVPT → MEVVEAEKIVLLTSA in isoform 5.
VSP_047845
Alternative sequence581 – 5822LF → VQ in isoform 10, isoform 11 and isoform 14.
VSP_047846
Alternative sequence583 – 1214632Missing in isoform 10, isoform 11 and isoform 14.
VSP_047847
Alternative sequence11881S → SVDPSIVNISDEMAKTAQWK ALSMNTENAKVTRSNMS in isoform 5, isoform 6, isoform 7, isoform 8 and isoform 13.
VSP_047848
Alternative sequence1189 – 121426PDKPV…AETSL → GDPSIGNISDEMAKTAQWKA LSMNTENAKVTRSNMSPDKP VSVK in isoform 3.
VSP_047849
Natural variant3261E → K. Ref.2 Ref.4
Corresponds to variant rs3755652 [ dbSNP | Ensembl ].
VAR_055317

Experimental info

Mutagenesis1135 – 11362DD → NN: Loss of interaction with CA2. Loss of regulation by CA2.
Mutagenesis1163 – 11653DDD → NNN: No effect on interaction with CA2. No effect on regulation by CA2. Ref.11
Mutagenesis12141L → G: Loss of interaction with ATP6V1B1. Ref.10

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (mNBC3) (NBCn1-A) [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 7B4ADA1E3F26813C

FASTA1,214136,044
        10         20         30         40         50         60 
MERFRLEKKL PGPDEEAVVD LGKTSSTVNT KFEKEELESH RAVYIGVHVP FSKESRRRHR 

        70         80         90        100        110        120 
HRGHKHHHRR RKDKESDKED GRESPSYDTP SQRVQFILGT EDDDEEHIPH DLFTEMDELC 

       130        140        150        160        170        180 
YRDGEEYEWK ETARWLKFEE DVEDGGDRWS KPYVATLSLH SLFELRSCIL NGTVMLDMRA 

       190        200        210        220        230        240 
STLDEIADMV LDNMIASGQL DESIRENVRE ALLKRHHHQN EKRFTSRIPL VRSFADIGKK 

       250        260        270        280        290        300 
HSDPHLLERN GEGLSASRHS LRTGLSASNL SLRGESPLSL LLGHLLPSSR AGTPAGSRCT 

       310        320        330        340        350        360 
TPVPTPQNSP PSSPSISRLT SRSSQESQRQ APELLVSPAS DDIPTVVIHP PEEDLEAALK 

       370        380        390        400        410        420 
GEEQKNEENV DLTPGILASP QSAPGNLDNS KSGEIKGNGS GGSRENSTVD FSKVDMNFMR 

       430        440        450        460        470        480 
KIPTGAEASN VLVGEVDFLE RPIIAFVRLA PAVLLTGLTE VPVPTRFLFL LLGPAGKAPQ 

       490        500        510        520        530        540 
YHEIGRSIAT LMTDEIFHDV AYKAKDRNDL LSGIDEFLDQ VTVLPPGEWD PSIRIEPPKS 

       550        560        570        580        590        600 
VPSQEKRKIP VFHNGSTPTL GETPKEAAHH AGPELQRTGR LFGGLILDIK RKAPFFLSDF 

       610        620        630        640        650        660 
KDALSLQCLA SILFLYCACM SPVITFGGLL GEATEGRISA IESLFGASLT GIAYSLFAGQ 

       670        680        690        700        710        720 
PLTILGSTGP VLVFEKILYK FCRDYQLSYL SLRTSIGLWT SFLCIVLVAT DASSLVCYIT 

       730        740        750        760        770        780 
RFTEEAFAAL ICIIFIYEAL EKLFDLGETY AFNMHNNLDK LTSYSCVCTE PPNPSNETLA 

       790        800        810        820        830        840 
QWKKDNITAH NISWRNLTVS ECKKLRGVFL GSACGHHGPY IPDVLFWCVI LFFTTFFLSS 

       850        860        870        880        890        900 
FLKQFKTKRY FPTKVRSTIS DFAVFLTIVI MVTIDYLVGV PSPKLHVPEK FEPTHPERGW 

       910        920        930        940        950        960 
IISPLGDNPW WTLLIAAIPA LLCTILIFMD QQITAVIINR KEHKLKKGAG YHLDLLMVGV 

       970        980        990       1000       1010       1020 
MLGVCSVMGL PWFVAATVLS ISHVNSLKVE SECSAPGEQP KFLGIREQRV TGLMIFILMG 

      1030       1040       1050       1060       1070       1080 
LSVFMTSVLK FIPMPVLYGV FLYMGVSSLK GIQLFDRIKL FGMPAKHQPD LIYLRYVPLW 

      1090       1100       1110       1120       1130       1140 
KVHIFTVIQL TCLVLLWVIK VSAAAVVFPM MVLALVFVRK LMDLCFTKRE LSWLDDLMPE 

      1150       1160       1170       1180       1190       1200 
SKKKKEDDKK KKEKEEAERM LQDDDDTVHL PFEGGSLLQI PVKALKYSPD KPVSVKISFE 

      1210 
DEPRKKYVDA ETSL 

« Hide

Isoform 2 (NBCn1-F) [UniParc].

Checksum: 541839CC9B565896
Show »

FASTA1,090123,081
Isoform 3 [UniParc].

Checksum: A37799D93A1E30BC
Show »

FASTA1,018114,205
Isoform 4 [UniParc].

Checksum: 50FAA40A31468223
Show »

FASTA1,000112,448
Isoform 5 [UniParc].

Checksum: D7FB5D3479BB0935
Show »

FASTA80089,745
Isoform 6 (NBCn1-G) [UniParc].

Checksum: D3DC49DE4DD7F133
Show »

FASTA1,131127,359
Isoform 7 (NBCn1-D) [UniParc].

Checksum: DDE8C01EB6C6E00F
Show »

FASTA1,259140,766
Isoform 8 (NBCn1-C) [UniParc].

Checksum: DEA67883267065E6
Show »

FASTA1,246139,254
Isoform 9 (NBCn1-E) [UniParc].

Checksum: A3CD8C2972A7DFB3
Show »

FASTA1,095123,409
Isoform 10 [UniParc].

Checksum: 57ECD93FDB48A158
Show »

FASTA57463,699
Isoform 11 [UniParc].

Checksum: BFD9ACB2B9362149
Show »

FASTA46352,249
Isoform 12 (NBCn1-H) [UniParc].

Checksum: 8A29DF5AD5ECE7E6
Show »

FASTA1,206134,860
Isoform 13 [UniParc].

Checksum: 77E065DA75256869
Show »

FASTA1,135127,803
Isoform 14 [UniParc].

Checksum: 80F478ACDCBA905A
Show »

FASTA46752,692

References

« Hide 'large scale' references
[1]"Molecular cloning of a new sodium bicarbonate cotransporter cDNA from human retina."
Ishibashi K., Sasaki S., Marumo F.
Biochem. Biophys. Res. Commun. 246:535-538(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
Tissue: Retina.
[2]"Cloning, tissue distribution, genomic organization, and functional characterization of NBC3, a new member of the sodium bicarbonate cotransporter family."
Pushkin A., Abuladze N., Lee I., Newman D., Hwang J., Kurtz I.
J. Biol. Chem. 274:16569-16575(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, REGULATION, VARIANT LYS-326.
Tissue: Kidney and Skeletal muscle.
[3]"Cloning of a HCO3 transporter, NT2-NBC, from human brain, similar to both the Anion exchangers (AEs) and the Na/Bicarbonate Cotransporters (NBCs)."
Romero M.F.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Neuroepithelium.
[4]"Cloning and identification of novel human NBCn1 splice variants."
Liu Y., Chen L.-M., Parker M.D., Boron W.F.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; 7; 8; 9; 10; 11 AND 12), ALTERNATIVE SPLICING, VARIANT LYS-326.
Tissue: Brain, Heart, Liver and Skeletal muscle.
[5]"Cloning and identification of two novel human NBCn1 splice variants."
Liu Y., Chen L., Parker M.D., Boron W.F.
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 13 AND 14).
Tissue: Brain.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Cervix.
[7]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: FUNCTION, INTERACTION WITH CFTR AND SLC9A3R1, DOMAIN.
[10]"The COOH termini of NBC3 and the 56-kDa H+-ATPase subunit are PDZ motifs involved in their interaction."
Pushkin A., Abuladze N., Newman D., Muronets V., Sassani P., Tatishchev S., Kurtz I.
Am. J. Physiol. 284:C667-C673(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATP6V1B1 AND SLC9A3R1, MUTAGENESIS OF LEU-1214.
[11]"Regulation of the human NBC3 Na+/HCO3- cotransporter by carbonic anhydrase II and PKA."
Loiselle F.B., Morgan P.E., Alvarez B.V., Casey J.R.
Am. J. Physiol. 286:C1423-C1433(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CA2, REGULATION, MUTAGENESIS OF 1135-ASP-ASP-1136 AND 1163-ASP--ASP-1165.
[12]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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.
[14]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1167 AND SER-1176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-1213, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 (ISOFORMS 11; 6 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1109 AND SER-1115 (ISOFORM 13), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267 (ISOFORMS 13 AND 14), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1010 AND SER-1016 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 (ISOFORMS 3 AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774 AND SER-780 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1105 AND SER-1111 (ISOFORM 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1233 AND SER-1239 (ISOFORM 7), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1220 AND SER-1226 (ISOFORM 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Modular structure of sodium-coupled bicarbonate transporters."
Boron W.F., Chen L., Parker M.D.
J. Exp. Biol. 212:1697-1706(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, ALTERNATIVE SPLICING.
[18]"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-776; ASN-786 AND ASN-791.
Tissue: Leukemic T-cell.
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1167 AND SER-1176, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 (ISOFORMS 11; 6 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1077 (ISOFORM 13), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267 (ISOFORMS 13 AND 14), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 (ISOFORMS 3 AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1073 (ISOFORM 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1201 (ISOFORM 7), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1188 (ISOFORM 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1176, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260 AND SER-263 (ISOFORMS 11; 6 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1106 AND SER-1109 (ISOFORM 13), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-267 (ISOFORMS 13 AND 14), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-258 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1007 AND SER-1010 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-168 (ISOFORMS 3 AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-771 AND SER-774 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1102 AND SER-1105 (ISOFORM 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1230 AND SER-1233 (ISOFORM 7), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217 AND SER-1220 (ISOFORM 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242 AND SER-403, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 (ISOFORMS 11; 6 AND 9), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1106 (ISOFORM 13), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267 (ISOFORMS 13 AND 14), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1007 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 (ISOFORMS 3 AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-771 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1102 (ISOFORM 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1230 (ISOFORM 7), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217 (ISOFORM 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB012130 mRNA. Translation: BAA25898.1.
AF047033 mRNA. Translation: AAD38322.1.
AF089726 mRNA. Translation: AAG16773.1.
AF053755 mRNA. Translation: AAF21720.1.
EU499349 mRNA. Translation: ACB47400.1.
EU934246 mRNA. Translation: ACH61958.1.
EU934248 mRNA. Translation: ACH61960.1.
EU934249 mRNA. Translation: ACH61961.1.
EU934250 mRNA. Translation: ACH61962.1.
FJ178574 mRNA. Translation: ACI24740.1.
FJ178575 mRNA. Translation: ACI24741.1.
FJ178576 mRNA. Translation: ACI24742.1.
GU354307 mRNA. Translation: ADC32649.1.
GU354308 mRNA. Translation: ADC32650.1.
GU354309 mRNA. Translation: ADC32651.1.
GU354310 mRNA. Translation: ADC32652.1.
CR627428 mRNA. Translation: CAH10515.1.
AC099535 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64382.1.
PIRJE0160.
RefSeqNP_001245308.1. NM_001258379.1.
NP_001245309.1. NM_001258380.1.
NP_003606.3. NM_003615.4.
XP_005265658.1. XM_005265601.1.
UniGeneHs.250072.

3D structure databases

ProteinModelPortalQ9Y6M7.
SMRQ9Y6M7. Positions 110-552, 592-632, 1052-1084.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114876. 2 interactions.
MINTMINT-1632023.
STRING9606.ENSP00000295736.

Protein family/group databases

TCDB2.A.31.2.11. the anion exchanger (ae) family.

PTM databases

PhosphoSiteQ9Y6M7.

Polymorphism databases

DMDM229462789.

Proteomic databases

PaxDbQ9Y6M7.
PRIDEQ9Y6M7.

Protocols and materials databases

DNASU9497.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295736; ENSP00000295736; ENSG00000033867. [Q9Y6M7-1]
ENST00000388777; ENSP00000373429; ENSG00000033867. [Q9Y6M7-5]
ENST00000425128; ENSP00000401949; ENSG00000033867. [Q9Y6M7-10]
ENST00000428386; ENSP00000416368; ENSG00000033867. [Q9Y6M7-2]
ENST00000435667; ENSP00000395336; ENSG00000033867. [Q9Y6M7-13]
ENST00000437179; ENSP00000394252; ENSG00000033867. [Q9Y6M7-9]
ENST00000437266; ENSP00000409418; ENSG00000033867. [Q9Y6M7-11]
ENST00000438530; ENSP00000407304; ENSG00000033867. [Q9Y6M7-10]
ENST00000440156; ENSP00000414797; ENSG00000033867. [Q9Y6M7-8]
ENST00000446700; ENSP00000406605; ENSG00000033867. [Q9Y6M7-12]
ENST00000454389; ENSP00000390394; ENSG00000033867. [Q9Y6M7-7]
ENST00000455077; ENSP00000407382; ENSG00000033867. [Q9Y6M7-6]
ENST00000457377; ENSP00000408323; ENSG00000033867. [Q9Y6M7-11]
GeneID9497.
KEGGhsa:9497.
UCSCuc003cdu.5. human.
uc003cdv.4. human. [Q9Y6M7-1]
uc003cdw.4. human. [Q9Y6M7-2]
uc011awx.3. human.
uc011axa.3. human.

Organism-specific databases

CTD9497.
GeneCardsGC03M027414.
HGNCHGNC:11033. SLC4A7.
HPACAB022494.
HPA035857.
MIM603353. gene.
neXtProtNX_Q9Y6M7.
PharmGKBPA35899.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG268067.
HOGENOMHOG000280684.
HOVERGENHBG004326.
InParanoidQ9Y6M7.
KOK13858.
PhylomeDBQ9Y6M7.
TreeFamTF313630.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ9Y6M7.
BgeeQ9Y6M7.
CleanExHS_SLC4A7.
GenevestigatorQ9Y6M7.

Family and domain databases

Gene3D3.40.1100.10. 2 hits.
InterProIPR013769. Band3_cytoplasmic_dom.
IPR011531. HCO3_transpt_C.
IPR003020. HCO3_transpt_euk.
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.
SUPFAMSSF55804. SSF55804. 2 hits.
TIGRFAMsTIGR00834. ae. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSLC4A7. human.
GeneWikiSLC4A7.
GenomeRNAi9497.
NextBio35478003.
PROQ9Y6M7.
SOURCESearch...

Entry information

Entry nameS4A7_HUMAN
AccessionPrimary (citable) accession number: Q9Y6M7
Secondary accession number(s): A6NIA8 expand/collapse secondary AC list , B2CI53, B5M449, B5M451, B5M452, B5M453, B6DY52, B6DY53, C9JST9, D3K174, D3K175, O60350, Q6AHZ9, Q9HC88, Q9UIB9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: May 5, 2009
Last modified: April 16, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM