O88343 (S4A4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Electrogenic sodium bicarbonate cotransporter 1
Short name=Sodium bicarbonate cotransporter

Alternative name(s):
Na(+)/HCO3(-) cotransporter
Solute carrier family 4 member 4

Gene names

Name:	Slc4a4
Synonyms:	Nbc1, Nbce1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1079 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Electrogenic sodium/bicarbonate cotransporter with a Na+:HCO3- stoichiometry varying from 1:2 to 1:3. May regulate bicarbonate influx/efflux at the basolateral membrane of cells and regulate intracellular pH.
Enzyme regulation	Inhibited by stilbene derivatives and regulated by cyclic AMP.
Subunit structure	Interacts with CA2/carbonic anhydrase 2 and CA4/carbonic anhydrase 4 which may regulate transporter activity. Ref.9 Ref.10
Subcellular location	Basolateral cell membrane; Multi-pass membrane protein Ref.2.
Tissue specificity	Isoform 1 is specifically expressed in pancreatic ducts and acini. Also expressed in parotid acinar cells and in the colonic crypts. Ref.1 Ref.2 Ref.7 Ref.8
Post-translational modification	Phosphorylation of Ser-1026 by PKA increases the binding of CA2 and changes the Na+:HCO3- stoichiometry of the transporter from 3:1 to 2:1 By similarity. N-glycosylated. May not be necessary for the transporter basic functions. Ref.6
Sequence similarities	Belongs to the anion exchanger (TC 2.A.31) family. [View classification]

Ontologies

Keywords
Biological process	Ion transport Sodium transport Symport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Ligand	Sodium
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of pH Traceable author statement Ref.1. Source: MGI
Cellular_component	basolateral plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Traceable author statement Ref.1. Source: MGI
Molecular_function	inorganic anion exchanger activity Inferred from electronic annotation. Source: InterPro sodium:bicarbonate symporter activity Inferred from sequence or structural similarity Ref.1. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O88343-1)

Also known as: pNBC;

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: O88343-2)

Also known as: kNBC;

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.
     45-85: HKRKAGHKEK...SSSSILKPLI → MSTENVEGKP...FNHSIFTSAV

Isoform 3 (identifier: O88343-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.
     45-85: HKRKAGHKEK...SSSSILKPLI → MSTENVEGKP...FNHSIFTSAV
     185-201: MIADHQIETGLLKPDLK → LLGESRKVIRPAGFIRP
     202-1079: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1079	1079	Electrogenic sodium bicarbonate cotransporter 1		PRO_0000079228
Regions
	Topological domain	1 – 468	468	Cytoplasmic Potential
	Transmembrane	469 – 488	20	Helical; Potential
	Topological domain	489 – 504	16	Extracellular Potential
	Transmembrane	505 – 526	22	Helical; Potential
	Topological domain	527 – 554	28	Cytoplasmic Potential
	Transmembrane	555 – 580	26	Helical; Potential
	Topological domain	581 – 691	111	Extracellular Potential
	Transmembrane	692 – 710	19	Helical; Potential
	Topological domain	711 – 725	15	Cytoplasmic Potential
	Transmembrane	726 – 748	23	Helical; Potential
	Topological domain	749 – 777	29	Extracellular Potential
	Transmembrane	778 – 797	20	Helical; Potential
	Topological domain	798 – 822	25	Cytoplasmic Potential
	Transmembrane	823 – 847	25	Helical; Potential
	Topological domain	848 – 881	34	Extracellular Potential
	Transmembrane	882 – 901	20	Helical; Potential
	Topological domain	902 – 949	48	Cytoplasmic Potential
	Transmembrane	950 – 967	18	Helical; Potential
	Topological domain	968 – 970	3	Extracellular Potential
	Transmembrane	971 – 986	16	Helical; Potential
	Topological domain	987 – 1079	93	Cytoplasmic Potential
	Region	748 – 779	32	Interaction with CA4 By similarity
	Region	1002 – 1004	3	CA2-binding By similarity
	Region	1030 – 1033	4	CA2-binding By similarity
	Region	1057 – 1059	3	Required for basolateral targeting By similarity
	Compositional bias	1009 – 1024	16	Lys-rich
Amino acid modifications
	Modified residue	30	1	Phosphotyrosine Ref.12
	Modified residue	254	1	Phosphothreonine Ref.11 Ref.14
	Modified residue	255	1	Phosphoserine Ref.11
	Modified residue	257	1	Phosphoserine Ref.14
	Modified residue	262	1	Phosphoserine Ref.14
	Modified residue	1026	1	Phosphoserine; by PKA By similarity
	Modified residue	1029	1	Phosphoserine Ref.14
	Modified residue	1034	1	Phosphoserine Ref.13 Ref.14
	Glycosylation	641	1	N-linked (GlcNAc...) By similarity
	Glycosylation	661	1	N-linked (GlcNAc...) By similarity
Natural variations
	Alternative sequence	1 – 44	44	Missing in isoform 2 and isoform 3.		VSP_016709
	Alternative sequence	45 – 85	41	HKRKA…LKPLI → MSTENVEGKPNNLGERGRAR SSTFLRVFQPMFNHSIFTSA V in isoform 2 and isoform 3.		VSP_016710
	Alternative sequence	185 – 201	17	MIADH…KPDLK → LLGESRKVIRPAGFIRP in isoform 3.		VSP_016711
	Alternative sequence	202 – 1079	878	Missing in isoform 3.		VSP_016712
Experimental info
	Sequence conflict	388	1	T → A in AAC40160. Ref.1
	Sequence conflict	546	1	H → N in AAC40160. Ref.1
	Sequence conflict	560	1	W → R in AAC40160. Ref.1
	Sequence conflict	564	1	M → L in AAC40160. Ref.1
	Sequence conflict	567	1	V → I in AAC40160. Ref.1
	Sequence conflict	589	1	S → P in AAC40160. Ref.1
	Sequence conflict	740	1	C → G in AAC40160. Ref.1
	Sequence conflict	775	1	G → E in AAC40160. Ref.1
	Sequence conflict	814	1	K → Q in AAC40160. Ref.1
	Sequence conflict	832	1	V → I in AAC40160. Ref.1
	Sequence conflict	835	1	F → L in AAC40160. Ref.1
	Sequence conflict	848	1	S → F in AAD31036. Ref.2
	Sequence conflict	876	1	Q → P in AAD31036. Ref.2
	Sequence conflict	884	1	F → L in AAC40160. Ref.1
	Sequence conflict	901	1	P → R in AAD31036. Ref.2
	Sequence conflict	909 – 910	2	FL → SW in AAD31036. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (pNBC) [UniParc]. Last modified December 20, 2005. Version 2. Checksum: DBC7C3DEBE10BE97	FASTA	1,079	121,484
	10 20 30 40 50 60 MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKAG HKEKKEKERI 70 80 90 100 110 120 SENYSDKSDV ENADESSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT ELDELLAVDG 130 140 150 160 170 180 QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCMEKGSI MLDREASSLP 190 200 210 220 230 240 QLVEMIADHQ IETGLLKPDL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASRMFSN 250 260 270 280 290 300 PDNGSPAMTH RNLTSSSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG EVDFLDTPFI 310 320 330 340 350 360 AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD EVFHDIAYKA 370 380 390 400 410 420 KDRHDLIAGI DEFLDEVIVL PPGEWDPTIR IEPPKSLPSS DKRKNMYSGG ENVQMNGDTP 430 440 450 460 470 480 HDGGHGGGGH GDCEELQRTG RFCGGLIKDI KRKAPFFASD FYDALNIQAL SAILFIYLAT 490 500 510 520 530 540 VTNAITFGGL LGDATDNMQG VLESFLGTAV SGAIFCLFAG QPLTILSSTG PVLVFERLLF 550 560 570 580 590 600 NFSKDHNFDY LEFRLWIGLW SAFMCLVLVA TDASFLVQYF TRFTEEGFSS LISFIFIYDA 610 620 630 640 650 660 FKKMIKLADY YPINSDFKVG YNTHFSCACL PPDPVNLSVS NDTTLAPEDL PTISSTDMYH 670 680 690 700 710 720 NVTFDWAYLS KKECVKYGGK LVGNNCDFVP DITLMSFILF LGTYTSSMAM KKFKTSRYFP 730 740 750 760 770 780 TTARKLISDF AIILSILIFC VIDALVGVDT PKLIVPSEFK PTSPNRGWFV PPFGGNPWWV 790 800 810 820 830 840 CLAAAIPALL VTILIFMDQQ ITAVIVNRKE HKLKKGAGYH LDLFWVAILM VVCSFMALPW 850 860 870 880 890 900 YVAATVISIA HIDSLKMETE TSAPGEQPKF LGVREQRVTG TLVFILTGLS VFMAPILKFI 910 920 930 940 950 960 PMPVLYGVFL YMGVASLNGV QFMDRLKLLL MPLKHQPDFI YLRHVPLRRV HLFTFLQVLC 970 980 990 1000 1010 1020 LALLWILKST VAAIIFPVMI LALVAVRKGM DYLFSQHDLS FLDDVIPEKD KKKKEDEKKK 1030 1040 1050 1060 1070 KKKKGSLDSD NDDSDCPYSE KVPSIKIPMD IMEQQPFLSD NKPLDRERSS TFLERHTSC
	Isoform 2 (kNBC) [UniParc]. Checksum: 75CD2F7008D52ADE	FASTA	1,035	116,182
	10 20 30 40 50 60 MSTENVEGKP NNLGERGRAR SSTFLRVFQP MFNHSIFTSA VSPAAERIRF ILGEEDDSPA 70 80 90 100 110 120 PPQLFTELDE LLAVDGQEME WKETARWIKF EEKVEQGGER WSKPHVATLS LHSLFELRTC 130 140 150 160 170 180 MEKGSIMLDR EASSLPQLVE MIADHQIETG LLKPDLKDKV TYTLLRKHRH QTKKSNLRSL 190 200 210 220 230 240 ADIGKTVSSA SRMFSNPDNG SPAMTHRNLT SSSLNDISDK PEKDQLKNKF MKKLPRDAEA 250 260 270 280 290 300 SNVLVGEVDF LDTPFIAFVR LQQAVMLGAL TEVPVPTRFL FILLGPKGKA KSYHEIGRAI 310 320 330 340 350 360 ATLMSDEVFH DIAYKAKDRH DLIAGIDEFL DEVIVLPPGE WDPTIRIEPP KSLPSSDKRK 370 380 390 400 410 420 NMYSGGENVQ MNGDTPHDGG HGGGGHGDCE ELQRTGRFCG GLIKDIKRKA PFFASDFYDA 430 440 450 460 470 480 LNIQALSAIL FIYLATVTNA ITFGGLLGDA TDNMQGVLES FLGTAVSGAI FCLFAGQPLT 490 500 510 520 530 540 ILSSTGPVLV FERLLFNFSK DHNFDYLEFR LWIGLWSAFM CLVLVATDAS FLVQYFTRFT 550 560 570 580 590 600 EEGFSSLISF IFIYDAFKKM IKLADYYPIN SDFKVGYNTH FSCACLPPDP VNLSVSNDTT 610 620 630 640 650 660 LAPEDLPTIS STDMYHNVTF DWAYLSKKEC VKYGGKLVGN NCDFVPDITL MSFILFLGTY 670 680 690 700 710 720 TSSMAMKKFK TSRYFPTTAR KLISDFAIIL SILIFCVIDA LVGVDTPKLI VPSEFKPTSP 730 740 750 760 770 780 NRGWFVPPFG GNPWWVCLAA AIPALLVTIL IFMDQQITAV IVNRKEHKLK KGAGYHLDLF 790 800 810 820 830 840 WVAILMVVCS FMALPWYVAA TVISIAHIDS LKMETETSAP GEQPKFLGVR EQRVTGTLVF 850 860 870 880 890 900 ILTGLSVFMA PILKFIPMPV LYGVFLYMGV ASLNGVQFMD RLKLLLMPLK HQPDFIYLRH 910 920 930 940 950 960 VPLRRVHLFT FLQVLCLALL WILKSTVAAI IFPVMILALV AVRKGMDYLF SQHDLSFLDD 970 980 990 1000 1010 1020 VIPEKDKKKK EDEKKKKKKK GSLDSDNDDS DCPYSEKVPS IKIPMDIMEQ QPFLSDNKPL 1030 DRERSSTFLE RHTSC
	Isoform 3 [UniParc]. Checksum: 95E7EA3165687E5D	FASTA	157	17,829
	10 20 30 40 50 60 MSTENVEGKP NNLGERGRAR SSTFLRVFQP MFNHSIFTSA VSPAAERIRF ILGEEDDSPA 70 80 90 100 110 120 PPQLFTELDE LLAVDGQEME WKETARWIKF EEKVEQGGER WSKPHVATLS LHSLFELRTC 130 140 150 MEKGSIMLDR EASSLPQLVE LLGESRKVIR PAGFIRP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, chromosomal localization, tissue distribution, and functional expression of the human pancreatic sodium bicarbonate cotransporter." Abuladze N., Lee I., Newman D., Hwang J., Boorer K., Pushkin A., Kurtz I. J. Biol. Chem. 273:17689-17695(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Pancreas.
[2]	"Molecular and functional evidence for electrogenic and electroneutral Na(+)-HCO(3)(-) cotransporters in murine duodenum." Praetorius J., Hager H., Nielsen S., Aalkjaer C., Friis U.G., Ainsworth M.A., Johansen T. Am. J. Physiol. 280:G332-G343(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Strain: C57BL/6. Tissue: Duodenum.
[3]	"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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-400 (ISOFORM 1). Strain: C57BL/6J. Tissue: Kidney and Medulla oblongata.
[4]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-9; 60-67; 168-174; 323-331; 343-359; 607-618; 753-766; 857-869 AND 935-943, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[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] OF 382-1079. Strain: FVB/N. Tissue: Kidney.
[6]	"Role of glycosylation in the renal electrogenic Na+-HCO3-cotransporter (NBCe1)." Choi I., Hu L., Rojas J.D., Schmitt B.M., Boron W.F. Am. J. Physiol. 284:F1199-F1206(2003) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION.
[7]	"cAMP-mediated regulation of murine intestinal/pancreatic Na+/HCO3-cotransporter subtype pNBC1." Bachmann O., Rossmann H., Berger U.V., Colledge W.H., Ratcliff R., Evans M.J., Gregor M., Seidler U. Am. J. Physiol. 284:G37-G45(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REGULATION BY CAMP, TISSUE SPECIFICITY.
[8]	"Expression of Na+/HCO3- cotransporter and its role in pH regulation in mouse parotid acinar cells." Kim Y.-B., Yang B.H., Piao Z.G., Oh S.B., Kim J.S., Park K. Biochem. Biophys. Res. Commun. 304:593-598(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"Direct extracellular interaction between carbonic anhydrase IV and the human NBC1 sodium/bicarbonate co-transporter." Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R. Biochemistry 42:12321-12329(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CA4.
[10]	"Molecular mechanism of kNBC1-carbonic anhydrase II interaction in proximal tubule cells." Pushkin A., Abuladze N., Gross E., Newman D., Tatishchev S., Lee I., Fedotoff O., Bondar G., Azimov R., Ngyuen M., Kurtz I. J. Physiol. (Lond.) 559:55-65(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CA2.
[11]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254 AND SER-255, MASS SPECTROMETRY. Tissue: Liver.
[12]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, MASS SPECTROMETRY. Tissue: Brain.
[13]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, MASS SPECTROMETRY. Tissue: Liver.
[14]	"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 THR-254; SER-257; SER-262; SER-1029 AND SER-1034, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF020195 mRNA. Translation: AAC40160.1. AF141934 mRNA. Translation: AAD31036.3. AK085387 mRNA. Translation: BAC39437.1. AK140443 mRNA. Translation: BAE24389.1. BC026592 mRNA. Translation: AAH26592.1.
IPI	IPI00314749. IPI00405057. IPI00662028.
PIR	T14031.
RefSeq	NP_001129732.1. NM_001136260.1. NP_061230.2. NM_018760.2.
UniGene	Mm.41044.
3D structure databases
ProteinModelPortal	O88343.
SMR	O88343. Positions 453-493.
ModBase	Search...
Protein-protein interaction databases
IntAct	O88343. 2 interactions.
STRING	10090.ENSMUSP00000121744.
PTM databases
PhosphoSite	O88343.
Proteomic databases
PaxDb	O88343.
PRIDE	O88343.
Protocols and materials databases
DNASU	54403.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000113216; ENSMUSP00000108842; ENSMUSG00000060961. ENSMUST00000130041; ENSMUSP00000118413; ENSMUSG00000060961. ENSMUST00000148750; ENSMUSP00000119325; ENSMUSG00000060961.
GeneID	54403.
KEGG	mmu:54403.
UCSC	uc008yak.1. mouse. uc012dyd.1. mouse.
Organism-specific databases
CTD	8671.
MGI	MGI:1927555. Slc4a4.
Phylogenomic databases
eggNOG	NOG251607.
GeneTree	ENSGT00560000076851.
HOGENOM	HOG000280684.
HOVERGEN	HBG004326.
InParanoid	O88343.
KO	K13575.
OrthoDB	EOG4320XB.
Gene expression databases
ArrayExpress	O88343.
Bgee	O88343.
Genevestigator	O88343.
GermOnline	ENSMUSG00000060961. Mus musculus.
Family and domain databases
Gene3D	3.40.1100.10. 1 hit.
InterPro	IPR013769. Band3_cytoplasmic_dom. IPR011531. HCO3_transpt_C. IPR003020. HCO3_transpt_euk. IPR003024. Na/HCO3_transpt. IPR016152. PTrfase/Anion_transptr. [Graphical view]
PANTHER	PTHR11453. PTHR11453. 1 hit.
Pfam	PF07565. Band_3_cyto. 1 hit. PF00955. HCO3_cotransp. 1 hit. [Graphical view]
PRINTS	PR01231. HCO3TRNSPORT. PR01232. NAHCO3TRSPRT.
SUPFAM	SSF55804. PTrfase/Anion_transptr. 1 hit.
TIGRFAMs	TIGR00834. ae. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	SLC4A4. mouse.
NextBio	311268.
SOURCE	Search...

Entry information

Entry name

S4A4_MOUSE

Accession

Primary (citable) accession number: O88343
Secondary accession number(s): Q3USE4 , Q8BUG0, Q8QZR9, Q9R1C4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program