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Electrogenic sodium bicarbonate cotransporter 1 (Sodium bicarbonate cotransporter) (Na( )/HCO3(-) cotransporter) (Solute carrier family 4 member 4) (kNBC1)

 S4A4_HUMAN              Reviewed;        1079 AA.
Q9Y6R1; C4B714; O15153; Q8NEJ2; Q9H262; Q9NRZ1; Q9UIC0; Q9UIC1;
Q9UP50;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
07-NOV-2018, entry version 150.
RecName: Full=Electrogenic sodium bicarbonate cotransporter 1;
Short=Sodium bicarbonate cotransporter;
AltName: Full=Na(+)/HCO3(-) cotransporter;
AltName: Full=Solute carrier family 4 member 4;
AltName: Full=kNBC1;
Name=SLC4A4; Synonyms=NBC, NBC1, NBCE1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Kidney;
PubMed=9235899; DOI=10.1074/jbc.272.31.19111;
Burnham C.E., Amlal H., Wang Z., Shull G.E., Soleimani M.;
"Cloning and functional expression of a human kidney Na+:HCO3-
cotransporter.";
J. Biol. Chem. 272:19111-19114(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Pancreas;
PubMed=9651366; DOI=10.1074/jbc.273.28.17689;
Abuladze N., Lee I., Newman D., Hwang J., Boorer K., Pushkin A.,
Kurtz I.;
"Molecular cloning, chromosomal localization, tissue distribution, and
functional expression of the human pancreatic sodium bicarbonate
cotransporter.";
J. Biol. Chem. 273:17689-17695(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Heart, Kidney, and Prostate;
PubMed=10069984;
Choi I., Romero M.F., Khandoudi N., Bril A., Boron W.F.;
"Cloning and characterization of a human electrogenic Na+-HCO-3
cotransporter isoform (hhNBC).";
Am. J. Physiol. 276:C576-C584(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN CORNEAL
ENDOTHELIAL CELLS, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
TISSUE=Corneal endothelium;
PubMed=12907161; DOI=10.1016/S0014-4835(03)00150-7;
Sun X.C., Bonanno J.A.;
"Identification and cloning of the Na/HCO3- cotransporter (NBC) in
human corneal endothelium.";
Exp. Eye Res. 77:287-295(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Skeletal muscle;
Pushkin A., Abuladze N., Kurtz I.;
"Homo sapiens sodium bicarbonate cotransporter NBC1 splice variant.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Yamada H., Nagayoshi A., Kuroda Y., Mizutani A., Ando H., Seki G.,
Mikoshiba K.;
"cDNA cloning and characterization of human sodium bicarbonate
cotransporter, bNBC, a brain type splicing variant of SLC4A4 gene.";
Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
REGULATION, MUTAGENESIS OF SER-1026, AND PHOSPHORYLATION AT SER-1026.
PubMed=11744745; DOI=10.1113/jphysiol.2001.012956;
Gross E., Hawkins K., Pushkin A., Sassani P., Dukkipati R.,
Abuladze N., Hopfer U., Kurtz I.;
"Phosphorylation of Ser(982) in the sodium bicarbonate cotransporter
kNBC1 shifts the HCO(3)(-):Na(+) stoichiometry from 3:1 to 2:1 in
murine proximal tubule cells.";
J. Physiol. (Lond.) 537:659-665(2001).
[10]
ERRATUM.
Gross E., Hawkins K., Pushkin A., Sassani P., Dukkipati R.,
Abuladze N., Hopfer U., Kurtz I.;
J. Physiol. (Lond.) 538:1003-1003(2002).
[11]
TISSUE SPECIFICITY.
PubMed=11743927; DOI=10.1016/S0003-9969(01)00098-X;
Park K., Hurley P.T., Roussa E., Cooper G.J., Smith C.P., Thevenod F.,
Steward M.C., Case R.M.;
"Expression of a sodium bicarbonate cotransporter in human parotid
salivary glands.";
Arch. Oral Biol. 47:1-9(2002).
[12]
REGULATION, MUTAGENESIS OF ASP-1030; ASP-1032 AND ASP-1033, AND
INTERACTION WITH CA2.
PubMed=12411514; DOI=10.1113/jphysiol.2002.029777;
Gross E., Pushkin A., Abuladze N., Fedotoff O., Kurtz I.;
"Regulation of the sodium bicarbonate cotransporter kNBC1 function:
role of Asp(986), Asp(988) and kNBC1-carbonic anhydrase II binding.";
J. Physiol. (Lond.) 544:679-685(2002).
[13]
GLYCOSYLATION.
PubMed=12604466; DOI=10.1152/ajprenal.00131.2002;
Choi I., Hu L., Rojas J.D., Schmitt B.M., Boron W.F.;
"Role of glycosylation in the renal electrogenic Na+-HCO3-
cotransporter (NBCe1).";
Am. J. Physiol. 284:F1199-F1206(2003).
[14]
TISSUE SPECIFICITY.
PubMed=14559244; DOI=10.1016/j.bbrc.2003.09.147;
Yamada H., Yamazaki S., Moriyama N., Hara C., Horita S., Enomoto Y.,
Kudo A., Kawakami H., Tanaka Y., Fujita T., Seki G.;
"Localization of NBC-1 variants in human kidney and renal cell
carcinoma.";
Biochem. Biophys. Res. Commun. 310:1213-1218(2003).
[15]
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=12534288; DOI=10.1021/bi026826q;
Tatishchev S., Abuladze N., Pushkin A., Newman D., Liu W., Weeks D.,
Sachs G., Kurtz I.;
"Identification of membrane topography of the electrogenic sodium
bicarbonate cotransporter pNBC1 by in vitro
transcription/translation.";
Biochemistry 42:755-765(2003).
[16]
REGULATION, INTERACTION WITH CA2 AND CA4, AND MUTAGENESIS OF GLY-767.
PubMed=14567693; DOI=10.1021/bi0353124;
Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R.;
"Direct extracellular interaction between carbonic anhydrase IV and
the human NBC1 sodium/bicarbonate co-transporter.";
Biochemistry 42:12321-12329(2003).
[17]
REGULATION, MUTAGENESIS OF THR-49 AND SER-1026, AND PHOSPHORYLATION AT
THR-49.
PubMed=12730338; DOI=10.1113/jphysiol.2003.042226;
Gross E., Fedotoff O., Pushkin A., Abuladze N., Newman D., Kurtz I.;
"Phosphorylation-induced modulation of pNBC1 function: distinct roles
for the amino- and carboxy-termini.";
J. Physiol. (Lond.) 549:673-682(2003).
[18]
TISSUE SPECIFICITY.
PubMed=15329059; DOI=10.1111/j.1365-201X.2004.01297.x;
Kristensen J.M., Kristensen M., Juel C.;
"Expression of Na+/HCO3- co-transporter proteins (NBCs) in rat and
human skeletal muscle.";
Acta Physiol. Scand. 182:69-76(2004).
[19]
MUTAGENESIS OF PHE-1057, AND SUBCELLULAR LOCATION.
PubMed=15273250; DOI=10.1074/jbc.M405780200;
Li H.C., Worrell R.T., Matthews J.B., Husseinzadeh H., Neumeier L.,
Petrovic S., Conforti L., Soleimani M.;
"Identification of a carboxyl-terminal motif essential for the
targeting of Na+-HCO-3 cotransporter NBC1 to the basolateral
membrane.";
J. Biol. Chem. 279:43190-43197(2004).
[20]
INTERACTION WITH CA2, AND MUTAGENESIS OF 1002-LEU--ASN-1004 AND
1030-ASP--ASP-1033.
PubMed=15218065; DOI=10.1113/jphysiol.2004.065110;
Pushkin A., Abuladze N., Gross E., Newman D., Tatishchev S., Lee I.,
Fedotoff O., Bondar G., Azimov R., Ngyuen M., Kurtz I.;
"Molecular mechanism of kNBC1-carbonic anhydrase II interaction in
proximal tubule cells.";
J. Physiol. (Lond.) 559:55-65(2004).
[21]
INTERACTION WITH CA4.
PubMed=15563508; DOI=10.1093/hmg/ddi023;
Yang Z., Alvarez B.V., Chakarova C., Jiang L., Karan G.,
Frederick J.M., Zhao Y., Sauve Y., Li X., Zrenner E., Wissinger B.,
Den Hollander A.I., Katz B., Baehr W., Cremers F.P., Casey J.R.,
Bhattacharya S.S., Zhang K.;
"Mutant carbonic anhydrase 4 impairs pH regulation and causes retinal
photoreceptor degeneration.";
Hum. Mol. Genet. 14:255-265(2005).
[22]
MUTAGENESIS OF TYR-477; ASP-493; ALA-494; GLU-503; SER-504; GLU-536;
GLU-552; ARG-554; ARG-582; GLU-586; ASP-599; ALA-600; LYS-602;
LYS-603; ASP-691; PHE-700; LYS-711; LYS-712; LYS-714; THR-715;
THR-721; ARG-724; LYS-725; SER-728; ASP-729; ASP-743; ASP-749;
LYS-752; ARG-766; GLU-775; ASP-798; 808-ARG--LYS-809;
814-LYS--LYS-815; HIS-820; ASP-822; HIS-851; ASP-853;
858-GLU--GLU-860; 875-GLU--ARG-877; LYS-898; 925-ARG--LYS-927;
ARG-948; ARG-949; HIS-951; LYS-968 AND ARG-987.
PubMed=15817634; DOI=10.1113/jphysiol.2005.084988;
Abuladze N., Azimov R., Newman D., Sassani P., Liu W., Tatishchev S.,
Pushkin A., Kurtz I.;
"Critical amino acid residues involved in the electrogenic sodium-
bicarbonate cotransporter kNBC1-mediated transport.";
J. Physiol. (Lond.) 565:717-730(2005).
[23]
FUNCTION, FUNCTION (ISOFORM 2), AND INTERACTION WITH AHCYL1 (ISOFORM
1).
PubMed=16769890; DOI=10.1073/pnas.0602250103;
Shirakabe K., Priori G., Yamada H., Ando H., Horita S., Fujita T.,
Fujimoto I., Mizutani A., Seki G., Mikoshiba K.;
"IRBIT, an inositol 1,4,5-trisphosphate receptor-binding protein,
specifically binds to and activates pancreas-type Na+/HCO3-
cotransporter 1 (pNBC1).";
Proc. Natl. Acad. Sci. U.S.A. 103:9542-9547(2006).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254; SER-257 AND
SER-1034, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-641 AND ASN-661.
PubMed=25568315; DOI=10.1074/jbc.M114.619320;
Zhu Q., Kao L., Azimov R., Abuladze N., Newman D., Kurtz I.;
"Interplay between disulfide bonding and N-glycosylation defines SLC4
Na+-coupled transporter extracellular topography.";
J. Biol. Chem. 290:5391-5404(2015).
[26] {ECO:0000244|PDB:6CAA}
STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 77-1079,
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF
SER-527; 527-SER--THR-529; ASP-798; THR-802; VAL-842; ALA-844; THR-845
AND ILE-847.
PubMed=29500354; DOI=10.1038/s41467-018-03271-3;
Huynh K.W., Jiang J., Abuladze N., Tsirulnikov K., Kao L., Shao X.,
Newman D., Azimov R., Pushkin A., Zhou Z.H., Kurtz I.;
"CryoEM structure of the human SLC4A4 sodium-coupled acid-base
transporter NBCe1.";
Nat. Commun. 9:900-900(2018).
[27]
VARIANTS PRTA-OA SER-342 AND HIS-554.
PubMed=10545938; DOI=10.1038/15440;
Igarashi T., Inatomi J., Sekine T., Cha S.H., Kanai Y., Kunimi M.,
Tsukamoto K., Satoh H., Shimadzu M., Tozawa F., Mori T., Shiobara M.,
Seki G., Endou H.;
"Mutations in SLC4A4 cause permanent isolated proximal renal tubular
acidosis with ocular abnormalities.";
Nat. Genet. 23:264-266(1999).
[28]
VARIANT PRTA-OA LEU-471.
PubMed=15471865; DOI=10.1074/jbc.M406591200;
Dinour D., Chang M.-H., Satoh J., Smith B.L., Angle N., Knecht A.,
Serban I., Holtzman E.J., Romero M.F.;
"A novel missense mutation in the sodium bicarbonate cotransporter
(NBCe1/SLC4A4) causes proximal tubular acidosis and glaucoma through
ion transport defects.";
J. Biol. Chem. 279:52238-52246(2004).
[29]
VARIANTS PRTA-OA SER-342; LEU-471 AND HIS-554, AND MUTAGENESIS OF
GLU-135.
PubMed=15713912; DOI=10.1152/ajprenal.00032.2005;
Li H.C., Szigligeti P., Worrell R.T., Matthews J.B., Conforti L.,
Soleimani M.;
"Missense mutations in Na+:HCO3- cotransporter NBC1 show abnormal
trafficking in polarized kidney cells: a basis of proximal renal
tubular acidosis.";
Am. J. Physiol. 289:F61-F71(2005).
[30]
VARIANTS PRTA-OA SER-342; SER-529; HIS-554; VAL-843 AND CYS-925.
PubMed=15930088; DOI=10.1681/ASN.2004080667;
Horita S., Yamada H., Inatomi J., Moriyama N., Sekine T., Igarashi T.,
Endo Y., Dasouki M., Ekim M., Al-Gazali L., Shimadzu M., Seki G.,
Fujita T.;
"Functional analysis of NBC1 mutants associated with proximal renal
tubular acidosis and ocular abnormalities.";
J. Am. Soc. Nephrol. 16:2270-2278(2005).
[31]
VARIANT PRTA-OA PRO-566, CHARACTERIZATION OF VARIANT PRTA-OA PRO-566,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16636648;
Demirci F.Y., Chang M.H., Mah T.S., Romero M.F., Gorin M.B.;
"Proximal renal tubular acidosis and ocular pathology: a novel
missense mutation in the gene (SLC4A4) for sodium bicarbonate
cotransporter protein (NBCe1).";
Mol. Vis. 12:324-330(2006).
[32]
VARIANT PRTA-OA ARG-530, CHARACTERIZATION OF VARIANTS PRTA-OA SER-342
SER-529; ARG-530 AND PRO-566, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17661077; DOI=10.1007/s00424-007-0319-y;
Suzuki M., Vaisbich M.H., Yamada H., Horita S., Li Y., Sekine T.,
Moriyama N., Igarashi T., Endo Y., Cardoso T.P., de Sa L.C.,
Koch V.H., Seki G., Fujita T.;
"Functional analysis of a novel missense NBC1 mutation and of other
mutations causing proximal renal tubular acidosis.";
Pflugers Arch. 455:583-593(2008).
-!- 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. {ECO:0000269|PubMed:10069984,
ECO:0000269|PubMed:12907161, ECO:0000269|PubMed:16636648,
ECO:0000269|PubMed:16769890, ECO:0000269|PubMed:17661077,
ECO:0000269|PubMed:29500354, ECO:0000269|PubMed:9235899,
ECO:0000269|PubMed:9651366}.
-!- FUNCTION: Isoform 2: May have a higher activity than isoform 1.
{ECO:0000269|PubMed:16769890}.
-!- ACTIVITY REGULATION: Inhibited by stilbene derivatives and
regulated by cyclic AMP.
-!- SUBUNIT: Homodimer (PubMed:29500354). Interacts with CA2/carbonic
anhydrase 2 and CA4/carbonic anhydrase 4 which may regulate
transporter activity (PubMed:12411514, PubMed:14567693,
PubMed:15218065, PubMed:15563508). Isoform 1 but not isoform 2
interacts with AHCYL1 (via PEST domain when phosphorylated); the
interaction increases SLC4A4 isoform 1 activity (PubMed:16769890).
Interacts with AHCYL2 (By similarity).
{ECO:0000250|UniProtKB:O88343, ECO:0000250|UniProtKB:Q9GL77,
ECO:0000269|PubMed:12411514, ECO:0000269|PubMed:14567693,
ECO:0000269|PubMed:15218065, ECO:0000269|PubMed:15563508,
ECO:0000269|PubMed:16769890, ECO:0000269|PubMed:29500354}.
-!- INTERACTION:
P48283:CA4 (xeno); NbExp=2; IntAct=EBI-6859278, EBI-6859264;
-!- SUBCELLULAR LOCATION: Basolateral cell membrane
{ECO:0000269|PubMed:12907161, ECO:0000269|PubMed:15273250,
ECO:0000269|PubMed:16636648, ECO:0000269|PubMed:17661077,
ECO:0000305|PubMed:12534288, ECO:0000305|PubMed:29500354}; Multi-
pass membrane protein {ECO:0000269|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=hcNBC, hhNBC, hNBC1, pNBC, pNCB1, pNBC-1, NBC1b;
IsoId=Q9Y6R1-1; Sequence=Displayed;
Name=2; Synonyms=hkNBC, hkNBCe1, kNBC, kNBC1, kNBC-1, NBC1a;
IsoId=Q9Y6R1-2; Sequence=VSP_016704, VSP_016705;
Name=3;
IsoId=Q9Y6R1-3; Sequence=VSP_016704, VSP_016705, VSP_016706,
VSP_016707;
Name=4;
IsoId=Q9Y6R1-4; Sequence=VSP_016708;
Name=5;
IsoId=Q9Y6R1-5; Sequence=VSP_041003;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed in pancreas and to a
lower extent in heart, skeletal muscle, liver, parotid salivary
glands, prostate, colon, stomach, thyroid, brain and spinal chord.
Corneal endothelium cells express only isoform 1 (at protein
level). Isoform 2 is specifically expressed in kidney at the level
of proximal tubules. {ECO:0000269|PubMed:10069984,
ECO:0000269|PubMed:11743927, ECO:0000269|PubMed:12907161,
ECO:0000269|PubMed:14559244, ECO:0000269|PubMed:15329059,
ECO:0000269|PubMed:9235899, ECO:0000269|PubMed:9651366}.
-!- PTM: 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. Phosphorylated in presence of STK39 and
dephosphorylated in presence of PP1 phosphatase; phosphorylation
seems to inhibit SLC4A4 activity. {ECO:0000250|UniProtKB:O88343,
ECO:0000269|PubMed:11744745, ECO:0000269|PubMed:12730338}.
-!- PTM: N-glycosylation is not necessary for the transporter basic
functions. {ECO:0000269|PubMed:12604466}.
-!- DISEASE: Renal tubular acidosis, proximal, with ocular
abnormalities and mental retardation (pRTA-OA) [MIM:604278]: An
extremely rare autosomal recessive syndrome characterized by short
stature, profound proximal renal tubular acidosis, mental
retardation, bilateral glaucoma, cataracts and bandkeratopathy.
pRTA is due to a failure of the proximal tubular cells to reabsorb
filtered bicarbonate from the urine, leading to urinary
bicarbonate wasting and subsequent acidemia.
{ECO:0000269|PubMed:10545938, ECO:0000269|PubMed:15471865,
ECO:0000269|PubMed:15713912, ECO:0000269|PubMed:15930088,
ECO:0000269|PubMed:16636648, ECO:0000269|PubMed:17661077}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Note=Loss of interaction with and stimulation by CA4 is
the cause of retinitis pigmentosa type 17 (RP17).
-!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
{ECO:0000305}.
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EMBL; AF007216; AAC51645.1; -; mRNA.
EMBL; AF011390; AAC39840.1; -; mRNA.
EMBL; AF053753; AAF21718.1; -; mRNA.
EMBL; AF053754; AAF21719.1; -; mRNA.
EMBL; AF069510; AAD42020.1; -; mRNA.
EMBL; AF310248; AAG47773.1; -; mRNA.
EMBL; AF157492; AAF80343.1; -; mRNA.
EMBL; AB470072; BAH58226.1; -; mRNA.
EMBL; AC019089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC096713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC110783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC112226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC030977; AAH30977.1; -; mRNA.
CCDS; CCDS3549.1; -. [Q9Y6R1-2]
CCDS; CCDS43236.1; -. [Q9Y6R1-1]
CCDS; CCDS47071.1; -. [Q9Y6R1-5]
RefSeq; NP_001091954.1; NM_001098484.2. [Q9Y6R1-1]
RefSeq; NP_003750.1; NM_003759.3. [Q9Y6R1-2]
UniGene; Hs.5462; -.
PDB; 6CAA; EM; 3.90 A; A/B=77-1079.
PDBsum; 6CAA; -.
ProteinModelPortal; Q9Y6R1; -.
SMR; Q9Y6R1; -.
BioGrid; 114219; 1.
DIP; DIP-59373N; -.
IntAct; Q9Y6R1; 5.
MINT; Q9Y6R1; -.
STRING; 9606.ENSP00000393557; -.
DrugBank; DB01390; Sodium bicarbonate.
TCDB; 2.A.31.2.12; the anion exchanger (ae) family.
iPTMnet; Q9Y6R1; -.
PhosphoSitePlus; Q9Y6R1; -.
SwissPalm; Q9Y6R1; -.
BioMuta; SLC4A4; -.
DMDM; 74721543; -.
PaxDb; Q9Y6R1; -.
PeptideAtlas; Q9Y6R1; -.
PRIDE; Q9Y6R1; -.
ProteomicsDB; 86772; -.
ProteomicsDB; 86773; -. [Q9Y6R1-2]
ProteomicsDB; 86774; -. [Q9Y6R1-3]
ProteomicsDB; 86775; -. [Q9Y6R1-4]
ProteomicsDB; 86776; -. [Q9Y6R1-5]
DNASU; 8671; -.
Ensembl; ENST00000264485; ENSP00000264485; ENSG00000080493. [Q9Y6R1-1]
Ensembl; ENST00000340595; ENSP00000344272; ENSG00000080493. [Q9Y6R1-2]
Ensembl; ENST00000351898; ENSP00000307349; ENSG00000080493. [Q9Y6R1-4]
Ensembl; ENST00000425175; ENSP00000393557; ENSG00000080493. [Q9Y6R1-5]
Ensembl; ENST00000512686; ENSP00000422400; ENSG00000080493. [Q9Y6R1-3]
GeneID; 8671; -.
KEGG; hsa:8671; -.
UCSC; uc003hfy.4; human. [Q9Y6R1-1]
CTD; 8671; -.
DisGeNET; 8671; -.
EuPathDB; HostDB:ENSG00000080493.13; -.
GeneCards; SLC4A4; -.
HGNC; HGNC:11030; SLC4A4.
HPA; CAB022493; -.
HPA; HPA035628; -.
HPA; HPA035629; -.
MalaCards; SLC4A4; -.
MIM; 603345; gene.
MIM; 604278; phenotype.
neXtProt; NX_Q9Y6R1; -.
OpenTargets; ENSG00000080493; -.
Orphanet; 93607; Autosomal recessive proximal renal tubular acidosis.
PharmGKB; PA35898; -.
eggNOG; KOG1172; Eukaryota.
eggNOG; ENOG410XPHD; LUCA.
GeneTree; ENSGT00760000119021; -.
HOVERGEN; HBG004326; -.
InParanoid; Q9Y6R1; -.
KO; K13575; -.
OMA; DMYHNAT; -.
PhylomeDB; Q9Y6R1; -.
TreeFam; TF313630; -.
Reactome; R-HSA-425381; Bicarbonate transporters.
Reactome; R-HSA-5619054; Defective SLC4A4 causes renal tubular acidosis, proximal, with ocular abnormalities and mental retardation (pRTA-OA).
ChiTaRS; SLC4A4; human.
GeneWiki; SLC4A4; -.
GenomeRNAi; 8671; -.
PRO; PR:Q9Y6R1; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000080493; Expressed in 200 organ(s), highest expression level in duodenum.
CleanEx; HS_SLC4A4; -.
ExpressionAtlas; Q9Y6R1; baseline and differential.
Genevisible; Q9Y6R1; HS.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
GO; GO:0008510; F:sodium:bicarbonate symporter activity; IMP:UniProtKB.
GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
GO; GO:0006814; P:sodium ion transport; IDA:UniProtKB.
Gene3D; 3.40.930.10; -; 1.
InterPro; IPR013769; Band3_cytoplasmic_dom.
InterPro; IPR011531; HCO3_transpt_C.
InterPro; IPR003020; HCO3_transpt_euk.
InterPro; IPR003024; Na/HCO3_transpt.
InterPro; IPR016152; PTrfase/Anion_transptr.
PANTHER; PTHR11453; PTHR11453; 1.
Pfam; PF07565; Band_3_cyto; 1.
Pfam; PF00955; HCO3_cotransp; 1.
PRINTS; PR01231; HCO3TRNSPORT.
PRINTS; PR01232; NAHCO3TRSPRT.
SUPFAM; SSF55804; SSF55804; 1.
TIGRFAMs; TIGR00834; ae; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disease mutation; Disulfide bond; Glycoprotein; Ion transport;
Membrane; Phosphoprotein; Reference proteome; Retinitis pigmentosa;
Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 1079 Electrogenic sodium bicarbonate
cotransporter 1.
/FTId=PRO_0000079227.
TOPO_DOM 1 466 Cytoplasmic.
{ECO:0000269|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TRANSMEM 467 491 Helical; Name=1.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TOPO_DOM 492 501 Extracellular.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TRANSMEM 502 520 Helical; Name=2.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TOPO_DOM 521 521 Cytoplasmic.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TRANSMEM 522 542 Discontinuously helical; Name=3.
{ECO:0000305|PubMed:29500354}.
TOPO_DOM 543 550 Extracellular.
{ECO:0000269|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TRANSMEM 551 571 Helical; Name=4.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TOPO_DOM 572 585 Cytoplasmic.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TRANSMEM 586 609 Helical; Name=5.
{ECO:0000305|PubMed:29500354}.
TOPO_DOM 610 692 Extracellular.
{ECO:0000269|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TRANSMEM 693 710 Helical; Name=6.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TOPO_DOM 711 725 Cytoplasmic.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TRANSMEM 726 745 Helical; Name=7.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TOPO_DOM 746 779 Extracellular.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TRANSMEM 780 807 Helical; Name=8.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TOPO_DOM 808 819 Cytoplasmic.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TRANSMEM 820 836 Helical; Name=9.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TOPO_DOM 837 837 Extracellular.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TRANSMEM 838 855 Discontinuously helical; Name=10.
{ECO:0000305|PubMed:29500354}.
TOPO_DOM 856 877 Cytoplasmic.
{ECO:0000269|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TRANSMEM 878 894 Helical; Name=11.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TOPO_DOM 895 901 Extracellular.
{ECO:0000305|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
TRANSMEM 902 918 Helical; Name=12.
{ECO:0000305|PubMed:29500354}.
TOPO_DOM 919 960 Cytoplasmic.
{ECO:0000269|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
INTRAMEM 961 986 Discontinuously helical.
{ECO:0000305|PubMed:29500354}.
TOPO_DOM 987 1079 Cytoplasmic.
{ECO:0000269|PubMed:12534288,
ECO:0000305|PubMed:29500354}.
REGION 1 62 Required for interaction with AHCYL1.
{ECO:0000269|PubMed:16769890}.
REGION 748 779 Interaction with CA4.
REGION 1002 1004 CA2-binding.
REGION 1030 1033 CA2-binding.
REGION 1057 1059 Required for basolateral targeting.
COMPBIAS 1009 1024 Lys-rich.
MOD_RES 30 30 Phosphotyrosine.
{ECO:0000250|UniProtKB:O88343}.
MOD_RES 49 49 Phosphothreonine; by PKA.
{ECO:0000269|PubMed:12730338}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000250|UniProtKB:O88343}.
MOD_RES 65 65 Phosphoserine.
{ECO:0000250|UniProtKB:O88343}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000250|UniProtKB:O88343}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000250|UniProtKB:O88343}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000250|UniProtKB:O88343}.
MOD_RES 233 233 Phosphoserine.
{ECO:0000250|UniProtKB:O88343}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000250|UniProtKB:O88343}.
MOD_RES 249 249 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9JI66}.
MOD_RES 254 254 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 256 256 Phosphoserine.
{ECO:0000250|UniProtKB:O88343}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 262 262 Phosphoserine.
{ECO:0000250|UniProtKB:O88343}.
MOD_RES 1026 1026 Phosphoserine; by PKA.
{ECO:0000269|PubMed:11744745}.
MOD_RES 1029 1029 Phosphoserine.
{ECO:0000250|UniProtKB:O88343}.
MOD_RES 1034 1034 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1044 1044 Phosphoserine.
{ECO:0000250|UniProtKB:O88343}.
MOD_RES 1069 1069 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JI66}.
CARBOHYD 641 641 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:25568315}.
CARBOHYD 661 661 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:25568315}.
DISULFID 627 629 {ECO:0000269|PubMed:25568315}.
DISULFID 674 686 {ECO:0000269|PubMed:25568315}.
VAR_SEQ 1 44 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9235899}.
/FTId=VSP_016704.
VAR_SEQ 45 85 HKRKTGHKEKKEKERISENYSDKSDIENADESSSSILKPLI
-> MSTENVEGKPSNLGERGRARSSTFLRVVQPMFNHSIFT
SAV (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9235899}.
/FTId=VSP_016705.
VAR_SEQ 635 690 ANISISNDTTLAPEYLPTMSSTDMYHNTTFDWAFLSKKECS
KYGGNLVGNNCNFVP -> GEGITLCVYARFVFGGRCRLHA
CKFSTCCHGPQELVLFFSLKNSATEFDVSLPEVF (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_016706.
VAR_SEQ 691 1079 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_016707.
VAR_SEQ 813 896 Missing (in isoform 4).
{ECO:0000303|Ref.5}.
/FTId=VSP_016708.
VAR_SEQ 1034 1079 SDCPYSEKVPSIKIPMDIMEQQPFLSDSKPSDRERSPTFLE
RHTSC -> EKDHQHSLNATHHADKIPFLQSLGMPSPPRTP
VKVVPQIRIELEPEDNDYFWRSKGTETTL (in isoform
5). {ECO:0000303|Ref.6}.
/FTId=VSP_041003.
VARIANT 342 342 R -> S (in pRTA-OA; decreased
localization to the basolateral membrane;
mistargeting to the apical membrane
probably explains the loss of the
cotransporter activity;
dbSNP:rs121908856).
{ECO:0000269|PubMed:10545938,
ECO:0000269|PubMed:15713912,
ECO:0000269|PubMed:15930088,
ECO:0000303|PubMed:17661077}.
/FTId=VAR_024751.
VARIANT 471 471 S -> L (in pRTA-OA; mistargeting to the
apical membrane and altered function).
{ECO:0000269|PubMed:15471865,
ECO:0000269|PubMed:15713912}.
/FTId=VAR_024752.
VARIANT 529 529 T -> S (in pRTA-OA; decreased
cotransporter activity).
{ECO:0000269|PubMed:15930088,
ECO:0000303|PubMed:17661077}.
/FTId=VAR_024753.
VARIANT 530 530 G -> R (in pRTA-OA; decreased
cotransporter activity; no effect on
localization to the basolateral
membrane). {ECO:0000303|PubMed:17661077}.
/FTId=VAR_071661.
VARIANT 554 554 R -> H (in pRTA-OA; mistargeting and
altered function; dbSNP:rs121908857).
{ECO:0000269|PubMed:10545938,
ECO:0000269|PubMed:15713912,
ECO:0000269|PubMed:15930088}.
/FTId=VAR_024754.
VARIANT 566 566 L -> P (in pRTA-OA; loss of localization
to the plasma membrane; the retention in
the cytoplasm probably explains the loss
of the cotransporter activity).
{ECO:0000269|PubMed:16636648,
ECO:0000303|PubMed:17661077}.
/FTId=VAR_071662.
VARIANT 843 843 A -> V (in pRTA-OA; altered function).
{ECO:0000269|PubMed:15930088}.
/FTId=VAR_024755.
VARIANT 925 925 R -> C (in pRTA-OA; altered function).
{ECO:0000269|PubMed:15930088}.
/FTId=VAR_024756.
MUTAGEN 49 49 T->A: Loss of conductance regulation by
cAMP; isoform 1.
{ECO:0000269|PubMed:12730338}.
MUTAGEN 49 49 T->D: Loss of conductance regulation by
cAMP; isoform 1.
{ECO:0000269|PubMed:12730338}.
MUTAGEN 135 135 E->R: Mistargeting and altered function.
{ECO:0000269|PubMed:15713912}.
MUTAGEN 477 477 Y->F: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 493 493 D->N: Prevents membrane targeting.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 494 494 A->K: Prevents membrane targeting.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 503 503 E->Q: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 504 504 S->L: Prevents membrane targeting.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 527 529 SST->GFS: Confers anion exchange
activity; when associated with E-798; S-
842; T-844 and R-847.
{ECO:0000269|PubMed:29500354}.
MUTAGEN 527 527 S->C: Severely reduces transporter
activity. {ECO:0000269|PubMed:29500354}.
MUTAGEN 536 536 E->Q: Prevents membrane targeting.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 552 552 E->N: Prevents membrane targeting.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 554 554 R->D: Prevents membrane targeting.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 582 582 R->N: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 582 582 R->Q: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 586 586 E->Q: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 599 599 D->N: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 600 600 A->T: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 602 602 K->Q: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 603 603 K->Q: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 691 691 D->R: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 700 700 F->M: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 711 711 K->E,N,Q: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 711 711 K->R: No effect on the sodium-dependent
ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 712 712 K->N: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 714 714 K->Q: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 715 715 T->N: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 721 721 T->G: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 724 724 R->E: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 725 725 K->N: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 728 728 S->G: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 729 729 D->N,R: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 743 743 D->K,N: Prevents membrane targeting.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 749 749 D->N: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 752 752 K->Q: Prevents membrane targeting.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 766 766 R->Q: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 767 767 G->T: Alters interaction with CA4.
{ECO:0000269|PubMed:14567693}.
MUTAGEN 775 775 E->N: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 798 798 D->C: Abolishes transporter activity.
{ECO:0000269|PubMed:29500354}.
MUTAGEN 798 798 D->E: Severely reduces transporter
activity. Confers anion exchange
activity; when associated with SST-527--
529-GFS; S-842; T-844 and R-847.
{ECO:0000269|PubMed:29500354}.
MUTAGEN 798 798 D->N,R: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 802 802 T->C: Abolishes transporter activity.
{ECO:0000269|PubMed:29500354}.
MUTAGEN 808 809 RK->NN: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 814 815 KK->NN: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 820 820 H->D,N,S,R: Moderate reduction of the
sodium-dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 822 822 D->N: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 842 842 V->S: Confers anion exchange activity;
when associated with SST-527--529-GFS; D-
798; T-844 and R-847.
{ECO:0000269|PubMed:29500354}.
MUTAGEN 844 844 A->T: Confers anion exchange activity;
when associated with SST-527--529-GFS; D-
798; S-842 and R-847.
{ECO:0000269|PubMed:29500354}.
MUTAGEN 845 845 T->C: Strongly reduces transporter
activity. {ECO:0000269|PubMed:29500354}.
MUTAGEN 847 847 I->R: Abolishes transporter activity.
Confers anion exchange activity; when
associated with SST-527--529-GFS; D-798;
S-842 and T-844.
{ECO:0000269|PubMed:29500354}.
MUTAGEN 851 851 H->N: Prevents membrane targeting.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 853 853 D->N: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 858 860 ETE->MSK: Moderate reduction of the
sodium-dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 875 877 EQR->QQQ: Prevents membrane targeting.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 875 875 E->Q: Strong reduction of the sodium-
dependent ion transport activity.
MUTAGEN 898 898 K->E: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 925 927 RLK->NLN: Prevents membrane targeting.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 948 948 R->E: Strong reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 949 949 R->E: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 951 951 H->D: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 951 951 H->N,R: Prevents membrane targeting.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 968 968 K->Q: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 987 987 R->E,N: Moderate reduction of the sodium-
dependent ion transport activity.
{ECO:0000269|PubMed:15817634}.
MUTAGEN 1002 1002 L->N: Partial loss of interaction with
CA2. {ECO:0000269|PubMed:15218065}.
MUTAGEN 1003 1003 D->N: Abolishes interaction with CA2.
{ECO:0000269|PubMed:15218065}.
MUTAGEN 1004 1004 D->N: Partial loss of interaction with
CA2. {ECO:0000269|PubMed:15218065}.
MUTAGEN 1026 1026 S->A: Prevents phosphorylation by PKA.
Loss of regulation by cAMP of the
transporter stoichiometry.
{ECO:0000269|PubMed:11744745,
ECO:0000269|PubMed:12730338}.
MUTAGEN 1026 1026 S->D: Loss of regulation by cAMP of the
transporter stoichiometry. Shifts
transporter stoichiometry from 3:1 to
2:1. {ECO:0000269|PubMed:11744745,
ECO:0000269|PubMed:12730338}.
MUTAGEN 1030 1033 DNDD->NNNN: Abolishes interaction with
CA2. {ECO:0000269|PubMed:15218065}.
MUTAGEN 1030 1030 D->N: Loss of regulation by cAMP of the
transporter stoichiometry. Abolishes
interaction with CA2.
{ECO:0000269|PubMed:12411514}.
MUTAGEN 1032 1032 D->N: Loss of regulation by cAMP of the
transporter stoichiometry. Partial loss
of interaction with CA2.
{ECO:0000269|PubMed:12411514}.
MUTAGEN 1033 1033 D->N: No effect on regulation by cAMP of
the transporter stoichiometry. Partial
loss of interaction with CA2.
{ECO:0000269|PubMed:12411514}.
MUTAGEN 1057 1057 F->A: Targeting to apical membrane.
{ECO:0000269|PubMed:15273250}.
CONFLICT 6 6 V -> A (in Ref. 4; AAG47773).
{ECO:0000305}.
CONFLICT 49 49 T -> A (in Ref. 6; BAH58226).
{ECO:0000305}.
CONFLICT 78 78 S -> G (in Ref. 3; AAF21718).
{ECO:0000305}.
CONFLICT 256 256 S -> F (in Ref. 3; AAD42020).
{ECO:0000305}.
CONFLICT 263 263 D -> E (in Ref. 3; AAF21718).
{ECO:0000305}.
CONFLICT 298 298 P -> H (in Ref. 6; BAH58226).
{ECO:0000305}.
CONFLICT 364 364 H -> R (in Ref. 3; AAF21719).
{ECO:0000305}.
CONFLICT 605 605 I -> V (in Ref. 3; AAF21718).
{ECO:0000305}.
CONFLICT 654 654 S -> P (in Ref. 3; AAF21718).
{ECO:0000305}.
CONFLICT 749 749 D -> G (in Ref. 3; AAF21719).
{ECO:0000305}.
CONFLICT 799 799 Q -> R (in Ref. 4; AAG47773).
{ECO:0000305}.
CONFLICT 856 856 K -> R (in Ref. 4; AAG47773).
{ECO:0000305}.
CONFLICT 912 912 M -> R (in Ref. 3; AAF21718).
{ECO:0000305}.
CONFLICT 913 913 G -> R (in Ref. 3; AAF21719).
{ECO:0000305}.
CONFLICT 940 940 I -> V (in Ref. 3; AAF21718).
{ECO:0000305}.
CONFLICT 1007 1007 P -> S (in Ref. 3; AAF21719).
{ECO:0000305}.
CONFLICT 1069 1069 S -> P (in Ref. 3; AAF21719).
{ECO:0000305}.
SEQUENCE 1079 AA; 121461 MW; 14B981A94DD64293 CRC64;
MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKTG HKEKKEKERI
SENYSDKSDI ENADESSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT ELDELLAVDG
QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCMEKGSI MLDREASSLP
QLVEMIVDHQ IETGLLKPEL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASRMFTN
PDNGSPAMTH RNLTSSSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG EVDFLDTPFI
AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD EVFHDIAYKA
KDRHDLIAGI DEFLDEVIVL PPGEWDPAIR IEPPKSLPSS DKRKNMYSGG ENVQMNGDTP
HDGGHGGGGH GDCEELQRTG RFCGGLIKDI KRKAPFFASD FYDALNIQAL SAILFIYLAT
VTNAITFGGL LGDATDNMQG VLESFLGTAV SGAIFCLFAG QPLTILSSTG PVLVFERLLF
NFSKDNNFDY LEFRLWIGLW SAFLCLILVA TDASFLVQYF TRFTEEGFSS LISFIFIYDA
FKKMIKLADY YPINSNFKVG YNTLFSCTCV PPDPANISIS NDTTLAPEYL PTMSSTDMYH
NTTFDWAFLS KKECSKYGGN LVGNNCNFVP DITLMSFILF LGTYTSSMAL KKFKTSPYFP
TTARKLISDF AIILSILIFC VIDALVGVDT PKLIVPSEFK PTSPNRGWFV PPFGENPWWV
CLAAAIPALL VTILIFMDQQ ITAVIVNRKE HKLKKGAGYH LDLFWVAILM VICSLMALPW
YVAATVISIA HIDSLKMETE TSAPGEQPKF LGVREQRVTG TLVFILTGLS VFMAPILKFI
PMPVLYGVFL YMGVASLNGV QFMDRLKLLL MPLKHQPDFI YLRHVPLRRV HLFTFLQVLC
LALLWILKST VAAIIFPVMI LALVAVRKGM DYLFSQHDLS FLDDVIPEKD KKKKEDEKKK
KKKKGSLDSD NDDSDCPYSE KVPSIKIPMD IMEQQPFLSD SKPSDRERSP TFLERHTSC


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