S4A10_MOUSE
ID S4A10_MOUSE Reviewed; 1118 AA.
AC Q5DTL9; E9NX85; F1DFN1; G3F8Y7; G3F8Y8; G3F8Y9; G3F8Z0; I6VS12; J7K287;
AC Q8CFS3; Q9EST0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Sodium-driven chloride bicarbonate exchanger {ECO:0000303|PubMed:10993873};
DE AltName: Full=Solute carrier family 4 member 10 {ECO:0000312|MGI:MGI:2150150};
GN Name=Slc4a10 {ECO:0000312|MGI:MGI:2150150};
GN Synonyms=Kiaa4136 {ECO:0000312|MGI:MGI:2150150},
GN Ncbe {ECO:0000303|PubMed:15567717};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10993873; DOI=10.1074/jbc.c000456200;
RA Wang C.-Z., Yano H., Nagashima K., Seino S.;
RT "The Na+-driven Cl-/HCO3- exchanger. Cloning, tissue distribution, and
RT functional characterization.";
RL J. Biol. Chem. 275:35486-35490(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=21439947; DOI=10.1016/j.brainres.2011.03.046;
RA Liu Y., Xu J.Y., Wang D.K., Boron W.F., Chen L.M.;
RT "Expression and distribution of NBCn2 (Slc4a10) splice variants in mouse
RT brain: cloning of novel variant NBCn2-D.";
RL Brain Res. 1390:33-40(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6; 7; 8; 9 AND 10), ALTERNATIVE
RP PROMOTER USAGE, AND ALTERNATIVE SPLICING.
RX PubMed=23409100; DOI=10.1371/journal.pone.0055974;
RA Liu Y., Wang D.K., Jiang D.Z., Qin X., Xie Z.D., Wang Q.K., Liu M.,
RA Chen L.M.;
RT "Cloning and functional characterization of novel variants and tissue-
RT specific expression of alternative amino and carboxyl termini of products
RT of slc4a10.";
RL PLoS ONE 8:E55974-E55974(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=14592810; DOI=10.1152/ajpcell.00240.2003;
RA Praetorius J., Nejsum L.N., Nielsen S.;
RT "A SCL4A10 gene product maps selectively to the basolateral plasma membrane
RT of choroid plexus epithelial cells.";
RL Am. J. Physiol. 286:C601-C610(2004).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15567717; DOI=10.1016/j.modgep.2004.08.002;
RA Huebner C.A., Hentschke M., Jacobs S., Hermans-Borgmeyer I.;
RT "Expression of the sodium-driven chloride bicarbonate exchanger NCBE during
RT prenatal mouse development.";
RL Gene Expr. Patterns 5:219-223(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP REPRESSION BY HYPOXIA.
RX PubMed=17928512; DOI=10.1152/ajpregu.00497.2007;
RA Chen L.M., Choi I., Haddad G.G., Boron W.F.;
RT "Chronic continuous hypoxia decreases the expression of SLC4A7 (NBCn1) and
RT SLC4A10 (NCBE) in mouse brain.";
RL Am. J. Physiol. 293:R2412-R2420(2007).
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=18061361; DOI=10.1016/j.neuroscience.2007.10.015;
RA Chen L.M., Kelly M.L., Rojas J.D., Parker M.D., Gill H.S., Davis B.A.,
RA Boron W.F.;
RT "Use of a new polyclonal antibody to study the distribution and
RT glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent
RT brain.";
RL Neuroscience 151:374-385(2008).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18165320; DOI=10.1073/pnas.0705487105;
RA Jacobs S., Ruusuvuori E., Sipilae S.T., Haapanen A., Damkier H.H.,
RA Kurth I., Hentschke M., Schweizer M., Rudhard Y., Laatikainen L.M.,
RA Tyynelae J., Praetorius J., Voipio J., Huebner C.A.;
RT "Mice with targeted Slc4a10 gene disruption have small brain ventricles and
RT show reduced neuronal excitability.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:311-316(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; THR-94; SER-276; SER-1057
RP AND SER-1085, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF GLU-585; GLU-891; GLU-893 AND HIS-977.
RX PubMed=20566632; DOI=10.1074/jbc.m110.108712;
RA Damkier H.H., Aalkjaer C., Praetorius J.;
RT "Na+-dependent HCO3- import by the slc4a10 gene product involves
RT Cl- export.";
RL J. Biol. Chem. 285:26998-27007(2010).
RN [14]
RP SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=20541593; DOI=10.1016/j.neuroscience.2010.06.005;
RA Liu Y., Xu K., Chen L.M., Sun X., Parker M.D., Kelly M.L., LaManna J.C.,
RA Boron W.F.;
RT "Distribution of NBCn2 (SLC4A10) splice variants in mouse brain.";
RL Neuroscience 169:951-964(2010).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23056253; DOI=10.1371/journal.pone.0046155;
RA Hilgen G., Huebner A.K., Tanimoto N., Sothilingam V., Seide C.,
RA Garcia Garrido M., Schmidt K.F., Seeliger M.W., Loewel S., Weiler R.,
RA Huebner C.A., Dedek K.;
RT "Lack of the sodium-driven chloride bicarbonate exchanger NCBE impairs
RT visual function in the mouse retina.";
RL PLoS ONE 7:E46155-E46155(2012).
RN [16]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24905082; DOI=10.1111/ejn.12636;
RA Song X., Yamasaki M., Miyazaki T., Konno K., Uchigashima M., Watanabe M.;
RT "Neuron type- and input pathway-dependent expression of Slc4a10 in adult
RT mouse brains.";
RL Eur. J. Neurosci. 40:2797-2810(2014).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26136660; DOI=10.3389/fncel.2015.00223;
RA Sinning A., Liebmann L., Huebner C.A.;
RT "Disruption of Slc4a10 augments neuronal excitability and modulates
RT synaptic short-term plasticity.";
RL Front. Cell. Neurosci. 9:223-223(2015).
CC -!- FUNCTION: Sodium/bicarbonate cotransporter which plays an important
CC role in regulating intracellular pH (PubMed:10993873, PubMed:20566632).
CC Has been shown to act as a sodium/bicarbonate cotransporter in exchange
CC for intracellular chloride (PubMed:10993873, PubMed:20566632). Has also
CC been shown to act as a sodium/biocarbonate cotransporter which is not
CC responsible for net efflux of chloride, with the observed chloride
CC efflux being due to chloride self-exchange (By similarity). Controls
CC neuronal pH and may contribute to the secretion of cerebrospinal fluid
CC (PubMed:18165320). Reduces the excitability of CA1 pyramidal neurons
CC and modulates short-term synaptic plasticity (PubMed:26136660).
CC Required in retinal cells to maintain normal pH which is necessary for
CC normal vision (PubMed:23056253). In the kidney, likely to mediate
CC bicarbonate reclamation in the apical membrane of the proximal tubules
CC (By similarity). {ECO:0000250|UniProtKB:Q6U841,
CC ECO:0000250|UniProtKB:Q80ZA5, ECO:0000269|PubMed:10993873,
CC ECO:0000269|PubMed:18165320, ECO:0000269|PubMed:20566632,
CC ECO:0000269|PubMed:23056253, ECO:0000269|PubMed:26136660}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:14592810, ECO:0000269|PubMed:18061361,
CC ECO:0000269|PubMed:18165320, ECO:0000269|PubMed:20541593}; Multi-pass
CC membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q80ZA5}; Multi-pass membrane protein
CC {ECO:0000255}. Cell projection, dendrite {ECO:0000269|PubMed:18165320,
CC ECO:0000269|PubMed:23056253, ECO:0000269|PubMed:24905082}. Cell
CC projection, axon {ECO:0000269|PubMed:23056253}. Perikaryon
CC {ECO:0000269|PubMed:23056253}. Presynapse {ECO:0000269|PubMed:23056253,
CC ECO:0000269|PubMed:26136660}. Postsynapse {ECO:0000269|PubMed:23056253,
CC ECO:0000269|PubMed:26136660}. Note=Detected in dendrites and axon
CC terminals of retinal OFF bipolar cells and in axon terminals of ON
CC bipolar cells (PubMed:23056253). In amacrine cells, located in the
CC perikaryon (PubMed:23056253). Also detected in basal and apical
CC dendrites of hippocampal pyramidal cells (PubMed:18165320).
CC {ECO:0000269|PubMed:18165320, ECO:0000269|PubMed:23056253}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=10;
CC Comment=The use of 2 alternative promoters gives rise to isoforms
CC which differ at the N-terminus. In addition, alternative splicing
CC gives rise to further isoform diversity.
CC {ECO:0000269|PubMed:23409100};
CC Name=1; Synonyms=NBCn2-B {ECO:0000303|PubMed:20541593};
CC IsoId=Q5DTL9-1; Sequence=Displayed;
CC Name=2; Synonyms=NBCn2-A {ECO:0000303|PubMed:20541593};
CC IsoId=Q5DTL9-2; Sequence=VSP_019654;
CC Name=3; Synonyms=NBCn2-C {ECO:0000303|PubMed:20541593};
CC IsoId=Q5DTL9-3; Sequence=VSP_019654, VSP_060134;
CC Name=4; Synonyms=NBCn2-D {ECO:0000303|PubMed:21439947};
CC IsoId=Q5DTL9-4; Sequence=VSP_060134;
CC Name=5; Synonyms=NBCn2-E {ECO:0000303|PubMed:23409100};
CC IsoId=Q5DTL9-5; Sequence=VSP_060132, VSP_019654;
CC Name=6; Synonyms=NBCn2-F {ECO:0000303|PubMed:23409100};
CC IsoId=Q5DTL9-6; Sequence=VSP_060132;
CC Name=7; Synonyms=NBCn2-G {ECO:0000303|PubMed:23409100};
CC IsoId=Q5DTL9-7; Sequence=VSP_060132, VSP_019654, VSP_060134;
CC Name=8; Synonyms=NBCn2-H {ECO:0000303|PubMed:23409100};
CC IsoId=Q5DTL9-8; Sequence=VSP_060132, VSP_060134;
CC Name=9; Synonyms=NBCn2-I {ECO:0000303|PubMed:23409100};
CC IsoId=Q5DTL9-9; Sequence=VSP_060132, VSP_019654, VSP_060133;
CC Name=10; Synonyms=NBCn2-J {ECO:0000303|PubMed:23409100};
CC IsoId=Q5DTL9-10; Sequence=VSP_060132, VSP_060133;
CC -!- TISSUE SPECIFICITY: In the brain, detected in cerebral cortex,
CC subcortex, cerebellum, hippocampus and medulla (at protein level)
CC (PubMed:20541593, PubMed:18061361, PubMed:21439947, PubMed:24905082).
CC In the cerebrum, expressed at high levels throughout the cortex, at
CC lower levels in striatum and not detectable in the corpus callosum (at
CC protein level) (PubMed:20541593). In the cerebellum, detected at high
CC levels in the molecular layer but at very low levels in the granular
CC layer (at protein level) (PubMed:20541593). In the central nervous
CC system, detected in neurons in the olfactory bulb, cortex and
CC cerebellum (at protein level) (PubMed:18165320). Within the
CC hippocampus, abundantly expressed in CA3 pyramidal cells (at protein
CC level) (PubMed:18165320). Strongly expressed in the retina with high
CC levels in bipolar and amacrine cells (at protein level)
CC (PubMed:23056253). Expressed at high levels in brain and at low levels
CC in the pituitary, testis, kidney and ileum (PubMed:10993873). Also
CC expressed in pancreatic islets (PubMed:10993873). Expressed in the
CC epithelial cells of the choroid plexus (PubMed:14592810,
CC PubMed:15567717). During embryonic development, expressed in neurons of
CC the central nervous system (PubMed:15567717). Also expressed in the
CC peripheral nervous system and in non-neuronal tissues such as the dura
CC and some epithelia including the acid-secreting epithelium of the
CC stomach and the duodenal epithelium (PubMed:15567717). In the embryonic
CC retina, expression is restricted to the neuronal cell layer and the
CC retinal pigment epithelium (PubMed:15567717).
CC {ECO:0000269|PubMed:10993873, ECO:0000269|PubMed:14592810,
CC ECO:0000269|PubMed:15567717, ECO:0000269|PubMed:18061361,
CC ECO:0000269|PubMed:18165320, ECO:0000269|PubMed:20541593,
CC ECO:0000269|PubMed:21439947, ECO:0000269|PubMed:23056253,
CC ECO:0000269|PubMed:24905082}.
CC -!- DEVELOPMENTAL STAGE: In the embryonic central nervous system, detected
CC at 12.5 dpc when expression is observed in all areas of the brain
CC including the cerebellum (PubMed:15567717). In the embryonic cerebral
CC cortex, detected at 14.5 dpc with levels increasing at 18.5 dpc
CC (PubMed:15567717). {ECO:0000269|PubMed:15567717}.
CC -!- INDUCTION: Repressed in the brain by chronic continuous hypoxia (at
CC protein level). {ECO:0000269|PubMed:17928512}.
CC -!- DOMAIN: The N-terminal cytoplasmic domain is likely to have a high
CC level of intrinsic disorder. {ECO:0000250|UniProtKB:Q80ZA5}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18061361}.
CC -!- DISRUPTION PHENOTYPE: Homozygotes are born at the expected Mendelian
CC ratio but most pups die around weaning (PubMed:18165320). When fed soft
CC food from the second week of life onward, most pups catch up with the
CC weight of their wild-type littermates and survive (PubMed:18165320).
CC Adults display normal weight and lifespan, are fertile and do not
CC display major behavioral abnormalities (PubMed:18165320). However,
CC brain ventricle size is drastically reduced and mutants show diminished
CC Na(+)-dependent recovery of pH following acid loading of choroid plexus
CC epithelial cells (PubMed:18165320). Mutants also show reduced
CC excitability of CA3 pyramidal neurson and have increased seizure
CC threshold (PubMed:18165320). Increased excitability of CA1 pyramidal
CC neurons and diminished paired pulse facilitation in the hippocampus
CC (PubMed:26136660). No obvious morphological changes in the retina but
CC mutants display decreased visual acuity and contrast sensitivity in
CC behavioral experiments, smaller scotopic and photopic b-wave amplitudes
CC and longer latencies in electroretinograms, and altered temporal
CC response properties of ganglion cells (PubMed:23056253).
CC {ECO:0000269|PubMed:18165320, ECO:0000269|PubMed:23056253,
CC ECO:0000269|PubMed:26136660}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
CC -!- CAUTION: Has been shown to act as a sodium/bicarbonate cotransporter in
CC exchange for intracellular chloride (PubMed:10993873, PubMed:20566632).
CC Has also been shown to act as a sodium/biocarbonate cotransporter which
CC is not responsible for net efflux of chloride, with the observed
CC chloride efflux being due to chloride self-exchange (By similarity).
CC {ECO:0000250|UniProtKB:Q6U841, ECO:0000269|PubMed:10993873,
CC ECO:0000269|PubMed:20566632}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90511.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB033759; BAB17922.1; -; mRNA.
DR EMBL; HQ825316; ADX99207.1; -; mRNA.
DR EMBL; HQ831517; ADW85802.1; -; mRNA.
DR EMBL; JF500487; AEN71161.1; -; mRNA.
DR EMBL; JF500488; AEN71162.1; -; mRNA.
DR EMBL; JF500489; AEN71163.1; -; mRNA.
DR EMBL; JF500490; AEN71164.1; -; mRNA.
DR EMBL; JX220977; AFN27376.1; -; mRNA.
DR EMBL; JX254917; AFQ60533.1; -; mRNA.
DR EMBL; AK220501; BAD90511.1; ALT_INIT; mRNA.
DR EMBL; BC039226; AAH39226.1; -; mRNA.
DR CCDS; CCDS16064.1; -. [Q5DTL9-2]
DR CCDS; CCDS57172.1; -. [Q5DTL9-1]
DR CCDS; CCDS57173.1; -. [Q5DTL9-3]
DR RefSeq; NP_001229307.1; NM_001242378.1. [Q5DTL9-4]
DR RefSeq; NP_001229309.1; NM_001242380.1. [Q5DTL9-1]
DR RefSeq; NP_001229310.1; NM_001242381.1.
DR RefSeq; NP_001229312.1; NM_001242383.1.
DR RefSeq; XP_006500511.1; XM_006500448.3.
DR RefSeq; XP_006500512.1; XM_006500449.3.
DR RefSeq; XP_006500513.1; XM_006500450.3.
DR RefSeq; XP_006500514.1; XM_006500451.3.
DR AlphaFoldDB; Q5DTL9; -.
DR SMR; Q5DTL9; -.
DR BioGRID; 220486; 2.
DR STRING; 10090.ENSMUSP00000099796; -.
DR TCDB; 2.A.31.2.3; the anion exchanger (ae) family.
DR GlyGen; Q5DTL9; 3 sites.
DR iPTMnet; Q5DTL9; -.
DR PhosphoSitePlus; Q5DTL9; -.
DR jPOST; Q5DTL9; -.
DR MaxQB; Q5DTL9; -.
DR PaxDb; Q5DTL9; -.
DR PRIDE; Q5DTL9; -.
DR ProteomicsDB; 256823; -. [Q5DTL9-1]
DR ProteomicsDB; 256824; -. [Q5DTL9-2]
DR Antibodypedia; 48063; 28 antibodies from 12 providers.
DR DNASU; 94229; -.
DR Ensembl; ENSMUST00000054484; ENSMUSP00000061411; ENSMUSG00000026904. [Q5DTL9-3]
DR Ensembl; ENSMUST00000102735; ENSMUSP00000099796; ENSMUSG00000026904. [Q5DTL9-2]
DR Ensembl; ENSMUST00000112480; ENSMUSP00000108099; ENSMUSG00000026904. [Q5DTL9-1]
DR GeneID; 94229; -.
DR KEGG; mmu:94229; -.
DR UCSC; uc008jve.3; mouse. [Q5DTL9-2]
DR UCSC; uc008jvf.3; mouse. [Q5DTL9-1]
DR CTD; 57282; -.
DR MGI; MGI:2150150; Slc4a10.
DR VEuPathDB; HostDB:ENSMUSG00000026904; -.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000156972; -.
DR HOGENOM; CLU_002289_5_2_1; -.
DR InParanoid; Q5DTL9; -.
DR OMA; KTHQFKD; -.
DR OrthoDB; 265068at2759; -.
DR PhylomeDB; Q5DTL9; -.
DR TreeFam; TF313630; -.
DR Reactome; R-MMU-425381; Bicarbonate transporters.
DR BioGRID-ORCS; 94229; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Slc4a10; mouse.
DR PRO; PR:Q5DTL9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q5DTL9; protein.
DR Bgee; ENSMUSG00000026904; Expressed in choroid plexus epithelium and 115 other tissues.
DR ExpressionAtlas; Q5DTL9; baseline and differential.
DR Genevisible; Q5DTL9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0043679; C:axon terminus; IDA:UniProtKB.
DR GO; GO:0097441; C:basal dendrite; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0097442; C:CA3 pyramidal cell dendrite; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0036477; C:somatodendritic compartment; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0015301; F:anion:anion antiporter activity; IDA:MGI.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR GO; GO:0008510; F:sodium:bicarbonate symporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR GO; GO:0048854; P:brain morphogenesis; IMP:MGI.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0035641; P:locomotory exploration behavior; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0006486; P:protein glycosylation; ISO:MGI.
DR GO; GO:1902600; P:proton transmembrane transport; IMP:MGI.
DR GO; GO:0021860; P:pyramidal neuron development; IMP:MGI.
DR GO; GO:0030641; P:regulation of cellular pH; IMP:MGI.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0006885; P:regulation of pH; IDA:MGI.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IMP:MGI.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR013769; Band3_cytoplasmic_dom.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR InterPro; IPR003024; Na/HCO3_transpt.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR PANTHER; PTHR11453; PTHR11453; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR PRINTS; PR01232; NAHCO3TRSPRT.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Antiport; Cell membrane;
KW Cell projection; Glycoprotein; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Sodium; Sodium transport; Symport; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1118
FT /note="Sodium-driven chloride bicarbonate exchanger"
FT /id="PRO_0000245241"
FT TOPO_DOM 1..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..538
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 560..562
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 584..596
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..720
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 742..762
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 763..783
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 784..809
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 810..830
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 831..855
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..912
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 913..933
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 934..935
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 936..956
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 957..998
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 999..1019
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1020..1118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..16
FT /note="MEIKDQGAQMEPLLPT -> MQPGSCEHFQSLSQE (in isoform 5,
FT isoform 6, isoform 7, isoform 8, isoform 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:23409100"
FT /id="VSP_060132"
FT VAR_SEQ 287..316
FT /note="Missing (in isoform 2, isoform 3, isoform 5, isoform
FT 7 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:10993873,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:20541593,
FT ECO:0000303|PubMed:21439947, ECO:0000303|PubMed:23409100"
FT /id="VSP_019654"
FT VAR_SEQ 1115..1118
FT /note="SSPS -> RS (in isoform 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:23409100"
FT /id="VSP_060133"
FT VAR_SEQ 1116..1118
FT /note="SPS -> NESRKEKKADSGKGVDRETCL (in isoform 3, isoform
FT 4, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:21439947,
FT ECO:0000303|PubMed:23409100"
FT /id="VSP_060134"
FT MUTAGEN 585
FT /note="E->A: Reduced recovery of intracellular sodium-
FT dependent pH."
FT /evidence="ECO:0000269|PubMed:20566632"
FT MUTAGEN 891
FT /note="E->A: Reduced recovery of intracellular sodium-
FT dependent pH."
FT /evidence="ECO:0000269|PubMed:20566632"
FT MUTAGEN 893
FT /note="E->A: Reduced recovery of intracellular sodium-
FT dependent pH."
FT /evidence="ECO:0000269|PubMed:20566632"
FT MUTAGEN 977
FT /note="H->L: Reduced recovery of intracellular sodium-
FT dependent pH."
FT /evidence="ECO:0000269|PubMed:20566632"
FT CONFLICT 239
FT /note="F -> L (in Ref. 1; BAB17922)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="Missing (in Ref. 2; ADW85802, 3; AFN27376 and 5;
FT AAH39226)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="T -> A (in Ref. 1; BAB17922)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="I -> M (in Ref. 1; BAB17922)"
FT /evidence="ECO:0000305"
FT CONFLICT 796..797
FT /note="RD -> IY (in Ref. 1; BAB17922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1118 AA; 125817 MW; 85E3110C976978A7 CRC64;
MEIKDQGAQM EPLLPTRNDE EAVVDRGGTR SILKTHFEKE DLEGHRTLFI GVHVPLGGRK
SHRRHRHRGH KHRKRDRERD SGLEDGRESP SFDTPSQRVQ FILGTEDDDE EHLPHDLFTE
LDEICWREGE DAEWRETARW LKFEEDVEDG GERWSKPYVA TLSLHSLFEL RSCILNGTVL
LDMHANTIEE IADMVLDQQV SSGQLNEDVR HRVHEALMKQ HHHQNQKKLA NRIPIVRSFA
DIGKKQSEPN SMDKNAGQVV SPQSAPACAE NKNDVSRENS TVDFSKGLGG QQKGHTSPCG
MKQRLDKGPP HQQEREVDLH FMKKIPPGAE ASNILVGELE FLDRTVVAFV RLSPAVLLQG
LAEVPIPSRF LFILLGPLGK GQQYHEIGRS IATLMTDEVF HDVAYKAKDR NDLVSGIDEF
LDQVTVLPPG EWDPSIRIEP PKNVPSQEKR KIPAVPNGTA AHGEAEPHGG HSGPELQRTG
RIFGGLILDI KRKAPFFWSD FRDAFSLQCL ASFLFLYCAC MSPVITFGGL LGEATEGRIS
AIESLFGASM TGIAYSLFGG QPLTILGSTG PVLVFEKILF KFCKEYGLSY LSLRASIGLW
TATLCIILVA TDASSLVCYI TRFTEEAFAS LICIIFIYEA LEKLFELSET YPINMHNDLE
LLTQYSCNCM EPHSPSNDTL KEWRESNLSA SDIIWGNLTV SECRSLHGEY VGRACGHGHP
YVPDVLFWSV ILFFSTVTMS ATLKQFKTSR YFPTKVRSIV SDFAVFLTIL CMVLIDYAIG
IPSPKLQVPS VFKPTRDDRG WFVTPLGPNP WWTIIAAIIP ALLCTILIFM DQQITAVIIN
RKEHKLKKGC GYHLDLLMVA VMLGVCSIMG LPWFVAATVL SITHVNSLKL ESECSAPGEQ
PKFLGIREQR VTGLMIFILM GSSVFMTSIL KFIPMPVLYG VFLYMGASSL KGIQLFDRIK
LFWMPAKHQP DFIYLRHVPL RKVHLFTVIQ MSCLGLLWII KVSRAAIVFP MMVLALVFVR
KLMDFLFTKR ELSWLDDLMP ESKKKKLEDA EKEEEQSMLA MEDEGTVQLP LEGHYRDDPS
VINISDEMSK TAMWGNLLVT ADNSKEKESR FPSKSSPS
