S4A10_RAT
ID S4A10_RAT Reviewed; 1117 AA.
AC Q80ZA5; D3ZGB5; D3ZY00; D4ADV4; J7FMV4; J7FPF5; J7FRI2; J7FTX0; Q6PU70;
AC Q6PU71; Q6PU72; Q6PU73; Q6PU74; Q80ZA6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Sodium-driven chloride bicarbonate exchanger {ECO:0000303|PubMed:14656289};
DE AltName: Full=Solute carrier family 4 member 10 {ECO:0000312|RGD:631407};
GN Name=Slc4a10 {ECO:0000312|RGD:631407};
GN Synonyms=Ncbe {ECO:0000303|PubMed:14656289};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=14656289; DOI=10.1046/j.1460-9568.2003.03053.x;
RA Giffard R.G., Lee Y.-S., Ouyang Y.-B., Murphy S.L., Monyer H.;
RT "Two variants of the rat brain sodium-driven chloride bicarbonate exchanger
RT (NCBE): developmental expression and addition of a PDZ motif.";
RL Eur. J. Neurosci. 18:2935-2945(2003).
RN [2] {ECO:0000312|EMBL:AFP48940.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 8; 9; 10 AND 11), FUNCTION, TISSUE
RP SPECIFICITY, ALTERNATIVE PROMOTER USAGE, AND ALTERNATIVE SPLICING.
RC STRAIN=Wistar {ECO:0000312|EMBL:AFP48940.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AFP48940.1}, and
RC Kidney {ECO:0000312|EMBL:AGX00872.1};
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 5; 6 AND 7).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Karim Z., Attmane-Elakeb A., Vernimmen C., Bichara M.M.;
RT "Cloning and functional characterization of 'rb5NCBE'.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [5]
RP 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 [6]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, 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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [8]
RP FUNCTION.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [10]
RP CRYSTALLIZATION, PRELIMINARY X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF
RP 96-396, AND INTRINSICALLY DISORDERED REGION.
RX PubMed=24223558; DOI=10.3389/fphys.2013.00320;
RA Bjerregaard-Andersen K., Perdreau-Dahl H., Guldsten H., Praetorius J.,
RA Jensen J.K., Morth J.P.;
RT "The N-terminal cytoplasmic region of NCBE displays features of an
RT intrinsic disordered structure and represents a novel target for specific
RT drug screening.";
RL Front. Physiol. 4:320-320(2013).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28280139; DOI=10.1681/asn.2016080930;
RA Guo Y.M., Liu Y., Liu M., Wang J.L., Xie Z.D., Chen K.J., Wang D.K.,
RA Occhipinti R., Boron W.F., Chen L.M.;
RT "Na+/HCO3- cotransporter NBCn2 mediates HCO3- reclamation in the apical
RT membrane of renal proximal tubules.";
RL J. Am. Soc. Nephrol. 28:2409-2419(2017).
CC -!- FUNCTION: Sodium/bicarbonate cotransporter which plays an important
CC role in regulating intracellular pH (PubMed:10993873, PubMed:20566632,
CC PubMed:23409100). Has been shown to act as a sodium/bicarbonate
CC cotransporter in exchange for intracellular chloride (PubMed:10993873,
CC PubMed:20566632). Has also been shown to act as a sodium/biocarbonate
CC cotransporter which does not couple net influx of bicarbonate to net
CC efflux of chloride, with the observed chloride efflux being due to
CC chloride self-exchange (By similarity). Controls neuronal pH and may
CC contribute to the secretion of cerebrospinal fluid (By similarity).
CC Reduces the excitability of CA1 pyramidal neurons and modulates short-
CC term synaptic plasticity (By similarity). Required in retinal cells to
CC maintain normal pH which is necessary for normal vision (By
CC similarity). In the kidney, likely to mediate bicarbonate reclamation
CC in the apical membrane of the proximal tubules (PubMed:28280139).
CC {ECO:0000250|UniProtKB:Q5DTL9, ECO:0000250|UniProtKB:Q6U841,
CC ECO:0000269|PubMed:10993873, ECO:0000269|PubMed:20566632,
CC ECO:0000269|PubMed:23409100, ECO:0000269|PubMed:28280139}.
CC -!- INTERACTION:
CC Q80ZA5-3; P70441: Slc9a3r1; Xeno; NbExp=3; IntAct=EBI-8613086, EBI-1184085;
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:14592810, ECO:0000269|PubMed:18061361,
CC ECO:0000269|PubMed:28280139}; Multi-pass membrane protein
CC {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:28280139};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q5DTL9}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q5DTL9}. Perikaryon
CC {ECO:0000250|UniProtKB:Q5DTL9}. Presynapse
CC {ECO:0000250|UniProtKB:Q5DTL9}. Postsynapse
CC {ECO:0000250|UniProtKB:Q5DTL9}. Note=Detected in dendrites and axon
CC terminals of retinal OFF bipolar cells and in axon terminals of ON
CC bipolar cells. In amacrine cells, located in the perikaryon. Also
CC detected in basal and apical dendrites of hippocampal pyramidal cells
CC (By similarity). In the kidney, isoforms starting with Met-Glu-Ile-Lys
CC localize predominantly to the basolateral membrane of renal thick
CC ascending limbs and inner medullary collecting ducts while isoforms
CC starting with Met-Cys-Asp-Leu localize to the apical membrane of
CC proximal tubules (PubMed:28280139). {ECO:0000250|UniProtKB:Q5DTL9,
CC ECO:0000269|PubMed:28280139}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=11;
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=rb1NCBE;
CC IsoId=Q80ZA5-1; Sequence=Displayed;
CC Name=2; Synonyms=rb4NCBE;
CC IsoId=Q80ZA5-2; Sequence=VSP_019655, VSP_019656, VSP_019663;
CC Name=3; Synonyms=rb2NCBE;
CC IsoId=Q80ZA5-3; Sequence=VSP_019656, VSP_019663;
CC Name=4; Synonyms=rb5NCBE;
CC IsoId=Q80ZA5-4; Sequence=VSP_019655, VSP_019656;
CC Name=5; Synonyms=rb3NCBE;
CC IsoId=Q80ZA5-5; Sequence=VSP_019655, VSP_019661, VSP_019662;
CC Name=6; Synonyms=rb6NCBE;
CC IsoId=Q80ZA5-6; Sequence=VSP_019655, VSP_019656, VSP_019659,
CC VSP_019660;
CC Name=7; Synonyms=rb7NCBE;
CC IsoId=Q80ZA5-7; Sequence=VSP_019655, VSP_019656, VSP_019657,
CC VSP_019658;
CC Name=8; Synonyms=NBCn2-E {ECO:0000303|PubMed:23409100};
CC IsoId=Q80ZA5-8; Sequence=VSP_060135, VSP_019655, VSP_019656;
CC Name=9; Synonyms=NBCn2-F {ECO:0000303|PubMed:23409100};
CC IsoId=Q80ZA5-9; Sequence=VSP_060135;
CC Name=10; Synonyms=NBCn2-G {ECO:0000303|PubMed:23409100};
CC IsoId=Q80ZA5-10; Sequence=VSP_060135, VSP_019655, VSP_019656,
CC VSP_019663;
CC Name=11; Synonyms=NBCn2-H {ECO:0000303|PubMed:23409100};
CC IsoId=Q80ZA5-11; Sequence=VSP_060135, VSP_019663;
CC -!- TISSUE SPECIFICITY: In the brain, detected in cerebral cortex,
CC subcortex, cerebellum, hippocampus and medulla (at protein level)
CC (PubMed:18061361). Expressed in neurons but not in astrocytes (at
CC protein level) (PubMed:18061361). Isoforms starting with Met-Glu-Ile-
CC Lys are found predominantly in the brain with lower levels in the eye
CC while isoforms starting with Met-Cys-Asp-Leu are most abundant in the
CC kidney with lower levels in the duodenum, jejunum and ileum (at protein
CC level) (PubMed:23409100). In the kidney, isoforms starting with Met-
CC Cys-Asp-Leu are primarily expressed in the cortex, the outer stripe of
CC the outer medulla and the inner stripe of the outer medulla (ISOM) but
CC are not detectable in the inner medulla (IM) while isoforms starting
CC with Met-Glu-Ile-Lys are predominantly expressed in the ISOM and IM
CC (PubMed:28280139). Expressed in the brain, in the hippocampus as well
CC as in dentate gyrus, cortical layers, cerebellum, olfactory bulb and in
CC the epithelial cells of the choroid plexus. Detected in pituitary,
CC testis, kidney and ileum. Detected also in spleen and lung.
CC {ECO:0000269|PubMed:10993873, ECO:0000269|PubMed:14592810,
CC ECO:0000269|PubMed:14656289, ECO:0000269|PubMed:18061361,
CC ECO:0000269|PubMed:23409100, ECO:0000269|PubMed:28280139}.
CC -!- DEVELOPMENTAL STAGE: Expressed in spinal cord and brain at E19 through
CC adulthood. {ECO:0000269|PubMed:14592810}.
CC -!- DOMAIN: The N-terminal cytoplasmic domain is likely to have a high
CC level of intrinsic disorder. {ECO:0000303|PubMed:24223558}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q5DTL9}.
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}.
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DR EMBL; AF439855; AAO59639.1; -; mRNA.
DR EMBL; AF439856; AAO59640.1; -; mRNA.
DR EMBL; JX073715; AFP48940.1; -; mRNA.
DR EMBL; JX073716; AFP48941.2; -; mRNA.
DR EMBL; JX073717; AFP48942.1; -; mRNA.
DR EMBL; JX073718; AFP48943.2; -; mRNA.
DR EMBL; KF305251; AGX00872.1; -; mRNA.
DR EMBL; KJ452197; AHX56802.1; -; mRNA.
DR EMBL; AY579373; AAS89262.1; -; mRNA.
DR EMBL; AY579374; AAS89263.1; -; mRNA.
DR EMBL; AY579375; AAS89264.1; -; mRNA.
DR EMBL; AY579376; AAS89265.1; -; mRNA.
DR EMBL; AY579377; AAS89266.1; -; mRNA.
DR EMBL; AABR07052345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07052346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07052347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_835193.1; NM_178092.2. [Q80ZA5-1]
DR RefSeq; XP_006234338.1; XM_006234276.3. [Q80ZA5-11]
DR RefSeq; XP_006234341.1; XM_006234279.3. [Q80ZA5-9]
DR RefSeq; XP_006234342.1; XM_006234280.3. [Q80ZA5-10]
DR RefSeq; XP_006234344.1; XM_006234282.3. [Q80ZA5-2]
DR RefSeq; XP_006234345.1; XM_006234283.3. [Q80ZA5-3]
DR RefSeq; XP_006234346.1; XM_006234284.3. [Q80ZA5-8]
DR RefSeq; XP_006234347.1; XM_006234285.3. [Q80ZA5-4]
DR AlphaFoldDB; Q80ZA5; -.
DR SMR; Q80ZA5; -.
DR IntAct; Q80ZA5; 1.
DR MINT; Q80ZA5; -.
DR STRING; 10116.ENSRNOP00000059155; -.
DR GlyGen; Q80ZA5; 3 sites.
DR iPTMnet; Q80ZA5; -.
DR PhosphoSitePlus; Q80ZA5; -.
DR SwissPalm; Q80ZA5; -.
DR jPOST; Q80ZA5; -.
DR PaxDb; Q80ZA5; -.
DR PRIDE; Q80ZA5; -.
DR Ensembl; ENSRNOT00000064344; ENSRNOP00000059915; ENSRNOG00000005307. [Q80ZA5-10]
DR Ensembl; ENSRNOT00000068238; ENSRNOP00000062481; ENSRNOG00000005307. [Q80ZA5-9]
DR GeneID; 295645; -.
DR KEGG; rno:295645; -.
DR UCSC; RGD:631407; rat. [Q80ZA5-1]
DR CTD; 57282; -.
DR RGD; 631407; Slc4a10.
DR VEuPathDB; HostDB:ENSRNOG00000005307; -.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000156972; -.
DR InParanoid; Q80ZA5; -.
DR OMA; KTHQFKD; -.
DR OrthoDB; 265068at2759; -.
DR PhylomeDB; Q80ZA5; -.
DR Reactome; R-RNO-425381; Bicarbonate transporters.
DR PRO; PR:Q80ZA5; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000005307; Expressed in Ammon's horn and 7 other tissues.
DR ExpressionAtlas; Q80ZA5; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0097441; C:basal dendrite; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0097442; C:CA3 pyramidal cell dendrite; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0036477; C:somatodendritic compartment; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0015301; F:anion:anion antiporter activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0035641; P:locomotory exploration behavior; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:1902600; P:proton transmembrane transport; ISO:RGD.
DR GO; GO:0021860; P:pyramidal neuron development; ISO:RGD.
DR GO; GO:0030641; P:regulation of cellular pH; ISO:RGD.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0006885; P:regulation of pH; ISO:RGD.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; ISO:RGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; ISS: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..1117
FT /note="Sodium-driven chloride bicarbonate exchanger"
FT /id="PRO_0000245242"
FT TOPO_DOM 1..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..537
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..561
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..595
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 617..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 647..719
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 720..740
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 741..761
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 762..782
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 783..808
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 809..829
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 830..854
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 855..875
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 876..911
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 912..932
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 933..934
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 935..955
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 956..997
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 998..1018
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1019..1117
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 282..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..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 282..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT MOD_RES 1056
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT MOD_RES 1084
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 686
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..16
FT /note="MEIKDQGAQMEPLLPT -> MCDLAGISGNRKVMQPGTCEHFQSLGQE (in
FT isoform 8, isoform 9, isoform 10 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:23409100"
FT /id="VSP_060135"
FT VAR_SEQ 255
FT /note="N -> NA (in isoform 2, isoform 4, isoform 5, isoform
FT 6, isoform 7, isoform 8 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:23409100, ECO:0000303|Ref.3"
FT /id="VSP_019655"
FT VAR_SEQ 286..315
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 6, isoform 7, isoform 8 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:14656289,
FT ECO:0000303|PubMed:23409100, ECO:0000303|Ref.3"
FT /id="VSP_019656"
FT VAR_SEQ 481..498
FT /note="IFGGLILDIKRKAPFFWS -> SPISGIFASPEFFHRLCG (in isoform
FT 7)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_019657"
FT VAR_SEQ 499..1117
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_019658"
FT VAR_SEQ 603..607
FT /note="LCIIL -> FLPLT (in isoform 6)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_019659"
FT VAR_SEQ 608..1117
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_019660"
FT VAR_SEQ 1053
FT /note="E -> H (in isoform 5)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_019661"
FT VAR_SEQ 1054..1117
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_019662"
FT VAR_SEQ 1115..1117
FT /note="SPS -> IESRKEKKADSGKGVDRETCL (in isoform 2, isoform
FT 3, isoform 10 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:14656289,
FT ECO:0000303|PubMed:23409100, ECO:0000303|Ref.3"
FT /id="VSP_019663"
SQ SEQUENCE 1117 AA; 125639 MW; 51A27EFE653C3232 CRC64;
MEIKDQGAQM EPLLPTRNDE EAVVDRGGTR SILKTHFEKE DLEGHRTLFI GVHVPLGGRK
SHRRHRHRGH KHRKRDRERD SGLEDGGESP SFDTPSQRVQ FILGTEDDDE EHIPHDLFTE
LDEICWREGE DAEWRETARW LKFEEDVEDG GERWSKPYVA TLSLHSLFEL RSCILNGTVL
LDMHANTLEE IADMVLDQQV SSGQLNEDVR HRVHEALMKQ HHHQSQKKLT NRIPIVRSFA
DIGKKQSEPN SMDKNGQVVS PQSAPACAEN KNDVSRENST VDFSKGLGGQ QKGHTSPCGM
KQRLDKGPPH QQEREVDLHF MKKIPPGAEA SNILVGELEF LDRTVVAFVR LSPAVLLQGL
AEVPIPSRFL FILLGPLGKG QQYHEIGRSI ATLMTDEVFH DVAYKAKDRN DLVSGIDEFL
DQVTVLPPGE WDPSIRIEPP KNVPSQEKRK TPSLPNGTAA HGGPEQHGGH SGPELQRTGR
IFGGLILDIK RKAPFFWSDF RDAFSLQCLA SFLFLYCACM SPVITFGGLL GEATEGRISA
IESLFGASMT GIAYSLFGGQ PLTILGSTGP VLVFEKILFK FCKEYGLSYL SLRASIGLWT
ATLCIILVAT DASSLVCYIT RFTEEAFASL ICIIFIYEAL EKLFELSESY PINMHNDLEL
LTQYSCNCME PHSPSNDTLK EWRESNISAS DIIWGNLTVS ECRSLHGEYV GRACGHGHPY
VPDVLFWSVI LFFSTVTMSA TLKQFKTSRY FPTKVRSIVS DFAVFLTILC MVLIDYAIGI
PSPKLQVPSV FKPTRDDRGW FVTPLGPNPW WTIIAAIIPA LLCTILIFMD QQITAVIINR
KEHKLKKGCG YHLDLLMVAV MLGVCSIMGL PWFVAATVLS ITHVNSLKLE SECSAPGEQP
KFLGIREQRV TGLMIFILMG SSVFMTSILK FIPMPVLYGV FLYMGASSLK GIQLFDRIKL
FWMPAKHQPD FIYLRHVPLR KVHLFTVIQM SCLGLLWIIK VSRAAIVFPM MVLALVFVRK
LMDFLFTKRE LSWLDDLMPE SKKKKLEDAE KEEEQSMLAM EDEGTVQLPL EGHYRDDPSV
INISDEMSKT AMWGNLLVTA DNSKEKESRF PSKSSPS
