NAC1_RAT
ID NAC1_RAT Reviewed; 971 AA.
AC Q01728; Q924Y2; Q9QW49; Q9R238; Q9R239; Q9WU29; Q9WU30;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Sodium/calcium exchanger 1;
DE AltName: Full=Na(+)/Ca(2+)-exchange protein 1;
DE AltName: Full=Solute carrier family 8 member 1;
DE Flags: Precursor;
GN Name=Slc8a1; Synonyms=Ncx1;
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] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Heart;
RX PubMed=8422940; DOI=10.1016/0014-5793(93)81737-k;
RA Low W., Kasir J., Rahamimoff H.;
RT "Cloning of the rat heart Na(+)-Ca2+ exchanger and its functional
RT expression in HeLa cells.";
RL FEBS Lett. 316:63-67(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, TRANSPORTER
RP ACTIVITY, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=8454039; DOI=10.1016/0014-5793(93)80046-w;
RA Furman I., Cook O., Kasir J., Rahamimoff H.;
RT "Cloning of two isoforms of the rat brain Na(+)-Ca2+ exchanger gene and
RT their functional expression in HeLa cells.";
RL FEBS Lett. 319:105-109(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
RC TISSUE=Aortic smooth muscle;
RX PubMed=8276763; DOI=10.1093/oxfordjournals.jbchem.a124211;
RA Nakasaki Y., Iwamoto T., Hanada H., Imagawa T., Shigekawa M.;
RT "Cloning of the rat aortic smooth muscle Na+/Ca2+ exchanger and tissue-
RT specific expression of isoforms.";
RL J. Biochem. 114:528-534(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND ALTERNATIVE SPLICING.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney cortex;
RX PubMed=8195112; DOI=10.1016/s0021-9258(17)36540-7;
RA Lee S.-L., Yu A.S.L., Lytton J.;
RT "Tissue-specific expression of Na(+)-Ca2+ exchanger isoforms.";
RL J. Biol. Chem. 269:14849-14852(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 7), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=Dahl salt-resistant, and Dahl salt-sensitive; TISSUE=Mesangial cell;
RX PubMed=10894800; DOI=10.1152/ajprenal.2000.279.1.f177;
RA Unlap M.T., Peti-Peterdi J., Bell P.D.;
RT "Cloning of mesangial cell Na(+)/Ca(2+) exchangers from Dahl/Rapp salt-
RT sensitive/resistant rats.";
RL Am. J. Physiol. 279:F177-F184(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=Sprague-Dawley; TISSUE=Mesangial cell;
RX PubMed=15040000; DOI=10.1002/jcp.10447;
RA Williams I., Williams C., Siroky B., Bates E., Kovacs G., Peti-Peterdi J.,
RA Unlap M.T., Bell P.D.;
RT "Regulation of mesangial cell Na+/Ca2+ exchanger isoforms.";
RL J. Cell. Physiol. 199:181-193(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 750-902, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Neuron;
RX PubMed=8255180; DOI=10.1016/0169-328x(93)90107-z;
RA Marlier L.N.J.-L., Zheng T., Tang J., Grayson D.R.;
RT "Regional distribution in the rat central nervous system of a mRNA encoding
RT a portion of the cardiac sodium/calcium exchanger isolated from cerebellar
RT granule neurons.";
RL Brain Res. Mol. Brain Res. 20:21-39(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 780-912, AND TISSUE SPECIFICITY.
RC STRAIN=CD Charles River; TISSUE=Kidney;
RX PubMed=1415740; DOI=10.1152/ajprenal.1992.263.4.f680;
RA Yu A.S.L., Hebert S.C., Lee S.-L., Brenner B.M., Lytton J.;
RT "Identification and localization of renal Na(+)-Ca2+ exchanger by
RT polymerase chain reaction.";
RL Am. J. Physiol. 263:F680-F685(1992).
RN [9]
RP TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=8798769; DOI=10.1074/jbc.271.40.24914;
RA Nicoll D.A., Quednau B.D., Qui Z., Xia Y.-R., Lusis A.J., Philipson K.D.;
RT "Cloning of a third mammalian Na+-Ca2+ exchanger, NCX3.";
RL J. Biol. Chem. 271:24914-24921(1996).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=12502557; DOI=10.1111/j.1749-6632.2002.tb04737.x;
RA Dong H., Dunn J., Lytton J.;
RT "Electrophysiological studies of the cloned rat cardiac NCX1.1 in
RT transfected HEK cells: a focus on the stoichiometry.";
RL Ann. N. Y. Acad. Sci. 976:159-165(2002).
RN [11]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16914199; DOI=10.1016/j.ceca.2006.06.004;
RA Minelli A., Castaldo P., Gobbi P., Salucci S., Magi S., Amoroso S.;
RT "Cellular and subcellular localization of Na+-Ca2+ exchanger protein
RT isoforms, NCX1, NCX2, and NCX3 in cerebral cortex and hippocampus of adult
RT rat.";
RL Cell Calcium 41:221-234(2007).
RN [12]
RP REVIEW.
RX PubMed=23506867; DOI=10.1016/j.mam.2012.07.003;
RA Khananshvili D.;
RT "The SLC8 gene family of sodium-calcium exchangers (NCX) - structure,
RT function, and regulation in health and disease.";
RL Mol. Aspects Med. 34:220-235(2013).
CC -!- FUNCTION: Mediates the exchange of one Ca(2+) ion against three to four
CC Na(+) ions across the cell membrane, and thereby contributes to the
CC regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular
CC processes (PubMed:8422940, PubMed:8454039, PubMed:10894800,
CC PubMed:12502557). Contributes to Ca(2+) transport during excitation-
CC contraction coupling in muscle. In a first phase, voltage-gated
CC channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to
CC release of Ca(2+) stores from the endoplasmic reticulum. SLC8A1
CC mediates the export of Ca(2+) from the cell during the next phase, so
CC that cytoplasmic Ca(2+) levels rapidly return to baseline. Required for
CC normal embryonic heart development and the onset of heart contractions
CC (By similarity). {ECO:0000250|UniProtKB:P70414,
CC ECO:0000269|PubMed:10894800, ECO:0000269|PubMed:12502557,
CC ECO:0000269|PubMed:15040000, ECO:0000269|PubMed:8422940,
CC ECO:0000269|PubMed:8454039}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in);
CC Xref=Rhea:RHEA:69955, ChEBI:CHEBI:29101, ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:8422940, ECO:0000269|PubMed:8454039};
CC -!- ACTIVITY REGULATION: Activated by micromolar levels of Ca(2+)
CC (PubMed:12502557). {ECO:0000269|PubMed:12502557}.
CC -!- ACTIVITY REGULATION: [Isoform 4]: Only active at low calcium
CC concentrations (PubMed:15040000). Not activated by PKC
CC (PubMed:15040000). {ECO:0000269|PubMed:15040000}.
CC -!- ACTIVITY REGULATION: [Isoform 5]: Active at all calcium levels tested
CC (PubMed:15040000). Activated by PKC (PubMed:15040000).
CC {ECO:0000269|PubMed:15040000}.
CC -!- ACTIVITY REGULATION: [Isoform 6]: Only active at low calcium
CC concentrations (PubMed:15040000). Activated by PKC (PubMed:15040000).
CC {ECO:0000269|PubMed:15040000}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10894800,
CC ECO:0000269|PubMed:12502557, ECO:0000269|PubMed:16914199,
CC ECO:0000269|PubMed:8422940}; Multi-pass membrane protein {ECO:0000305}.
CC Cell projection, dendrite {ECO:0000269|PubMed:16914199}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=Heart, NaCa1;
CC IsoId=Q01728-1; Sequence=Displayed;
CC Name=2; Synonyms=Brain-1, NaCa5;
CC IsoId=Q01728-2; Sequence=VSP_003402, VSP_003403;
CC Name=3; Synonyms=Brain-2, NaCa4;
CC IsoId=Q01728-3; Sequence=VSP_003402, VSP_003404;
CC Name=4; Synonyms=Kidney-1, NaCa7, SNCX1;
CC IsoId=Q01728-4; Sequence=VSP_003401, VSP_003402, VSP_003403;
CC Name=5; Synonyms=Kidney-2, NaCa3, RNCX1;
CC IsoId=Q01728-5; Sequence=VSP_003401, VSP_003402, VSP_003404;
CC Name=6; Synonyms=SDNCX1.10;
CC IsoId=Q01728-6; Sequence=VSP_003401, VSP_003402, VSP_029836;
CC Name=7;
CC IsoId=Q01728-7; Sequence=VSP_003401, VSP_029836;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain cortex and hippocampus (at
CC protein level) (PubMed:16914199). Cardiac sarcolemma or brain, and
CC spleen. Expressed in all regions of the kidney, highest levels of
CC expression in the distal convoluted tubule. Expressed throughout the
CC CNS, in decreasing order of abundance in hippocampus, cortex,
CC cerebellum, hypothalamus, midbrain and striatum. Expressed in numerous
CC regions of the brain including multiple cortical layers, hippocampus,
CC septal nuclei, thalamic nuclei, cerebellum, hypothalamus, olfactory
CC bulb and brainstem. Also expressed in various regions of the spinal
CC cord, ventricles and atria of the heart, lung, adrenals and kidney.
CC Isoform 4 seems to be a predominant isoform in aorta, stomach, liver,
CC and kidney. {ECO:0000269|PubMed:1415740, ECO:0000269|PubMed:16914199,
CC ECO:0000269|PubMed:8255180, ECO:0000269|PubMed:8276763,
CC ECO:0000269|PubMed:8798769}.
CC -!- DOMAIN: The cytoplasmic Calx-beta domains bind the regulatory Ca(2+).
CC The first Calx-beta domain can bind up to four Ca(2+) ions. The second
CC domain can bind another two Ca(2+) ions that are essential for calcium-
CC regulated ion exchange. {ECO:0000250|UniProtKB:P23685}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. SLC8 subfamily. {ECO:0000305}.
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DR EMBL; X68191; CAA48273.1; -; mRNA.
DR EMBL; X68812; CAA48707.1; -; mRNA.
DR EMBL; X68813; CAA48708.1; -; mRNA.
DR EMBL; U04933; AAB39952.1; -; mRNA.
DR EMBL; U04934; AAA19124.1; -; mRNA.
DR EMBL; U04936; AAA19125.1; -; mRNA.
DR EMBL; AF109163; AAD23386.1; -; mRNA.
DR EMBL; AF109164; AAD23387.1; -; mRNA.
DR EMBL; AF109165; AAD23388.1; -; mRNA.
DR EMBL; AF109166; AAD23389.1; -; mRNA.
DR EMBL; AY033398; AAK52307.1; -; mRNA.
DR PIR; A53789; A53789.
DR PIR; I52640; I52640.
DR PIR; S28833; S28833.
DR PIR; S32435; S32435.
DR PIR; S43730; S43730.
DR RefSeq; NP_001257701.1; NM_001270772.1. [Q01728-3]
DR RefSeq; NP_001257702.1; NM_001270773.1. [Q01728-5]
DR RefSeq; NP_001257703.1; NM_001270774.1. [Q01728-2]
DR RefSeq; NP_001257704.1; NM_001270775.1. [Q01728-4]
DR RefSeq; NP_001257705.1; NM_001270776.1. [Q01728-7]
DR RefSeq; NP_001257706.1; NM_001270777.1. [Q01728-6]
DR RefSeq; XP_008762655.1; XM_008764433.2. [Q01728-7]
DR RefSeq; XP_008762659.1; XM_008764437.2. [Q01728-6]
DR RefSeq; XP_008762660.1; XM_008764438.2. [Q01728-2]
DR RefSeq; XP_008762661.1; XM_008764439.2. [Q01728-4]
DR RefSeq; XP_017449552.1; XM_017594063.1. [Q01728-3]
DR RefSeq; XP_017449553.1; XM_017594064.1. [Q01728-5]
DR AlphaFoldDB; Q01728; -.
DR SMR; Q01728; -.
DR BioGRID; 248332; 45.
DR CORUM; Q01728; -.
DR IntAct; Q01728; 29.
DR MINT; Q01728; -.
DR STRING; 10116.ENSRNOP00000040751; -.
DR GlyGen; Q01728; 2 sites.
DR iPTMnet; Q01728; -.
DR PhosphoSitePlus; Q01728; -.
DR SwissPalm; Q01728; -.
DR PaxDb; Q01728; -.
DR PRIDE; Q01728; -.
DR Ensembl; ENSRNOT00000046246; ENSRNOP00000043539; ENSRNOG00000008479. [Q01728-6]
DR Ensembl; ENSRNOT00000052367; ENSRNOP00000050918; ENSRNOG00000008479. [Q01728-2]
DR GeneID; 29715; -.
DR KEGG; rno:29715; -.
DR UCSC; RGD:3717; rat. [Q01728-1]
DR CTD; 6546; -.
DR RGD; 3717; Slc8a1.
DR VEuPathDB; HostDB:ENSRNOG00000008479; -.
DR eggNOG; KOG1306; Eukaryota.
DR GeneTree; ENSGT00940000155129; -.
DR InParanoid; Q01728; -.
DR OMA; VSAETEM; -.
DR OrthoDB; 490546at2759; -.
DR PhylomeDB; Q01728; -.
DR TreeFam; TF314308; -.
DR Reactome; R-RNO-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-RNO-425561; Sodium/Calcium exchangers.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR PRO; PR:Q01728; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000008479; Expressed in heart and 20 other tissues.
DR ExpressionAtlas; Q01728; baseline and differential.
DR Genevisible; Q01728; RN.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0043679; C:axon terminus; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR GO; GO:0030506; F:ankyrin binding; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:1905060; F:calcium:cation antiporter activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IMP:SynGO.
DR GO; GO:0005432; F:calcium:sodium antiporter activity; IDA:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0015491; F:cation:cation antiporter activity; IBA:GO_Central.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0099580; F:ion antiporter activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:1901660; P:calcium ion export; IDA:BHF-UCL.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:RGD.
DR GO; GO:0070509; P:calcium ion import; IDA:BHF-UCL.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0060402; P:calcium ion transport into cytosol; IDA:RGD.
DR GO; GO:0055013; P:cardiac muscle cell development; ISO:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:RGD.
DR GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; IDA:BHF-UCL.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:RGD.
DR GO; GO:0071313; P:cellular response to caffeine; ISO:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:BHF-UCL.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; ISO:RGD.
DR GO; GO:0035050; P:embryonic heart tube development; ISO:RGD.
DR GO; GO:0001892; P:embryonic placenta development; ISO:RGD.
DR GO; GO:0003007; P:heart morphogenesis; ISO:RGD.
DR GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
DR GO; GO:0055001; P:muscle cell development; ISO:RGD.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:RGD.
DR GO; GO:0098735; P:positive regulation of the force of heart contraction; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IDA:BHF-UCL.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0002028; P:regulation of sodium ion transport; IMP:RGD.
DR GO; GO:0002026; P:regulation of the force of heart contraction; ISO:RGD.
DR GO; GO:0044557; P:relaxation of smooth muscle; ISO:RGD.
DR GO; GO:0033198; P:response to ATP; IDA:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IDA:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:0035994; P:response to muscle stretch; ISO:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006814; P:sodium ion transport; IDA:RGD.
DR GO; GO:0021537; P:telencephalon development; IEP:RGD.
DR GO; GO:0014829; P:vascular associated smooth muscle contraction; ISO:RGD.
DR Gene3D; 1.20.1420.30; -; 2.
DR Gene3D; 2.60.40.2030; -; 2.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR004836; Na_Ca_Ex.
DR InterPro; IPR032452; Na_Ca_Ex_C-exten.
DR InterPro; IPR002987; NaCa_exhngr1.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR Pfam; PF03160; Calx-beta; 2.
DR Pfam; PF01699; Na_Ca_ex; 2.
DR Pfam; PF16494; Na_Ca_ex_C; 1.
DR PRINTS; PR01259; NACAEXCHNGR.
DR PRINTS; PR01260; NACAEXCHNGR1.
DR SMART; SM00237; Calx_beta; 2.
DR SUPFAM; SSF141072; SSF141072; 2.
DR TIGRFAMs; TIGR00845; caca; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Calcium; Calcium transport;
KW Calmodulin-binding; Cell membrane; Cell projection; Glycoprotein;
KW Ion transport; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..971
FT /note="Sodium/calcium exchanger 1"
FT /id="PRO_0000019381"
FT TOPO_DOM 33..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..798
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 799..819
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 820..822
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 823..843
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 873..893
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 894..904
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 905..925
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 926..942
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 943..963
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 964..971
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REPEAT 138..178
FT /note="Alpha-1"
FT DOMAIN 393..493
FT /note="Calx-beta 1"
FT DOMAIN 524..624
FT /note="Calx-beta 2"
FT REPEAT 840..876
FT /note="Alpha-2"
FT REGION 251..270
FT /note="Putative calmodulin-binding region"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 481
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 486
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 531
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 532
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 532
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 548
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 584
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 610
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 610
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 611
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 612
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 612
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 716
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70414"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70414"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 602..635
FT /note="TISVKVIDDEEYEKNKTFFIEIGEPRLVEMSEKK -> IITIRIFDREEYEK
FT ECSFSLVLEEPKWIRRGMK (in isoform 4, isoform 5, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:10894800,
FT ECO:0000303|PubMed:15040000, ECO:0000303|PubMed:8195112,
FT ECO:0000303|PubMed:8276763"
FT /id="VSP_003401"
FT VAR_SEQ 636..642
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10894800,
FT ECO:0000303|PubMed:15040000, ECO:0000303|PubMed:8195112,
FT ECO:0000303|PubMed:8276763, ECO:0000303|PubMed:8454039"
FT /id="VSP_003402"
FT VAR_SEQ 649..677
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10894800,
FT ECO:0000303|PubMed:8454039"
FT /id="VSP_003404"
FT VAR_SEQ 649..654
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10894800,
FT ECO:0000303|PubMed:8195112, ECO:0000303|PubMed:8276763,
FT ECO:0000303|PubMed:8454039"
FT /id="VSP_003403"
FT VAR_SEQ 649
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10894800,
FT ECO:0000303|PubMed:15040000"
FT /id="VSP_029836"
FT CONFLICT 148
FT /note="L -> P (in Ref. 5; AAD23388/AAD23389 and 6;
FT AAK52307)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="I -> F (in Ref. 5; AAD23387)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="D -> A (in Ref. 1; CAA48273)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="P -> A (in Ref. 1; CAA48273)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="F -> S (in Ref. 5; AAD23386/AAD23387)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="E -> G (in Ref. 5; AAD23388 and 6; AAK52307)"
FT /evidence="ECO:0000305"
FT CONFLICT 789
FT /note="F -> N (in Ref. 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="A -> R (in Ref. 8)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 971 AA; 108185 MW; EC456CFE3AFC6A69 CRC64;
MLRLSLPPNV SMGFRLVTLV ALLFTHVDHI TADTEAETGG NETTECTGSY YCKKGVILPI
WEPQDPSFGD KIARATVYFV AMVYMFLGVS IIADRFMSSI EVITSQEKEI TIKKPNGETT
KTTVRIWNET VSNLTLMALG SSAPEILLSV IEVCGHNFTA GDLGPSTIVG SAAFNMFIII
ALCVYVVPDG ETRKIKHLRV FFVTAAWSIF AYTWLYIILS VSSPGVVEVW EGLLTFFFFP
ICVVFAWVAD RRLLFYKYVY KRYRAGKQRG MIIEHEGDRP ASKTEIEMDG KVVNSHVDNF
LDGALVLEVD ERDQDDEEAR REMARILKEL KQKHPDKEIE QLIELANYQV LSQQQKSRAF
YRIQATRLMT GAGNILKRHA ADQARKAVSM HEVNMDVVEN DPVSKVFFEQ GTYQCLENCG
TVALTIIRRG GDLTNTVFVD FRTEDGTANA GSDYEFTEGT VIFKPGETQK EIRVGIIDDD
IFEEDENFLV HLSNVRVSSE VSEDGILDSN HVSAIACLGS PNTATITIFD DDHAGIFTFE
EPVTHVSESI GIMEVKVLRT SGARGNVIIP YKTIEGTARG GGEDFEDTCG ELEFQNDEIV
KTISVKVIDD EEYEKNKTFF IEIGEPRLVE MSEKKALLLN ELGGFTLTEG KKMYGQPVFR
KVHARDHPIP STVISISEEY DDKQPLTSKE EEERRIAEMG RPILGEHTKL EVIIEESYEF
KSTVDKLIKK TNLALVVGTN SWREQFIEAI TVSAGEDDDD DECGEEKLPS CFDYVMHFLT
VFWKVLFAFV PPTEYWNGWA CFIVSILMIG LLTAFIGDLA SHFGCTIGLK DSVTAVVFVA
LGTSVPDTFA SKVAATQDQY ADASIGNVTG SNAVNVFLGI GVAWSIAAIY HAANGEQFKV
SPGTLAFSVT LFTIFAFINV GVLLYRRRPE IGGELGGPRT AKLLTSSLFV LLWLLYIFFS
SLEAYCHIKG F
