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Sodium/calcium exchanger 1 (Na( )/Ca(2 )-exchange protein 1) (Solute carrier family 8 member 1)

 NAC1_HUMAN              Reviewed;         973 AA.
P32418; A8K6N1; D6W595; O95849; Q4QQG6; Q587I6; Q59GN4; Q9UBL8;
Q9UD55; Q9UDN1; Q9UDN2; Q9UKX6;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 3.
22-NOV-2017, entry version 173.
RecName: Full=Sodium/calcium exchanger 1;
AltName: Full=Na(+)/Ca(2+)-exchange protein 1;
AltName: Full=Solute carrier family 8 member 1;
Flags: Precursor;
Name=SLC8A1;
Synonyms=CNC, NCX1 {ECO:0000303|PubMed:11241183,
ECO:0000303|PubMed:23376057};
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 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=1374913; DOI=10.1073/pnas.89.10.4769;
Komuro I., Wenninger K.E., Philipson K.D., Izumo S.;
"Molecular cloning and characterization of the human cardiac Na+/Ca2+
exchanger cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 89:4769-4773(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 7), FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=11241183; DOI=10.1677/joe.0.1680517;
Van Eylen F., Bollen A., Herchuelz A.;
"NCX1 Na/Ca exchanger splice variants in pancreatic islet cells.";
J. Endocrinol. 168:517-526(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
Mangini N.J., Chen W., Wang Q., Kennedy B.G.;
"Na+/Ca2+ exchanger isoforms in cultured human retinal pigment
epithelium.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 459-681 (ISOFORM 10).
PubMed=10908415; DOI=10.1007/s00223001098;
Lundquist P., Lundgren T., Gritli-Linde A., Linde A.;
"Na+/Ca2+ exchanger isoforms of rat odontoblasts and osteoblasts.";
Calcif. Tissue Int. 67:60-67(2000).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 558-973 (ISOFORM 5).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 594-973 (ISOFORM 5).
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 600-684 (ISOFORM 3).
TISSUE=Embryonic kidney;
PubMed=8048567;
Loo T.W., Clarke D.M.;
"Functional expression of human renal Na+/Ca2+ exchanger in insect
cells.";
Am. J. Physiol. 267:F70-F74(1994).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=1476165;
Kofuji P., Hadley R.W., Kieval R.S., Lederer W.J., Schulze D.H.;
"Expression of the Na-Ca exchanger in diverse tissues: a study using
the cloned human cardiac Na-Ca exchanger.";
Am. J. Physiol. 263:C1241-C1249(1992).
[12]
TOPOLOGY.
PubMed=23376057; DOI=10.1016/j.yjmcc.2013.01.010;
Ren X., Philipson K.D.;
"The topology of the cardiac Na(+)/Ca(2)(+) exchanger, NCX1.";
J. Mol. Cell. Cardiol. 57:68-71(2013).
[13]
REVIEW.
PubMed=23506867; DOI=10.1016/j.mam.2012.07.003;
Khananshvili D.;
"The SLC8 gene family of sodium-calcium exchangers (NCX) - structure,
function, and regulation in health and disease.";
Mol. Aspects Med. 34:220-235(2013).
-!- FUNCTION: Mediates the exchange of one Ca(2+) ion against three to
four Na(+) ions across the cell membrane, and thereby contributes
to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-
dependent cellular processes (PubMed:1374913, PubMed:11241183,
PubMed:1476165). Contributes to Ca(2+) transport during
excitation-contraction coupling in muscle. In a first phase,
voltage-gated channels mediate the rapid increase of cytoplasmic
Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic
reticulum. SLC8A1 mediates the export of Ca(2+) from the cell
during the next phase, so that cytoplasmic Ca(2+) levels rapidly
return to baseline. Required for normal embryonic heart
development and the onset of heart contractions.
{ECO:0000250|UniProtKB:P70414, ECO:0000269|PubMed:11241183,
ECO:0000269|PubMed:1374913, ECO:0000269|PubMed:1476165}.
-!- ENZYME REGULATION: Activated by micromolar levels of Ca(2+).
{ECO:0000305}.
-!- INTERACTION:
Q01484-2:ANK2; NbExp=2; IntAct=EBI-2682189, EBI-941994;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11241183,
ECO:0000269|PubMed:1374913, ECO:0000269|PubMed:1476165}; Multi-
pass membrane protein {ECO:0000269|PubMed:23376057}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=NaCa1, NCX1.1;
IsoId=P32418-1; Sequence=Displayed;
Name=3; Synonyms=NaCa3, NCX1.3;
IsoId=P32418-2; Sequence=VSP_003397, VSP_003398, VSP_003400;
Name=7; Synonyms=NaCa7, NCX1.7;
IsoId=P32418-3; Sequence=VSP_003397, VSP_003398, VSP_003399;
Name=10; Synonyms=NaCa10, NCX1.10;
IsoId=P32418-4; Sequence=VSP_003397, VSP_003398;
Name=5;
IsoId=P32418-5; Sequence=VSP_003399;
-!- TISSUE SPECIFICITY: Detected primarily in heart and at lower
levels in brain (PubMed:1374913). Expressed in cardiac sarcolemma,
brain, kidney, liver, pancreas, skeletal muscle, placenta and lung
(PubMed:1476165). {ECO:0000269|PubMed:1374913,
ECO:0000269|PubMed:1476165}.
-!- DOMAIN: The cytoplasmic Calx-beta domains bind the regulatory
Ca(2+). The first Calx-beta domain can bind up to four Ca(2+)
ions. The second domain can bind another two Ca(2+) ions that are
essential for calcium-regulated ion exchange.
{ECO:0000250|UniProtKB:P23685}.
-!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC
2.A.19) family. SLC8 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH98308.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; M91368; AAA35702.1; -; mRNA.
EMBL; AF108388; AAF08987.1; -; mRNA.
EMBL; AF108389; AAF08988.1; -; mRNA.
EMBL; AF128524; AAD26362.1; -; mRNA.
EMBL; AK291696; BAF84385.1; -; mRNA.
EMBL; AC007254; AAF19235.1; -; Genomic_DNA.
EMBL; AC007281; AAF19237.1; -; Genomic_DNA.
EMBL; AC007377; AAX81985.1; -; Genomic_DNA.
EMBL; CH471053; EAX00331.1; -; Genomic_DNA.
EMBL; CH471053; EAX00332.1; -; Genomic_DNA.
EMBL; CH471053; EAX00333.1; -; Genomic_DNA.
EMBL; CH471053; EAX00334.1; -; Genomic_DNA.
EMBL; CH471053; EAX00335.1; -; Genomic_DNA.
EMBL; CH471053; EAX00336.1; -; Genomic_DNA.
EMBL; AF115505; AAD17213.1; -; mRNA.
EMBL; AB209075; BAD92312.1; -; mRNA.
EMBL; BC098308; AAH98308.1; ALT_INIT; mRNA.
CCDS; CCDS1806.1; -. [P32418-1]
CCDS; CCDS46264.1; -. [P32418-2]
CCDS; CCDS46265.1; -. [P32418-5]
CCDS; CCDS59430.1; -. [P32418-4]
PIR; S32815; S32815.
RefSeq; NP_001106271.1; NM_001112800.1. [P32418-5]
RefSeq; NP_001106272.1; NM_001112801.1. [P32418-3]
RefSeq; NP_001106273.1; NM_001112802.1. [P32418-2]
RefSeq; NP_001239553.1; NM_001252624.1. [P32418-4]
RefSeq; NP_066920.1; NM_021097.2. [P32418-1]
RefSeq; XP_005264571.1; XM_005264514.3.
RefSeq; XP_006712144.1; XM_006712081.2. [P32418-1]
RefSeq; XP_006712145.1; XM_006712082.3. [P32418-1]
RefSeq; XP_006712146.1; XM_006712083.3. [P32418-1]
RefSeq; XP_006712147.1; XM_006712084.3. [P32418-1]
RefSeq; XP_006712148.1; XM_006712085.3. [P32418-1]
RefSeq; XP_011531356.1; XM_011533054.2. [P32418-1]
RefSeq; XP_011531357.1; XM_011533055.2. [P32418-1]
RefSeq; XP_011531358.1; XM_011533056.1. [P32418-1]
RefSeq; XP_016860235.1; XM_017004746.1. [P32418-1]
RefSeq; XP_016860237.1; XM_017004748.1. [P32418-1]
RefSeq; XP_016860238.1; XM_017004749.1. [P32418-1]
RefSeq; XP_016860239.1; XM_017004750.1. [P32418-1]
RefSeq; XP_016860240.1; XM_017004751.1. [P32418-1]
RefSeq; XP_016860241.1; XM_017004752.1. [P32418-1]
RefSeq; XP_016860242.1; XM_017004753.1. [P32418-1]
RefSeq; XP_016860243.1; XM_017004754.1.
RefSeq; XP_016860247.1; XM_017004758.1.
UniGene; Hs.31961; -.
UniGene; Hs.468274; -.
UniGene; Hs.744988; -.
ProteinModelPortal; P32418; -.
SMR; P32418; -.
BioGrid; 112436; 1.
DIP; DIP-48356N; -.
ELM; P32418; -.
IntAct; P32418; 2.
STRING; 9606.ENSP00000332931; -.
BindingDB; P32418; -.
ChEMBL; CHEMBL4076; -.
DrugBank; DB00132; Alpha-Linolenic Acid.
DrugBank; DB00159; Icosapent.
TCDB; 2.A.19.3.4; the ca(2+):cation antiporter (caca) family.
iPTMnet; P32418; -.
PhosphoSitePlus; P32418; -.
BioMuta; SLC8A1; -.
DMDM; 12644210; -.
EPD; P32418; -.
PaxDb; P32418; -.
PeptideAtlas; P32418; -.
PRIDE; P32418; -.
Ensembl; ENST00000332839; ENSP00000332931; ENSG00000183023. [P32418-1]
Ensembl; ENST00000402441; ENSP00000385188; ENSG00000183023. [P32418-2]
Ensembl; ENST00000403092; ENSP00000384763; ENSG00000183023. [P32418-1]
Ensembl; ENST00000405269; ENSP00000385535; ENSG00000183023. [P32418-2]
Ensembl; ENST00000405901; ENSP00000385678; ENSG00000183023. [P32418-5]
Ensembl; ENST00000406391; ENSP00000385811; ENSG00000183023. [P32418-2]
Ensembl; ENST00000406785; ENSP00000383886; ENSG00000183023. [P32418-2]
Ensembl; ENST00000408028; ENSP00000384908; ENSG00000183023. [P32418-4]
GeneID; 6546; -.
KEGG; hsa:6546; -.
UCSC; uc002rrx.4; human. [P32418-1]
CTD; 6546; -.
DisGeNET; 6546; -.
EuPathDB; HostDB:ENSG00000183023.18; -.
GeneCards; SLC8A1; -.
HGNC; HGNC:11068; SLC8A1.
HPA; CAB022694; -.
HPA; HPA070007; -.
MIM; 182305; gene.
neXtProt; NX_P32418; -.
OpenTargets; ENSG00000183023; -.
PharmGKB; PA314; -.
eggNOG; KOG1306; Eukaryota.
eggNOG; ENOG410XPJP; LUCA.
GeneTree; ENSGT00730000110414; -.
HOGENOM; HOG000266971; -.
HOVERGEN; HBG006441; -.
InParanoid; P32418; -.
KO; K05849; -.
OMA; DDEECGE; -.
OrthoDB; EOG091G0EC1; -.
PhylomeDB; P32418; -.
TreeFam; TF314308; -.
Reactome; R-HSA-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-HSA-425561; Sodium/Calcium exchangers.
Reactome; R-HSA-5578775; Ion homeostasis.
ChiTaRS; SLC8A1; human.
GenomeRNAi; 6546; -.
PRO; PR:P32418; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000183023; -.
CleanEx; HS_SLC8A1; -.
ExpressionAtlas; P32418; baseline and differential.
Genevisible; P32418; HS.
GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
GO; GO:0014704; C:intercalated disc; ISS:BHF-UCL.
GO; GO:0005874; C:microtubule; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
GO; GO:0042383; C:sarcolemma; ISS:BHF-UCL.
GO; GO:0030315; C:T-tubule; ISS:BHF-UCL.
GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0005432; F:calcium:sodium antiporter activity; IDA:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0008092; F:cytoskeletal protein binding; IDA:BHF-UCL.
GO; GO:0099580; F:ion antiporter activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl.
GO; GO:0044325; F:ion channel binding; ISS:BHF-UCL.
GO; GO:1901660; P:calcium ion export; IDA:BHF-UCL.
GO; GO:0055074; P:calcium ion homeostasis; ISS:BHF-UCL.
GO; GO:0070509; P:calcium ion import; IDA:BHF-UCL.
GO; GO:0070588; P:calcium ion transmembrane transport; IGI:UniProtKB.
GO; GO:0060402; P:calcium ion transport into cytosol; ISS:BHF-UCL.
GO; GO:0055013; P:cardiac muscle cell development; ISS:BHF-UCL.
GO; GO:0060048; P:cardiac muscle contraction; TAS:BHF-UCL.
GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; ISS:BHF-UCL.
GO; GO:0071313; P:cellular response to caffeine; ISS:BHF-UCL.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:BHF-UCL.
GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
GO; GO:0060401; P:cytosolic calcium ion transport; TAS:BHF-UCL.
GO; GO:0006811; P:ion transport; TAS:Reactome.
GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; TAS:BHF-UCL.
GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
GO; GO:0030501; P:positive regulation of bone mineralization; IMP:UniProtKB.
GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl.
GO; GO:0098735; P:positive regulation of the force of heart contraction; IMP:BHF-UCL.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; TAS:BHF-UCL.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISS:BHF-UCL.
GO; GO:0010649; P:regulation of cell communication by electrical coupling; TAS:BHF-UCL.
GO; GO:0002027; P:regulation of heart rate; ISS:BHF-UCL.
GO; GO:0002028; P:regulation of sodium ion transport; IEA:Ensembl.
GO; GO:0002026; P:regulation of the force of heart contraction; ISS:BHF-UCL.
GO; GO:0055119; P:relaxation of cardiac muscle; TAS:BHF-UCL.
GO; GO:0044557; P:relaxation of smooth muscle; ISS:BHF-UCL.
GO; GO:0033198; P:response to ATP; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
GO; GO:0035994; P:response to muscle stretch; IMP:BHF-UCL.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0071436; P:sodium ion export; IDA:BHF-UCL.
GO; GO:0097369; P:sodium ion import; IDA:BHF-UCL.
GO; GO:0035725; P:sodium ion transmembrane transport; IMP:UniProtKB.
GO; GO:0021537; P:telencephalon development; IEA:Ensembl.
GO; GO:0014829; P:vascular smooth muscle contraction; ISS:BHF-UCL.
InterPro; IPR003644; Calx_beta.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR004836; Na_Ca_Ex.
InterPro; IPR032452; Na_Ca_Ex_C-exten.
InterPro; IPR002987; NaCa_exhngr1.
InterPro; IPR004837; NaCa_Exmemb.
Pfam; PF03160; Calx-beta; 2.
Pfam; PF01699; Na_Ca_ex; 2.
Pfam; PF16494; Na_Ca_ex_C; 1.
PRINTS; PR01259; NACAEXCHNGR.
PRINTS; PR01260; NACAEXCHNGR1.
SMART; SM00237; Calx_beta; 2.
TIGRFAMs; TIGR00845; caca; 1.
1: Evidence at protein level;
Alternative splicing; Antiport; Calcium; Calcium transport;
Calmodulin-binding; Cell membrane; Complete proteome; Glycoprotein;
Ion transport; Membrane; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Signal; Sodium; Sodium transport;
Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 35 {ECO:0000255}.
CHAIN 36 973 Sodium/calcium exchanger 1.
/FTId=PRO_0000019379.
TOPO_DOM 36 74 Extracellular. {ECO:0000255}.
TRANSMEM 75 95 Helical. {ECO:0000255}.
TOPO_DOM 96 136 Cytoplasmic. {ECO:0000255}.
TRANSMEM 137 157 Helical. {ECO:0000255}.
TOPO_DOM 158 170 Extracellular. {ECO:0000255}.
TRANSMEM 171 191 Helical. {ECO:0000255}.
TOPO_DOM 192 204 Cytoplasmic. {ECO:0000255}.
TRANSMEM 205 225 Helical. {ECO:0000255}.
TOPO_DOM 226 231 Extracellular. {ECO:0000255}.
TRANSMEM 232 252 Helical. {ECO:0000255}.
TOPO_DOM 253 800 Cytoplasmic. {ECO:0000255}.
TRANSMEM 801 821 Helical. {ECO:0000255}.
TOPO_DOM 822 824 Extracellular. {ECO:0000255}.
TRANSMEM 825 845 Helical. {ECO:0000255}.
TOPO_DOM 846 874 Cytoplasmic. {ECO:0000255}.
TRANSMEM 875 895 Helical. {ECO:0000255}.
TOPO_DOM 896 906 Extracellular. {ECO:0000255}.
TRANSMEM 907 927 Helical. {ECO:0000255}.
TOPO_DOM 928 944 Cytoplasmic. {ECO:0000255}.
TRANSMEM 945 965 Helical. {ECO:0000255}.
TOPO_DOM 966 973 Extracellular. {ECO:0000255}.
REPEAT 141 181 Alpha-1.
DOMAIN 396 496 Calx-beta 1.
DOMAIN 527 627 Calx-beta 2.
REPEAT 842 878 Alpha-2.
REGION 254 273 Putative calmodulin-binding region.
{ECO:0000250|UniProtKB:P23685}.
COMPBIAS 239 242 Poly-Phe.
COMPBIAS 692 695 Poly-Glu.
COMPBIAS 759 763 Poly-Asp.
METAL 420 420 Calcium 1.
{ECO:0000250|UniProtKB:P23685}.
METAL 420 420 Calcium 2.
{ECO:0000250|UniProtKB:P23685}.
METAL 420 420 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 456 456 Calcium 1.
{ECO:0000250|UniProtKB:P23685}.
METAL 456 456 Calcium 4.
{ECO:0000250|UniProtKB:P23685}.
METAL 481 481 Calcium 2.
{ECO:0000250|UniProtKB:P23685}.
METAL 482 482 Calcium 1.
{ECO:0000250|UniProtKB:P23685}.
METAL 482 482 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P23685}.
METAL 482 482 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 482 482 Calcium 4.
{ECO:0000250|UniProtKB:P23685}.
METAL 484 484 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P23685}.
METAL 486 486 Calcium 1.
{ECO:0000250|UniProtKB:P23685}.
METAL 486 486 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 486 486 Calcium 4.
{ECO:0000250|UniProtKB:P23685}.
METAL 489 489 Calcium 4.
{ECO:0000250|UniProtKB:P23685}.
METAL 533 533 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 534 534 Calcium 2.
{ECO:0000250|UniProtKB:P23685}.
METAL 535 535 Calcium 2.
{ECO:0000250|UniProtKB:P23685}.
METAL 535 535 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 551 551 Calcium 5.
{ECO:0000250|UniProtKB:P23685}.
METAL 587 587 Calcium 6.
{ECO:0000250|UniProtKB:P23685}.
METAL 613 613 Calcium 5.
{ECO:0000250|UniProtKB:P23685}.
METAL 613 613 Calcium 6.
{ECO:0000250|UniProtKB:P23685}.
METAL 614 614 Calcium 6.
{ECO:0000250|UniProtKB:P23685}.
METAL 615 615 Calcium 5; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P23685}.
METAL 615 615 Calcium 6.
{ECO:0000250|UniProtKB:P23685}.
METAL 718 718 Calcium 5.
{ECO:0000250|UniProtKB:P23685}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000250|UniProtKB:P70414}.
MOD_RES 392 392 Phosphoserine.
{ECO:0000250|UniProtKB:P70414,
ECO:0000255}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 605 613 TISVKVIDD -> IITIRIFDR (in isoform 3,
isoform 7 and isoform 10).
{ECO:0000303|PubMed:10908415,
ECO:0000303|PubMed:11241183,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:8048567,
ECO:0000303|Ref.3}.
/FTId=VSP_003397.
VAR_SEQ 619 645 NKTFFLEIGEPRLVEMSEKKALLLNEL -> ECSFSLVLEE
PKWIRRGMK (in isoform 3, isoform 7 and
isoform 10).
{ECO:0000303|PubMed:10908415,
ECO:0000303|PubMed:11241183,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:8048567,
ECO:0000303|Ref.3}.
/FTId=VSP_003398.
VAR_SEQ 652 679 Missing (in isoform 3).
{ECO:0000303|PubMed:11241183,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:8048567}.
/FTId=VSP_003400.
VAR_SEQ 652 656 Missing (in isoform 7 and isoform 5).
{ECO:0000303|PubMed:11241183,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.3, ECO:0000303|Ref.8}.
/FTId=VSP_003399.
VARIANT 692 692 E -> V (in dbSNP:rs5557).
/FTId=VAR_014847.
SEQUENCE 973 AA; 108547 MW; 17DFC1B1F15921D8 CRC64;
MYNMRRLSLS PTFSMGFHLL VTVSLLFSHV DHVIAETEME GEGNETGECT GSYYCKKGVI
LPIWEPQDPS FGDKIARATV YFVAMVYMFL GVSIIADRFM SSIEVITSQE KEITIKKPNG
ETTKTTVRIW NETVSNLTLM ALGSSAPEIL LSVIEVCGHN FTAGDLGPST IVGSAAFNMF
IIIALCVYVV PDGETRKIKH LRVFFVTAAW SIFAYTWLYI ILSVISPGVV EVWEGLLTFF
FFPICVVFAW VADRRLLFYK YVYKRYRAGK QRGMIIEHEG DRPSSKTEIE MDGKVVNSHV
ENFLDGALVL EVDERDQDDE EARREMARIL KELKQKHPDK EIEQLIELAN YQVLSQQQKS
RAFYRIQATR LMTGAGNILK RHAADQARKA VSMHEVNTEV TENDPVSKIF FEQGTYQCLE
NCGTVALTII RRGGDLTNTV FVDFRTEDGT ANAGSDYEFT EGTVVFKPGD TQKEIRVGII
DDDIFEEDEN FLVHLSNVKV SSEASEDGIL EANHVSTLAC LGSPSTATVT IFDDDHAGIF
TFEEPVTHVS ESIGIMEVKV LRTSGARGNV IVPYKTIEGT ARGGGEDFED TCGELEFQND
EIVKTISVKV IDDEEYEKNK TFFLEIGEPR LVEMSEKKAL LLNELGGFTI TGKYLFGQPV
FRKVHAREHP ILSTVITIAD EYDDKQPLTS KEEEERRIAE MGRPILGEHT KLEVIIEESY
EFKSTVDKLI KKTNLALVVG TNSWREQFIE AITVSAGEDD DDDECGEEKL PSCFDYVMHF
LTVFWKVLFA FVPPTEYWNG WACFIVSILM IGLLTAFIGD LASHFGCTIG LKDSVTAVVF
VALGTSVPDT FASKVAATQD QYADASIGNV TGSNAVNVFL GIGVAWSIAA IYHAANGEQF
KVSPGTLAFS VTLFTIFAFI NVGVLLYRRR PEIGGELGGP RTAKLLTSCL FVLLWLLYIF
FSSLEAYCHI KGF


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