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Sodium/calcium exchanger 3 (Na( )/Ca(2 )-exchange protein 3) (Solute carrier family 8 member 3)

 NAC3_MOUSE              Reviewed;         928 AA.
S4R2P9; Q7TS90; Q8VHJ8;
09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
18-SEP-2013, sequence version 1.
27-SEP-2017, entry version 36.
RecName: Full=Sodium/calcium exchanger 3;
AltName: Full=Na(+)/Ca(2+)-exchange protein 3;
AltName: Full=Solute carrier family 8 member 3;
Flags: Precursor;
Name=Slc8a3 {ECO:0000312|MGI:MGI:107976};
Synonyms=Ncx3 {ECO:0000303|PubMed:21959935,
ECO:0000303|PubMed:24616101};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAL39160.1};
TISSUE=Skeletal muscle {ECO:0000312|EMBL:AAL39160.1};
Kraev A.;
"Towards complete inventory of calcium transporters of the house
mouse.";
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE38073.1};
TISSUE=Embryo {ECO:0000312|EMBL:BAE38073.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000138735,
ECO:0000312|Proteomes:UP000000589};
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH52435.1};
TISSUE=Brain {ECO:0000312|EMBL:AAH52435.1};
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).
[5]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=14722618; DOI=10.1172/JCI18688;
Sokolow S., Manto M., Gailly P., Molgo J., Vandebrouck C.,
Vanderwinden J.M., Herchuelz A., Schurmans S.;
"Impaired neuromuscular transmission and skeletal muscle fiber
necrosis in mice lacking Na/Ca exchanger 3.";
J. Clin. Invest. 113:265-273(2004).
[6]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=21593315; DOI=10.1523/JNEUROSCI.6296-10.2011;
Molinaro P., Viggiano D., Nistico R., Sirabella R., Secondo A.,
Boscia F., Pannaccione A., Scorziello A., Mehdawy B., Sokolow S.,
Herchuelz A., Di Renzo G.F., Annunziato L.;
"Na+ -Ca2+ exchanger (NCX3) knock-out mice display an impairment in
hippocampal long-term potentiation and spatial learning and memory.";
J. Neurosci. 31:7312-7321(2011).
[7]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=21959935; DOI=10.1038/cdd.2011.125;
Boscia F., D'Avanzo C., Pannaccione A., Secondo A., Casamassa A.,
Formisano L., Guida N., Sokolow S., Herchuelz A., Annunziato L.;
"Silencing or knocking out the Na(+)/Ca(2+) exchanger-3 (NCX3) impairs
oligodendrocyte differentiation.";
Cell Death Differ. 19:562-572(2012).
[8]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AKAP1, AND TISSUE
SPECIFICITY.
PubMed=24101730; DOI=10.1242/jcs.129668;
Scorziello A., Savoia C., Sisalli M.J., Adornetto A., Secondo A.,
Boscia F., Esposito A., Polishchuk E.V., Polishchuk R.S., Molinaro P.,
Carlucci A., Lignitto L., Di Renzo G., Feliciello A., Annunziato L.;
"NCX3 regulates mitochondrial Ca(2+) handling through the AKAP121-
anchored signaling complex and prevents hypoxia-induced neuronal
death.";
J. Cell Sci. 126:5566-5577(2013).
[9]
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).
[10]
FUNCTION (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2),
TISSUE SPECIFICITY (ISOFORMS 1 AND 2), AND ENZYME REGULATION (ISOFORMS
1 AND 2).
PubMed=24616101; DOI=10.1074/jbc.M113.529388;
Michel L.Y., Verkaart S., Koopman W.J., Willems P.H., Hoenderop J.G.,
Bindels R.J.;
"Function and regulation of the Na+-Ca2+ exchanger NCX3 splice
variants in brain and skeletal muscle.";
J. Biol. Chem. 289:11293-11303(2014).
[11] {ECO:0000244|PDB:2LT9}
STRUCTURE BY NMR OF 528-675.
PubMed=22806131; DOI=10.1007/s10858-012-9654-1;
Breukels V., Touw W.G., Vuister G.W.;
"NMR structure note: solution structure of Ca binding domain 2B of the
third isoform of the Na/Ca exchanger.";
J. Biomol. NMR 54:115-121(2012).
-!- FUNCTION: Mediates the electrogenic exchange of Ca(2+) against
Na(+) ions across the cell membrane, and thereby contributes to
the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent
cellular processes. Contributes to cellular Ca(2+) homeostasis in
excitable cells, both in muscle and in brain (PubMed:14722618,
PubMed:21593315). 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. SLC8A3 mediates the
export of Ca(2+) from the cell during the next phase, so that
cytoplasmic Ca(2+) levels rapidly return to baseline
(PubMed:14722618, PubMed:21593315). Contributes to Ca(2+)
transport during excitation-contraction coupling in muscle
(PubMed:14722618). In neurons, contributes to the rapid decrease
of cytoplasmic Ca(2+) levels back to baseline after neuronal
activation, and thereby contributes to modulate synaptic
plasticity, learning and memory (PubMed:21593315). Required for
normal oligodendrocyte differentiation and for normal myelination
(PubMed:21959935). Mediates Ca(2+) efflux from mitochondria and
contributes to mitochondrial Ca(2+) ion homeostasis
(PubMed:24616101). Isoform 1 displays higher calcium exchanger
activity than isoform 2, probably because isoform 1 has a lower
threshold for activation by cytoplasmic Ca(2+) (PubMed:24616101).
{ECO:0000269|PubMed:14722618, ECO:0000269|PubMed:21593315,
ECO:0000269|PubMed:21959935, ECO:0000269|PubMed:24616101}.
-!- ENZYME REGULATION: Calcium transport is stimulated by cytoplasmic
Ca(2+) and is inhibited by Na(+). Isoform 1 is more sensitive to
stimulation by Ca(2+) than isoform 2. Isoform 2 is more sensitive
to inactivation by Na(+). {ECO:0000269|PubMed:24616101}.
-!- SUBUNIT: Interacts with AKAP1. {ECO:0000269|PubMed:24616101}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14722618,
ECO:0000269|PubMed:24101730}; Multi-pass membrane protein
{ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:P70549}. Cell
projection, dendrite {ECO:0000250|UniProtKB:P70549}. Cell
projection, dendritic spine {ECO:0000250|UniProtKB:P70549}. Cell
membrane, sarcolemma {ECO:0000269|PubMed:14722618}. Cytoplasm,
sarcoplasm {ECO:0000269|PubMed:14722618}. Cell junction
{ECO:0000269|PubMed:14722618}. Mitochondrion outer membrane
{ECO:0000269|PubMed:24101730}; Multi-pass membrane protein
{ECO:0000305}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:P57103}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:24101730}; Multi-pass membrane protein
{ECO:0000305}. Note=Detected at neuromuscular junctions.
{ECO:0000269|PubMed:14722618}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:24616101}; Multi-pass membrane protein
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane
{ECO:0000269|PubMed:24616101}; Multi-pass membrane protein
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=NCX3-AC {ECO:0000303|PubMed:24616101};
IsoId=S4R2P9-1; Sequence=Displayed;
Name=2; Synonyms=NCX3-B {ECO:0000303|PubMed:24616101};
IsoId=S4R2P9-2; Sequence=VSP_057981;
-!- TISSUE SPECIFICITY: Detected in gray and white matter in the
spinal cord (PubMed:21959935). Detected in hippocampus neurons
(PubMed:21593315). Detected in brain cortex neurons
(PubMed:24101730). Detected in skeletal muscle (at protein level)
(PubMed:14722618). Isoform 1 and isoform 2 are highly expressed in
brain; levels are higher for isoform 2 (PubMed:24616101). Isoform
1 and isoform 2 are detected in soleus muscle; levels are higher
for isoform 1 (PubMed:24616101). Detected in gastrocnemius muscle
(PubMed:14722618). {ECO:0000269|PubMed:14722618,
ECO:0000269|PubMed:21593315, ECO:0000269|PubMed:21959935,
ECO:0000269|PubMed:24101730, ECO:0000269|PubMed:24616101}.
-!- INDUCTION: Down-regulated by hypoxia combined with glucose
deprivation (at protein level). {ECO:0000269|PubMed:24101730}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: Mice appear grossly normal, are viable and
fertile, but display muscle fiber necrosis; this affects less than
10% of all fibers. Muscle fibers from flexor digitorum brevis show
lack of calcium exchange activity, and very slow return of
cytoplasmic Ca(2+) to baseline levels after stimulation with
caffeine, a stimulus that triggers release of Ca(2+) stores from
the sarcoplasmic reticulum. Mutant mice display decreased
endurance and perform poorly on the rota-rod test or when hanging
from a taut wire, indicating poor coordination and increased
fatigue (PubMed:14722618). Mutant mice display increased
cytoplasmic Ca(2+) levels and increased delays in the decrease of
cytoplasmic Ca(2+) back to baseline levels after stimulation of
hippocampus neurons (PubMed:21593315). They show impaired synaptic
transmisison, impaired long-term potentiation, impaired learning
and memory (PubMed:21593315). Besides, mutant mice display a
decreased size of the spinal cord, decreased myelination,
decreased numbers of oligodendrocytes and increased numbers of
oligodendrocyte precursor cells (PubMed:21959935).
{ECO:0000269|PubMed:14722618, ECO:0000269|PubMed:21959935}.
-!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC
2.A.19) family. SLC8 subfamily. {ECO:0000305}.
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EMBL; AF453257; AAL39160.1; -; mRNA.
EMBL; AK165197; BAE38073.1; -; mRNA.
EMBL; AC124384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC052435; AAH52435.1; -; mRNA.
EMBL; BC080862; AAH80862.1; -; mRNA.
CCDS; CCDS36485.1; -. [S4R2P9-1]
CCDS; CCDS49103.1; -. [S4R2P9-2]
RefSeq; NP_001161392.1; NM_001167920.1. [S4R2P9-2]
RefSeq; NP_536688.2; NM_080440.3. [S4R2P9-1]
UniGene; Mm.443748; -.
PDB; 2LT9; NMR; -; A=528-682.
PDBsum; 2LT9; -.
ProteinModelPortal; S4R2P9; -.
SMR; S4R2P9; -.
STRING; 10090.ENSMUSP00000063258; -.
iPTMnet; S4R2P9; -.
PhosphoSitePlus; S4R2P9; -.
PaxDb; S4R2P9; -.
PRIDE; S4R2P9; -.
Ensembl; ENSMUST00000085238; ENSMUSP00000082334; ENSMUSG00000079055. [S4R2P9-2]
Ensembl; ENSMUST00000182208; ENSMUSP00000138735; ENSMUSG00000079055. [S4R2P9-1]
GeneID; 110893; -.
KEGG; mmu:110893; -.
UCSC; uc007obv.2; mouse. [S4R2P9-1]
UCSC; uc007obw.2; mouse.
CTD; 6547; -.
MGI; MGI:107976; Slc8a3.
eggNOG; KOG1306; Eukaryota.
eggNOG; ENOG410XPJP; LUCA.
GeneTree; ENSGT00730000110414; -.
HOGENOM; HOG000266971; -.
HOVERGEN; HBG006441; -.
KO; K05849; -.
OMA; LPIWYPE; -.
OrthoDB; EOG091G0EC1; -.
Reactome; R-MMU-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-MMU-425561; Sodium/Calcium exchangers.
Reactome; R-MMU-5578775; Ion homeostasis.
PRO; PR:S4R2P9; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000079055; -.
ExpressionAtlas; S4R2P9; baseline and differential.
Genevisible; Q8VHJ8; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:MGI.
GO; GO:0005874; C:microtubule; IEA:Ensembl.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
GO; GO:0016528; C:sarcoplasm; IEA:UniProtKB-SubCell.
GO; GO:0015368; F:calcium:cation antiporter activity; IDA:MGI.
GO; GO:0005432; F:calcium:sodium antiporter activity; IMP:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0099580; F:ion antiporter activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1990034; P:calcium ion export from cell; IEA:Ensembl.
GO; GO:0098703; P:calcium ion import across plasma membrane; IEA:Ensembl.
GO; GO:0070588; P:calcium ion transmembrane transport; IMP:UniProtKB.
GO; GO:0007154; P:cell communication; IEA:InterPro.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
GO; GO:0007612; P:learning; IMP:UniProtKB.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:UniProtKB.
GO; GO:0007613; P:memory; IMP:UniProtKB.
GO; GO:0030001; P:metal ion transport; IDA:MGI.
GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IMP:UniProtKB.
GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IMP:UniProtKB.
GO; GO:0042552; P:myelination; IMP:UniProtKB.
GO; GO:0048709; P:oligodendrocyte differentiation; IMP:UniProtKB.
GO; GO:0014819; P:regulation of skeletal muscle contraction; IMP:UniProtKB.
GO; GO:0035725; P:sodium ion transmembrane transport; IMP:UniProtKB.
GO; GO:0021537; P:telencephalon development; IEA:Ensembl.
InterPro; IPR003644; Calx_beta.
InterPro; IPR004836; Na_Ca_Ex.
InterPro; IPR032452; Na_Ca_Ex_C-exten.
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.
SMART; SM00237; Calx_beta; 2.
TIGRFAMs; TIGR00845; caca; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Antiport; Calcium;
Calcium transport; Calmodulin-binding; Cell junction; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Endoplasmic reticulum;
Glycoprotein; Ion transport; Membrane; Metal-binding; Mitochondrion;
Mitochondrion outer membrane; Reference proteome; Repeat; Signal;
Sodium; Sodium transport; Transmembrane; Transmembrane helix;
Transport.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 928 Sodium/calcium exchanger 3.
/FTId=PRO_0000434797.
TOPO_DOM 31 73 Extracellular. {ECO:0000305}.
TRANSMEM 74 94 Helical. {ECO:0000255}.
TOPO_DOM 95 147 Cytoplasmic. {ECO:0000305}.
TRANSMEM 148 168 Helical. {ECO:0000255}.
TOPO_DOM 169 169 Extracellular. {ECO:0000305}.
TRANSMEM 170 190 Helical. {ECO:0000255}.
TOPO_DOM 191 201 Cytoplasmic. {ECO:0000305}.
TRANSMEM 202 222 Helical. {ECO:0000255}.
TOPO_DOM 223 230 Extracellular. {ECO:0000305}.
TRANSMEM 231 251 Helical. {ECO:0000255}.
TOPO_DOM 252 727 Cytoplasmic. {ECO:0000305}.
TRANSMEM 728 748 Helical. {ECO:0000255}.
TOPO_DOM 749 755 Extracellular. {ECO:0000305}.
TRANSMEM 756 776 Helical. {ECO:0000255}.
TOPO_DOM 777 779 Cytoplasmic. {ECO:0000305}.
TRANSMEM 780 800 Helical. {ECO:0000255}.
TOPO_DOM 801 829 Extracellular. {ECO:0000305}.
TRANSMEM 830 850 Helical. {ECO:0000255}.
TOPO_DOM 851 861 Cytoplasmic. {ECO:0000305}.
TRANSMEM 862 882 Helical. {ECO:0000255}.
TOPO_DOM 883 904 Extracellular. {ECO:0000305}.
TRANSMEM 905 925 Helical. {ECO:0000255}.
TOPO_DOM 926 928 Cytoplasmic. {ECO:0000305}.
DOMAIN 390 485 Calx-beta 1. {ECO:0000255}.
DOMAIN 519 618 Calx-beta 2. {ECO:0000255}.
REGION 253 272 Putative calmodulin-binding region.
{ECO:0000250|UniProtKB:P23685}.
METAL 409 409 Calcium 1.
{ECO:0000250|UniProtKB:P23685}.
METAL 409 409 Calcium 2.
{ECO:0000250|UniProtKB:P23685}.
METAL 409 409 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 445 445 Calcium 1.
{ECO:0000250|UniProtKB:P23685}.
METAL 445 445 Calcium 4.
{ECO:0000250|UniProtKB:P23685}.
METAL 470 470 Calcium 2.
{ECO:0000250|UniProtKB:P23685}.
METAL 471 471 Calcium 1.
{ECO:0000250|UniProtKB:P23685}.
METAL 471 471 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P23685}.
METAL 471 471 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 471 471 Calcium 4.
{ECO:0000250|UniProtKB:P23685}.
METAL 473 473 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P23685}.
METAL 475 475 Calcium 1.
{ECO:0000250|UniProtKB:P23685}.
METAL 475 475 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 475 475 Calcium 4.
{ECO:0000250|UniProtKB:P23685}.
METAL 478 478 Calcium 4.
{ECO:0000250|UniProtKB:P23685}.
METAL 525 525 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 526 526 Calcium 2.
{ECO:0000250|UniProtKB:P23685}.
METAL 527 527 Calcium 2.
{ECO:0000250|UniProtKB:P23685}.
METAL 527 527 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 543 543 Calcium 5.
{ECO:0000250|UniProtKB:P23685}.
METAL 579 579 Calcium 6.
{ECO:0000250|UniProtKB:P23685}.
METAL 605 605 Calcium 5.
{ECO:0000250|UniProtKB:P23685}.
METAL 605 605 Calcium 6.
{ECO:0000250|UniProtKB:P23685}.
METAL 673 673 Calcium 5.
{ECO:0000250|UniProtKB:P23685}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 824 824 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
VAR_SEQ 599 636 HIKVIDDKAYEKNKNYVIEMMGPRMVDMSVQKALLLSP ->
RVKIVDEEEYERQENFFIALGEPKWMERGIS (in
isoform 2). {ECO:0000305}.
/FTId=VSP_057981.
CONFLICT 754 754 H -> P (in Ref. 1; AAL39160).
{ECO:0000305}.
STRAND 532 535 {ECO:0000244|PDB:2LT9}.
STRAND 537 541 {ECO:0000244|PDB:2LT9}.
HELIX 543 545 {ECO:0000244|PDB:2LT9}.
STRAND 546 554 {ECO:0000244|PDB:2LT9}.
STRAND 562 573 {ECO:0000244|PDB:2LT9}.
STRAND 578 580 {ECO:0000244|PDB:2LT9}.
STRAND 585 589 {ECO:0000244|PDB:2LT9}.
STRAND 595 602 {ECO:0000244|PDB:2LT9}.
STRAND 612 618 {ECO:0000244|PDB:2LT9}.
TURN 624 626 {ECO:0000244|PDB:2LT9}.
HELIX 645 656 {ECO:0000244|PDB:2LT9}.
STRAND 666 674 {ECO:0000244|PDB:2LT9}.
SEQUENCE 928 AA; 102984 MW; 748C4E947C1A43A1 CRC64;
MAWLRLQPLT SAFLHFGLVT FVLFLNCLRA EAGDSGDVPS AGQNNESCSG SSDCKEGVIL
PIWYPENPSL GDKIARVIVY FVALIYMFLG VSIIADRFMA SIEVITSQER EVTIKKPNGE
TSTTTIRVWN ETVSNLTLMA LGSSAPEILL SLIEVCGHGF IAGDLGPSTI VGSAAFNMFI
IIGICVYVIP DGETRKIKHL RVFFVTAAWS IFAYIWLYMI LAVFSPGVVQ VWEGLLTLFF
FPVCVLLAWV ADKRLLFYKY MHKKYRTDKH RGIIIETEGD HPKGIEMDGK MMNSHFLDGN
FTPLEGKEVD ESRREMIRIL KDLKQKHPEK DLDQLVEMAN YYALSHQQKS RAFYRIQATR
MMTGAGNILK KHAAEQAKKT SSMSEVHTDE PEDFASKVFF DPCSYQCLEN CGAVLLTVVR
KGGDISKTMY VDYKTEDGSA NAGADYEFTE GTVVLKPGET QKEFSVGIID DDIFEEDEHF
FVRLSNVRVE EEQLAEGMLP AILNSLPLPR AVLASPCVAT VTILDDDHAG IFTFECDTIH
VSESIGVMEV KVLRTSGARG TVIVPFRTVE GTAKGGGEDF EDAYGELEFK NDETVKTIHI
KVIDDKAYEK NKNYVIEMMG PRMVDMSVQK ALLLSPEVTD RKLTVEEEEA KRIAEMGKPV
LGEHPKLEVI IEESYEFKST VDKLIKKTNL ALVVGTHSWR DQFMEAITVS AGGDEDEDES
GEERLPSCFD YVMHFLTVFW KVLFACVPPT EYCHGWACFV VSILIIGMLT AIIGDLASHF
GCTIGLKDSV TAVVFVAFGT SVPDTFASKA AALQDVYADA SIGNVTGSNA VNVFLGIGLA
WSVAAIYWAM QGQEFHVSAG TLAFSVTLFT IFAFVCLSVL LYRRRPHLGG ELGGPRGCKL
ATTWLFVSLW LLYILFATLE AYCYIKGF


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