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

 NAC1_RAT                Reviewed;         971 AA.
Q01728; Q924Y2; Q9QW49; Q9R238; Q9R239; Q9WU29; Q9WU30;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 3.
27-SEP-2017, entry version 156.
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=Ncx1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Heart;
PubMed=8422940; DOI=10.1016/0014-5793(93)81737-K;
Low W., Kasir J., Rahamimoff H.;
"Cloning of the rat heart Na(+)-Ca2+ exchanger and its functional
expression in HeLa cells.";
FEBS Lett. 316:63-67(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULAR
LOCATION, AND ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=8454039; DOI=10.1016/0014-5793(93)80046-W;
Furman I., Cook O., Kasir J., Rahamimoff H.;
"Cloning of two isoforms of the rat brain Na(+)-Ca2+ exchanger gene
and their functional expression in HeLa cells.";
FEBS Lett. 319:105-109(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
TISSUE=Aortic smooth muscle;
PubMed=8276763; DOI=10.1093/oxfordjournals.jbchem.a124211;
Nakasaki Y., Iwamoto T., Hanada H., Imagawa T., Shigekawa M.;
"Cloning of the rat aortic smooth muscle Na+/Ca2+ exchanger and
tissue-specific expression of isoforms.";
J. Biochem. 114:528-534(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND ALTERNATIVE SPLICING.
STRAIN=Sprague-Dawley; TISSUE=Kidney cortex;
PubMed=8195112;
Lee S.-L., Yu A.S.L., Lytton J.;
"Tissue-specific expression of Na(+)-Ca2+ exchanger isoforms.";
J. Biol. Chem. 269:14849-14852(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 7), FUNCTION, AND
SUBCELLULAR LOCATION.
STRAIN=Dahl salt-resistant, and Dahl salt-sensitive;
TISSUE=Mesangial cell;
PubMed=10894800;
Unlap M.T., Peti-Peterdi J., Bell P.D.;
"Cloning of mesangial cell Na(+)/Ca(2+) exchangers from Dahl/Rapp
salt-sensitive/resistant rats.";
Am. J. Physiol. 279:F177-F184(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION, AND ENZYME
REGULATION.
STRAIN=Sprague-Dawley; TISSUE=Mesangial cell;
PubMed=15040000; DOI=10.1002/jcp.10447;
Williams I., Williams C., Siroky B., Bates E., Kovacs G.,
Peti-Peterdi J., Unlap M.T., Bell P.D.;
"Regulation of mesangial cell Na+/Ca2+ exchanger isoforms.";
J. Cell. Physiol. 199:181-193(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 750-902, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Neuron;
PubMed=8255180; DOI=10.1016/0169-328X(93)90107-Z;
Marlier L.N.J.-L., Zheng T., Tang J., Grayson D.R.;
"Regional distribution in the rat central nervous system of a mRNA
encoding a portion of the cardiac sodium/calcium exchanger isolated
from cerebellar granule neurons.";
Brain Res. Mol. Brain Res. 20:21-39(1993).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 780-912, AND TISSUE SPECIFICITY.
STRAIN=CD Charles River; TISSUE=Kidney;
PubMed=1415740;
Yu A.S.L., Hebert S.C., Lee S.-L., Brenner B.M., Lytton J.;
"Identification and localization of renal Na(+)-Ca2+ exchanger by
polymerase chain reaction.";
Am. J. Physiol. 263:F680-F685(1992).
[9]
TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley;
PubMed=8798769; DOI=10.1074/jbc.271.40.24914;
Nicoll D.A., Quednau B.D., Qui Z., Xia Y.-R., Lusis A.J.,
Philipson K.D.;
"Cloning of a third mammalian Na+-Ca2+ exchanger, NCX3.";
J. Biol. Chem. 271:24914-24921(1996).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=12502557;
Dong H., Dunn J., Lytton J.;
"Electrophysiological studies of the cloned rat cardiac NCX1.1 in
transfected HEK cells: a focus on the stoichiometry.";
Ann. N. Y. Acad. Sci. 976:159-165(2002).
[11]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=16914199; DOI=10.1016/j.ceca.2006.06.004;
Minelli A., Castaldo P., Gobbi P., Salucci S., Magi S., Amoroso S.;
"Cellular and subcellular localization of Na+-Ca2+ exchanger protein
isoforms, NCX1, NCX2, and NCX3 in cerebral cortex and hippocampus of
adult rat.";
Cell Calcium 41:221-234(2007).
[12]
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:8422940, PubMed:8454039,
PubMed:10894800, PubMed:12502557). 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 (By similarity).
{ECO:0000250|UniProtKB:P70414, ECO:0000269|PubMed:10894800,
ECO:0000269|PubMed:12502557, ECO:0000269|PubMed:15040000,
ECO:0000269|PubMed:8422940, ECO:0000269|PubMed:8454039}.
-!- ENZYME REGULATION: Activated by micromolar levels of Ca(2+)
(PubMed:12502557). Isoform 4 and isoform 6 are only active at low
calcium concentrations but isoform 5 is active at all calcium
levels tested. Isoform 5 and isoform 6, but not isoform 4, are
activated by PKC (PubMed:15040000). {ECO:0000269|PubMed:12502557,
ECO:0000269|PubMed:15040000}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10894800,
ECO:0000269|PubMed:12502557, ECO:0000269|PubMed:16914199,
ECO:0000269|PubMed:8422940}; Multi-pass membrane protein
{ECO:0000305}. Cell projection, dendrite
{ECO:0000269|PubMed:16914199}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=Heart, NaCa1;
IsoId=Q01728-1; Sequence=Displayed;
Name=2; Synonyms=Brain-1, NaCa5;
IsoId=Q01728-2; Sequence=VSP_003402, VSP_003403;
Name=3; Synonyms=Brain-2, NaCa4;
IsoId=Q01728-3; Sequence=VSP_003402, VSP_003404;
Name=4; Synonyms=Kidney-1, NaCa7, SNCX1;
IsoId=Q01728-4; Sequence=VSP_003401, VSP_003402, VSP_003403;
Name=5; Synonyms=Kidney-2, NaCa3, RNCX1;
IsoId=Q01728-5; Sequence=VSP_003401, VSP_003402, VSP_003404;
Name=6; Synonyms=SDNCX1.10;
IsoId=Q01728-6; Sequence=VSP_003401, VSP_003402, VSP_029836;
Name=7;
IsoId=Q01728-7; Sequence=VSP_003401, VSP_029836;
-!- TISSUE SPECIFICITY: Detected in heart, brain cortex and
hippocampus (at protein level) (PubMed:16914199). Cardiac
sarcolemma or brain, and spleen. Expressed in all regions of the
kidney, highest levels of expression in the distal convoluted
tubule. Expressed throughout the CNS, in decreasing order of
abundance in hippocampus, cortex, cerebellum, hypothalamus,
midbrain and striatum. Expressed in numerous regions of the brain
including multiple cortical layers, hippocampus, septal nuclei,
thalamic nuclei, cerebellum, hypothalamus, olfactory bulb and
brainstem. Also expressed in various regions of the spinal cord,
ventricles and atria of the heart, lung, adrenals and kidney.
Isoform 4 seems to be a predominant isoform in aorta, stomach,
liver, and kidney. {ECO:0000269|PubMed:1415740,
ECO:0000269|PubMed:16914199, ECO:0000269|PubMed:8255180,
ECO:0000269|PubMed:8276763, ECO:0000269|PubMed:8798769}.
-!- 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}.
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EMBL; X68191; CAA48273.1; -; mRNA.
EMBL; X68812; CAA48707.1; -; mRNA.
EMBL; X68813; CAA48708.1; -; mRNA.
EMBL; U04933; AAB39952.1; -; mRNA.
EMBL; U04934; AAA19124.1; -; mRNA.
EMBL; U04936; AAA19125.1; -; mRNA.
EMBL; AF109163; AAD23386.1; -; mRNA.
EMBL; AF109164; AAD23387.1; -; mRNA.
EMBL; AF109165; AAD23388.1; -; mRNA.
EMBL; AF109166; AAD23389.1; -; mRNA.
EMBL; AY033398; AAK52307.1; -; mRNA.
PIR; A53789; A53789.
PIR; I52640; I52640.
PIR; S28833; S28833.
PIR; S32435; S32435.
PIR; S43730; S43730.
RefSeq; NP_001257701.1; NM_001270772.1. [Q01728-3]
RefSeq; NP_001257702.1; NM_001270773.1. [Q01728-5]
RefSeq; NP_001257703.1; NM_001270774.1. [Q01728-2]
RefSeq; NP_001257704.1; NM_001270775.1. [Q01728-4]
RefSeq; NP_001257705.1; NM_001270776.1. [Q01728-7]
RefSeq; NP_001257706.1; NM_001270777.1. [Q01728-6]
RefSeq; XP_008762655.1; XM_008764433.2. [Q01728-7]
RefSeq; XP_008762659.1; XM_008764437.2. [Q01728-6]
RefSeq; XP_008762660.1; XM_008764438.2. [Q01728-2]
RefSeq; XP_008762661.1; XM_008764439.2. [Q01728-4]
RefSeq; XP_017449552.1; XM_017594063.1. [Q01728-3]
RefSeq; XP_017449553.1; XM_017594064.1. [Q01728-5]
UniGene; Rn.118972; -.
UniGene; Rn.935; -.
ProteinModelPortal; Q01728; -.
SMR; Q01728; -.
BioGrid; 248332; 9.
CORUM; Q01728; -.
IntAct; Q01728; 1.
MINT; MINT-4563844; -.
STRING; 10116.ENSRNOP00000040751; -.
iPTMnet; Q01728; -.
PhosphoSitePlus; Q01728; -.
SwissPalm; Q01728; -.
PaxDb; Q01728; -.
PRIDE; Q01728; -.
Ensembl; ENSRNOT00000042230; ENSRNOP00000040751; ENSRNOG00000008479. [Q01728-1]
Ensembl; ENSRNOT00000042251; ENSRNOP00000040765; ENSRNOG00000008479. [Q01728-3]
Ensembl; ENSRNOT00000043870; ENSRNOP00000044094; ENSRNOG00000008479. [Q01728-7]
Ensembl; ENSRNOT00000046246; ENSRNOP00000043539; ENSRNOG00000008479. [Q01728-6]
Ensembl; ENSRNOT00000052367; ENSRNOP00000050918; ENSRNOG00000008479. [Q01728-2]
GeneID; 29715; -.
KEGG; rno:29715; -.
UCSC; RGD:3717; rat. [Q01728-1]
CTD; 6546; -.
RGD; 3717; Slc8a1.
eggNOG; KOG1306; Eukaryota.
eggNOG; ENOG410XPJP; LUCA.
GeneTree; ENSGT00730000110414; -.
HOGENOM; HOG000266971; -.
HOVERGEN; HBG006441; -.
InParanoid; Q01728; -.
KO; K05849; -.
OMA; DDEECGE; -.
OrthoDB; EOG091G0EC1; -.
PhylomeDB; Q01728; -.
TreeFam; TF314308; -.
Reactome; R-RNO-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-RNO-425561; Sodium/Calcium exchangers.
Reactome; R-RNO-5578775; Ion homeostasis.
PRO; PR:Q01728; -.
Proteomes; UP000002494; Chromosome 6.
Bgee; ENSRNOG00000008479; -.
ExpressionAtlas; Q01728; baseline and differential.
Genevisible; Q01728; RN.
GO; GO:0042995; C:cell projection; IDA:RGD.
GO; GO:0043198; C:dendritic shaft; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
GO; GO:0005874; C:microtubule; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
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:0099580; F:ion antiporter activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
GO; GO:1901660; P:calcium ion export; IDA:BHF-UCL.
GO; GO:0070509; P:calcium ion import; IDA:BHF-UCL.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:RGD.
GO; GO:0006816; P:calcium ion transport; TAS:RGD.
GO; GO:0060402; P:calcium ion transport into cytosol; IDA:RGD.
GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; IDA:BHF-UCL.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:RGD.
GO; GO:0071320; P:cellular response to cAMP; IDA:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:BHF-UCL.
GO; GO:0006883; P:cellular sodium ion homeostasis; IEA:Ensembl.
GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:RGD.
GO; GO:0098735; P:positive regulation of the force of heart contraction; IEA:Ensembl.
GO; GO:0051924; P:regulation of calcium ion transport; IMP:RGD.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IDA:BHF-UCL.
GO; GO:0002028; P:regulation of sodium ion transport; IMP:RGD.
GO; GO:0033198; P:response to ATP; IDA:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IDA:RGD.
GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0071436; P:sodium ion export; IDA:BHF-UCL.
GO; GO:0097369; P:sodium ion import; IDA:BHF-UCL.
GO; GO:0006814; P:sodium ion transport; IDA:RGD.
GO; GO:0021537; P:telencephalon development; IEP:RGD.
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; Cell projection; Complete proteome;
Glycoprotein; Ion transport; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Repeat; Signal; Sodium; Sodium transport;
Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 971 Sodium/calcium exchanger 1.
/FTId=PRO_0000019381.
TOPO_DOM 33 71 Extracellular. {ECO:0000255}.
TRANSMEM 72 92 Helical. {ECO:0000255}.
TOPO_DOM 93 133 Cytoplasmic. {ECO:0000255}.
TRANSMEM 134 154 Helical. {ECO:0000255}.
TOPO_DOM 155 167 Extracellular. {ECO:0000255}.
TRANSMEM 168 188 Helical. {ECO:0000255}.
TOPO_DOM 189 201 Cytoplasmic. {ECO:0000255}.
TRANSMEM 202 222 Helical. {ECO:0000255}.
TOPO_DOM 223 228 Extracellular. {ECO:0000255}.
TRANSMEM 229 249 Helical. {ECO:0000255}.
TOPO_DOM 250 798 Cytoplasmic. {ECO:0000255}.
TRANSMEM 799 819 Helical. {ECO:0000255}.
TOPO_DOM 820 822 Extracellular. {ECO:0000255}.
TRANSMEM 823 843 Helical. {ECO:0000255}.
TOPO_DOM 844 872 Cytoplasmic. {ECO:0000255}.
TRANSMEM 873 893 Helical. {ECO:0000255}.
TOPO_DOM 894 904 Extracellular. {ECO:0000255}.
TRANSMEM 905 925 Helical. {ECO:0000255}.
TOPO_DOM 926 942 Cytoplasmic. {ECO:0000255}.
TRANSMEM 943 963 Helical. {ECO:0000255}.
TOPO_DOM 964 971 Extracellular. {ECO:0000255}.
REPEAT 138 178 Alpha-1.
DOMAIN 393 493 Calx-beta 1.
DOMAIN 524 624 Calx-beta 2.
REPEAT 840 876 Alpha-2.
REGION 251 270 Putative calmodulin-binding region.
{ECO:0000250|UniProtKB:P23685}.
COMPBIAS 236 239 Poly-Phe.
COMPBIAS 690 693 Poly-Glu.
COMPBIAS 757 761 Poly-Asp.
METAL 417 417 Calcium 1.
{ECO:0000250|UniProtKB:P23685}.
METAL 417 417 Calcium 2.
{ECO:0000250|UniProtKB:P23685}.
METAL 417 417 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 453 453 Calcium 1.
{ECO:0000250|UniProtKB:P23685}.
METAL 453 453 Calcium 4.
{ECO:0000250|UniProtKB:P23685}.
METAL 478 478 Calcium 2.
{ECO:0000250|UniProtKB:P23685}.
METAL 479 479 Calcium 1.
{ECO:0000250|UniProtKB:P23685}.
METAL 479 479 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P23685}.
METAL 479 479 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 479 479 Calcium 4.
{ECO:0000250|UniProtKB:P23685}.
METAL 481 481 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P23685}.
METAL 483 483 Calcium 1.
{ECO:0000250|UniProtKB:P23685}.
METAL 483 483 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 483 483 Calcium 4.
{ECO:0000250|UniProtKB:P23685}.
METAL 486 486 Calcium 4.
{ECO:0000250|UniProtKB:P23685}.
METAL 530 530 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 531 531 Calcium 2.
{ECO:0000250|UniProtKB:P23685}.
METAL 532 532 Calcium 2.
{ECO:0000250|UniProtKB:P23685}.
METAL 532 532 Calcium 3.
{ECO:0000250|UniProtKB:P23685}.
METAL 548 548 Calcium 5.
{ECO:0000250|UniProtKB:P23685}.
METAL 584 584 Calcium 6.
{ECO:0000250|UniProtKB:P23685}.
METAL 610 610 Calcium 5.
{ECO:0000250|UniProtKB:P23685}.
METAL 610 610 Calcium 6.
{ECO:0000250|UniProtKB:P23685}.
METAL 611 611 Calcium 6.
{ECO:0000250|UniProtKB:P23685}.
METAL 612 612 Calcium 5; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P23685}.
METAL 612 612 Calcium 6.
{ECO:0000250|UniProtKB:P23685}.
METAL 716 716 Calcium 5.
{ECO:0000250|UniProtKB:P23685}.
MOD_RES 282 282 Phosphoserine.
{ECO:0000250|UniProtKB:P70414}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000250|UniProtKB:P70414}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 602 635 TISVKVIDDEEYEKNKTFFIEIGEPRLVEMSEKK -> IIT
IRIFDREEYEKECSFSLVLEEPKWIRRGMK (in
isoform 4, isoform 5, isoform 6 and
isoform 7). {ECO:0000303|PubMed:10894800,
ECO:0000303|PubMed:15040000,
ECO:0000303|PubMed:8195112,
ECO:0000303|PubMed:8276763}.
/FTId=VSP_003401.
VAR_SEQ 636 642 Missing (in isoform 2, isoform 3, isoform
4, isoform 5 and isoform 6).
{ECO:0000303|PubMed:10894800,
ECO:0000303|PubMed:15040000,
ECO:0000303|PubMed:8195112,
ECO:0000303|PubMed:8276763,
ECO:0000303|PubMed:8454039}.
/FTId=VSP_003402.
VAR_SEQ 649 677 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:10894800,
ECO:0000303|PubMed:8454039}.
/FTId=VSP_003404.
VAR_SEQ 649 654 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:10894800,
ECO:0000303|PubMed:8195112,
ECO:0000303|PubMed:8276763,
ECO:0000303|PubMed:8454039}.
/FTId=VSP_003403.
VAR_SEQ 649 649 Missing (in isoform 6 and isoform 7).
{ECO:0000303|PubMed:10894800,
ECO:0000303|PubMed:15040000}.
/FTId=VSP_029836.
CONFLICT 148 148 L -> P (in Ref. 5; AAD23388/AAD23389 and
6; AAK52307). {ECO:0000305}.
CONFLICT 218 218 I -> F (in Ref. 5; AAD23387).
{ECO:0000305}.
CONFLICT 250 250 D -> A (in Ref. 1; CAA48273).
{ECO:0000305}.
CONFLICT 402 402 P -> A (in Ref. 1; CAA48273).
{ECO:0000305}.
CONFLICT 438 438 F -> S (in Ref. 5; AAD23386/AAD23387).
{ECO:0000305}.
CONFLICT 500 500 E -> G (in Ref. 5; AAD23388 and 6;
AAK52307). {ECO:0000305}.
CONFLICT 789 789 F -> N (in Ref. 8). {ECO:0000305}.
CONFLICT 861 861 A -> R (in Ref. 8). {ECO:0000305}.
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


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