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

 NAC3_HUMAN              Reviewed;         927 AA.
P57103; Q5K3P6; Q5K3P7; Q8IUE9; Q8IUF0; Q8NFI7; Q96QG1; Q96QG2;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
29-AUG-2003, sequence version 2.
05-DEC-2018, entry version 151.
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; Synonyms=NCX3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2; 3; 4; 7 AND 8).
PubMed=12406570; DOI=10.1016/S0378-1119(02)00982-4;
Gabellini N., Bortoluzzi S., Danieli G.A., Carafoli E.;
"The human SLC8A3 gene and the tissue-specific Na+/Ca2+ exchanger 3
isoforms.";
Gene 298:1-7(2002).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
PubMed=12558991; DOI=10.1046/j.1471-4159.2003.01511.x;
Gabellini N., Bortoluzzi S., Danieli G.A., Carafoli E.;
"Control of the Na+/Ca2+ exchanger 3 promoter by cyclic adenosine
monophosphate and Ca2+ in differentiating neurons.";
J. Neurochem. 84:282-293(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=15777725; DOI=10.1016/j.gene.2005.01.003;
Lindgren R.M., Zhao J., Heller S., Berglind H., Nister M.;
"Molecular cloning and characterization of two novel truncated
isoforms of human Na+/Ca2+ exchanger 3, expressed in fetal brain.";
Gene 348:143-155(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-595.
Kraev A.S., Chumakov I.M., Carafoli E.;
"The organization of the human gene of the sodium-calcium exchanger.";
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
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).
[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]
VARIANT [LARGE SCALE ANALYSIS] GLN-612.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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. 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. Contributes to Ca(2+) transport during
excitation-contraction coupling in muscle. 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 (By similarity).
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 (By similarity). {ECO:0000250|UniProtKB:S4R2P9,
ECO:0000269|PubMed:21959935}.
-!- ACTIVITY REGULATION: Calcium transport is down-regulated by Na(+)
and stimulated by Ca(2+). {ECO:0000250|UniProtKB:P70549}.
-!- SUBUNIT: Interacts with AKAP1. {ECO:0000250|UniProtKB:S4R2P9}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21959935};
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:0000250|UniProtKB:S4R2P9}. Cytoplasm, sarcoplasm
{ECO:0000250|UniProtKB:S4R2P9}. Cell junction
{ECO:0000250|UniProtKB:S4R2P9}. Mitochondrion outer membrane
{ECO:0000250|UniProtKB:S4R2P9}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:S4R2P9}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:21959935}. Endoplasmic reticulum membrane
{ECO:0000305|PubMed:21959935}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:S4R2P9}. Note=Detected at neuromuscular
junctions. {ECO:0000250|UniProtKB:S4R2P9}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=3; Synonyms=NCX3.3;
IsoId=P57103-1; Sequence=Displayed;
Name=2; Synonyms=NCX3.2;
IsoId=P57103-2; Sequence=VSP_008116;
Name=4; Synonyms=NCX3.4;
IsoId=P57103-3; Sequence=VSP_008117, VSP_008118;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay. No
experimental confirmation available.;
Name=5; Synonyms=NCX3-tN.1;
IsoId=P57103-4; Sequence=VSP_043125;
Note=Expressed in fetal brain.;
Name=6; Synonyms=NCX3-tN.2;
IsoId=P57103-5; Sequence=VSP_043126, VSP_008116;
Note=Expressed in fetal brain.;
Name=7;
IsoId=P57103-6; Sequence=VSP_043850;
Name=8;
IsoId=P57103-7; Sequence=VSP_044502;
-!- TISSUE SPECIFICITY: Isoform 2 is expressed in brain and skeletal
muscle. Isoform 3 is expressed in excitable cells of brain, retina
and skeletal muscle. Isoform 4 is expressed in skeletal muscle.
{ECO:0000269|PubMed:15777725}.
-!- DEVELOPMENTAL STAGE: Up-regulated during in vitro differentiation
of oligodendrocytes (at protein level). Up-regulated during in
vitro differentiation of oligodendrocytes.
{ECO:0000269|PubMed:21959935}.
-!- 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; AF510501; AAN60790.1; -; mRNA.
EMBL; AF510502; AAN60791.1; -; mRNA.
EMBL; AF510503; AAN60792.1; -; mRNA.
EMBL; AF508982; AAM90955.1; -; Genomic_DNA.
EMBL; AJ304852; CAC40984.1; -; mRNA.
EMBL; AJ304853; CAC40985.1; -; mRNA.
EMBL; AJ745101; CAG33739.1; -; mRNA.
EMBL; AJ745102; CAG33740.1; -; mRNA.
EMBL; AL135747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL160191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW81019.1; -; Genomic_DNA.
EMBL; CH471061; EAW81021.1; -; Genomic_DNA.
EMBL; CH471061; EAW81026.1; -; Genomic_DNA.
EMBL; BC142969; AAI42970.1; -; mRNA.
EMBL; X93017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS35498.1; -. [P57103-1]
CCDS; CCDS41967.1; -. [P57103-4]
CCDS; CCDS45131.1; -. [P57103-5]
CCDS; CCDS53904.1; -. [P57103-6]
CCDS; CCDS9799.1; -. [P57103-7]
CCDS; CCDS9800.1; -. [P57103-2]
RefSeq; NP_001123889.1; NM_001130417.2. [P57103-5]
RefSeq; NP_150287.1; NM_033262.4. [P57103-7]
RefSeq; NP_489479.1; NM_058240.3. [P57103-6]
RefSeq; NP_891977.1; NM_182932.2. [P57103-2]
RefSeq; NP_891981.1; NM_182936.2. [P57103-4]
RefSeq; NP_892114.1; NM_183002.2. [P57103-1]
RefSeq; XP_016877095.1; XM_017021606.1. [P57103-1]
RefSeq; XP_016877097.1; XM_017021608.1. [P57103-2]
UniGene; Hs.337696; -.
ProteinModelPortal; P57103; -.
SMR; P57103; -.
BioGrid; 112437; 8.
IntAct; P57103; 1.
STRING; 9606.ENSP00000370669; -.
GuidetoPHARMACOLOGY; 947; -.
TCDB; 2.A.19.3.3; the ca(2+):cation antiporter (caca) family.
iPTMnet; P57103; -.
PhosphoSitePlus; P57103; -.
DMDM; 34395973; -.
EPD; P57103; -.
PaxDb; P57103; -.
PeptideAtlas; P57103; -.
PRIDE; P57103; -.
ProteomicsDB; 56998; -.
ProteomicsDB; 56999; -. [P57103-2]
ProteomicsDB; 57000; -. [P57103-3]
ProteomicsDB; 57001; -. [P57103-4]
ProteomicsDB; 57002; -. [P57103-5]
ProteomicsDB; 57003; -. [P57103-6]
TopDownProteomics; P57103-2; -. [P57103-2]
DNASU; 6547; -.
Ensembl; ENST00000216568; ENSP00000216568; ENSG00000100678. [P57103-5]
Ensembl; ENST00000356921; ENSP00000349392; ENSG00000100678. [P57103-2]
Ensembl; ENST00000357887; ENSP00000350560; ENSG00000100678. [P57103-7]
Ensembl; ENST00000381269; ENSP00000370669; ENSG00000100678. [P57103-1]
Ensembl; ENST00000394330; ENSP00000377863; ENSG00000100678. [P57103-4]
Ensembl; ENST00000494208; ENSP00000436332; ENSG00000100678. [P57103-3]
Ensembl; ENST00000528359; ENSP00000433531; ENSG00000100678. [P57103-7]
Ensembl; ENST00000534137; ENSP00000436688; ENSG00000100678. [P57103-6]
GeneID; 6547; -.
KEGG; hsa:6547; -.
UCSC; uc001xlu.5; human. [P57103-1]
CTD; 6547; -.
DisGeNET; 6547; -.
EuPathDB; HostDB:ENSG00000100678.18; -.
GeneCards; SLC8A3; -.
HGNC; HGNC:11070; SLC8A3.
MIM; 607991; gene.
neXtProt; NX_P57103; -.
OpenTargets; ENSG00000100678; -.
PharmGKB; PA315; -.
eggNOG; KOG1306; Eukaryota.
eggNOG; ENOG410XPJP; LUCA.
GeneTree; ENSGT00940000157547; -.
HOGENOM; HOG000266971; -.
HOVERGEN; HBG006441; -.
InParanoid; P57103; -.
KO; K05849; -.
OMA; SRKEMIR; -.
OrthoDB; EOG091G0EC1; -.
PhylomeDB; P57103; -.
TreeFam; TF314308; -.
Reactome; R-HSA-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-HSA-425561; Sodium/Calcium exchangers.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-8949215; Mitochondrial calcium ion transport.
ChiTaRS; SLC8A3; human.
GenomeRNAi; 6547; -.
PRO; PR:P57103; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100678; Expressed in 113 organ(s), highest expression level in quadriceps femoris.
CleanEx; HS_SLC8A3; -.
ExpressionAtlas; P57103; baseline and differential.
Genevisible; P57103; HS.
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; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:Ensembl.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
GO; GO:0016528; C:sarcoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005432; F:calcium:sodium antiporter activity; ISS:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0099580; F:ion antiporter activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1990034; P:calcium ion export across plasma membrane; IEA:Ensembl.
GO; GO:0098703; P:calcium ion import across plasma membrane; IEA:Ensembl.
GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
GO; GO:0007154; P:cell communication; IEA:InterPro.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
GO; GO:0006811; P:ion transport; TAS:Reactome.
GO; GO:0007612; P:learning; ISS:UniProtKB.
GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
GO; GO:0007613; P:memory; ISS:UniProtKB.
GO; GO:0051560; P:mitochondrial calcium ion homeostasis; ISS:UniProtKB.
GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; ISS:UniProtKB.
GO; GO:0042552; P:myelination; ISS:UniProtKB.
GO; GO:0048709; P:oligodendrocyte differentiation; ISS:UniProtKB.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0014819; P:regulation of skeletal muscle contraction; ISS:UniProtKB.
GO; GO:0035725; P:sodium ion transmembrane transport; ISS:UniProtKB.
GO; GO:0021537; P:telencephalon development; IEA:Ensembl.
Gene3D; 2.60.40.2030; -; 2.
InterPro; IPR038081; CalX-like_sf.
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.
SUPFAM; SSF141072; SSF141072; 2.
TIGRFAMs; TIGR00845; caca; 1.
1: Evidence at protein level;
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; Polymorphism; Reference proteome;
Repeat; Signal; Sodium; Sodium transport; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 927 Sodium/calcium exchanger 3.
/FTId=PRO_0000019384.
TOPO_DOM 31 73 Extracellular. {ECO:0000255}.
TRANSMEM 74 94 Helical. {ECO:0000255}.
TOPO_DOM 95 147 Cytoplasmic. {ECO:0000255}.
TRANSMEM 148 168 Helical. {ECO:0000255}.
TOPO_DOM 169 169 Extracellular. {ECO:0000255}.
TRANSMEM 170 190 Helical. {ECO:0000255}.
TOPO_DOM 191 202 Cytoplasmic. {ECO:0000255}.
TRANSMEM 203 223 Helical. {ECO:0000255}.
TOPO_DOM 224 230 Extracellular. {ECO:0000255}.
TRANSMEM 231 251 Helical. {ECO:0000255}.
TOPO_DOM 252 726 Cytoplasmic. {ECO:0000255}.
TRANSMEM 727 747 Helical. {ECO:0000255}.
TOPO_DOM 748 754 Extracellular. {ECO:0000255}.
TRANSMEM 755 775 Helical. {ECO:0000255}.
TOPO_DOM 776 778 Cytoplasmic. {ECO:0000255}.
TRANSMEM 779 799 Helical. {ECO:0000255}.
TOPO_DOM 800 828 Extracellular. {ECO:0000255}.
TRANSMEM 829 849 Helical. {ECO:0000255}.
TOPO_DOM 850 860 Cytoplasmic. {ECO:0000255}.
TRANSMEM 861 881 Helical. {ECO:0000255}.
TOPO_DOM 882 903 Extracellular. {ECO:0000255}.
TRANSMEM 904 924 Helical. {ECO:0000255}.
TOPO_DOM 925 927 Cytoplasmic. {ECO:0000255}.
REPEAT 140 180 Alpha-1.
DOMAIN 386 485 Calx-beta 1.
DOMAIN 519 619 Calx-beta 2.
REPEAT 796 832 Alpha-2.
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 606 606 Calcium 6.
{ECO:0000250|UniProtKB:P23685}.
METAL 607 607 Calcium 5; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P23685}.
METAL 607 607 Calcium 6.
{ECO:0000250|UniProtKB:P23685}.
METAL 672 672 Calcium 5.
{ECO:0000250|UniProtKB:P23685}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 823 823 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 643 Missing (in isoform 5).
{ECO:0000303|PubMed:15777725}.
/FTId=VSP_043125.
VAR_SEQ 1 623 Missing (in isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15777725}.
/FTId=VSP_043126.
VAR_SEQ 596 620 KTIRVKIVDEEEYERQENFFIALGE -> CDRQEADYGRRG
GQEDSRDGKASIG (in isoform 4).
{ECO:0000303|PubMed:12406570}.
/FTId=VSP_008117.
VAR_SEQ 599 638 RVKIVDEEEYERQENFFIALGEPKWMERGISALLLSPDVT
-> HIKVIDDEAYEKNKNYFIEMMGPRMVDMSFQKALLLSP
(in isoform 8).
{ECO:0000303|PubMed:12406570}.
/FTId=VSP_044502.
VAR_SEQ 621 927 Missing (in isoform 4).
{ECO:0000303|PubMed:12406570}.
/FTId=VSP_008118.
VAR_SEQ 630 635 Missing (in isoform 2 and isoform 6).
{ECO:0000303|PubMed:12406570,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15777725}.
/FTId=VSP_008116.
VAR_SEQ 636 638 Missing (in isoform 7).
{ECO:0000303|PubMed:12406570}.
/FTId=VSP_043850.
VARIANT 612 612 E -> Q (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036463.
SEQUENCE 927 AA; 103010 MW; 7B43CB6A9D77615E CRC64;
MAWLRLQPLT SAFLHFGLVT FVLFLNGLRA EAGGSGDVPS TGQNNESCSG SSDCKEGVIL
PIWYPENPSL GDKIARVIVY FVALIYMFLG VSIIADRFMA SIEVITSQER EVTIKKPNGE
TSTTTIRVWN ETVSNLTLMA LGSSAPEILL SLIEVCGHGF IAGDLGPSTI VGSAAFNMFI
IIGICVYVIP DGETRKIKHL RVFFITAAWS IFAYIWLYMI LAVFSPGVVQ VWEGLLTLFF
FPVCVLLAWV ADKRLLFYKY MHKKYRTDKH RGIIIETEGD HPKGIEMDGK MMNSHFLDGN
LVPLEGKEVD ESRREMIRIL KDLKQKHPEK DLDQLVEMAN YYALSHQQKS RAFYRIQATR
MMTGAGNILK KHAAEQAKKA SSMSEVHTDE PEDFISKVFF DPCSYQCLEN CGAVLLTVVR
KGGDMSKTMY VDYKTEDGSA NAGADYEFTE GTVVLKPGET QKEFSVGIID DDIFEEDEHF
FVRLSNVRIE EEQPEEGMPP AIFNSLPLPR AVLASPCVAT VTILDDDHAG IFTFECDTIH
VSESIGVMEV KVLRTSGARG TVIVPFRTVE GTAKGGGEDF EDTYGELEFK NDETVKTIRV
KIVDEEEYER QENFFIALGE PKWMERGISA LLLSPDVTDR KLTMEEEEAK RIAEMGKPVL
GEHPKLEVII EESYEFKTTV DKLIKKTNLA LVVGTHSWRD QFMEAITVSA AGDEDEDESG
EERLPSCFDY VMHFLTVFWK VLFACVPPTE YCHGWACFAV SILIIGMLTA IIGDLASHFG
CTIGLKDSVT AVVFVAFGTS VPDTFASKAA ALQDVYADAS IGNVTGSNAV NVFLGIGLAW
SVAAIYWALQ GQEFHVSAGT LAFSVTLFTI FAFVCISVLL YRRRPHLGGE LGGPRGCKLA
TTWLFVSLWL LYILFATLEA YCYIKGF


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