NAC1_MOUSE
ID NAC1_MOUSE Reviewed; 970 AA.
AC P70414;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 174.
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=Ncx;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=C57BL/6J;
RX PubMed=8659820; DOI=10.1111/j.1749-6632.1996.tb44779.x;
RA Kim I., Lee C.O.;
RT "Cloning of the mouse cardiac Na(+)-Ca2+ exchanger and functional
RT expression in Xenopus oocytes.";
RL Ann. N. Y. Acad. Sci. 779:126-128(1996).
RN [2]
RP DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10967099; DOI=10.1074/jbc.m004035200;
RA Wakimoto K., Kobayashi K., Kuro-O M., Yao A., Iwamoto T., Yanaka N.,
RA Kita S., Nishida A., Azuma S., Toyoda Y., Omori K., Imahie H., Oka T.,
RA Kudoh S., Kohmoto O., Yazaki Y., Shigekawa M., Imai Y., Nabeshima Y.,
RA Komuro I.;
RT "Targeted disruption of Na+/Ca2+ exchanger gene leads to cardiomyocyte
RT apoptosis and defects in heartbeat.";
RL J. Biol. Chem. 275:36991-36998(2000).
RN [3]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=12781968; DOI=10.1016/s1096-4959(03)00057-5;
RA Wakimoto K., Fujimura H., Iwamoto T., Oka T., Kobayashi K., Kita S.,
RA Kudoh S., Kuro-o M., Nabeshima Y., Shigekawa M., Imai Y., Komuro I.;
RT "Na+/Ca2+ exchanger-deficient mice have disorganized myofibrils and swollen
RT mitochondria in cardiomyocytes.";
RL Comp. Biochem. Physiol. 135:9-15(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-389, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
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:8659820). Contributes to Ca(2+) transport during
CC excitation-contraction coupling in muscle (PubMed:8659820). In a first
CC phase, voltage-gated channels mediate the rapid increase of cytoplasmic
CC Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic
CC reticulum (PubMed:8659820). SLC8A1 mediates the export of Ca(2+) from
CC the cell during the next phase, so that cytoplasmic Ca(2+) levels
CC rapidly return to baseline (PubMed:10967099). Required for normal
CC embryonic heart development and the onset of heart contractions
CC (PubMed:10967099). {ECO:0000269|PubMed:10967099,
CC ECO:0000269|PubMed:8659820, ECO:0000305}.
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:0000305|PubMed:8659820};
CC -!- ACTIVITY REGULATION: Activated by micromolar levels of Ca(2+).
CC {ECO:0000250|UniProtKB:Q01728}.
CC -!- INTERACTION:
CC P70414; Q80Z64: Nanog; NbExp=9; IntAct=EBI-2312694, EBI-2312517;
CC P70414; Q61066: Nr0b1; NbExp=2; IntAct=EBI-2312694, EBI-2312665;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8659820};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in heart, kidney and brain (at protein
CC level). {ECO:0000269|PubMed:12781968}.
CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc, expression is restricted to the
CC embryonic heart, and is not detectable in any other part of the body.
CC {ECO:0000269|PubMed:10967099}.
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 -!- DISRUPTION PHENOTYPE: Complete embryonic lethality at about 9.5 dpc. At
CC 9.5 dpc, mutant embryos display strongly decreased body size, an
CC absence of blood vessels in the vitelline sac, and defective heart
CC beat. Contrary to wild type hearts that show regular contractions,
CC about 70% of the mutants have no spontaneous contractions of the heart,
CC and the remainder show only very slow and arrhythmic heart
CC contractions. Mutant hearts have thinner ventricles, contain fewer
CC cardiac myocytes, and display an increased number of apoptotic cells.
CC Mutant hearts do not show fast Ca(2+) transients and display lack of
CC sodium/calcium exchange activity. In mutant hearts, caffeine stimulates
CC normal release of intracellular Ca(2+) stores from the endoplasmic
CC reticulum into the cytoplasm, but the subsequent decrease of the high
CC cytoplasmic Ca(2+) levels is impaired (PubMed:10967099). At 9.5 dpc,
CC embryonic cardiomyocytes show severe disorganization of the myofibrils
CC and swollen mitochondria (PubMed:12781968).
CC {ECO:0000269|PubMed:10967099, ECO:0000269|PubMed:12781968}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. SLC8 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U70033; AAB46708.1; -; mRNA.
DR CCDS; CCDS37706.1; -.
DR RefSeq; NP_035536.2; NM_011406.3.
DR AlphaFoldDB; P70414; -.
DR SMR; P70414; -.
DR BioGRID; 203320; 41.
DR IntAct; P70414; 16.
DR STRING; 10090.ENSMUSP00000083725; -.
DR GlyGen; P70414; 2 sites.
DR iPTMnet; P70414; -.
DR PhosphoSitePlus; P70414; -.
DR SwissPalm; P70414; -.
DR jPOST; P70414; -.
DR MaxQB; P70414; -.
DR PaxDb; P70414; -.
DR PeptideAtlas; P70414; -.
DR PRIDE; P70414; -.
DR ProteomicsDB; 287557; -.
DR DNASU; 20541; -.
DR GeneID; 20541; -.
DR KEGG; mmu:20541; -.
DR CTD; 6546; -.
DR MGI; MGI:107956; Slc8a1.
DR eggNOG; KOG1306; Eukaryota.
DR InParanoid; P70414; -.
DR OrthoDB; 490546at2759; -.
DR PhylomeDB; P70414; -.
DR Reactome; R-MMU-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-MMU-425561; Sodium/Calcium exchangers.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR BioGRID-ORCS; 20541; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Slc8a1; mouse.
DR PRO; PR:P70414; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P70414; protein.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; IMP:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; TAS:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IMP:ARUK-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; IDA:ARUK-UCL.
DR GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
DR GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
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; ISO:MGI.
DR GO; GO:0005432; F:calcium:sodium antiporter activity; IMP:BHF-UCL.
DR GO; GO:0086038; F:calcium:sodium antiporter activity involved in regulation of cardiac muscle cell membrane potential; TAS:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0015491; F:cation:cation antiporter activity; IBA:GO_Central.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0099580; F:ion antiporter activity involved in regulation of postsynaptic membrane potential; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:1901660; P:calcium ion export; IMP:BHF-UCL.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:BHF-UCL.
DR GO; GO:0070509; P:calcium ion import; IMP: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; IGI:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR GO; GO:0060402; P:calcium ion transport into cytosol; IMP:BHF-UCL.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:BHF-UCL.
DR GO; GO:0060048; P:cardiac muscle contraction; IGI:MGI.
DR GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; ISO:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
DR GO; GO:0071313; P:cellular response to caffeine; IMP:BHF-UCL.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:MGI.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; ISO:MGI.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IGI:MGI.
DR GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
DR GO; GO:0055001; P:muscle cell development; IGI:MGI.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:BHF-UCL.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:ARUK-UCL.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; ISO:MGI.
DR GO; GO:0098735; P:positive regulation of the force of heart contraction; ISO:MGI.
DR GO; GO:0009791; P:post-embryonic development; IGI:MGI.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; TAS:BHF-UCL.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISO:MGI.
DR GO; GO:0002026; P:regulation of the force of heart contraction; IMP:MGI.
DR GO; GO:0044557; P:relaxation of smooth muscle; IMP:BHF-UCL.
DR GO; GO:0033198; P:response to ATP; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0035994; P:response to muscle stretch; ISO:MGI.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IMP:BHF-UCL.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IMP:BHF-UCL.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR GO; GO:0014829; P:vascular associated smooth muscle contraction; IMP:BHF-UCL.
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 Antiport; Calcium; Calcium transport; Calmodulin-binding; Cell membrane;
KW Glycoprotein; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Sodium; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..970
FT /note="Sodium/calcium exchanger 1"
FT /id="PRO_0000019380"
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..797
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 798..818
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 819..821
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 843..871
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 872..892
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 893..903
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 904..924
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 925..941
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 942..962
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 963..970
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 839..875
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 715
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:0007744|PubMed:21183079"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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"
SQ SEQUENCE 970 AA; 108035 MW; F5FC0BD07F2B6602 CRC64;
MLRLSLPPNV SMGFRLVALV ALLFSHVDHI 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 KQKHPEKEIE QLIELANYQV LSQQQKSRAF
YRIQATRLMT GAGNILKRHA ADQARKAVSM HEVNMEMAEN DPVSKIFFEQ GTYQCLENCG
TVALTIMRRG GDLSTTVFVD FRTEDGTANA ASDYEFTEGT VIFKPGETQK EIRVGIIDDD
IFEEDENFLV HLSNVRVSSD VSEDGILESN HASSIACLGS PSTATITIFD DDHAGIFTFE
EPVTHVSESI GIMEVKVLRT SGARGNVIIP YKTIEGTARG GGEDFEDTCG EPEFQNDEIV
KTISVKVIDD EEYEKNKTFF IEIGEPRLVE MSEKKALLLN ELGGFTLTGK EMYGQPIFRK
VHARDHPIPS TVITISEEYD DKQPLTSKEE EERRIAEMGR PILGEHTKLE VIIQESYEFK
STVDKLIKKT NLALVVGTNS WREQFIEAIT VSAGEDDDDD ECGEEKLPSC FDYVMHFLTV
FWKVLFAFVP PTEYWNGWAC FIVSILMIGL LTAFIGDLAS HFGCTIGLKD SVTAVVFVAL
GTSVPDTFAS KVAATQDQYA DASIGNVTGS NAVNVFLGIG VAWSIAAIYH AANGEQFKVS
PGTLAFSVTL FTIFAFINVG VLLYRRRPEI GGELGGPRTA KLLTSSLFVL LWLLYIFFSS
LEAYCHIKGF
