NAC2_MOUSE
ID NAC2_MOUSE Reviewed; 921 AA.
AC Q8K596; Q68EG0; Q8R504;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Sodium/calcium exchanger 2;
DE AltName: Full=Na(+)/Ca(2+)-exchange protein 2;
DE AltName: Full=Solute carrier family 8 member 2;
DE Flags: Precursor;
GN Name=Slc8a2 {ECO:0000312|MGI:MGI:107996};
GN Synonyms=Ncx2 {ECO:0000303|PubMed:25498502};
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] {ECO:0000312|EMBL:AAM22231.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum {ECO:0000312|EMBL:AAM22231.1};
RA Kraev A.;
RT "Towards a complete inventory of calcium transporters of the house mouse.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 230-400.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:BAB85834.1};
RC TISSUE=Brain capillary {ECO:0000312|EMBL:BAB85834.1};
RX PubMed=12581871; DOI=10.1016/s0167-4889(02)00397-x;
RA Yamaji R., Fujita K., Takahashi S., Yoneda H., Nagao K., Masuda W.,
RA Naito M., Tsuruo T., Miyatake K., Inui H., Nakano Y.;
RT "Hypoxia up-regulates glyceraldehyde-3-phosphate dehydrogenase in mouse
RT brain capillary endothelial cells: involvement of Na+/Ca2+ exchanger.";
RL Biochim. Biophys. Acta 1593:269-276(2003).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12818181; DOI=10.1016/s0896-6273(03)00334-9;
RA Jeon D., Yang Y.M., Jeong M.J., Philipson K.D., Rhim H., Shin H.S.;
RT "Enhanced learning and memory in mice lacking Na+/Ca2+ exchanger 2.";
RL Neuron 38:965-976(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-622, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
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 [8]
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).
RN [9]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=25498502; DOI=10.1016/j.bbrc.2014.12.016;
RA Gotoh Y., Kita S., Fujii M., Tagashira H., Horie I., Arai Y., Uchida S.,
RA Iwamoto T.;
RT "Genetic knockout and pharmacologic inhibition of NCX2 cause natriuresis
RT and hypercalciuria.";
RL Biochem. Biophys. Res. Commun. 456:670-675(2015).
CC -!- FUNCTION: Mediates the electrogenic exchange of Ca(2+) against Na(+)
CC 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:12818181). Contributes to cellular Ca(2+) homeostasis
CC in excitable cells (PubMed:12818181). Contributes to the rapid decrease
CC of cytoplasmic Ca(2+) levels back to baseline after neuronal
CC activation, and thereby contributes to modulate synaptic plasticity,
CC learning and memory (PubMed:12818181). Plays a role in regulating
CC urinary Ca(2+) and Na(+) excretion (PubMed:25498502).
CC {ECO:0000269|PubMed:12818181}.
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:0000250|UniProtKB:P48768};
CC -!- ACTIVITY REGULATION: Calcium transport is down-regulated by Na(+) and
CC stimulated by Ca(2+). {ECO:0000250|UniProtKB:P48768}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12818181};
CC Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane
CC {ECO:0000269|PubMed:25498502}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K596-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K596-2; Sequence=VSP_057980;
CC -!- TISSUE SPECIFICITY: Detected in kidney cortex, in distal convoluted
CC tubules and connecting segments (PubMed:25498502). Detected in brain
CC and spinal cord (at protein level) (PubMed:12818181). Detected in
CC brain, especially in hippocampus CA1, CA2 and CA3 fiels, dentate gyrus,
CC cerebellum and brain cortex (PubMed:12818181).
CC {ECO:0000269|PubMed:12818181, ECO:0000269|PubMed:25498502}.
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: No obvious phenotype. In hippocampus pyramidal
CC neurons, calcium exchange activity is reduced by about half, suggesting
CC that other, additional calcium exchangers are active in these neurons.
CC In these neurons, the neurotransmitter glutamate triggers a sharp
CC increase in cellular Ca(2+) that does not depend on calcium exchanger
CC activity. In contrast, the decrease to basal levels is mediated by
CC calcium exchangers, and is considerably slower in mutant mice than in
CC wild-type. Basal synaptic function is not impaired in mutant mice, but
CC they display enhanced short-term plasticity and facilitated long-term
CC potentiation, probably due to the slower decrease of Ca(2+) after an
CC initial impulse. Mutant mice display an increased capacity for spatial
CC learning and memory (PubMed:12818181). Heterozygous mutants show
CC increased basal urine volume and increased urinary secretion of Ca(2+)
CC and Na(+) (PubMed:25498502). {ECO:0000269|PubMed:12818181,
CC ECO:0000269|PubMed:25498502}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. SLC8 subfamily. {ECO:0000305}.
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DR EMBL; AF503502; AAM22231.1; -; mRNA.
DR EMBL; AC151733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466654; EDL42109.1; -; Genomic_DNA.
DR EMBL; BC058704; AAH58704.1; -; mRNA.
DR EMBL; BC080277; AAH80277.1; -; mRNA.
DR EMBL; AB080745; BAB85834.1; -; mRNA.
DR CCDS; CCDS20845.1; -. [Q8K596-1]
DR CCDS; CCDS85220.1; -. [Q8K596-2]
DR RefSeq; NP_001334490.1; NM_001347561.1. [Q8K596-2]
DR RefSeq; NP_683748.1; NM_148946.3. [Q8K596-1]
DR AlphaFoldDB; Q8K596; -.
DR SMR; Q8K596; -.
DR STRING; 10090.ENSMUSP00000128926; -.
DR GlyGen; Q8K596; 2 sites.
DR iPTMnet; Q8K596; -.
DR PhosphoSitePlus; Q8K596; -.
DR SwissPalm; Q8K596; -.
DR MaxQB; Q8K596; -.
DR PaxDb; Q8K596; -.
DR PRIDE; Q8K596; -.
DR ProteomicsDB; 286141; -. [Q8K596-1]
DR ProteomicsDB; 286142; -. [Q8K596-2]
DR Antibodypedia; 54559; 82 antibodies from 17 providers.
DR DNASU; 110891; -.
DR Ensembl; ENSMUST00000168693; ENSMUSP00000128926; ENSMUSG00000030376. [Q8K596-2]
DR Ensembl; ENSMUST00000211649; ENSMUSP00000147497; ENSMUSG00000030376. [Q8K596-1]
DR GeneID; 110891; -.
DR KEGG; mmu:110891; -.
DR UCSC; uc009fgz.1; mouse. [Q8K596-1]
DR UCSC; uc012fac.1; mouse.
DR CTD; 6543; -.
DR MGI; MGI:107996; Slc8a2.
DR VEuPathDB; HostDB:ENSMUSG00000030376; -.
DR eggNOG; KOG1306; Eukaryota.
DR GeneTree; ENSGT00940000158344; -.
DR HOGENOM; CLU_012872_1_0_1; -.
DR InParanoid; Q8K596; -.
DR OMA; HRQEFIE; -.
DR OrthoDB; 490546at2759; -.
DR PhylomeDB; Q8K596; -.
DR TreeFam; TF314308; -.
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; 110891; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Slc8a2; mouse.
DR PRO; PR:Q8K596; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K596; protein.
DR Bgee; ENSMUSG00000030376; Expressed in dentate gyrus of hippocampal formation granule cell and 43 other tissues.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IMP:ARUK-UCL.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:ARUK-UCL.
DR GO; GO:0015085; F:calcium ion transmembrane transporter activity; IMP:ARUK-UCL.
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:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0015491; F:cation:cation antiporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:1990034; P:calcium ion export across plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0060402; P:calcium ion transport into cytosol; ISO:MGI.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0050890; P:cognition; IMP:ARUK-UCL.
DR GO; GO:0007612; P:learning; IMP:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IMP:ARUK-UCL.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0007613; P:memory; IMP:UniProtKB.
DR GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IMP:ARUK-UCL.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:ARUK-UCL.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:ARUK-UCL.
DR GO; GO:0099608; P:regulation of action potential firing pattern; IMP:ARUK-UCL.
DR GO; GO:0106056; P:regulation of calcineurin-mediated signaling; IMP:ARUK-UCL.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:ARUK-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; IMP:ARUK-UCL.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; ISO:MGI.
DR GO; GO:0050808; P:synapse organization; IMP:ARUK-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; IPR004836; Na_Ca_Ex.
DR InterPro; IPR032452; Na_Ca_Ex_C-exten.
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 SMART; SM00237; Calx_beta; 2.
DR SUPFAM; SSF141072; SSF141072; 2.
DR TIGRFAMs; TIGR00845; caca; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Calcium; Calcium transport;
KW Calmodulin-binding; Cell membrane; Glycoprotein; Ion transport; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Signal; Sodium;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..921
FT /note="Sodium/calcium exchanger 2"
FT /id="PRO_0000434796"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..806
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 823..843
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 855..875
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 893..913
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 389..482
FT /note="Calx-beta 1"
FT /evidence="ECO:0000255"
FT DOMAIN 512..611
FT /note="Calx-beta 2"
FT /evidence="ECO:0000255"
FT REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..267
FT /note="Putative calmodulin-binding region"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT REGION 371..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 518
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 520
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 520
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 536
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 598
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 598
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 599
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT BINDING 665
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:P23685"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 623..628
FT /note="Missing (in isoform 2)"
FT /id="VSP_057980"
FT CONFLICT 260
FT /note="Y -> C (in Ref. 5; BAB85834)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="D -> G (in Ref. 5; BAB85834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 921 AA; 100711 MW; 5F5A378FF982073D CRC64;
MAPLALMGVV LLLGVPHCLG EATPTPSLPP PTANDSDASP EGCQGSYRCQ PGVLLPVWEP
EDPSLGDKVA RAVVYFVAMV YMFLGVSIIA DRFMASIEVI TSKEKEITIT KANGETSVGT
VRIWNETVSN LTLMALGSSA PEILLTVIEV CGHNFQAGEL GPGTIVGSAA FNMFVVIAVC
VYVIPAGESR KIKHLRVFFV TASWSIFAYV WLYLILAVFS PGVVQVWEAL LTLIFFPVCV
VFAWMADKRL LFYKYVYKRY RTDPRSGIII GAEGDPPKSI ELDGTFVGTE VPGELGALGT
GPAEARELDA SRREVIQILK DLKQKHPDKD LEQLMGIAKY YALLHQQKSR AFYRIQATRL
MTGAGNVLRR HAADAARRPG ATDGAPDDED DGASRIFFEP SLYHCLENCG SVLLSVACQG
GEGNSTFYVD YRTEDGSAKA GSDYEYSEGT LVFKPGETQK DLRIGIIDDD IFEEDEHFFV
RLLNLRVGDA QGMFEPDGGG RPKGRLVAPL LATVTILDDD HAGIFSFQDR LLHVSECMGT
VDVRVVRSSG ARGTVRLPYR TVDGTARGGG VHYEDACGEL EFGDDETMKT LQVKIVDDEE
YEKKDNFFIE LGQPQWLKRG ISALLLNQGN GDKKITAEQE EAQRIAEMGK PVLGENNRLE
VIIEESYDFK NTVDKLIKKT NLALVIGTHS WREQFIEAVT VSAGDEEEDE DGPREERLPS
CFDYVMHFLT VFWKVLFACV PPTEYCNGWA CFGVCILVIG VLTALIGDLA SHFGCTVGLK
DSVNAVVFVA LGTSIPDTFA SKVAALQDQC ADASIGNVTG SNAVNVFLGL GVAWSVAAVY
WAVQGRPFEV RAGTLAFSVT LFTVFAFVCI AVLLYRRRPQ IGGELGGPRG PKLATTALFL
GLWFLYILFS SLEAYCHIRG F
