NAC1_CANLF
ID NAC1_CANLF Reviewed; 970 AA.
AC P23685;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 159.
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=NCX1 {ECO:0000303|PubMed:9486131};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=1700476; DOI=10.1126/science.1700476;
RA Nicoll D.A., Longoni S., Philipson K.D.;
RT "Molecular cloning and functional expression of the cardiac sarcolemmal
RT Na(+)-Ca2+ exchanger.";
RL Science 250:562-565(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Heart;
RX PubMed=1785844; DOI=10.1111/j.1749-6632.1991.tb17305.x;
RA Nicoll D.A., Philipson K.D.;
RT "Molecular studies of the cardiac sarcolemmal sodium-calcium exchanger.";
RL Ann. N. Y. Acad. Sci. 639:181-188(1991).
RN [3]
RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND ACTIVITY
RP REGULATION.
RX PubMed=9486131; DOI=10.1152/ajpcell.1998.274.2.c415;
RA Linck B., Qiu Z., He Z., Tong Q., Hilgemann D.W., Philipson K.D.;
RT "Functional comparison of the three isoforms of the Na+/Ca2+ exchanger
RT (NCX1, NCX2, NCX3).";
RL Am. J. Physiol. 274:C415-C423(1998).
RN [4]
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 402-541 IN COMPLEX WITH CALCIUM,
RP CALCIUM-BINDING SITES, AND DOMAIN.
RX PubMed=16774926; DOI=10.1074/jbc.c600117200;
RA Nicoll D.A., Sawaya M.R., Kwon S., Cascio D., Philipson K.D., Abramson J.;
RT "The crystal structure of the primary Ca2+ sensor of the Na+/Ca2+ exchanger
RT reveals a novel Ca2+ binding motif.";
RL J. Biol. Chem. 281:21577-21581(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 533-721 ALONE AND IN COMPLEX WITH
RP CALCIUM IONS, CALCIUM-BINDING SITES, FUNCTION, SUBCELLULAR LOCATION,
RP ACTIVITY REGULATION, AND MUTAGENESIS OF GLU-548; ASP-584; ASP-610 AND
RP LYS-617.
RX PubMed=17962412; DOI=10.1073/pnas.0707417104;
RA Besserer G.M., Ottolia M., Nicoll D.A., Chaptal V., Cascio D.,
RA Philipson K.D., Abramson J.;
RT "The second Ca2+-binding domain of the Na+ Ca2+ exchanger is essential for
RT regulation: crystal structures and mutational analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18467-18472(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 402-541 IN COMPLEX WITH CALCIUM,
RP FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=19332552; DOI=10.1074/jbc.c900037200;
RA Chaptal V., Ottolia M., Mercado-Besserer G., Nicoll D.A., Philipson K.D.,
RA Abramson J.;
RT "Structure and functional analysis of a Ca2+ sensor mutant of the Na+/Ca2+
RT exchanger.";
RL J. Biol. Chem. 284:14688-14692(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 403-724 IN COMPLEX WITH CALCIUM,
RP AND DOMAIN.
RX PubMed=22768191; DOI=10.1371/journal.pone.0039985;
RA Giladi M., Sasson Y., Fang X., Hiller R., Buki T., Wang Y.X., Hirsch J.A.,
RA Khananshvili D.;
RT "A common Ca2+-driven interdomain module governs eukaryotic NCX
RT regulation.";
RL PLoS ONE 7:E39985-E39985(2012).
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:1700476, PubMed:1785844, PubMed:9486131,
CC PubMed:17962412). Contributes to Ca(2+) transport during excitation-
CC contraction coupling in muscle. In a first phase, voltage-gated
CC channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to
CC release of Ca(2+) stores from the endoplasmic reticulum. SLC8A1
CC mediates the export of Ca(2+) from the cell during the next phase, so
CC that cytoplasmic Ca(2+) levels rapidly return to baseline. Required for
CC normal embryonic heart development and the onset of heart contractions
CC (By similarity). {ECO:0000250|UniProtKB:P70414,
CC ECO:0000269|PubMed:1700476, ECO:0000269|PubMed:1785844,
CC ECO:0000269|PubMed:17962412, ECO:0000269|PubMed:19332552,
CC ECO:0000269|PubMed:9486131}.
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:0000269|PubMed:1700476, ECO:0000269|PubMed:1785844,
CC ECO:0000269|PubMed:9486131};
CC -!- ACTIVITY REGULATION: Activated by micromolar levels of Ca(2+). In the
CC absence of regulatory Ca(2+), channels open rapidly, and then
CC inactivate rapidly. Inactivation is enhanced by Na(+) and is inhibited
CC by micromolar levels of Ca(2+). {ECO:0000269|PubMed:17962412,
CC ECO:0000269|PubMed:19332552, ECO:0000269|PubMed:9486131}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1700476,
CC ECO:0000269|PubMed:1785844, ECO:0000269|PubMed:17962412,
CC ECO:0000269|PubMed:19332552, ECO:0000269|PubMed:9486131}; Multi-pass
CC membrane protein {ECO:0000305}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:1700476}.
CC -!- TISSUE SPECIFICITY: Cardiac sarcolemma (at protein level).
CC {ECO:0000269|PubMed:1700476}.
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
CC (PubMed:16774926, PubMed:19332552, PubMed:22768191). The second domain
CC can bind another two Ca(2+) ions that are essential for calcium-
CC regulated ion exchange (PubMed:17962412). {ECO:0000269|PubMed:16774926,
CC ECO:0000269|PubMed:17962412, ECO:0000269|PubMed:19332552,
CC ECO:0000269|PubMed:22768191}.
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; M57523; AAA62766.1; -; mRNA.
DR PIR; A36417; A36417.
DR RefSeq; NP_001291891.1; NM_001304962.1.
DR RefSeq; XP_013975680.1; XM_014120205.1.
DR RefSeq; XP_013975681.1; XM_014120206.1.
DR RefSeq; XP_013975682.1; XM_014120207.1.
DR RefSeq; XP_013975683.1; XM_014120208.1.
DR RefSeq; XP_013975684.1; XM_014120209.1.
DR RefSeq; XP_013975685.1; XM_014120210.1.
DR RefSeq; XP_013975686.1; XM_014120211.1.
DR RefSeq; XP_013975687.1; XM_014120212.1.
DR RefSeq; XP_013975688.1; XM_014120213.1.
DR RefSeq; XP_013975689.1; XM_014120214.1.
DR PDB; 2DPK; X-ray; 2.50 A; A=402-541.
DR PDB; 2FWS; NMR; -; A=403-541.
DR PDB; 2FWU; NMR; -; A=533-724.
DR PDB; 2QVK; X-ray; 1.45 A; A=533-721.
DR PDB; 2QVM; X-ray; 1.70 A; A=533-721.
DR PDB; 3GIN; X-ray; 2.40 A; A/B=402-541.
DR PDB; 3US9; X-ray; 2.68 A; A=403-724.
DR PDB; 6BV7; NMR; -; A=306-359.
DR PDBsum; 2DPK; -.
DR PDBsum; 2FWS; -.
DR PDBsum; 2FWU; -.
DR PDBsum; 2QVK; -.
DR PDBsum; 2QVM; -.
DR PDBsum; 3GIN; -.
DR PDBsum; 3US9; -.
DR PDBsum; 6BV7; -.
DR AlphaFoldDB; P23685; -.
DR BMRB; P23685; -.
DR SMR; P23685; -.
DR DIP; DIP-59598N; -.
DR STRING; 9615.ENSCAFP00000009692; -.
DR iPTMnet; P23685; -.
DR SwissPalm; P23685; -.
DR PaxDb; P23685; -.
DR Ensembl; ENSCAFT00000010451; ENSCAFP00000009692; ENSCAFG00000023592.
DR Ensembl; ENSCAFT00845044459; ENSCAFP00845034837; ENSCAFG00845024998.
DR GeneID; 475738; -.
DR KEGG; cfa:475738; -.
DR CTD; 6546; -.
DR VEuPathDB; HostDB:ENSCAFG00845024998; -.
DR VGNC; VGNC:46480; SLC8A1.
DR eggNOG; KOG1306; Eukaryota.
DR GeneTree; ENSGT00940000155129; -.
DR HOGENOM; CLU_012872_1_0_1; -.
DR InParanoid; P23685; -.
DR OMA; VSAETEM; -.
DR OrthoDB; 490546at2759; -.
DR TreeFam; TF314308; -.
DR EvolutionaryTrace; P23685; -.
DR Proteomes; UP000002254; Chromosome 17.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:1905060; F:calcium:cation antiporter activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IMP:SynGO.
DR GO; GO:0005432; F:calcium:sodium antiporter activity; IDA: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:0070509; P:calcium ion import; IEA:Ensembl.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IEA:Ensembl.
DR GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0098735; P:positive regulation of the force of heart contraction; IEA:Ensembl.
DR GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA:UniProtKB.
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 3D-structure; Antiport; Calcium; Calcium transport; Calmodulin-binding;
KW Cell membrane; Glycoprotein; Ion transport; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Sodium;
KW Sodium transport; 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_0000019376"
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:0000305"
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:0000305|PubMed:1700476"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:3GIN, ECO:0007744|PDB:3US9"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:3GIN, ECO:0007744|PDB:3US9"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:2DPK, ECO:0007744|PDB:3GIN,
FT ECO:0007744|PDB:3US9"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:3GIN"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:2DPK, ECO:0007744|PDB:2FWS"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:2DPK, ECO:0007744|PDB:3GIN,
FT ECO:0007744|PDB:3US9"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:3GIN"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:2DPK, ECO:0007744|PDB:3GIN,
FT ECO:0007744|PDB:3US9"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:2DPK, ECO:0007744|PDB:3GIN,
FT ECO:0007744|PDB:3US9"
FT BINDING 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:2FWS"
FT BINDING 481
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:2DPK, ECO:0007744|PDB:3GIN,
FT ECO:0007744|PDB:3US9"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:3US9"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:2DPK, ECO:0007744|PDB:3US9"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:2DPK, ECO:0007744|PDB:2FWS"
FT BINDING 486
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:2DPK, ECO:0007744|PDB:2FWS"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:2DPK, ECO:0007744|PDB:3GIN,
FT ECO:0007744|PDB:3US9"
FT BINDING 531
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:2DPK, ECO:0007744|PDB:3GIN,
FT ECO:0007744|PDB:3US9"
FT BINDING 532
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:2DPK, ECO:0007744|PDB:3GIN,
FT ECO:0007744|PDB:3US9"
FT BINDING 532
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:2DPK, ECO:0007744|PDB:3GIN,
FT ECO:0007744|PDB:3US9"
FT BINDING 548
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:2QVM"
FT BINDING 584
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:2FWU"
FT BINDING 610
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:2QVM"
FT BINDING 610
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:2FWU"
FT BINDING 611
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:2FWU"
FT BINDING 612
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:2QVM"
FT BINDING 612
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:2FWU"
FT BINDING 715
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:2QVM"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70414"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70414, ECO:0000255"
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"
FT MUTAGEN 548
FT /note="E->L: Abolishes regulation by micromolar Ca(2+)."
FT /evidence="ECO:0000269|PubMed:17962412"
FT MUTAGEN 584
FT /note="D->V: No effect on regulation by micromolar Ca(2+)."
FT /evidence="ECO:0000269|PubMed:17962412"
FT MUTAGEN 610
FT /note="D->V: Abolishes regulation by micromolar Ca(2+)."
FT /evidence="ECO:0000269|PubMed:17962412"
FT MUTAGEN 617
FT /note="K->E: Decreases affinity for Ca(2+), but retains
FT regulation by micromolar Ca(2+)."
FT /evidence="ECO:0000269|PubMed:17962412"
FT HELIX 316..333
FT /evidence="ECO:0007829|PDB:6BV7"
FT HELIX 339..354
FT /evidence="ECO:0007829|PDB:6BV7"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:3GIN"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:3GIN"
FT STRAND 419..431
FT /evidence="ECO:0007829|PDB:3GIN"
FT STRAND 437..448
FT /evidence="ECO:0007829|PDB:3GIN"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:3GIN"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:3GIN"
FT STRAND 469..476
FT /evidence="ECO:0007829|PDB:3GIN"
FT STRAND 486..496
FT /evidence="ECO:0007829|PDB:3GIN"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:3GIN"
FT STRAND 522..529
FT /evidence="ECO:0007829|PDB:3GIN"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:2QVK"
FT STRAND 542..547
FT /evidence="ECO:0007829|PDB:2QVK"
FT STRAND 552..561
FT /evidence="ECO:0007829|PDB:2QVK"
FT STRAND 567..578
FT /evidence="ECO:0007829|PDB:2QVK"
FT TURN 580..583
FT /evidence="ECO:0007829|PDB:2QVK"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:3US9"
FT STRAND 589..594
FT /evidence="ECO:0007829|PDB:2QVK"
FT STRAND 600..607
FT /evidence="ECO:0007829|PDB:2QVK"
FT STRAND 615..623
FT /evidence="ECO:0007829|PDB:2QVK"
FT STRAND 627..629
FT /evidence="ECO:0007829|PDB:2QVM"
FT HELIX 687..696
FT /evidence="ECO:0007829|PDB:3US9"
FT STRAND 708..714
FT /evidence="ECO:0007829|PDB:2QVK"
SQ SEQUENCE 970 AA; 108004 MW; BBDBCC584846AE08 CRC64;
MLQLRLLPTF SMGCHLLAVV ALLFSHVDLI SAETEMEGEG NETGECTGSY YCKKGVILPI
WEPQDPSFGD KIARATVYFV AMVYMFLGVS IIADRFMSSI EVITSQEKEI TIKKPNGETT
KTTVRIWNET VSNLTLMALG SSAPEILLSV IEVCGHNFTA GDLGPSTIVG SAAFNMFIII
ALCVYVVPDG ETRKIKHLRV FFVTAAWSIF AYTWLYIILS VISPGVVEVW EGLLTFFFFP
ICVVFAWVAD RRLLFYKYVY KRYRAGKQRG MIIEHEGDRP SSKTEIEMDG KVVNSHVDNF
LDGALVLEVD ERDQDDEEAR REMARILKEL KQKHPEKEIE QLIELANYQV LSQQQKSRAF
YRIQATRLMT GAGNILKRHA ADQARKAVSM HEVNTEVAEN DPVSKIFFEQ GTYQCLENCG
TVALTIIRRG GDLTNTVFVD FRTEDGTANA GSDYEFTEGT VVFKPGETQK EIRVGIIDDD
IFEEDENFLV HLSNVKVSSE ASEDGILEAN HVSALACLGS PSTATVTIFD DDHAGIFTFE
EPVTHVSESI GIMEVKVLRT SGARGNVIVP YKTIEGTARG GGEDFEDTCG ELEFQNDEIV
KTISVKVIDD EEYEKNKTFF LEIGEPRLVE MSEKKALLLN ELGGFTITGK YLYGQPVFRK
VHAREHPIPS TVITIAEEYD DKQPLTSKEE EERRIAEMGR PILGEHTKLE VIIEESYEFK
STVDKLIKKT NLALVVGTNS WREQFIEAIT VSAGEDDDDD ECGEEKLPSC FDYVMHFLTV
FWKVLFAFVP PTEYWNGWAC FIVSILMIGI LTAFIGDLAS HFGCTIGLKD SVTAVVFVAL
GTSVPDTFAS KVAATQDQYA DASIGNVTGS NAVNVFLGIG VAWSIAAIYH AANGEQFKVS
PGTLAFSVTL FTIFAFINVG VLLYRRRPEI GGELGGPRTA KLLTSCLFVL LWLLYIFFSS
LEAYCHIKGF
