ID   ATC1_DROME              Reviewed;        1020 AA.
AC   P22700; A4UZU0; Q2MGN2; Q95TX1; Q9W1G2; Q9W1G3;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 216.
DE   RecName: Full=Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type;
DE            EC=7.2.2.10;
DE   AltName: Full=Calcium ATPase at 60A;
DE   AltName: Full=Calcium pump;
DE   AltName: Full=Sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase {ECO:0000312|FlyBase:FBgn0263006};
GN   Name=SERCA {ECO:0000312|FlyBase:FBgn0263006};
GN   Synonyms=Ca-P60A {ECO:0000312|FlyBase:FBgn0263006};
GN   ORFNames=CG3725 {ECO:0000312|FlyBase:FBgn0263006};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX   PubMed=2148477; DOI=10.1016/s0006-291x(05)80867-8;
RA   Magyar A., Varadi A.;
RT   "Molecular cloning and chromosomal localization of a sarco/endoplasmic
RT   reticulum-type Ca2(+)-ATPase of Drosophila melanogaster.";
RL   Biochem. Biophys. Res. Commun. 173:872-877(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 357-513.
RX   PubMed=2557235; DOI=10.1016/0014-5793(89)81653-9;
RA   Varadi A., Gilmore-Heber M., Benz E.J. Jr.;
RT   "Amplification of the phosphorylation site-ATP-binding site cDNA fragment
RT   of the Na+,K(+)-ATPase and the Ca2(+)-ATPase of Drosophila melanogaster by
RT   polymerase chain reaction.";
RL   FEBS Lett. 258:203-207(1989).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
RN   [7]
RP   INTERACTION WITH SCLA AND SCLB, AND SUBCELLULAR LOCATION.
RX   PubMed=23970561; DOI=10.1126/science.1238802;
RA   Magny E.G., Pueyo J.I., Pearl F.M., Cespedes M.A., Niven J.E., Bishop S.A.,
RA   Couso J.P.;
RT   "Conserved regulation of cardiac calcium uptake by peptides encoded in
RT   small open reading frames.";
RL   Science 341:1116-1120(2013).
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC       ATP coupled with the transport of calcium.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.10;
CC   -!- SUBUNIT: Interacts with SclA and SclB. {ECO:0000269|PubMed:23970561}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:23970561}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:23970561}. Sarcoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:23970561}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:23970561}. Note=Colocalizes with SclA and SclB at
CC       the sarcoplasmic reticulum and the diad, a structure composed of a
CC       single t-tubule paired with a terminal cisterna of the sarcoplasmic
CC       reticulum. {ECO:0000269|PubMed:23970561}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=B; Synonyms=C, D, E, F, G, H;
CC         IsoId=P22700-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=P22700-2; Sequence=VSP_010297;
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. {ECO:0000305}.
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DR   EMBL; M62892; AAB00735.1; -; mRNA.
DR   EMBL; AE013599; AAF47101.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF47102.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF47103.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM68278.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM68279.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM68280.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM68281.1; -; Genomic_DNA.
DR   EMBL; AY058465; AAL13694.1; -; mRNA.
DR   EMBL; X17472; CAA35505.1; -; mRNA.
DR   PIR; A36691; A36691.
DR   RefSeq; NP_476832.1; NM_057484.3. [P22700-2]
DR   RefSeq; NP_726381.1; NM_166633.2. [P22700-1]
DR   RefSeq; NP_726382.1; NM_166634.2. [P22700-1]
DR   RefSeq; NP_726383.1; NM_166635.2. [P22700-1]
DR   RefSeq; NP_726384.1; NM_166636.2. [P22700-1]
DR   RefSeq; NP_726385.1; NM_166637.2. [P22700-1]
DR   RefSeq; NP_726386.1; NM_166638.2. [P22700-1]
DR   RefSeq; NP_726387.1; NM_166639.2. [P22700-1]
DR   AlphaFoldDB; P22700; -.
DR   SMR; P22700; -.
DR   BioGRID; 72161; 129.
DR   DIP; DIP-20129N; -.
DR   IntAct; P22700; 6.
DR   STRING; 7227.FBpp0072125; -.
DR   iPTMnet; P22700; -.
DR   PaxDb; 7227-FBpp0072125; -.
DR   DNASU; 49297; -.
DR   EnsemblMetazoa; FBtr0072211; FBpp0072120; FBgn0263006. [P22700-1]
DR   EnsemblMetazoa; FBtr0072212; FBpp0072121; FBgn0263006. [P22700-1]
DR   EnsemblMetazoa; FBtr0072213; FBpp0072122; FBgn0263006. [P22700-1]
DR   EnsemblMetazoa; FBtr0072214; FBpp0072123; FBgn0263006. [P22700-1]
DR   EnsemblMetazoa; FBtr0072215; FBpp0072124; FBgn0263006. [P22700-2]
DR   EnsemblMetazoa; FBtr0072216; FBpp0072125; FBgn0263006. [P22700-1]
DR   EnsemblMetazoa; FBtr0072217; FBpp0072126; FBgn0263006. [P22700-1]
DR   EnsemblMetazoa; FBtr0072218; FBpp0072127; FBgn0263006. [P22700-1]
DR   GeneID; 49297; -.
DR   KEGG; dme:Dmel_CG3725; -.
DR   AGR; FB:FBgn0263006; -.
DR   CTD; 49297; -.
DR   FlyBase; FBgn0263006; SERCA.
DR   VEuPathDB; VectorBase:FBgn0263006; -.
DR   eggNOG; KOG0202; Eukaryota.
DR   GeneTree; ENSGT00940000155668; -.
DR   InParanoid; P22700; -.
DR   OMA; PLWNNMM; -.
DR   OrthoDB; 203629at2759; -.
DR   PhylomeDB; P22700; -.
DR   Reactome; R-DME-418359; Reduction of cytosolic Ca++ levels.
DR   Reactome; R-DME-5578775; Ion homeostasis.
DR   Reactome; R-DME-936837; Ion transport by P-type ATPases.
DR   SignaLink; P22700; -.
DR   BioGRID-ORCS; 49297; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 49297; -.
DR   PRO; PR:P22700; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0263006; Expressed in thoracico-abdominal ganglion (Drosophila) and 50 other cell types or tissues.
DR   ExpressionAtlas; P22700; baseline and differential.
DR   GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:FlyBase.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IDA:FlyBase.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IMP:FlyBase.
DR   GO; GO:1990845; P:adaptive thermogenesis; IMP:FlyBase.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:1903515; P:calcium ion transport from cytosol to endoplasmic reticulum; IMP:FlyBase.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IMP:FlyBase.
DR   GO; GO:0007629; P:flight behavior; IGI:FlyBase.
DR   GO; GO:0030707; P:follicle cell of egg chamber development; IMP:FlyBase.
DR   GO; GO:0060047; P:heart contraction; IMP:FlyBase.
DR   GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IMP:FlyBase.
DR   GO; GO:0008610; P:lipid biosynthetic process; IMP:FlyBase.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR   GO; GO:0010884; P:positive regulation of lipid storage; IMP:FlyBase.
DR   GO; GO:0051282; P:regulation of sequestering of calcium ion; IMP:FlyBase.
DR   GO; GO:0030322; P:stabilization of membrane potential; IGI:FlyBase.
DR   GO; GO:0048863; P:stem cell differentiation; IMP:FlyBase.
DR   CDD; cd02083; P-type_ATPase_SERCA; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR005782; P-type_ATPase_IIA.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF127; CALCIUM-TRANSPORTING ATPASE SARCOPLASMIC_ENDOPLASMIC RETICULUM TYPE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   Genevisible; P22700; DM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Calcium; Calcium transport;
KW   Endoplasmic reticulum; Ion transport; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Sarcoplasmic reticulum; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..1020
FT                   /note="Calcium-transporting ATPase sarcoplasmic/endoplasmic
FT                   reticulum type"
FT                   /id="PRO_0000046208"
FT   TOPO_DOM        1..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        49..69
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        70..89
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        90..110
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        111..253
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        254..273
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        274..295
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        296..313
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        314..757
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        758..777
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        778..787
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        788..808
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        809..828
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        829..851
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        852..897
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        898..917
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        918..930
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        931..949
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        950..964
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        965..985
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        986..1020
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        351
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         703
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         707
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         768
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         771
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         796
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         799
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         800
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         800
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         908
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         240
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   VAR_SEQ         994..1020
FT                   /note="GESPIYKMHGIVLMWAVFFGLLYAMML -> VPDVVVDRM (in isoform
FT                   A)"
FT                   /evidence="ECO:0000303|PubMed:2148477"
FT                   /id="VSP_010297"
FT   CONFLICT        158
FT                   /note="K -> R (in Ref. 4; AAL13694)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302
FT                   /note="L -> V (in Ref. 1; AAB00735)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        357
FT                   /note="T -> L (in Ref. 5; CAA35505)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        495
FT                   /note="S -> P (in Ref. 4; AAL13694)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1020 AA;  111701 MW;  6A62D350BF316984 CRC64;
     MEDGHSKTVE QSLNFFGTDP ERGLTLDQIK ANQKKYGPNE LPTEEGKSIW QLVLEQFDDL
     LVKILLLAAI ISFVLALFEE HEETFTAFVE PLVILLILIA NAVVGVWQER NAESAIEALK
     EYEPEMGKVV RQDKSGIQKV RAKEIVPGDL VEVSVGDKIP ADIRITHIYS TTLRIDQSIL
     TGESVSVIKH TDAIPDPRAV NQDKKNILFS GTNVAAGKAR GVVIGTGLST AIGKIRTEMS
     ETEEIKTPLQ QKLDEFGEQL SKVISVICVA VWAINIGHFN DPAHGGSWIK GAIYYFKIAV
     ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
     MSVSRMFIFD KVEGNDSSFL EFEMTGSTYE PIGEVFLNGQ RIKAADYDTL QELSTICIMC
     NDSAIDYNEF KQAFEKVGEA TETALIVLAE KLNSFSVNKS GLDRRSAAIA CRGEIETKWK
     KEFTLEFSRD RKSMSSYCTP LKASRLGTGP KLFVKGAPEG VLERCTHARV GTTKVPLTSA
     LKAKILALTG QYGTGRDTLR CLALAVADSP MKPDEMDLGD STKFYQYEVN LTFVGVVGML
     DPPRKEVFDS IVRCRAAGIR VIVITGDNKA TAEAICRRIG VFAEDEDTTG KSYSGREFDD
     LSPTEQKAAV ARSRLFSRVE PQHKSKIVEF LQSMNEISAM TGDGVNDAPA LKKAEIGIAM
     GSGTAVAKSA AEMVLADDNF SSIVSAVEEG RAIYNNMKQF IRYLISSNIG EVVSIFLTAA
     LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMEKP PRKADEGLIS GWLFFRYMAI
     GFYVGAATVG AAAWWFVFSD EGPKLSYWQL THHLSCLGGG DEFKGVDCKI FSDPHAMTMA
     LSVLVTIEML NAMNSLSENQ SLITMPPWCN LWLIGSMALS FTLHFVILYV DVLSTVFQVT
     PLSAEEWITV MKFSIPVVLL DETLKFVARK IADGESPIYK MHGIVLMWAV FFGLLYAMML
//