AT2B1_MOUSE
ID AT2B1_MOUSE Reviewed; 1220 AA.
AC G5E829;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Plasma membrane calcium-transporting ATPase 1 {ECO:0000305};
DE EC=7.2.2.10 {ECO:0000305|PubMed:24805951};
DE AltName: Full=Plasma membrane calcium ATPase isoform 1 {ECO:0000303|PubMed:12209837};
DE Short=PMCA1 {ECO:0000303|PubMed:12209837};
DE AltName: Full=Plasma membrane calcium pump isoform 1 {ECO:0000305};
GN Name=Atp2b1 {ECO:0000312|MGI:MGI:104653};
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 {ECO:0000312|Ensembl:ENSMUSP00000020107};
RN [1] {ECO:0000312|Ensembl:ENSMUSP00000020107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000020107};
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 [2] {ECO:0000312|EMBL:EDL21639.1}
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12209837; DOI=10.1002/cne.10281;
RA Krizaj D., Demarco S.J., Johnson J., Strehler E.E., Copenhagen D.R.;
RT "Cell-specific expression of plasma membrane calcium ATPase isoforms in
RT retinal neurons.";
RL J. Comp. Neurol. 451:1-21(2002).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15178683; DOI=10.1074/jbc.m404628200;
RA Okunade G.W., Miller M.L., Pyne G.J., Sutliff R.L., O'Connor K.T.,
RA Neumann J.C., Andringa A., Miller D.A., Prasad V., Doetschman T.,
RA Paul R.J., Shull G.E.;
RT "Targeted ablation of plasma membrane Ca2+-ATPase (PMCA) 1 and 4 indicates
RT a major housekeeping function for PMCA1 and a critical role in
RT hyperactivated sperm motility and male fertility for PMCA4.";
RL J. Biol. Chem. 279:33742-33750(2004).
RN [5]
RP FUNCTION.
RX PubMed=16956963; DOI=10.1152/ajpcell.00313.2006;
RA Liu L., Ishida Y., Okunade G., Pyne-Geithman G.J., Shull G.E., Paul R.J.;
RT "Distinct roles of PMCA isoforms in Ca2+ homeostasis of bladder smooth
RT muscle: evidence from PMCA gene-ablated mice.";
RL Am. J. Physiol. 292:C423-C431(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1155 AND THR-1165, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-338; SER-1155;
RP THR-1165; SER-1178 AND SER-1182, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-338; SER-1155;
RP THR-1165 AND SER-1182, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [11]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22311909; DOI=10.1161/hypertensionaha.110.165068;
RA Kobayashi Y., Hirawa N., Tabara Y., Muraoka H., Fujita M., Miyazaki N.,
RA Fujiwara A., Ichikawa Y., Yamamoto Y., Ichihara N., Saka S., Wakui H.,
RA Yoshida S., Yatsu K., Toya Y., Yasuda G., Kohara K., Kita Y., Takei K.,
RA Goshima Y., Ishikawa Y., Ueshima H., Miki T., Umemura S.;
RT "Mice lacking hypertension candidate gene ATP2B1 in vascular smooth muscle
RT cells show significant blood pressure elevation.";
RL Hypertension 59:854-860(2012).
RN [12] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=23266958; DOI=10.1083/jcb.201204067;
RA Kim H.J., Prasad V., Hyung S.W., Lee Z.H., Lee S.W., Bhargava A.,
RA Pearce D., Lee Y., Kim H.H.;
RT "Plasma membrane calcium ATPase regulates bone mass by fine-tuning
RT osteoclast differentiation and survival.";
RL J. Cell Biol. 199:1145-1158(2012).
RN [13]
RP TISSUE SPECIFICITY, INTERACTION WITH EPB41, AND SUBCELLULAR LOCATION.
RX PubMed=23460639; DOI=10.1074/jbc.m112.436659;
RA Liu C., Weng H., Chen L., Yang S., Wang H., Debnath G., Guo X., Wu L.,
RA Mohandas N., An X.;
RT "Impaired intestinal calcium absorption in protein 4.1R-deficient mice due
RT to altered expression of plasma membrane calcium ATPase 1b (PMCA1b).";
RL J. Biol. Chem. 288:11407-11415(2013).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24805951; DOI=10.1097/hjh.0000000000000206;
RA Fujiwara A., Hirawa N., Fujita M., Kobayashi Y., Okuyama Y., Yatsu K.,
RA Katsumata M., Yamamoto Y., Ichihara N., Saka S., Toya Y., Yasuda G.,
RA Goshima Y., Tabara Y., Miki T., Ueshima H., Ishikawa Y., Umemura S.;
RT "Impaired nitric oxide production and increased blood pressure in systemic
RT heterozygous ATP2B1 null mice.";
RL J. Hypertens. 32:1415-1423(2014).
RN [15]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=26392310; DOI=10.1016/j.bbrc.2015.09.087;
RA Ryan Z.C., Craig T.A., Filoteo A.G., Westendorf J.J., Cartwright E.J.,
RA Neyses L., Strehler E.E., Kumar R.;
RT "Deletion of the intestinal plasma membrane calcium pump, isoform 1,
RT Atp2b1, in mice is associated with decreased bone mineral density and
RT impaired responsiveness to 1, 25-dihydroxyvitamin D3.";
RL Biochem. Biophys. Res. Commun. 467:152-156(2015).
RN [16]
RP INTERACTION WITH NPTN, INDUCTION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=28827723; DOI=10.1038/s41598-017-08519-4;
RA Korthals M., Langnaese K., Smalla K.H., Kaehne T., Herrera-Molina R.,
RA Handschuh J., Lehmann A.C., Mamula D., Naumann M., Seidenbecher C.,
RA Zuschratter W., Tedford K., Gundelfinger E.D., Montag D., Fischer K.D.,
RA Thomas U.;
RT "A complex of Neuroplastin and Plasma Membrane Ca2+ ATPase controls T cell
RT activation.";
RL Sci. Rep. 7:8358-8358(2017).
RN [17]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=29950683; DOI=10.1038/s41440-018-0067-8;
RA Ehara Y., Hirawa N., Sumida K., Fujiwara A., Kagimoto M., Ooki-Okuyama Y.,
RA Fujita M., Katsumata M., Kobayashi Y., Saka S., Katou I., Yatsu K.,
RA Umemura S., Tamura K.;
RT "Reduced secretion of parathyroid hormone and hypocalcemia in systemic
RT heterozygous ATP2B1-null hypertensive mice.";
RL Hypertens. Res. 41:699-707(2018).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=30862855; DOI=10.1038/s41598-019-40557-y;
RA Ono Y., Mori Y., Egashira Y., Sumiyama K., Takamori S.;
RT "Expression of plasma membrane calcium ATPases confers Ca2+/H+ exchange in
RT rodent synaptic vesicles.";
RL Sci. Rep. 9:4289-4289(2019).
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium from the cytoplasm to the extracellular space thereby
CC maintaining intracellular calcium homeostasis (PubMed:22311909,
CC PubMed:16956963, PubMed:28827723, PubMed:26392310, PubMed:29950683,
CC PubMed:24805951, PubMed:23266958). Plays a role in blood pressure
CC regulation through regulation of intracellular calcium concentration
CC and nitric oxide production leading to regulation of vascular smooth
CC muscle cells vasoconstriction (PubMed:24805951, PubMed:29950683,
CC PubMed:22311909). Positively regulates bone mineralization through
CC absorption of calcium from the intestine (PubMed:23266958,
CC PubMed:26392310). Plays dual roles in osteoclast differentiation and
CC survival by regulating RANKL-induced calcium oscillations in
CC preosteoclasts and mediating calcium extrusion in mature osteoclasts
CC (PubMed:23266958). Regulates insulin sensitivity through
CC calcium/calmodulin signaling pathway by regulating AKT1 activation and
CC NOS3 activation in endothelial cells (By similarity). May play a role
CC in synaptic transmission by modulating calcium and proton dynamics at
CC the synaptic vesicles. {ECO:0000250|UniProtKB:P20020,
CC ECO:0000269|PubMed:16956963, ECO:0000269|PubMed:22311909,
CC ECO:0000269|PubMed:23266958, ECO:0000269|PubMed:24805951,
CC ECO:0000269|PubMed:26392310, ECO:0000269|PubMed:28827723,
CC ECO:0000269|PubMed:29950683, ECO:0000269|PubMed:30862855}.
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 Evidence={ECO:0000305|PubMed:24805951, ECO:0000305|PubMed:30862855};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000305|PubMed:24805951, ECO:0000305|PubMed:30862855};
CC -!- SUBUNIT: Monomer. Dimer. Oligomer. Calmodulin binding. Interacts with
CC PDZD11. Interacts with SLC35G1 and STIM1. Interacts with YWHAE;
CC interacts with the monomeric and dimeric forms of the YWHAE but prefer
CC the monomer form; this interaction inhibits calcium-transporting ATPase
CC activity (By similarity). Interacts with NPTN; this interaction
CC stabilizes ATP2B1 and increases ATPase activity; this interaction
CC controls T cell calcium homeostasis following T cell activation
CC (PubMed:28827723). Interacts with EPB41; regulates small intestinal
CC calcium absorption through regulation of membrane expression of ATP2B1
CC (PubMed:23460639). {ECO:0000250|UniProtKB:P20020,
CC ECO:0000269|PubMed:23460639, ECO:0000269|PubMed:28827723}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20020};
CC Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000269|PubMed:23460639}. Synapse {ECO:0000269|PubMed:12209837}.
CC Presynaptic cell membrane {ECO:0000269|PubMed:30862855}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000269|PubMed:30862855}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Colocalizes with SV2A in
CC photoreceptor synaptic terminals (PubMed:12209837). Colocalizes with
CC NPTN to the immunological synapse (PubMed:28827723). Colocalizes with
CC EPB41 to the basolateral membrane in enterocyte (PubMed:23460639).
CC Preferentially sorted to recycling synaptic vesicles.
CC {ECO:0000269|PubMed:12209837, ECO:0000269|PubMed:23460639,
CC ECO:0000269|PubMed:28827723, ECO:0000269|PubMed:30862855}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina, with strongest expression
CC in the outer plexiform layer and lower expression levels in the inner
CC nuclear layer and the inner plexiform layer (PubMed:12209837).
CC Specifically expressed in the following retinal cell types:
CC photoreceptor cells, cone bipolar cells and horizontal cells
CC (PubMed:12209837). Expressed in osteoclasts (at protein level)
CC (PubMed:23266958). Expressed at highest levels in brain, intestine,
CC kidney, and stomach, and at lower levels in liver, lung, aorta, portal
CC vein, urinary bladder, diaphragm, seminal vesicles and testes
CC (PubMed:15178683). Expressed in small intestinal epithelium
CC (PubMed:23460639). {ECO:0000269|PubMed:12209837,
CC ECO:0000269|PubMed:15178683, ECO:0000269|PubMed:23266958,
CC ECO:0000269|PubMed:23460639}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in differentiating osteoclasts.
CC {ECO:0000269|PubMed:23266958}.
CC -!- INDUCTION: Up-regulated following T cell activation.
CC {ECO:0000269|PubMed:28827723}.
CC -!- DISRUPTION PHENOTYPE: Complete embryonic lethality (PubMed:15178683).
CC Mice with conditional knockout of ATP2B1 in enterocytes, are born at a
CC lower frequency and are smaller at birth and into adulthood than wild-
CC type. At two months of age, mice have a decreased bone mineral density
CC (PubMed:26392310). Mice with conditional knockout of ATP2B1 in vascular
CC smooth muscle cells (VSMCs) are born at the expected Mendelian ratio
CC and grow normaly but have a higher blood pressure than wild-type under
CC resting conditions (PubMed:22311909). Heterozygous ATP2B1 mice are
CC hypertensive and exhibit hypocalcemia and a higher bone mineral density
CC (PubMed:29950683). {ECO:0000269|PubMed:15178683,
CC ECO:0000269|PubMed:22311909, ECO:0000269|PubMed:26392310,
CC ECO:0000269|PubMed:29950683}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000255|RuleBase:RU361146}.
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DR EMBL; AC153906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC160410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466539; EDL21639.1; -; Genomic_DNA.
DR CCDS; CCDS24145.1; -.
DR RefSeq; NP_080758.1; NM_026482.2.
DR RefSeq; XP_011241851.1; XM_011243549.2.
DR AlphaFoldDB; G5E829; -.
DR SMR; G5E829; -.
DR BioGRID; 212573; 21.
DR CORUM; G5E829; -.
DR IntAct; G5E829; 4.
DR MINT; G5E829; -.
DR STRING; 10090.ENSMUSP00000020107; -.
DR iPTMnet; G5E829; -.
DR PhosphoSitePlus; G5E829; -.
DR SwissPalm; G5E829; -.
DR EPD; G5E829; -.
DR jPOST; G5E829; -.
DR MaxQB; G5E829; -.
DR PaxDb; G5E829; -.
DR PeptideAtlas; G5E829; -.
DR PRIDE; G5E829; -.
DR ProteomicsDB; 277121; -.
DR Antibodypedia; 2168; 135 antibodies from 29 providers.
DR DNASU; 67972; -.
DR Ensembl; ENSMUST00000020107; ENSMUSP00000020107; ENSMUSG00000019943.
DR GeneID; 67972; -.
DR KEGG; mmu:67972; -.
DR UCSC; uc007gxf.2; mouse.
DR CTD; 490; -.
DR MGI; MGI:104653; Atp2b1.
DR VEuPathDB; HostDB:ENSMUSG00000019943; -.
DR eggNOG; KOG0204; Eukaryota.
DR GeneTree; ENSGT00940000158686; -.
DR HOGENOM; CLU_002360_9_0_1; -.
DR InParanoid; G5E829; -.
DR OMA; KTAHVGF; -.
DR OrthoDB; 115892at2759; -.
DR PhylomeDB; G5E829; -.
DR TreeFam; TF300330; -.
DR Reactome; R-MMU-418359; Reduction of cytosolic Ca++ levels.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 67972; 20 hits in 74 CRISPR screens.
DR ChiTaRS; Atp2b1; mouse.
DR PRO; PR:G5E829; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; G5E829; protein.
DR Bgee; ENSMUSG00000019943; Expressed in otolith organ and 229 other tissues.
DR ExpressionAtlas; G5E829; baseline and differential.
DR Genevisible; G5E829; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0032590; C:dendrite membrane; ISO:MGI.
DR GO; GO:0032591; C:dendritic spine membrane; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015085; F:calcium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR GO; GO:1905056; F:P-type calcium transporter activity involved in regulation of presynaptic cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:1901660; P:calcium ion export; ISO:MGI.
DR GO; GO:1990034; P:calcium ion export across plasma membrane; ISO:MGI.
DR GO; GO:0006816; P:calcium ion transport; TAS:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0071386; P:cellular response to corticosterone stimulus; IEA:Ensembl.
DR GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl.
DR GO; GO:0001818; P:negative regulation of cytokine production; IMP:UniProtKB.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:UniProtKB.
DR GO; GO:0003407; P:neural retina development; IEA:Ensembl.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:UniProtKB.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:UniProtKB.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:UniProtKB.
DR GO; GO:0003056; P:regulation of vascular associated smooth muscle contraction; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030320; ATP2B1.
DR InterPro; IPR022141; ATP_Ca_trans_C.
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; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PANTHER; PTHR24093:SF245; PTHR24093:SF245; 1.
DR Pfam; PF12424; ATP_Ca_trans_C; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Calcium; Calcium transport; Calmodulin-binding;
KW Cell membrane; Cell projection; Cytoplasmic vesicle; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Synapse; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT CHAIN 2..1220
FT /note="Plasma membrane calcium-transporting ATPase 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000430669"
FT TOPO_DOM 2..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 127..154
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 176..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 367..386
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 387..418
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..855
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..882
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 883..903
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 904..927
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 928..948
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 949..971
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 972..991
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 992..1005
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1006..1027
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 1028..1039
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1040..1060
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT TOPO_DOM 1061..1220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 297..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1117
FT /note="Calmodulin-binding subdomain A"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT REGION 1118..1220
FT /note="Required for basolateral membrane targeting"
FT /evidence="ECO:0000250|UniProtKB:P11505"
FT REGION 1160..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 475
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT BINDING 797
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q5ZWR1"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1116
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P20020"
FT MOD_RES 1140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11505"
FT MOD_RES 1155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1165
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1220 AA; 134747 MW; 6B3DDAA2DBB001C3 CRC64;
MGDMANNSVA YSGVKNSLKE ANHDGDFGIT LTELRALMEL RSTDALRKIQ ESYGDVYGIC
TKLKTSPNEG LSGNPADLER REAVFGKNFI PPKKPKTFLQ LVWEALQDVT LIILEIAAIV
SLGLSFYQPP EGDNALCGEV SVGEEEGEGE TGWIEGAAIL LSVVCVVLVT AFNDWSKEKQ
FRGLQSRIEQ EQKFTVIRGG QVIQIPVADI TVGDIAQVKY GDLLPADGIL IQGNDLKIDE
SSLTGESDHV KKSLDKDPLL LSGTHVMEGS GRMVVTAVGV NSQTGIIFTL LGAGGEEEEK
KDEKKKEKKN KKQDGAIENR NKAKAQDGAA MEMQPLKSEE GGDGDEKDKK KANLPKKEKS
VLQGKLTKLA VQIGKAGLLM SAITVIILVL YFVIDTFWVQ KRPWLAECTP IYIQYFVKFF
IIGVTVLVVA VPEGLPLAVT ISLAYSVKKM MKDNNLVRHL DACETMGNAT AICSDKTGTL
TMNRMTVVQA YINEKHYKKV PEPEAIPPNI LSYLVTGISV NCAYTSKILP PEKEGGLPRH
VGNKTECALL GFLLDLKRDY QDVRNEIPEE ALYKVYTFNS VRKSMSTVLK NSDGSFRIFS
KGASEIILKK CFKILSANGE AKVFRPRDRD DIVKTVIEPM ASEGLRTICL AFRDFPAGEP
EPEWDNENDV VTGLTCIAVV GIEDPVRPEV PEAIKKCQRA GITVRMVTGD NINTARAIAT
KCGILHPGED FLCLEGKDFN RRIRNEKGEI EQERIDKIWP KLRVLARSSP TDKHTLVKGI
IDSTVSEQRQ VVAVTGDGTN DGPALKKADV GFAMGIAGTD VAKEASDIIL TDDNFTSIVK
AVMWGRNVYD SISKFLQFQL TVNVVAVIVA FTGACITQDS PLKAVQMLWV NLIMDTLASL
ALATEPPTES LLLRKPYGRN KPLISRTMMK NILGHAFYQL VVVFTLLFAG EKFFDIDSGR
NAPLHAPPSE HYTIVFNTFV LMQLFNEINA RKIHGERNVF EGIFNNAIFC TIVLGTFVVQ
IIIVQFGGKP FSCSELSIEQ WLWSIFLGMG TLLWGQLIST IPTSRLKFLK EAGHGTQKEE
IPEEELAEDV EEIDHAEREL RRGQILWFRG LNRIQTQIRV VNAFRSSLYE GLEKPESRSS
IHNFMTHPEF RIEDSEPHIP LIDDTDAEDD APTKRNSSPP PSPNKNNNAV DSGIHLTIEM
NKSATSSSPG SPLHSLETSL
