ID E9Q559_MOUSE Unreviewed; 1026 AA. AC E9Q559; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 02-OCT-2024, entry version 103. DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146}; DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146}; GN Name=Atp2a3 {ECO:0000313|Ensembl:ENSMUSP00000127036.2, GN ECO:0000313|MGI:MGI:1194503}; 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:0000313|Ensembl:ENSMUSP00000127036.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000127036.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000127036.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RG Mouse Genome Sequencing Consortium; 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:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [3] {ECO:0000313|Ensembl:ENSMUSP00000127036.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000127036.2}; RX PubMed=21750661; RA Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N., RA Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D., RA Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L., RA Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J., RA Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P., RA Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G., RA Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.; RT "Modernizing reference genome assemblies."; RL PLoS Biol. 9:e1001091-e1001091(2011). RN [4] {ECO:0000313|Ensembl:ENSMUSP00000127036.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000127036.2}; RG Ensembl; RL Submitted (JUN-2024) to UniProtKB. CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of CC calcium. {ECO:0000256|RuleBase:RU361146}. CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of CC ATP coupled with the transport of calcium. Transports calcium ions from CC the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. CC Contributes to calcium sequestration involved in muscular CC excitation/contraction. {ECO:0000256|ARBA:ARBA00002367}. 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:0000256|ARBA:ARBA00024147}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106; CC Evidence={ECO:0000256|ARBA:ARBA00024147}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004477}. Membrane CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141, CC ECO:0000256|RuleBase:RU361146}. Sarcoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004326}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004326}. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) CC family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675, CC ECO:0000256|RuleBase:RU361146}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|RuleBase:RU361146}. 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 RefSeq; NP_001156809.1; NM_001163337.1. DR AlphaFoldDB; E9Q559; -. DR SMR; E9Q559; -. DR jPOST; E9Q559; -. DR ProteomicsDB; 316039; -. DR Antibodypedia; 1517; 175 antibodies from 29 providers. DR DNASU; 53313; -. DR Ensembl; ENSMUST00000163326.8; ENSMUSP00000127036.2; ENSMUSG00000020788.16. DR GeneID; 53313; -. DR UCSC; uc011xym.1; mouse. DR AGR; MGI:1194503; -. DR CTD; 489; -. DR MGI; MGI:1194503; Atp2a3. DR VEuPathDB; HostDB:ENSMUSG00000020788; -. DR GeneTree; ENSGT00940000155668; -. DR OrthoDB; 203629at2759; -. DR BioGRID-ORCS; 53313; 6 hits in 78 CRISPR screens. DR ChiTaRS; Atp2a3; mouse. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; ENSMUSG00000020788; Expressed in submandibular gland and 180 other cell types or tissues. DR ExpressionAtlas; E9Q559; baseline and differential. DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC. 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; 2. DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1. DR PANTHER; PTHR42861:SF6; SARCOPLASMIC_ENDOPLASMIC RETICULUM CALCIUM ATPASE 3; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146}; KW Calcium {ECO:0000256|RuleBase:RU361146}; KW Calcium transport {ECO:0000256|RuleBase:RU361146}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, KW ECO:0000256|RuleBase:RU361146}; Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU361146}; KW Proteomics identification {ECO:0007829|PeptideAtlas:E9Q559, KW ECO:0007829|ProteomicsDB:E9Q559}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU361146}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}. FT TRANSMEM 60..78 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT TRANSMEM 84..107 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT TRANSMEM 260..280 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT TRANSMEM 292..321 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT TRANSMEM 760..781 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT TRANSMEM 833..857 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT TRANSMEM 932..957 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361146" FT DOMAIN 3..77 FT /note="Cation-transporting P-type ATPase N-terminal" FT /evidence="ECO:0000259|SMART:SM00831" FT REGION 1007..1026 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1026 AA; 112504 MW; E8EC0928C4E8F278 CRC64; MEEAHLLSAA DVLRRFSVTA EGGLSLEQVT DARERYGPNE LPTEEGKSLW ELVVEQFEDL LVRILLLAAL VSFVLAWFEE GEETTTAFVE PLVIMLILVA NAIVGVWQER NAESAIEALK EYEPEMGKVI RSDRKGVQRI RARDIVPGDI VEVAVGDKVP ADLRLIEIKS TTLRVDQSIL TGESVSVTKH TDAIPDPRAV NQDKKNMLFS GTNIASGKAL GVAVATGLQT ELGKIRSQMA AVEPERTPLQ RKLDEFGRQL SHAISVICVA VWVINIGHFA DPAHGGSWLR GAVYYFKIAV ALAVAAIPEG LPAVITTCLA LGTRRMARKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ MSVCRMFVVA EAEAGTCRLH EFTISGTTYT PEGEVRQGEQ PVRCGQFDGL VELATICALC NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTDLK GLSRVERAGA CNSVIKQLMR KEFTLEFSRD RKSMSVYCTP TRADPKVQGS KMFVKGAPES VIERCSSVRV GSRTAPLSTT SREHILAKIR DWGSGSDTLR CLALATRDTP PRKEDMHLDD CSRFVQYETD LTFVGCVGML DPPRPEVAAC ITRCSRAGIR VVMITGDNKG TAVAICRRLG IFGDTEDVLG KAYTGREFDD LSPEQQRQAC RTARCFARVE PAHKSRIVEN LQSFNEITAM TGDGVNDAPA LKKAEIGIAM GSGTAVAKSA AEMVLSDDNF ASIVAAVEEG RAIYNNMKQF IRYLISSNVG EVVCIFLTAI LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMEKP PRNPREALIS GWLFFRYLAI GVYVGLATVA AATWWFLYDT EGPQVTFYQL RNFLKCSEDN PLFAGIDCKV FESRFPTTMA LSVLVTIEMC NALNSVSENQ SLLRMPPWLN PWLLGAVVMS MALHFLILLV PPLPLIFQVT PLSGRQWGVV LQMSLPVILL DEALKYLSRN HMDGVLGTFM QARSRQLPTT SRTPYHTGLA SWKKRT //