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Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (SERCA1) (SR Ca(2 )-ATPase 1) (EC 3.6.3.8) (Calcium pump 1) (Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2 ) ATPase)

 AT2A1_HUMAN             Reviewed;        1001 AA.
O14983; A8K5J9; B3KY17; O14984;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 180.
RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 1;
Short=SERCA1;
Short=SR Ca(2+)-ATPase 1;
EC=3.6.3.8;
AltName: Full=Calcium pump 1;
AltName: Full=Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform;
AltName: Full=Endoplasmic reticulum class 1/2 Ca(2+) ATPase;
Name=ATP2A1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS SERCA1A AND
SERCA1B), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
TISSUE=Skeletal muscle;
PubMed=8825625; DOI=10.1006/geno.1995.1259;
Zhang Y., Fujii J., Phillips M.S., Chen H.-S., Karpati G., Yee W.-C.,
Schrank B., Cornblath D.R., Boylan K.B., Maclennan D.H.;
"Characterization of cDNA and genomic DNA encoding SERCA1, the Ca(2+)-
ATPase of human fast-twitch skeletal muscle sarcoplasmic reticulum,
and its elimination as a candidate gene for Brody disease.";
Genomics 30:415-424(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SERCA1A AND 3).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
TISSUE=Thymus;
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
DISULFIDE BOND.
PubMed=11438520; DOI=10.1074/jbc.M101229200;
Daiho T., Yamasaki K., Saino T., Kamidochi M., Satoh K., Iizuka H.,
Suzuki H.;
"Mutations of either or both Cys876 and Cys888 residues of
sarcoplasmic reticulum Ca2+-ATPase result in a complete loss of Ca2+
transport activity without a loss of Ca2+-dependent ATPase activity.
Role of the Cys876-Cys888 disulfide bond.";
J. Biol. Chem. 276:32771-32778(2001).
[5]
VARIANT BRM LEU-789.
PubMed=10914677; DOI=10.1007/s004390000297;
Odermatt A., Barton K., Khanna V.K., Mathieu J., Escolar D.,
Kuntzer T., Karpati G., MacLennan D.H.;
"The mutation of Pro(789) to Leu reduces the activity of the fast-
twitch skeletal muscle sarco(endo)plasmic reticulum Ca(2+) ATPase
(SERCA1) and is associated with Brody disease.";
Hum. Genet. 106:482-491(2000).
-!- FUNCTION: Key regulator of striated muscle performance by acting
as the major Ca(2+) ATPase responsible for the reuptake of
cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the
hydrolysis of ATP coupled with the translocation of calcium from
the cytosol to the sarcoplasmic reticulum lumen. Contributes to
calcium sequestration involved in muscular excitation/contraction.
{ECO:0000250|UniProtKB:Q8R429}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Ca(2+)(Side 1) = ADP + phosphate
+ Ca(2+)(Side 2).
-!- ENZYME REGULATION: Inhibited by sarcolipin (SLN), phospholamban
(PLN) and myoregulin (MRLN) (By similarity). Reversibly inhibited
by phospholamban (PLN) at low calcium concentrations (By
similarity). Dephosphorylated PLN decreases the apparent affinity
of the ATPase for calcium. This inhibition is regulated by the
phosphorylation of PLN (By similarity). Enhanced by DWORF; DWORF
increases activity by displacing sarcolipin (SLN), phospholamban
(PLN) and myoregulin (MRLN) (By similarity).
{ECO:0000250|UniProtKB:P04191, ECO:0000250|UniProtKB:Q8R429}.
-!- SUBUNIT: Interacts with sarcolipin (SLN) (By similarity).
Interacts with phospholamban (PLN) (By similarity). Interacts with
myoregulin (MRLN). Interacts with DWORF (By similarity).
{ECO:0000250|UniProtKB:Q8R429}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein
{ECO:0000255}. Sarcoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=SERCA1B; Synonyms=ATP2A1B, Neonatal;
IsoId=O14983-1; Sequence=Displayed;
Name=SERCA1A; Synonyms=ATP2A1A, Adult;
IsoId=O14983-2; Sequence=VSP_000355;
Name=3;
IsoId=O14983-3; Sequence=VSP_054770, VSP_000355;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Skeletal muscle, fast twitch muscle (type II)
fibers. {ECO:0000269|PubMed:8825625}.
-!- DEVELOPMENTAL STAGE: Isoform SERCA1A accounts for more than 99% of
SERCA1 isoforms expressed in adult skeletal muscle, while isoform
SERCA1B predominates in neo-natal skeletal muscle.
{ECO:0000269|PubMed:8825625}.
-!- INDUCTION: Increased contractile activity leads to a decrease in
SERCA1 expression, while decreased contractile activity leads to
an increase in SERCA1 expression. {ECO:0000269|PubMed:8825625}.
-!- DISEASE: Brody myopathy (BRM) [MIM:601003]: A disorder of muscle
function that is characterized by painless muscle cramping and
exercise-induced impairment of muscle relaxation.
{ECO:0000269|PubMed:10914677}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIA subfamily. {ECO:0000305}.
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EMBL; U96781; AAB53113.1; -; Genomic_DNA.
EMBL; U96773; AAB53113.1; JOINED; Genomic_DNA.
EMBL; U96774; AAB53113.1; JOINED; Genomic_DNA.
EMBL; U96775; AAB53113.1; JOINED; Genomic_DNA.
EMBL; U96776; AAB53113.1; JOINED; Genomic_DNA.
EMBL; U96777; AAB53113.1; JOINED; Genomic_DNA.
EMBL; U96778; AAB53113.1; JOINED; Genomic_DNA.
EMBL; U96779; AAB53113.1; JOINED; Genomic_DNA.
EMBL; U96780; AAB53113.1; JOINED; Genomic_DNA.
EMBL; U96781; AAB53112.1; -; Genomic_DNA.
EMBL; U96773; AAB53112.1; JOINED; Genomic_DNA.
EMBL; U96774; AAB53112.1; JOINED; Genomic_DNA.
EMBL; U96775; AAB53112.1; JOINED; Genomic_DNA.
EMBL; U96776; AAB53112.1; JOINED; Genomic_DNA.
EMBL; U96777; AAB53112.1; JOINED; Genomic_DNA.
EMBL; U96778; AAB53112.1; JOINED; Genomic_DNA.
EMBL; U96779; AAB53112.1; JOINED; Genomic_DNA.
EMBL; U96780; AAB53112.1; JOINED; Genomic_DNA.
EMBL; AK128456; BAG54679.1; -; mRNA.
EMBL; AK291314; BAF84003.1; -; mRNA.
EMBL; AC109460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC133550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS10643.1; -. [O14983-1]
CCDS; CCDS42139.1; -. [O14983-2]
CCDS; CCDS66997.1; -. [O14983-3]
RefSeq; NP_001273004.1; NM_001286075.1. [O14983-3]
RefSeq; NP_004311.1; NM_004320.4. [O14983-2]
RefSeq; NP_775293.1; NM_173201.3. [O14983-1]
UniGene; Hs.657344; -.
ProteinModelPortal; O14983; -.
SMR; O14983; -.
BioGrid; 106977; 21.
CORUM; O14983; -.
IntAct; O14983; 5.
MINT; MINT-1158140; -.
STRING; 9606.ENSP00000349595; -.
BindingDB; O14983; -.
ChEMBL; CHEMBL3136; -.
DrugBank; DB04444; Tetrafluoroaluminate Ion.
GuidetoPHARMACOLOGY; 840; -.
iPTMnet; O14983; -.
PhosphoSitePlus; O14983; -.
SwissPalm; O14983; -.
BioMuta; ATP2A1; -.
EPD; O14983; -.
MaxQB; O14983; -.
PaxDb; O14983; -.
PeptideAtlas; O14983; -.
PRIDE; O14983; -.
DNASU; 487; -.
Ensembl; ENST00000357084; ENSP00000349595; ENSG00000196296. [O14983-1]
Ensembl; ENST00000395503; ENSP00000378879; ENSG00000196296. [O14983-2]
Ensembl; ENST00000536376; ENSP00000443101; ENSG00000196296. [O14983-3]
GeneID; 487; -.
KEGG; hsa:487; -.
UCSC; uc002drn.1; human. [O14983-1]
CTD; 487; -.
DisGeNET; 487; -.
EuPathDB; HostDB:ENSG00000196296.13; -.
GeneCards; ATP2A1; -.
HGNC; HGNC:811; ATP2A1.
HPA; CAB002310; -.
HPA; CAB032706; -.
MalaCards; ATP2A1; -.
MIM; 108730; gene.
MIM; 601003; phenotype.
neXtProt; NX_O14983; -.
OpenTargets; ENSG00000196296; -.
Orphanet; 53347; Brody myopathy.
PharmGKB; PA25105; -.
eggNOG; KOG0202; Eukaryota.
eggNOG; COG0474; LUCA.
GeneTree; ENSGT00890000139334; -.
HOGENOM; HOG000265621; -.
HOVERGEN; HBG105648; -.
InParanoid; O14983; -.
KO; K05853; -.
OMA; TTRVPMT; -.
OrthoDB; EOG091G01LE; -.
PhylomeDB; O14983; -.
TreeFam; TF300651; -.
Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
Reactome; R-HSA-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
SIGNOR; O14983; -.
GeneWiki; ATP2A1; -.
GenomeRNAi; 487; -.
PRO; PR:O14983; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000196296; -.
CleanEx; HS_ATP2A1; -.
ExpressionAtlas; O14983; baseline and differential.
Genevisible; O14983; HS.
GO; GO:0034704; C:calcium channel complex; IC:BHF-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
GO; GO:0031673; C:H zone; IDA:UniProtKB.
GO; GO:0031674; C:I band; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0031095; C:platelet dense tubular network membrane; TAS:Reactome.
GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IMP:UniProtKB.
GO; GO:0005388; F:calcium-transporting ATPase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0008637; P:apoptotic mitochondrial changes; IMP:BHF-UCL.
GO; GO:0070509; P:calcium ion import; IMP:BHF-UCL.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:BHF-UCL.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0051659; P:maintenance of mitochondrion location; IMP:BHF-UCL.
GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; IMP:BHF-UCL.
GO; GO:0045988; P:negative regulation of striated muscle contraction; IMP:UniProtKB.
GO; GO:0032470; P:positive regulation of endoplasmic reticulum calcium ion concentration; IMP:BHF-UCL.
GO; GO:0031448; P:positive regulation of fast-twitch skeletal muscle fiber contraction; IDA:UniProtKB.
GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IMP:BHF-UCL.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0006942; P:regulation of striated muscle contraction; IMP:UniProtKB.
GO; GO:0090076; P:relaxation of skeletal muscle; IDA:BHF-UCL.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:BHF-UCL.
Gene3D; 3.40.1110.10; -; 2.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
InterPro; IPR023299; ATPase_P-typ_cyto_domN.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR005782; P-type_ATPase_IIA.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00689; Cation_ATPase_C; 1.
Pfam; PF00690; Cation_ATPase_N; 1.
PRINTS; PR00120; HATPASE.
SMART; SM00831; Cation_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01116; ATPase-IIA1_Ca; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Calcium; Calcium transport;
Complete proteome; Disease mutation; Disulfide bond;
Endoplasmic reticulum; Hydrolase; Ion transport; Magnesium; Membrane;
Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
Sarcoplasmic reticulum; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1001 Sarcoplasmic/endoplasmic reticulum
calcium ATPase 1.
/FTId=PRO_0000046187.
TOPO_DOM 1 48 Cytoplasmic. {ECO:0000250}.
TRANSMEM 49 69 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 70 89 Lumenal. {ECO:0000250}.
TRANSMEM 90 110 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 111 253 Cytoplasmic. {ECO:0000250}.
TRANSMEM 254 273 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 274 295 Lumenal. {ECO:0000250}.
TRANSMEM 296 313 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 314 757 Cytoplasmic. {ECO:0000250}.
TRANSMEM 758 777 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 778 787 Lumenal. {ECO:0000250}.
TRANSMEM 788 808 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 809 828 Cytoplasmic. {ECO:0000250}.
TRANSMEM 829 851 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 852 897 Lumenal. {ECO:0000250}.
TRANSMEM 898 917 Helical; Name=8. {ECO:0000250}.
TOPO_DOM 918 930 Cytoplasmic. {ECO:0000250}.
TRANSMEM 931 949 Helical; Name=9. {ECO:0000250}.
TOPO_DOM 950 964 Lumenal. {ECO:0000250}.
TRANSMEM 965 985 Helical; Name=10. {ECO:0000250}.
TOPO_DOM 986 1001 Cytoplasmic. {ECO:0000250}.
REGION 370 400 Interaction with phospholamban 1.
{ECO:0000250|UniProtKB:P04191}.
REGION 788 808 Interaction with phospholamban 2.
{ECO:0000250|UniProtKB:P04191}.
ACT_SITE 351 351 4-aspartylphosphate intermediate.
{ECO:0000250|UniProtKB:P04191}.
METAL 304 304 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P04191}.
METAL 305 305 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P04191}.
METAL 307 307 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P04191}.
METAL 309 309 Calcium 2.
{ECO:0000250|UniProtKB:P04191}.
METAL 703 703 Magnesium. {ECO:0000250}.
METAL 707 707 Magnesium. {ECO:0000250}.
METAL 768 768 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 771 771 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 796 796 Calcium 2.
{ECO:0000250|UniProtKB:P04191}.
METAL 799 799 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 800 800 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 800 800 Calcium 2.
{ECO:0000250|UniProtKB:P04191}.
METAL 908 908 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
MOD_RES 441 441 Phosphothreonine.
{ECO:0000250|UniProtKB:Q64578}.
MOD_RES 569 569 Phosphothreonine.
{ECO:0000250|UniProtKB:Q64578}.
MOD_RES 581 581 Phosphoserine.
{ECO:0000250|UniProtKB:Q64578}.
DISULFID 876 888 {ECO:0000269|PubMed:11438520}.
VAR_SEQ 1 125 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054770.
VAR_SEQ 994 1001 DPEDERRK -> G (in isoform SERCA1A and
isoform 3). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:8825625}.
/FTId=VSP_000355.
VARIANT 789 789 P -> L (in BRM; almost complete loss of
Ca(2+) transport activity because of
reduced Ca(2+) affinity;
dbSNP:rs121918115).
{ECO:0000269|PubMed:10914677}.
/FTId=VAR_015588.
SEQUENCE 1001 AA; 110252 MW; C8F33809B56FDDEE CRC64;
MEAAHAKTTE ECLAYFGVSE TTGLTPDQVK RNLEKYGLNE LPAEEGKTLW ELVIEQFEDL
LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILIA NAIVGVWQER NAENAIEALK
EYEPEMGKVY RADRKSVQRI KARDIVPGDI VEVAVGDKVP ADIRILAIKS TTLRVDQSIL
TGESVSVIKH TEPVPDPRAV NQDKKNMLFS GTNIAAGKAL GIVATTGVGT EIGKIRDQMA
ATEQDKTPLQ QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWFR GAIYYFKIAV
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
MSVCKMFIID KVDGDICLLN EFSITGSTYA PEGEVLKNDK PVRPGQYDGL VELATICALC
NDSSLDFNEA KGVYEKVGEA TETALTTLVE KMNVFNTDVR SLSKVERANA CNSVIRQLMK
KEFTLEFSRD RKSMSVYCSP AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPLTGP
VKEKIMAVIK EWGTGRDTLR CLALATRDTP PKREEMVLDD SARFLEYETD LTFVGVVGML
DPPRKEVTGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFGENEEVAD RAYTGREFDD
LPLAEQREAC RRACCFARVE PSHKSKIVEY LQSYDEITAM TGDGVNDAPA LKKAEIGIAM
GSGTAVAKTA SEMVLADDNF STIVAAVEEG RAIYNNMKQF IRYLISSNVG EVVCIFLTAA
LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMDRP PRSPKEPLIS GWLFFRYMAI
GGYVGAATVG AAAWWFLYAE DGPHVNYSQL THFMQCTEDN THFEGIDCEV FEAPEPMTMA
LSVLVTIEMC NALNSLSENQ SLLRMPPWVN IWLLGSICLS MSLHFLILYV DPLPMIFKLR
ALDLTQWLMV LKISLPVIGL DEILKFVARN YLEDPEDERR K


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