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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_RABIT             Reviewed;        1001 AA.
P04191; P11719;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
22-NOV-2017, entry version 172.
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;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SERCA1B).
PubMed=2936465; DOI=10.1016/0092-8674(86)90269-2;
Brandl C.J., Green N.M., Korczak B., McLennan D.H.;
"Two Ca2+ ATPase genes: homologies and mechanistic implications of
deduced amino acid sequences.";
Cell 44:597-607(1986).
[2]
PROTEIN SEQUENCE OF 134-140 AND 490-495.
PubMed=8761469; DOI=10.1042/bj3180179;
Corbalan-Garcia S., Teruel J.A., Gomez-Fernandez J.C.;
"Involvement of an arginyl residue in the nucleotide-binding site of
Ca(2+)-ATPase from sarcoplasmic reticulum as seen by reaction with
phenylglyoxal.";
Biochem. J. 318:179-185(1996).
[3]
PROTEIN SEQUENCE OF 199-212; 335-348 AND 506-519.
PubMed=2948019; DOI=10.1007/BF01871021;
Andersen J.P., Vilsen B., Collins J.H., Jorgensen P.L.;
"Localization of E1-E2 conformational transitions of sarcoplasmic
reticulum Ca-ATPase by tryptic cleavage and hydrophobic labeling.";
J. Membr. Biol. 93:85-92(1986).
[4]
PROTEIN SEQUENCE OF 335-365; 468-476; 493-502; 513-529; 606-615;
630-637 AND 668-671.
PubMed=8218393;
Wawrzynow A., Collins J.H.;
"Chemical modification of the Ca(2+)-ATPase of rabbit skeletal muscle
sarcoplasmic reticulum: identification of sites labeled with aryl
isothiocyanates and thiol-directed conformational probes.";
Biochim. Biophys. Acta 1203:60-70(1993).
[5]
PROTEIN SEQUENCE OF 506-513 AND 584-591.
PubMed=8117720; DOI=10.1021/bi00175a030;
Lacapere J.J., Garin J.;
"Interaction of 4-azido-2-nitrophenyl phosphate, a pseudosubstrate,
with the sarcoplasmic reticulum Ca-ATPase.";
Biochemistry 33:2586-2593(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 973-1001 (ISOFORMS SERCA1A AND SERCA1B),
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=3029125;
Brandl C.J., Deleon S., Martin D.R., McLennan D.H.;
"Adult forms of the Ca2+ATPase of sarcoplasmic reticulum. Expression
in developing skeletal muscle.";
J. Biol. Chem. 262:3768-3774(1987).
[7]
SUBCELLULAR LOCATION.
PubMed=2993904; DOI=10.1038/316696a0;
McLennan D.H., Brandl C.J., Korczak B., Green N.M.;
"Amino-acid sequence of a Ca2+ + Mg2+-dependent ATPase from rabbit
muscle sarcoplasmic reticulum, deduced from its complementary DNA
sequence.";
Nature 316:696-700(1985).
[8]
SUBCELLULAR LOCATION.
PubMed=12585965; DOI=10.1042/BJ20021477;
Newton T., Black J.P., Butler J., Lee A.G., Chad J., East J.M.;
"Sarco/endoplasmic-reticulum calcium ATPase SERCA1 is maintained in
the endoplasmic reticulum by a retrieval signal located between
residues 1 and 211.";
Biochem. J. 371:775-782(2003).
[9]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CALCIUM, AND
ACTIVE SITE.
PubMed=10864315; DOI=10.1038/35015017;
Toyoshima C., Nakasako M., Nomura H., Ogawa H.;
"Crystal structure of the calcium pump of sarcoplasmic reticulum at
2.6 A resolution.";
Nature 405:647-655(2000).
[10]
INTERACTION WITH PHOSPHOLAMBAN, AND ENZYME REGULATION.
PubMed=8428955;
Toyofuku T., Kurzydlowski K., Tada M., McLennan D.H.;
"Identification of regions in the Ca(2+)-ATPase of sarcoplasmic
reticulum that affect functional association with phospholamban.";
J. Biol. Chem. 268:2809-2815(1993).
[11]
INTERACTION WITH PHOSPHOLAMBAN, AND ENZYME REGULATION.
PubMed=10551848; DOI=10.1074/jbc.274.46.32855;
Asahi M., Kimura Y., Kurzydlowski K., Tada M., McLennan D.H.;
"Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase
forms a functional interaction site with phospholamban. Evidence for
physical interactions at other sites.";
J. Biol. Chem. 274:32855-32862(1999).
-!- 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) and myoregulin
(MRLN) (PubMed:10551848, PubMed:8428955). Inhibited by
phospholamban (PLN) (PubMed:10551848, PubMed:8428955). Reversibly
inhibited by phospholamban (PLN) at low calcium concentrations
(PubMed:10551848, PubMed:8428955). Dephosphorylated PLN decreases
the apparent affinity of the ATPase for calcium (PubMed:10551848,
PubMed:8428955). This inhibition is regulated by the
phosphorylation of PLN (PubMed:10551848, PubMed:8428955). Enhanced
by DWORF; DWORF increases activity by displacing sarcolipin (SLN),
phospholamban (PLN) and myoregulin (MRLN) (By similarity).
{ECO:0000250|UniProtKB:Q8R429, ECO:0000269|PubMed:10551848,
ECO:0000269|PubMed:8428955}.
-!- SUBUNIT: Interacts with sarcolipin (SLN) (By similarity).
Interacts with phospholamban (PLN) (PubMed:10551848,
PubMed:8428955). Interacts with myoregulin (MRLN) (By similarity).
Interacts with DWORF (By similarity).
{ECO:0000250|UniProtKB:Q8R429, ECO:0000269|PubMed:10551848,
ECO:0000269|PubMed:8428955}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:12585965}; Multi-pass membrane protein
{ECO:0000255}. Sarcoplasmic reticulum membrane
{ECO:0000269|PubMed:2993904}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=SERCA1B; Synonyms=Neonatal;
IsoId=P04191-1; Sequence=Displayed;
Name=SERCA1A; Synonyms=Adult;
IsoId=P04191-2; Sequence=VSP_000356;
-!- TISSUE SPECIFICITY: Skeletal muscle, fast twitch muscle (type II)
fibers. {ECO:0000269|PubMed:3029125}.
-!- DEVELOPMENTAL STAGE: Isoform SERCA1A and isoform SERCA1B are
predominantly found in adult and neonatal skeletal muscle
respectively. {ECO:0000269|PubMed:3029125}.
-!- INDUCTION: Increased contractile activity leads to a decrease in
SERCA1 expression, while decreased contractile activity leads to
an increase in SERCA1 expression.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIA subfamily. {ECO:0000305}.
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EMBL; M12898; AAA31165.1; -; mRNA.
EMBL; M15351; AAA31166.1; -; mRNA.
EMBL; M15158; AAA31167.1; -; mRNA.
PIR; A01075; PWRBFC.
RefSeq; NP_001082787.1; NM_001089318.1. [P04191-1]
UniGene; Ocu.1829; -.
UniGene; Ocu.6937; -.
PDB; 1FQU; Model; -; A=1-993.
PDB; 1IWO; X-ray; 3.10 A; A/B=1-994.
PDB; 1KJU; EM; 6.00 A; A=1-994.
PDB; 1SU4; X-ray; 2.40 A; A=1-994.
PDB; 1T5S; X-ray; 2.60 A; A=1-993.
PDB; 1T5T; X-ray; 2.90 A; A=1-993.
PDB; 1VFP; X-ray; 2.90 A; A/B=1-994.
PDB; 1WPG; X-ray; 2.30 A; A/B/C/D=1-993.
PDB; 1XP5; X-ray; 3.00 A; A=1-993.
PDB; 2AGV; X-ray; 2.40 A; A/B=1-993.
PDB; 2BY4; X-ray; 3.30 A; A=1-993.
PDB; 2C88; X-ray; 3.10 A; A=1-993.
PDB; 2C8K; X-ray; 2.80 A; A=1-993.
PDB; 2C8L; X-ray; 3.10 A; A=1-993.
PDB; 2C9M; X-ray; 3.00 A; A/B=1-993.
PDB; 2DQS; X-ray; 2.50 A; A=1-993.
PDB; 2EAR; X-ray; 3.10 A; A=1-993.
PDB; 2EAT; X-ray; 2.90 A; A=1-993.
PDB; 2EAU; X-ray; 2.80 A; A=1-993.
PDB; 2O9J; X-ray; 2.65 A; A=1-993.
PDB; 2OA0; X-ray; 3.40 A; A=1-993.
PDB; 2VOY; EM; 18.00 A; B=36-77, C=967-988, D=832-854, E=86-115, G=243-278, H=289-336, K=749-780, L=789-809.
PDB; 2YFY; X-ray; 3.10 A; A=1-993.
PDB; 2ZBD; X-ray; 2.40 A; A=1-993.
PDB; 2ZBE; X-ray; 3.80 A; A/B=1-993.
PDB; 2ZBF; X-ray; 2.40 A; A=1-993.
PDB; 2ZBG; X-ray; 2.55 A; A=1-993.
PDB; 3AR2; X-ray; 2.50 A; A=1-994.
PDB; 3AR3; X-ray; 2.30 A; A=1-994.
PDB; 3AR4; X-ray; 2.15 A; A=1-994.
PDB; 3AR5; X-ray; 2.20 A; A=1-994.
PDB; 3AR6; X-ray; 2.20 A; A=1-994.
PDB; 3AR7; X-ray; 2.15 A; A=1-994.
PDB; 3AR8; X-ray; 2.60 A; A=1-994.
PDB; 3AR9; X-ray; 2.60 A; A=1-994.
PDB; 3B9B; X-ray; 2.65 A; A=1-993.
PDB; 3B9R; X-ray; 3.00 A; A/B=1-993.
PDB; 3BA6; X-ray; 2.80 A; A=1-993.
PDB; 3FGO; X-ray; 2.50 A; A/B=1-994.
PDB; 3FPB; X-ray; 2.55 A; A=1-994.
PDB; 3FPS; X-ray; 3.20 A; A=1-994.
PDB; 3J7T; EM; 3.40 A; A=1-994.
PDB; 3N5K; X-ray; 2.20 A; A/B=1-994.
PDB; 3N8G; X-ray; 2.58 A; A=1-993.
PDB; 3W5A; X-ray; 3.01 A; A/B=1-993.
PDB; 3W5B; X-ray; 3.20 A; A=1-993.
PDB; 3W5C; X-ray; 2.50 A; A=1-993.
PDB; 3W5D; X-ray; 2.45 A; A=1-993.
PDB; 4BEW; X-ray; 2.50 A; A/B=1-994.
PDB; 4H1W; X-ray; 3.10 A; A=1-993.
PDB; 4J2T; X-ray; 3.20 A; A=1-993.
PDB; 4KYT; X-ray; 2.83 A; A=1-993.
PDB; 4NAB; X-ray; 3.50 A; A=1-993.
PDB; 4UU0; X-ray; 2.50 A; A=1-993.
PDB; 4UU1; X-ray; 2.80 A; A=1-993.
PDB; 4XOU; X-ray; 2.80 A; A=1-993.
PDB; 4Y3U; X-ray; 3.51 A; A=1-993.
PDB; 4YCL; X-ray; 3.25 A; A=1-993.
PDB; 4YCM; X-ray; 3.20 A; A=2-993.
PDB; 4YCN; X-ray; 3.50 A; A=2-993.
PDB; 5A3Q; X-ray; 3.05 A; A=1-993.
PDB; 5A3R; X-ray; 3.05 A; A=1-993.
PDB; 5A3S; X-ray; 3.30 A; A/B=1-993.
PDB; 5XA7; X-ray; 3.20 A; A=1-993.
PDB; 5XA8; X-ray; 3.20 A; A=1-993.
PDB; 5XA9; X-ray; 3.20 A; A=1-993.
PDB; 5XAA; X-ray; 3.20 A; A=1-993.
PDB; 5XAB; X-ray; 3.20 A; A=1-993.
PDBsum; 1FQU; -.
PDBsum; 1IWO; -.
PDBsum; 1KJU; -.
PDBsum; 1SU4; -.
PDBsum; 1T5S; -.
PDBsum; 1T5T; -.
PDBsum; 1VFP; -.
PDBsum; 1WPG; -.
PDBsum; 1XP5; -.
PDBsum; 2AGV; -.
PDBsum; 2BY4; -.
PDBsum; 2C88; -.
PDBsum; 2C8K; -.
PDBsum; 2C8L; -.
PDBsum; 2C9M; -.
PDBsum; 2DQS; -.
PDBsum; 2EAR; -.
PDBsum; 2EAT; -.
PDBsum; 2EAU; -.
PDBsum; 2O9J; -.
PDBsum; 2OA0; -.
PDBsum; 2VOY; -.
PDBsum; 2YFY; -.
PDBsum; 2ZBD; -.
PDBsum; 2ZBE; -.
PDBsum; 2ZBF; -.
PDBsum; 2ZBG; -.
PDBsum; 3AR2; -.
PDBsum; 3AR3; -.
PDBsum; 3AR4; -.
PDBsum; 3AR5; -.
PDBsum; 3AR6; -.
PDBsum; 3AR7; -.
PDBsum; 3AR8; -.
PDBsum; 3AR9; -.
PDBsum; 3B9B; -.
PDBsum; 3B9R; -.
PDBsum; 3BA6; -.
PDBsum; 3FGO; -.
PDBsum; 3FPB; -.
PDBsum; 3FPS; -.
PDBsum; 3J7T; -.
PDBsum; 3N5K; -.
PDBsum; 3N8G; -.
PDBsum; 3W5A; -.
PDBsum; 3W5B; -.
PDBsum; 3W5C; -.
PDBsum; 3W5D; -.
PDBsum; 4BEW; -.
PDBsum; 4H1W; -.
PDBsum; 4J2T; -.
PDBsum; 4KYT; -.
PDBsum; 4NAB; -.
PDBsum; 4UU0; -.
PDBsum; 4UU1; -.
PDBsum; 4XOU; -.
PDBsum; 4Y3U; -.
PDBsum; 4YCL; -.
PDBsum; 4YCM; -.
PDBsum; 4YCN; -.
PDBsum; 5A3Q; -.
PDBsum; 5A3R; -.
PDBsum; 5A3S; -.
PDBsum; 5XA7; -.
PDBsum; 5XA8; -.
PDBsum; 5XA9; -.
PDBsum; 5XAA; -.
PDBsum; 5XAB; -.
ProteinModelPortal; P04191; -.
SMR; P04191; -.
IntAct; P04191; 5.
STRING; 9986.ENSOCUP00000002327; -.
BindingDB; P04191; -.
ChEMBL; CHEMBL4693; -.
TCDB; 3.A.3.2.43; the p-type atpase (p-atpase) superfamily.
SwissPalm; P04191; -.
PRIDE; P04191; -.
GeneID; 100037716; -.
KEGG; ocu:100037716; -.
CTD; 487; -.
eggNOG; KOG0202; Eukaryota.
eggNOG; COG0474; LUCA.
HOVERGEN; HBG105648; -.
InParanoid; P04191; -.
KO; K05853; -.
BRENDA; 3.6.3.8; 1749.
SABIO-RK; P04191; -.
EvolutionaryTrace; P04191; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO; GO:0031673; C:H zone; ISS:UniProtKB.
GO; GO:0031674; C:I band; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0005388; F:calcium-transporting ATPase activity; IDA:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0045988; P:negative regulation of striated muscle contraction; ISS:UniProtKB.
GO; GO:0031448; P:positive regulation of fast-twitch skeletal muscle fiber contraction; ISS:UniProtKB.
GO; GO:0006942; P:regulation of striated muscle contraction; ISS:UniProtKB.
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_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
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;
3D-structure; Alternative splicing; ATP-binding; Calcium;
Calcium transport; Complete proteome; Direct protein sequencing;
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_0000046189.
TOPO_DOM 1 48 Cytoplasmic.
TRANSMEM 49 69 Helical; Name=1.
TOPO_DOM 70 89 Lumenal.
TRANSMEM 90 110 Helical; Name=2.
TOPO_DOM 111 253 Cytoplasmic.
TRANSMEM 254 273 Helical; Name=3.
TOPO_DOM 274 295 Lumenal.
TRANSMEM 296 313 Helical; Name=4.
TOPO_DOM 314 757 Cytoplasmic.
TRANSMEM 758 777 Helical; Name=5.
TOPO_DOM 778 787 Lumenal.
TRANSMEM 788 808 Helical; Name=6.
TOPO_DOM 809 828 Cytoplasmic.
TRANSMEM 829 851 Helical; Name=7.
TOPO_DOM 852 897 Lumenal.
TRANSMEM 898 917 Helical; Name=8.
TOPO_DOM 918 930 Cytoplasmic.
TRANSMEM 931 949 Helical; Name=9.
TOPO_DOM 950 964 Lumenal.
TRANSMEM 965 985 Helical; Name=10.
TOPO_DOM 986 1001 Cytoplasmic.
REGION 370 400 Interaction with phospholamban 1.
{ECO:0000269|PubMed:10551848}.
REGION 788 808 Interaction with phospholamban 2.
{ECO:0000269|PubMed:10551848}.
ACT_SITE 351 351 4-aspartylphosphate intermediate.
{ECO:0000269|PubMed:10864315}.
METAL 304 304 Calcium 2; via carbonyl oxygen.
{ECO:0000244|PDB:1SU4,
ECO:0000269|PubMed:10864315}.
METAL 305 305 Calcium 2; via carbonyl oxygen.
{ECO:0000244|PDB:1SU4,
ECO:0000269|PubMed:10864315}.
METAL 307 307 Calcium 2; via carbonyl oxygen.
{ECO:0000244|PDB:1SU4,
ECO:0000269|PubMed:10864315}.
METAL 309 309 Calcium 2. {ECO:0000244|PDB:1SU4,
ECO:0000269|PubMed:10864315}.
METAL 703 703 Magnesium. {ECO:0000250}.
METAL 707 707 Magnesium. {ECO:0000250}.
METAL 768 768 Calcium 1. {ECO:0000244|PDB:1SU4,
ECO:0000269|PubMed:10864315}.
METAL 771 771 Calcium 1. {ECO:0000244|PDB:1SU4,
ECO:0000269|PubMed:10864315}.
METAL 796 796 Calcium 2. {ECO:0000244|PDB:1SU4,
ECO:0000269|PubMed:10864315}.
METAL 799 799 Calcium 1. {ECO:0000244|PDB:1SU4,
ECO:0000269|PubMed:10864315}.
METAL 800 800 Calcium 1. {ECO:0000244|PDB:1SU4,
ECO:0000269|PubMed:10864315}.
METAL 800 800 Calcium 2. {ECO:0000244|PDB:1SU4,
ECO:0000269|PubMed:10864315}.
METAL 908 908 Calcium 1. {ECO:0000244|PDB:1SU4,
ECO:0000269|PubMed:10864315}.
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:10864315}.
VAR_SEQ 994 1001 DPEDERRK -> G (in isoform SERCA1A).
{ECO:0000303|PubMed:3029125}.
/FTId=VSP_000356.
HELIX 4 6 {ECO:0000244|PDB:3AR4}.
HELIX 9 16 {ECO:0000244|PDB:3AR4}.
TURN 20 22 {ECO:0000244|PDB:3AR4}.
HELIX 26 36 {ECO:0000244|PDB:3AR4}.
HELIX 49 54 {ECO:0000244|PDB:3AR4}.
HELIX 55 57 {ECO:0000244|PDB:3AR4}.
HELIX 60 75 {ECO:0000244|PDB:3AR4}.
STRAND 76 78 {ECO:0000244|PDB:2ZBG}.
STRAND 80 82 {ECO:0000244|PDB:3AR7}.
HELIX 83 85 {ECO:0000244|PDB:3AR4}.
STRAND 86 88 {ECO:0000244|PDB:3AR4}.
HELIX 89 111 {ECO:0000244|PDB:3AR4}.
HELIX 115 119 {ECO:0000244|PDB:3AR4}.
HELIX 120 122 {ECO:0000244|PDB:3AR4}.
STRAND 125 131 {ECO:0000244|PDB:3AR4}.
STRAND 132 136 {ECO:0000244|PDB:3J7T}.
STRAND 138 141 {ECO:0000244|PDB:3AR4}.
HELIX 142 144 {ECO:0000244|PDB:3AR4}.
STRAND 150 154 {ECO:0000244|PDB:3AR4}.
STRAND 161 168 {ECO:0000244|PDB:3AR4}.
STRAND 170 172 {ECO:0000244|PDB:2EAU}.
STRAND 173 176 {ECO:0000244|PDB:3AR4}.
HELIX 178 181 {ECO:0000244|PDB:3AR4}.
STRAND 187 189 {ECO:0000244|PDB:3AR4}.
HELIX 201 203 {ECO:0000244|PDB:3AR4}.
STRAND 213 216 {ECO:0000244|PDB:3AR4}.
STRAND 218 225 {ECO:0000244|PDB:3AR4}.
HELIX 227 229 {ECO:0000244|PDB:3AR4}.
HELIX 231 240 {ECO:0000244|PDB:3AR4}.
HELIX 248 273 {ECO:0000244|PDB:3AR4}.
HELIX 274 280 {ECO:0000244|PDB:3AR4}.
STRAND 283 286 {ECO:0000244|PDB:3AR4}.
HELIX 288 306 {ECO:0000244|PDB:3AR4}.
HELIX 311 328 {ECO:0000244|PDB:3AR4}.
STRAND 331 334 {ECO:0000244|PDB:3AR4}.
HELIX 338 343 {ECO:0000244|PDB:3AR4}.
STRAND 347 352 {ECO:0000244|PDB:3AR4}.
TURN 353 355 {ECO:0000244|PDB:3AR4}.
STRAND 362 373 {ECO:0000244|PDB:3AR4}.
STRAND 376 384 {ECO:0000244|PDB:3AR4}.
STRAND 387 391 {ECO:0000244|PDB:3AR4}.
STRAND 395 397 {ECO:0000244|PDB:3AR4}.
STRAND 400 402 {ECO:0000244|PDB:4KYT}.
HELIX 404 406 {ECO:0000244|PDB:3AR4}.
HELIX 408 419 {ECO:0000244|PDB:3AR4}.
STRAND 424 428 {ECO:0000244|PDB:3AR4}.
TURN 429 432 {ECO:0000244|PDB:3AR4}.
STRAND 433 438 {ECO:0000244|PDB:3AR4}.
HELIX 440 452 {ECO:0000244|PDB:3AR4}.
TURN 453 455 {ECO:0000244|PDB:3J7T}.
STRAND 460 462 {ECO:0000244|PDB:1WPG}.
TURN 464 466 {ECO:0000244|PDB:3AR4}.
HELIX 467 469 {ECO:0000244|PDB:3W5C}.
HELIX 470 478 {ECO:0000244|PDB:3AR4}.
STRAND 479 488 {ECO:0000244|PDB:3AR4}.
TURN 489 492 {ECO:0000244|PDB:3AR4}.
STRAND 493 502 {ECO:0000244|PDB:3AR4}.
HELIX 503 508 {ECO:0000244|PDB:1WPG}.
STRAND 511 516 {ECO:0000244|PDB:3AR4}.
HELIX 518 523 {ECO:0000244|PDB:3AR4}.
STRAND 525 530 {ECO:0000244|PDB:3AR4}.
STRAND 533 536 {ECO:0000244|PDB:3AR4}.
HELIX 539 554 {ECO:0000244|PDB:3AR4}.
TURN 555 557 {ECO:0000244|PDB:3N5K}.
STRAND 560 569 {ECO:0000244|PDB:3AR4}.
HELIX 573 575 {ECO:0000244|PDB:3AR4}.
HELIX 581 583 {ECO:0000244|PDB:3AR4}.
HELIX 584 587 {ECO:0000244|PDB:3AR4}.
STRAND 590 600 {ECO:0000244|PDB:3AR4}.
HELIX 607 616 {ECO:0000244|PDB:3AR4}.
STRAND 620 627 {ECO:0000244|PDB:3AR4}.
HELIX 629 638 {ECO:0000244|PDB:3AR4}.
STRAND 640 642 {ECO:0000244|PDB:3W5D}.
STRAND 644 646 {ECO:0000244|PDB:4YCN}.
TURN 649 651 {ECO:0000244|PDB:3AR4}.
STRAND 652 654 {ECO:0000244|PDB:3AR4}.
HELIX 655 659 {ECO:0000244|PDB:3AR4}.
HELIX 663 672 {ECO:0000244|PDB:3AR4}.
STRAND 675 678 {ECO:0000244|PDB:3AR4}.
HELIX 683 692 {ECO:0000244|PDB:3AR4}.
TURN 693 695 {ECO:0000244|PDB:3AR4}.
STRAND 698 702 {ECO:0000244|PDB:3AR4}.
HELIX 705 707 {ECO:0000244|PDB:3AR4}.
HELIX 708 713 {ECO:0000244|PDB:3AR4}.
STRAND 716 720 {ECO:0000244|PDB:3AR4}.
HELIX 725 729 {ECO:0000244|PDB:3AR4}.
STRAND 732 735 {ECO:0000244|PDB:3AR4}.
HELIX 740 780 {ECO:0000244|PDB:3AR4}.
HELIX 789 797 {ECO:0000244|PDB:3AR4}.
TURN 798 800 {ECO:0000244|PDB:3AR4}.
HELIX 801 807 {ECO:0000244|PDB:3AR4}.
HELIX 816 818 {ECO:0000244|PDB:3AR4}.
STRAND 824 826 {ECO:0000244|PDB:2ZBD}.
HELIX 831 855 {ECO:0000244|PDB:3AR4}.
TURN 856 858 {ECO:0000244|PDB:3AR3}.
STRAND 860 862 {ECO:0000244|PDB:3AR4}.
TURN 866 868 {ECO:0000244|PDB:3AR5}.
HELIX 870 872 {ECO:0000244|PDB:3AR4}.
HELIX 873 875 {ECO:0000244|PDB:1SU4}.
STRAND 876 879 {ECO:0000244|PDB:3N5K}.
TURN 880 882 {ECO:0000244|PDB:3N5K}.
STRAND 884 886 {ECO:0000244|PDB:3W5D}.
HELIX 890 892 {ECO:0000244|PDB:3AR4}.
HELIX 894 913 {ECO:0000244|PDB:3AR4}.
STRAND 916 919 {ECO:0000244|PDB:1SU4}.
TURN 922 924 {ECO:0000244|PDB:3AR4}.
HELIX 927 929 {ECO:0000244|PDB:3AR4}.
HELIX 931 949 {ECO:0000244|PDB:3AR4}.
HELIX 952 956 {ECO:0000244|PDB:3AR4}.
HELIX 964 974 {ECO:0000244|PDB:3AR4}.
HELIX 976 990 {ECO:0000244|PDB:3AR4}.
TURN 991 993 {ECO:0000244|PDB:5A3Q}.
SEQUENCE 1001 AA; 110459 MW; 1F0D8C36CF975266 CRC64;
MEAAHSKSTE ECLAYFGVSE TTGLTPDQVK RHLEKYGHNE LPAEEGKSLW ELVIEQFEDL
LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILIA NAIVGVWQER NAENAIEALK
EYEPEMGKVY RADRKSVQRI KARDIVPGDI VEVAVGDKVP ADIRILSIKS TTLRVDQSIL
TGESVSVIKH TEPVPDPRAV NQDKKNMLFS GTNIAAGKAL GIVATTGVST EIGKIRDQMA
ATEQDKTPLQ QKLDEFGEQL SKVISLICVA VWLINIGHFN DPVHGGSWIR GAIYYFKIAV
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
MSVCKMFIID KVDGDFCSLN EFSITGSTYA PEGEVLKNDK PIRSGQFDGL VELATICALC
NDSSLDFNET KGVYEKVGEA TETALTTLVE KMNVFNTEVR NLSKVERANA CNSVIRQLMK
KEFTLEFSRD RKSMSVYCSP AKSSRAAVGN KMFVKGAPEG VIDRCNYVRV GTTRVPMTGP
VKEKILSVIK EWGTGRDTLR CLALATRDTP PKREEMVLDD SSRFMEYETD LTFVGVVGML
DPPRKEVMGS IQLCRDAGIR VIMITGDNKG TAIAICRRIG IFGENEEVAD RAYTGREFDD
LPLAEQREAC RRACCFARVE PSHKSKIVEY LQSYDEITAM TGDGVNDAPA LKKAEIGIAM
GSGTAVAKTA SEMVLADDNF STIVAAVEEG RAIYNNMKQF IRYLISSNVG EVVCIFLTAA
LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMDRP PRSPKEPLIS GWLFFRYMAI
GGYVGAATVG AAAWWFMYAE DGPGVTYHQL THFMQCTEDH PHFEGLDCEI FEAPEPMTMA
LSVLVTIEMC NALNSLSENQ SLMRMPPWVN IWLLGSICLS MSLHFLILYV DPLPMIFKLK
ALDLTQWLMV LKISLPVIGL DEILKFIARN YLEDPEDERR K


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