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UniProtKB/Swiss-Prot entry P04191


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AT2A1_RABIT
Primary accession number P04191
Secondary accession number P11719
Integrated into Swiss-Prot on March 20, 1987
Sequence was last modified on March 20, 1987 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 95)
Name and origin of the protein
Protein name Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
Synonyms SERCA1
EC 3.6.3.8
Calcium pump 1
Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform
SR Ca(2+)-ATPase 1
Endoplasmic reticulum class 1/2 Ca(2+) ATPase
Gene name
Name: ATP2A1
From
Oryctolagus cuniculus (Rabbit) [TaxID: 9986] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SERCA1B).
DOI=10.1016/0092-8674(86)90269-2; PubMed=2936465 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1007/BF01871021; PubMed=2948019 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1021/bi00175a030; PubMed=8117720 [NCBI, ExPASy, EBI, Israel, Japan]
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).
PubMed=3029125 [NCBI, ExPASy, EBI, Israel, Japan]
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]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF ISOFORM SERCA1A.
DOI=10.1038/35015017; PubMed=10864315 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
INTERACTION WITH PHOSPHOLAMBAN.
PubMed=8428955 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
INTERACTION WITH PHOSPHOLAMBAN.
DOI=10.1074/jbc.274.46.32855; PubMed=10551848 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M12898; AAA31165.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M15351; AAA31166.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M15158; AAA31167.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A01075; PWRBFC.
RefSeq NP_001082787.1; -.
UniGene Ocu.1829
3D structure databases
PDB
1FQU; Model; -; A=1-993.[ExPASy / RCSB / EBI]
1IWO; X-ray; 3.10 A; A/B=1-993.[ExPASy / RCSB / EBI]
1KJU; EM; 6.00 A; A=1-993.[ExPASy / RCSB / EBI]
1SU4; X-ray; 2.40 A; A=1-993.[ExPASy / RCSB / EBI]
1T5S; X-ray; 2.60 A; A=1-993.[ExPASy / RCSB / EBI]
1T5T; X-ray; 2.90 A; A=1-993.[ExPASy / RCSB / EBI]
1VFP; X-ray; 2.90 A; A/B=1-993.[ExPASy / RCSB / EBI]
1WPE; X-ray; 2.70 A; A=1-993.[ExPASy / RCSB / EBI]
1WPG; X-ray; 2.30 A; A/B/C/D=1-993.[ExPASy / RCSB / EBI]
1XP5; X-ray; 3.00 A; A=1-993.[ExPASy / RCSB / EBI]
2AGV; X-ray; 2.40 A; A/B=1-993.[ExPASy / RCSB / EBI]
2BY4; X-ray; 3.30 A; A=1-993.[ExPASy / RCSB / EBI]
2C88; X-ray; 3.10 A; A=1-993.[ExPASy / RCSB / EBI]
2C8K; X-ray; 2.80 A; A=1-993.[ExPASy / RCSB / EBI]
2C8L; X-ray; 3.10 A; A=1-993.[ExPASy / RCSB / EBI]
2C9M; X-ray; 3.00 A; A=1-993, B=-.[ExPASy / RCSB / EBI]
2DQS; X-ray; 2.50 A; A=1-993.[ExPASy / RCSB / EBI]
2EAR; X-ray; 3.10 A; A=1-993.[ExPASy / RCSB / EBI]
2EAS; X-ray; 3.40 A; A=1-993.[ExPASy / RCSB / EBI]
2EAT; X-ray; 2.90 A; A=1-993.[ExPASy / RCSB / EBI]
2EAU; X-ray; 2.80 A; A=1-993.[ExPASy / RCSB / EBI]
2O9J; X-ray; 2.65 A; A=1-993.[ExPASy / RCSB / EBI]
2OA0; X-ray; 3.40 A; A=1-993.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FQU; -.
1IWO; -.
1KJU; -.
1SU4; -.
1T5S; -.
1T5T; -.
1VFP; -.
1WPE; -.
1WPG; -.
1XP5; -.
2AGV; -.
2BY4; -.
2C88; -.
2C8K; -.
2C8L; -.
2C9M; -.
2DQS; -.
2EAR; -.
2EAS; -.
2EAT; -.
2EAU; -.
2O9J; -.
2OA0; -.
ModBase P04191.
Protein-protein interaction databases
IntAct P04191; -.
Ontologies
GO
GO:0005509; Molecular function: calcium ion binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005388; Molecular function: calcium-transporting ATPase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from sequence or structural similarity from UniProtKB).
GO:0006816; Biological process: calcium ion transport (inferred from sequence or structural similarity from UniProtKB).
GO:0031448; Biological process: positive regulation of fast-twitch skeletal muscle fiber contraction (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001757; ATPase_P.
IPR006068; ATPase_P_cat_C.
IPR004014; ATPase_P_cat_N.
IPR005782; Calcium_ATPase.
IPR005834; Dehalogen-like_hydro.
IPR008250; E1-E2_ATPase_reg.
IPR000695; H_ATPase.
Graphical view of domain structure.
PANTHER PTHR11939; ATPase_P; 1.
Pfam PF00689; Cation_ATPase_C; 1.
PF00690; Cation_ATPase_N; 1.
PF00122; E1-E2_ATPase; 1.
PF00702; Hydrolase; 1.
Pfam graphical view of domain structure.
PRINTS PR00119; CATATPASE.
PR00120; HATPASE.
TIGRFAMs TIGR01116; ATPase-IIA1_Ca; 1.
TIGR01494; ATPase_P-type; 4.
PROSITE PS00154; ATPASE_E1_E2; 1.
BLOCKS P04191.
ProtoNet P04191.
Genome annotation databases
GeneID 100037716; -.
Phylogenomic databases
HOVERGEN P04191; -.
Other
LinkHub P04191; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Calcium; Calcium transport; Direct protein sequencing; Endoplasmic reticulum; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Sarcoplasmic reticulum; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   1001  1001     Sarcoplasmic/endoplasmic reticulum calcium ATPase 1. PRO_0000046189
TOPO_DOM   1     48  48     Cytoplasmic. 
TRANSMEM   49     69  21     1. 
TOPO_DOM   70     89  20     Lumenal. 
TRANSMEM   90    110  21     2. 
TOPO_DOM   111    253  143     Cytoplasmic. 
TRANSMEM   254    273  20     3. 
TOPO_DOM   274    295  22     Lumenal. 
TRANSMEM   296    313  18     4. 
TOPO_DOM   314    757  444     Cytoplasmic. 
TRANSMEM   758    777  20     5. 
TOPO_DOM   778    787  10     Lumenal. 
TRANSMEM   788    808  21     6. 
TOPO_DOM   809    828  20     Cytoplasmic. 
TRANSMEM   829    851  23     7. 
TOPO_DOM   852    897  46     Lumenal. 
TRANSMEM   898    917  20     8. 
TOPO_DOM   918    930  13     Cytoplasmic. 
TRANSMEM   931    949  19     9. 
TOPO_DOM   950    964  15     Lumenal. 
TRANSMEM   965    985  21     10. 
TOPO_DOM   986   1001  16     Cytoplasmic. 
REGION   370    400  31     Interacts with phospholamban 1. 
REGION   788    808  21     Interacts with phospholamban 2. 
ACT_SITE   351    351        4-aspartylphosphate intermediate. 
METAL   304    304        Calcium 2; via carbonyl oxygen. 
METAL   305    305        Calcium 2; via carbonyl oxygen. 
METAL   307    307        Calcium 2; via carbonyl oxygen. 
METAL   309    309        Calcium 2. 
METAL   703    703        Magnesium (By similarity). 
METAL   707    707        Magnesium (By similarity). 
METAL   768    768        Calcium 1. 
METAL   771    771        Calcium 1. 
METAL   796    796        Calcium 2. 
METAL   799    799        Calcium 1. 
METAL   800    800        Calcium 1. 
METAL   800    800        Calcium 2. 
METAL   908    908        Calcium 1. 
DISULFID   876    888         
VAR_SEQ   994   1001        DPEDERRK -> G (in isoform SERCA1A). VSP_000356
TURN   4      6  3      
HELIX   9     15  7      
TURN   20     22  3      
HELIX   26     36  11      
HELIX   49     53  5      
HELIX   55     78  24      
HELIX   86    117  32      
HELIX   118    122  5      
STRAND   128    133  6      
HELIX   142    144  3      
STRAND   149    153  5      
STRAND   161    168  8      
STRAND   174    176  3      
TURN   178    180  3      
HELIX   201    203  3      
STRAND   213    216  4      
STRAND   219    225  7      
HELIX   227    229  3      
TURN   231    235  5      
STRAND   236    241  6      
HELIX   248    273  26      
HELIX   276    278  3      
HELIX   282    284  3      
HELIX   290    306  17      
HELIX   311    328  18      
HELIX   337    343  7      
STRAND   347    353  7      
TURN   354    356  3      
STRAND   362    373  12      
STRAND   376    384  9      
STRAND   388    391  4      
STRAND   395    397  3      
HELIX   404    406  3      
HELIX   408    419  12      
STRAND   424    428  5      
TURN   429    432  4      
STRAND   433    438  6      
HELIX   440    452  13      
HELIX   464    467  4      
HELIX   470    478  9      
STRAND   479    488  10      
TURN   489    492  4      
STRAND   493    500  8      
STRAND   511    516  6      
HELIX   518    523  6      
STRAND   525    530  6      
STRAND   533    536  4      
HELIX   539    554  16      
STRAND   560    569  10      
HELIX   573    575  3      
HELIX   581    583  3      
HELIX   584    587  4      
STRAND   590    600  11      
HELIX   607    616  10      
STRAND   620    627  8      
HELIX   629    638  10      
STRAND   651    654  4      
HELIX   655    659  5      
HELIX   663    672  10      
STRAND   675    678  4      
HELIX   681    692  12      
TURN   693    695  3      
STRAND   698    702  5      
HELIX   705    707  3      
HELIX   708    713  6      
STRAND   714    720  7      
HELIX   725    729  5      
STRAND   732    737  6      
HELIX   740    781  42      
HELIX   789    799  11      
HELIX   802    807  6      
HELIX   831    856  26      
STRAND   860    863  4      
HELIX   873    875  3      
TURN   876    878  3      
HELIX   880    882  3  &n