Reviewed,
UniProtKB/Swiss-Prot P20647 (AT2A2_RABIT)
Last modified
October 13, 2009.
Version 98.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 Short name=SERCA2 EC=3.6.3.8 Alternative name(s): Calcium pump 2 Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform SR Ca(2+)-ATPase 2 Endoplasmic reticulum class 1/2 Ca(2+) ATPase | ||
| Gene names |
| ||
| Organism | Oryctolagus cuniculus (Rabbit) | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 1042 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform SERCA2A is involved in the regulation of the contraction/relaxation cycle. |
| Catalytic activity | ATP + H2O + Ca2+(Cis) = ADP + phosphate + Ca2+(Trans). |
| Enzyme regulation | Reversibly inhibited by phospholamban (PLN) at low calcium concentrations. Dephosphorylated PLN decreases the apparent affinity of the ATPase for calcium. This inhibition is regulated by the phosphorylation of PLN. |
| Subunit structure | Associated with phospholamban (PLN). Isoform SERCA2B interacts with TRAM2 (via C-terminus) By similarity. |
| Subcellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein. |
| Tissue specificity | Isoform SERCA2A is highly expressed in heart and slow twitch skeletal muscle. Isoform SERCA2B is widely expressed. |
| Post-translational modification | Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity By similarity. |
| Sequence similarities | Belongs to the cation transport ATPase (P-type) family. Type IIA subfamily. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform SERCA2B (identifier: P20647-1) Also known as: ATP2A2B; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform SERCA2A (identifier: P20647-2) Also known as: ATP2A2A; The sequence of this isoform differs from the canonical sequence as follows: 994-1042: GKECVQPAPQSCSLWACTEGVSWPFVLLIVPLVMWVYSTDTNFSDLLWS → AILE |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1042 | 1042 | Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 | PRO_0000046199 | |||||
Regions | |||||||||
| Topological domain | 1 – 48 | 48 | Cytoplasmic By similarity | ||||||
| Transmembrane | 49 – 69 | 21 | 1 By similarity | ||||||
| Topological domain | 70 – 89 | 20 | Lumenal By similarity | ||||||
| Transmembrane | 90 – 110 | 21 | 2 By similarity | ||||||
| Topological domain | 111 – 253 | 143 | Cytoplasmic By similarity | ||||||
| Transmembrane | 254 – 273 | 20 | 3 By similarity | ||||||
| Topological domain | 274 – 295 | 22 | Lumenal By similarity | ||||||
| Transmembrane | 296 – 313 | 18 | 4 By similarity | ||||||
| Topological domain | 314 – 756 | 443 | Cytoplasmic By similarity | ||||||
| Transmembrane | 757 – 776 | 20 | 5 By similarity | ||||||
| Topological domain | 777 – 786 | 10 | Lumenal By similarity | ||||||
| Transmembrane | 787 – 807 | 21 | 6 By similarity | ||||||
| Topological domain | 808 – 827 | 20 | Cytoplasmic By similarity | ||||||
| Transmembrane | 828 – 850 | 23 | 7 By similarity | ||||||
| Topological domain | 851 – 896 | 46 | Lumenal By similarity | ||||||
| Transmembrane | 897 – 916 | 20 | 8 By similarity | ||||||
| Topological domain | 917 – 929 | 13 | Cytoplasmic By similarity | ||||||
| Transmembrane | 930 – 948 | 19 | 9 By similarity | ||||||
| Topological domain | 949 – 963 | 15 | Lumenal By similarity | ||||||
| Transmembrane | 964 – 984 | 21 | 10 By similarity | ||||||
| Topological domain | 985 – 1042 | 58 | Cytoplasmic By similarity | ||||||
| Region | 370 – 400 | 31 | Interacts with phospholamban 1 By similarity | ||||||
| Region | 787 – 807 | 21 | Interacts with phospholamban 2 By similarity | ||||||
Sites | |||||||||
| Active site | 351 | 1 | 4-aspartylphosphate intermediate By similarity | ||||||
| Metal binding | 304 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 305 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 307 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 309 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 702 | 1 | Magnesium By similarity | ||||||
| Metal binding | 706 | 1 | Magnesium By similarity | ||||||
| Metal binding | 767 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 770 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 795 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 798 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 799 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 799 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 907 | 1 | Calcium 1 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 294 | 1 | Nitrated tyrosine | ||||||
| Modified residue | 295 | 1 | Nitrated tyrosine | ||||||
| Modified residue | 464 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 537 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 663 | 1 | Phosphoserine By similarity | ||||||
| Cross-link | 143 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||
Natural variations | |||||||||
| Alternative sequence | 994 – 1042 | 49 | GKECV…DLLWS → AILE in isoform SERCA2A. | VSP_000361 | |||||
Experimental info | |||||||||
| Sequence conflict | 578 | 1 | K → E in AAA31150. Ref.1 | ||||||
Sequences
| ||||||||||||||||||||||||
References
| [1] | "Molecular cloning of the mammalian smooth muscle sarco(endo)plasmic reticulum Ca2+-ATPase." Lytton J., Zarain-Herzberg A., Periasamy M., McLennan D.H. J. Biol. Chem. 264:7059-7065(1989) [PubMed: 2523389] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SERCA2B). Tissue: Smooth muscle. |
| [2] | "Cloning of internal Ca pump from rabbit stomach smooth muscle." Khan I., Grover A.K. Nucleic Acids Res. 18:4026-4026(1990) [PubMed: 2165260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SERCA2B). Tissue: Smooth muscle. |
| [3] | "Amino-acid sequence of a Ca2+ + Mg2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence." McLennan D.H., Brandl C.J., Korczak B., Green N.M. Nature 316:696-700(1985) [PubMed: 2993904] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SERCA2A). |
Cross-references
Sequence databases | |
|---|---|
| J04703 mRNA. Translation: AAA31150.1. X52496 mRNA. Translation: CAA36737.1. X02814 mRNA. Translation: CAA26583.1. | |
| PIR | PWRBSC. A01076. A33881. PWRBMC. S10335. |
| RefSeq | NP_001082789.1. NP_001082790.1. |
| UniGene | Ocu.3251 Ocu.6938 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EUL based on UniProtKB P04191. |
| SMR | P20647. Positions 1-992. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P20647. |
Genome annotation databases | |
| GeneID | 100037721. 100038308. |
Organism-specific databases | |
| CTD | 100038308. |
Phylogenomic databases | |
| HOVERGEN | P20647. |
Enzyme and pathway databases | |
| BRENDA | 3.6.3.8. 255. |
Family and domain databases | |
| InterPro | IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR005782. ATPase_P-typ_Ca-transp. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR000695. ATPase_P-typ_H-transp. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR005834. Dehalogen-like_hydro. [Graphical view] |
| PANTHER | PTHR11939. ATPase_P. 1 hit. |
| Pfam | PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view] |
| PRINTS | PR00119. CATATPASE. PR00120. HATPASE. |
| TIGRFAMs | TIGR01116. ATPase-IIA1_Ca. 1 hit. TIGR01494. ATPase_P-type. 4 hits. |
| PROSITE | PS00154. ATPASE_E1_E2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AT2A2_RABIT | ||||||||
| Accession | Primary (citable) accession number: P20647 Secondary accession number(s): P04192 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


