Reviewed,
UniProtKB/Swiss-Prot Q08853 (ATC_PLAFK)
Last modified
February 9, 2010.
Version 65.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Calcium-transporting ATPase EC=3.6.3.8 Alternative name(s): Calcium pump | ||
| Gene names |
| ||
| Organism | Plasmodium falciparum (isolate K1 / Thailand) | ||
| Taxonomic identifier | 5839 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania) |
Protein attributes
| Sequence length | 1228 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium. |
| Catalytic activity | ATP + H2O + Ca2+(Cis) = ADP + phosphate + Ca2+(Trans). |
| Subcellular location | |
| Sequence similarities | Belongs to the cation transport ATPase (P-type) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Calcium transport Ion transport Transport |
| Cellular component | Membrane |
| Domain | Transmembrane |
| Ligand | ATP-binding Calcium Magnesium Nucleotide-binding |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | ATP biosynthetic process Inferred from electronic annotation. Source: InterPro calcium ion transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion bindingInferred from electronic annotation. Source: UniProtKB-KW calcium-transporting ATPase activityInferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1228 | 1228 | Calcium-transporting ATPase | PRO_0000046227 | |||||
Regions | |||||||||
| Topological domain | 1 – 63 | 63 | Cytoplasmic Potential | ||||||
| Transmembrane | 64 – 81 | 18 | Potential | ||||||
| Topological domain | 82 – 92 | 11 | Extracellular Potential | ||||||
| Transmembrane | 93 – 112 | 20 | Potential | ||||||
| Topological domain | 113 – 270 | 158 | Cytoplasmic Potential | ||||||
| Transmembrane | 271 – 291 | 21 | Potential | ||||||
| Topological domain | 292 – 300 | 9 | Extracellular Potential | ||||||
| Transmembrane | 301 – 321 | 21 | Potential | ||||||
| Topological domain | 322 – 974 | 653 | Cytoplasmic Potential | ||||||
| Transmembrane | 975 – 994 | 20 | Potential | ||||||
| Topological domain | 995 – 1000 | 6 | Extracellular Potential | ||||||
| Transmembrane | 1001 – 1021 | 21 | Potential | ||||||
| Topological domain | 1022 – 1042 | 21 | Cytoplasmic Potential | ||||||
| Transmembrane | 1043 – 1067 | 25 | Potential | ||||||
| Topological domain | 1068 – 1118 | 51 | Extracellular Potential | ||||||
| Transmembrane | 1119 – 1140 | 22 | Potential | ||||||
| Topological domain | 1141 – 1151 | 11 | Cytoplasmic Potential | ||||||
| Transmembrane | 1152 – 1172 | 21 | Potential | ||||||
| Topological domain | 1173 – 1185 | 13 | Extracellular Potential | ||||||
| Transmembrane | 1186 – 1206 | 21 | Potential | ||||||
| Topological domain | 1207 – 1228 | 22 | Cytoplasmic Potential | ||||||
| Compositional bias | 457 – 465 | 9 | Poly-Asn | ||||||
| Compositional bias | 661 – 671 | 11 | Poly-Asn | ||||||
Sites | |||||||||
| Active site | 358 | 1 | 4-aspartylphosphate intermediate | ||||||
| Binding site | 716 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Cloning of a Ca(2+)-ATPase gene of Plasmodium falciparum and comparison with vertebrate Ca(2+)-ATPases." Kimura M., Yamaguchi Y., Takada S., Tanabe K. J. Cell Sci. 104:1129-1136(1993) [PubMed: 8314897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X71765 Genomic DNA. Translation: CAA50664.1. | ||||||||||||
| PIR | S37621. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ModBase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR005782. ATPase_P-typ_Ca-transp. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. 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. | ||||||||||||
| SMART | SM00831. Cation_ATPase_N. 1 hit. [Graphical view] | ||||||||||||
| 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 | ATC_PLAFK | ||||||||
| Accession | Primary (citable) accession number: Q08853 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


