Q7PPA5 (ATC1_ANOGA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 74.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type EC=3.6.3.8 Alternative name(s): Calcium pump | ||||
| Gene names |
| ||||
| Organism | Anopheles gambiae (African malaria mosquito) | ||||
| Taxonomic identifier | 7165 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles |
Protein attributes
| Sequence length | 1018 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 calcium. |
| Catalytic activity | ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]. |
| Subcellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein By similarity. |
| Sequence similarities | Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. [View classification] |
Ontologies
| Keywords | |
|---|---|
| Biological process | Calcium transport Ion transport Transport |
| Cellular component | Endoplasmic reticulum Membrane Sarcoplasmic reticulum |
| Coding sequence diversity | Alternative splicing |
| Domain | Transmembrane Transmembrane helix |
| Ligand | ATP-binding Calcium Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | ATP biosynthetic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW sarcoplasmic reticulum membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-transporting ATPase activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform C (identifier: Q7PPA5-1) Also known as: E; D; 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. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform A (identifier: Q7PPA5-2) The sequence of this isoform differs from the canonical sequence as follows: 993-1018: GESYIKNMHGLVLAWAVFFAYIIWGP → VNPDFH | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform B (identifier: Q7PPA5-3) The sequence of this isoform differs from the canonical sequence as follows: 993-1018: GESYIKNMHGLVLAWAVFFAYIIWGP → ANEVIKTWE | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1018 | 1018 | Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type | PRO_0000233305 | |||||
Regions | |||||||||
| Topological domain | 1 – 48 | 48 | Cytoplasmic By similarity UniProtKB P04191 | ||||||
| Transmembrane | 49 – 69 | 21 | Helical; Name=1; By similarity UniProtKB P04191 | ||||||
| Topological domain | 70 – 88 | 19 | Lumenal By similarity UniProtKB P04191 | ||||||
| Transmembrane | 89 – 109 | 21 | Helical; Name=2; By similarity UniProtKB P04191 | ||||||
| Topological domain | 110 – 252 | 143 | Cytoplasmic By similarity UniProtKB P04191 | ||||||
| Transmembrane | 253 – 272 | 20 | Helical; Name=3; By similarity UniProtKB P04191 | ||||||
| Topological domain | 273 – 294 | 22 | Lumenal By similarity UniProtKB P04191 | ||||||
| Transmembrane | 295 – 312 | 18 | Helical; Name=4; By similarity UniProtKB P04191 | ||||||
| Topological domain | 313 – 756 | 444 | Cytoplasmic By similarity UniProtKB P04191 | ||||||
| Transmembrane | 757 – 776 | 20 | Helical; Name=5; By similarity UniProtKB P04191 | ||||||
| Topological domain | 777 – 786 | 10 | Lumenal By similarity UniProtKB P04191 | ||||||
| Transmembrane | 787 – 807 | 21 | Helical; Name=6; By similarity UniProtKB P04191 | ||||||
| Topological domain | 808 – 827 | 20 | Cytoplasmic By similarity UniProtKB P04191 | ||||||
| Transmembrane | 828 – 850 | 23 | Helical; Name=7; By similarity UniProtKB P04191 | ||||||
| Topological domain | 851 – 896 | 46 | Lumenal By similarity UniProtKB P04191 | ||||||
| Transmembrane | 897 – 916 | 20 | Helical; Name=8; By similarity UniProtKB P04191 | ||||||
| Topological domain | 917 – 929 | 13 | Cytoplasmic By similarity UniProtKB P04191 | ||||||
| Transmembrane | 930 – 948 | 19 | Helical; Name=9; By similarity UniProtKB P04191 | ||||||
| Topological domain | 949 – 963 | 15 | Lumenal By similarity UniProtKB P04191 | ||||||
| Transmembrane | 964 – 984 | 21 | Helical; Name=10; By similarity UniProtKB P04191 | ||||||
| Topological domain | 985 – 1018 | 34 | Cytoplasmic By similarity UniProtKB P04191 | ||||||
Sites | |||||||||
| Active site | 350 | 1 | 4-aspartylphosphate intermediate By similarity UniProtKB P04191 | ||||||
| Metal binding | 303 | 1 | Calcium 2; via carbonyl oxygen By similarity UniProtKB P04191 | ||||||
| Metal binding | 304 | 1 | Calcium 2; via carbonyl oxygen By similarity UniProtKB P04191 | ||||||
| Metal binding | 306 | 1 | Calcium 2; via carbonyl oxygen By similarity UniProtKB P04191 | ||||||
| Metal binding | 308 | 1 | Calcium 2 By similarity UniProtKB P04191 | ||||||
| Metal binding | 702 | 1 | Magnesium By similarity UniProtKB P04191 | ||||||
| Metal binding | 706 | 1 | Magnesium By similarity UniProtKB P04191 | ||||||
| Metal binding | 767 | 1 | Calcium 1 By similarity UniProtKB P04191 | ||||||
| Metal binding | 770 | 1 | Calcium 1 By similarity UniProtKB P04191 | ||||||
| Metal binding | 795 | 1 | Calcium 2 By similarity UniProtKB P04191 | ||||||
| Metal binding | 798 | 1 | Calcium 1 By similarity UniProtKB P04191 | ||||||
| Metal binding | 799 | 1 | Calcium 1 By similarity UniProtKB P04191 | ||||||
| Metal binding | 799 | 1 | Calcium 2 By similarity UniProtKB P04191 | ||||||
| Metal binding | 907 | 1 | Calcium 1 By similarity UniProtKB P04191 | ||||||
Natural variations | |||||||||
| Alternative sequence | 993 – 1018 | 26 | GESYI…IIWGP → VNPDFH in isoform A. | VSP_030291 | |||||
| Alternative sequence | 993 – 1018 | 26 | GESYI…IIWGP → ANEVIKTWE in isoform B. | VSP_030292 | |||||
Sequences
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References
| [1] | "The genome sequence of the malaria mosquito Anopheles gambiae." Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. Hoffman S.L.Science 298:129-149(2002) [PubMed: 12364791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PEST. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AAAB01008960 Genomic DNA. Translation: EAA10790.5. AAAB01008960 Genomic DNA. Translation: EDO63821.1. AAAB01008960 Genomic DNA. Translation: EDO63822.1. AAAB01008960 Genomic DNA. Translation: EDO63823.1. AAAB01008960 Genomic DNA. Translation: EDO63824.1. |
| RefSeq | XP_001688815.1. XM_001688763.1. XP_001688816.1. XM_001688764.1. XP_001688817.1. XM_001688765.1. XP_001688818.1. XM_001688766.1. XP_316251.4. XM_316251.4. |
3D structure databases | |
| ProteinModelPortal | Q7PPA5. |
| SMR | Q7PPA5. Positions 1-988. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | AGAP006186-RC; AGAP006186-PC; AGAP006186. AGAP006186-RD; AGAP006186-PD; AGAP006186. AGAP006186-RE; AGAP006186-PE; AGAP006186. |
| GeneID | 1276852. |
| KEGG | aga:AgaP_AGAP006186. |
| VectorBase | AGAP006186. Anopheles gambiae. |
Organism-specific databases | |
| CTD | 1276852. |
Phylogenomic databases | |
| eggNOG | inNOG09096. |
| GeneTree | EMGT00050000001937. |
| HOGENOM | HBG456486. |
| InParanoid | Q7PPA5. |
| OMA | QVKRNLE. |
| OrthoDB | EOG4XD25Z. |
| PhylomeDB | Q7PPA5. |
Family and domain databases | |
| InterPro | IPR023306. ATPase_cation_domN. 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. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR023298. ATPase_P-typ_TM_dom. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. [Graphical view] |
| Gene3D | G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 2 hits. |
| KO | K05853. |
| 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] |
| SUPFAM | SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit. |
| TIGRFAMs | TIGR01116. ATPase-IIA1_Ca. 1 hit. TIGR01494. ATPase_P-type. 3 hits. |
| PROSITE | PS00154. ATPASE_E1_E2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ATC1_ANOGA | ||||||||
| Accession | Primary (citable) accession number: Q7PPA5 Secondary accession number(s): A7UU43, A7UU44, A7UU45 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with