Reviewed,
UniProtKB/Swiss-Prot P00818 (ACYP2_HORSE)
Last modified
November 25, 2008.
Version 63.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Acylphosphatase-2 EC=3.6.1.7 Alternative name(s): Acylphosphate phosphohydrolase 2 Acylphosphatase, muscle type isozyme | ||||
| Gene names |
| ||||
| Organism | Equus caballus (Horse) | ||||
| Taxonomic identifier | 9796 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus |
Protein attributes
| Sequence length | 99 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Its physiological role is not yet clear. |
| Catalytic activity | An acylphosphate + H(2)O = a carboxylate + phosphate. |
| Sequence similarities | Belongs to the acylphosphatase family. Contains 1 acylphosphatase-like domain. |
Ontologies
Keywords | |
|---|---|
| Molecular function | Hydrolase |
| PTM | Acetylation Glutathionylation |
| Technical term | 3D-structure Direct protein sequencing |
Gene Ontology (GO) | |
| Molecular function | acylphosphatase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||||||||||||||||||
| Chain | 2 – 99 | 98 | Acylphosphatase-2 | PRO_0000158541 | |||||||||||||||||||||
Regions | |||||||||||||||||||||||||
| Domain | 9 – 99 | 91 | Acylphosphatase-like | ||||||||||||||||||||||
Sites | |||||||||||||||||||||||||
| Active site | 24 | 1 | Potential | ||||||||||||||||||||||
| Active site | 42 | 1 | Potential | ||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylserine | ||||||||||||||||||||||
| Modified residue | 22 | 1 | S-glutathionyl cysteine | ||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||
| Beta strand | 7 – 15 | 9 | |||||||||||||||||||||||
| Helix | 26 – 34 | 9 | |||||||||||||||||||||||
| Beta strand | 37 – 41 | 5 | |||||||||||||||||||||||
| Beta strand | 47 – 55 | 9 | |||||||||||||||||||||||
| Helix | 56 – 64 | 9 | |||||||||||||||||||||||
| Beta strand | 65 – 68 | 4 | |||||||||||||||||||||||
| Beta strand | 72 – 74 | 3 | |||||||||||||||||||||||
| Beta strand | 79 – 89 | 11 | |||||||||||||||||||||||
| Beta strand | 92 – 98 | 7 | |||||||||||||||||||||||
Sequences
References
| [1] | "The complete amino acid sequence of horse muscle acylphosphatase." Cappugi G., Manao G., Camici G., Ramponi G. J. Biol. Chem. 255:6868-6874(1980) [PubMed: 6248536] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-99. Tissue: Muscle. |
| [2] | "Identification and description of alpha-helical regions in horse muscle acylphosphatase by 1H nuclear magnetic resonance spectroscopy." Saudek V., Atkinson R.A., Williams R.J.P., Ramponi G. J. Mol. Biol. 205:229-239(1989) [PubMed: 2538623] [Abstract] Cited for: STRUCTURE BY NMR OF ALPHA HELICES. |
| [3] | "Identification and description of beta-structure in horse muscle acylphosphatase by nuclear magnetic resonance spectroscopy." Saudek V., Wormald M.R., Williams R.J.P., Boyd J., Stefani M., Ramponi G. J. Mol. Biol. 207:405-415(1989) [PubMed: 2547076] [Abstract] Cited for: STRUCTURE BY NMR OF BETA-STRUCTURES. |
| [4] | "Three-dimensional structure of acylphosphatase. Refinement and structure analysis." Pastore A., Saudek V., Ramponi G., Williams R.J.P. J. Mol. Biol. 224:427-440(1992) [PubMed: 1313885] [Abstract] Cited for: STRUCTURE BY NMR. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PIR | QPHO. A01015. | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | P00818. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001792. Acylphosphatase. [Graphical view] | ||||||||||||
| PANTHER | PTHR10029. Acylphosphatase. 1 hit. | ||||||||||||
| Pfam | PF00708. Acylphosphatase. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00112. ACYLPHPHTASE. | ||||||||||||
| ProDom | PD001884. Acylphosphatase. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| PROSITE | PS00150. ACYLPHOSPHATASE_1. 1 hit. PS00151. ACYLPHOSPHATASE_2. 1 hit. PS51160. ACYLPHOSPHATASE_3. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| LinkHub | P00818. | ||||||||||||
Entry information
| Entry name | ACYP2_HORSE | ||||||||
| Accession | Primary (citable) accession number: P00818 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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