Reviewed,
UniProtKB/Swiss-Prot P00598 (PA21_NAJAT)
Last modified
June 16, 2009.
Version 89.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Phospholipase A2 1 EC=3.1.1.4 Alternative name(s): Muscarinic protein Short name=MP Phosphatidylcholine 2-acylhydrolase |
| Organism | Naja atra (Chinese cobra) |
| Taxonomic identifier | 8656 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Naja |
Protein attributes
| Sequence length | 146 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 | PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. In guinea-pig ileum, this protein produces an onset and dose-dependent contraction. Has a high affinity for muscarinic acetylcholine receptors mAChRs and has the ability to activate them. Ref.3 |
| Catalytic activity | Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate. |
| Cofactor | Binds 1 calcium ion per subunit. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| Sequence similarities | Belongs to the phospholipase A2 family. Group I subfamily. |
| Mass spectrometry |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 21 | 21 | Potential | |||||||||||||||||||||||||||
| Propeptide | 22 – 27 | 6 | PRO_0000022916 | |||||||||||||||||||||||||||
| Chain | 28 – 146 | 119 | Phospholipase A2 1 | PRO_0000022917 | ||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||
| Active site | 74 | 1 | ||||||||||||||||||||||||||||
| Active site | 120 | 1 | ||||||||||||||||||||||||||||
| Metal binding | 54 | 1 | Calcium; via carbonyl oxygen | |||||||||||||||||||||||||||
| Metal binding | 56 | 1 | Calcium; via carbonyl oxygen | |||||||||||||||||||||||||||
| Metal binding | 58 | 1 | Calcium; via carbonyl oxygen | |||||||||||||||||||||||||||
| Metal binding | 75 | 1 | Calcium | |||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Disulfide bond | 38 ↔ 98 | |||||||||||||||||||||||||||||
| Disulfide bond | 53 ↔ 145 | |||||||||||||||||||||||||||||
| Disulfide bond | 55 ↔ 71 | |||||||||||||||||||||||||||||
| Disulfide bond | 70 ↔ 126 | |||||||||||||||||||||||||||||
| Disulfide bond | 77 ↔ 119 | |||||||||||||||||||||||||||||
| Disulfide bond | 87 ↔ 112 | |||||||||||||||||||||||||||||
| Disulfide bond | 105 ↔ 117 | |||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||
| Sequence conflict | 111 – 112 | 2 | AC → CA AA sequence Ref.2 | |||||||||||||||||||||||||||
| Sequence conflict | 134 – 136 | 3 | NNN → DND AA sequence Ref.2 | |||||||||||||||||||||||||||
| Sequence conflict | 140 | 1 | D → N AA sequence Ref.2 | |||||||||||||||||||||||||||
| Sequence conflict | 146 | 1 | Q → QE AA sequence Ref.2 | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Helix | 29 – 39 | 11 | ||||||||||||||||||||||||||||
| Helix | 45 – 48 | 4 | ||||||||||||||||||||||||||||
| Turn | 52 – 54 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 55 – 57 | 3 | ||||||||||||||||||||||||||||
| Helix | 66 – 81 | 16 | ||||||||||||||||||||||||||||
| Turn | 89 – 91 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 96 – 99 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 102 – 105 | 4 | ||||||||||||||||||||||||||||
| Helix | 111 – 127 | 17 | ||||||||||||||||||||||||||||
| Helix | 134 – 136 | 3 | ||||||||||||||||||||||||||||
| Helix | 141 – 144 | 4 | ||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Sequence analysis and expression of phospholipase A2 from Taiwan cobra." Pan F.M., Yeh M.S., Chang W.C., Hung C.C., Chiou S.H. Biochem. Biophys. Res. Commun. 199:969-976(1994) [PubMed: 7510963] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland. |
| [2] | "Complete amino acid sequence of a phospholipase A2 from the venom of Naja naja atra (Taiwan cobra)." Tsai I.-H., Wu S.-H., Lo T.-B. Toxicon 19:141-152(1981) [PubMed: 7222082] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-146. Tissue: Venom. |
| [3] | "A snake venom phospholipase A(2) with high affinity for muscarinic acetylcholine receptors acts on guinea pig ileum." Huang L.-F., Zheng J.-B., Xu Y., Song H.-T., Yu C.-X. Toxicon 51:1008-1016(2008) [PubMed: 18281071] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-43, FUNCTION, MASS SPECTROMETRY. Tissue: Venom. |
| [4] | "Crystal structure of cobra-venom phospholipase A2 in a complex with a transition-state analogue." White S.P., Scott D.L., Otwinowski Z., Gelb M.H., Sigler P.B. Science 250:1560-1563(1990) [PubMed: 2274787] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). |
| [5] | "Interfacial catalysis: the mechanism of phospholipase A2." Scott D.L., White S.P., Otwinowski Z., Yuan W., Gelb M.H., Sigler P.B. Science 250:1541-1546(1990) [PubMed: 2274785] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| X73225 mRNA. Translation: CAA51694.1. | |||||||||||||||||||
| PIR | PSNJAF. JC2137. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOVERGEN | P00598. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BRENDA | 3.1.1.4. 279483. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR016090. Phospholipase_A2. IPR013090. Phospholipase_A2_AS. IPR001211. Phospholipase_A2_euk. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:1.20.90.10. Phospholipase_A2. 1 hit. | ||||||||||||||||||
| PANTHER | PTHR11716. Phospholipase_A2. 1 hit. | ||||||||||||||||||
| Pfam | PF00068. Phospholip_A2_1. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR00389. PHPHLIPASEA2. | ||||||||||||||||||
| ProDom | PD000303. PhospholipaseA2. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||
| SMART | SM00085. PA2c. 1 hit. [Graphical view] | ||||||||||||||||||
| PROSITE | PS00119. PA2_ASP. 1 hit. PS00118. PA2_HIS. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | PA21_NAJAT | ||||||||
| Accession | Primary (citable) accession number: P00598 | ||||||||
| Entry history |
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| 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


