P51972 · PA2B1_AGKPI
- ProteinBasic phospholipase A2 APP-D49
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids123 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
Features
Showing features for binding site, active site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent phospholipase A2 activity | |
Molecular Function | phospholipid binding | |
Biological Process | arachidonic acid secretion | |
Biological Process | lipid catabolic process | |
Biological Process | negative regulation of T cell proliferation | |
Biological Process | phospholipid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBasic phospholipase A2 APP-D49
- EC number
- Short namessvPLA2
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Crotalinae > Agkistrodon
Accessions
- Primary accessionP51972
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 6 | 75% decrease in catalytic efficiency. | ||||
Sequence: E → R | ||||||
Mutagenesis | 7 | 95% decrease in catalytic efficiency. 500-fold decrease in catalytic efficiency; when associated with E-10. | ||||
Sequence: K → E | ||||||
Mutagenesis | 10 | 95% decrease in catalytic efficiency. 500-fold decrease in catalytic efficiency; when associated with E-7. | ||||
Sequence: K → E | ||||||
Mutagenesis | 11 | 75% decrease in catalytic efficiency. | ||||
Sequence: K → E | ||||||
Mutagenesis | 15 | 60% decrease in catalytic efficiency. | ||||
Sequence: K → E | ||||||
Mutagenesis | 53 | No effect on catalytic efficiency. | ||||
Sequence: K → E | ||||||
Mutagenesis | 60 | No effect on catalytic efficiency. | ||||
Sequence: K → E |
PTM/Processing
Features
Showing features for chain, lipidation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000161605 | 1-123 | Basic phospholipase A2 APP-D49 | |||
Sequence: NLFQFEKLIKKMTGKSGMLWYSAYGCYCGWGGQGRPKDATDRCCFVHDCCYGKVTGCNPKMDIYTYSVDNGNIVCGGTNPCKKQICECDRAAAICFRDNLKTYDSKTYWKYPKKNCKEESEPC | ||||||
Lipidation | 7 | N6-palmitoyl lysine | ||||
Sequence: K | ||||||
Lipidation | 10 | N6-palmitoyl lysine | ||||
Sequence: K | ||||||
Disulfide bond | 26↔116 | |||||
Sequence: CYCGWGGQGRPKDATDRCCFVHDCCYGKVTGCNPKMDIYTYSVDNGNIVCGGTNPCKKQICECDRAAAICFRDNLKTYDSKTYWKYPKKNC | ||||||
Disulfide bond | 28↔44 | |||||
Sequence: CGWGGQGRPKDATDRCC | ||||||
Disulfide bond | 43↔95 | |||||
Sequence: CCFVHDCCYGKVTGCNPKMDIYTYSVDNGNIVCGGTNPCKKQICECDRAAAIC | ||||||
Disulfide bond | 49↔123 | |||||
Sequence: CCYGKVTGCNPKMDIYTYSVDNGNIVCGGTNPCKKQICECDRAAAICFRDNLKTYDSKTYWKYPKKNCKEESEPC | ||||||
Disulfide bond | 50↔88 | |||||
Sequence: CYGKVTGCNPKMDIYTYSVDNGNIVCGGTNPCKKQICEC | ||||||
Disulfide bond | 57↔81 | |||||
Sequence: CNPKMDIYTYSVDNGNIVCGGTNPC | ||||||
Disulfide bond | 75↔86 | |||||
Sequence: CGGTNPCKKQIC |
Post-translational modification
Acylation causes dimerization.
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
Interaction
Subunit
Monomer or homodimer.
Structure
Family & Domains
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length123
- Mass (Da)13,989
- Last updated1998-07-15 v2
- ChecksumC39986552D990D72
Mass Spectrometry
Keywords
- Technical term