Q90358 · PLIGA_CRODU
- ProteinPhospholipase A2 inhibitor CNF
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids200 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Inhibits the PLA2 activity of crotoxin (CTX) by replacing the acid subunit (CA) in the CTX complex (PubMed:10903514, PubMed:1949070, PubMed:7851385, PubMed:8195214).
Displays a pro-inflammatory action through activation of important main signaling pathways for human leukocytes, in vitro (PubMed:32183984).
Abolishes both the muscle-paralyzing and muscle-damaging activities of CTX in mice phrenic nerve-diaphragm muscle preparations (PubMed:33387548).
Displays a pro-inflammatory action through activation of important main signaling pathways for human leukocytes, in vitro (PubMed:32183984).
Abolishes both the muscle-paralyzing and muscle-damaging activities of CTX in mice phrenic nerve-diaphragm muscle preparations (PubMed:33387548).
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 | phospholipase A2 inhibitor activity | |
Biological Process | regulation of phospholipase A2 activity |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended namePhospholipase A2 inhibitor CNF
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Crotalinae > Crotalus
Accessions
- Primary accessionQ90358
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MKYLHTICLLFIFVARGNS | ||||||
Chain | PRO_0000022999 | 20-200 | Phospholipase A2 inhibitor CNF | |||
Sequence: RSCDFCHNIGKDCDGYEEECSSPEDVCGKVLLEISSASLSVRTVHKNCFSSSICKLGQFDVNIGHHSYIRGRINCCEKELCEDQPFPGLPLSKPNGYYCPGAIGLFTKDSTEYEAICKGTETKCINIVGHRYEQFPGDISYNLKGCVSSCPLLSLSNATFEQNRNYLEKVECKDAIRLASL | ||||||
Disulfide bond | 22↔46 | |||||
Sequence: CDFCHNIGKDCDGYEEECSSPEDVC | ||||||
Disulfide bond | 25↔32 | |||||
Sequence: CHNIGKDC | ||||||
Disulfide bond | 39↔67 | |||||
Sequence: CSSPEDVCGKVLLEISSASLSVRTVHKNC | ||||||
Disulfide bond | 73↔94 | |||||
Sequence: CKLGQFDVNIGHHSYIRGRINC | ||||||
Disulfide bond | 95↔100 | |||||
Sequence: CEKELC | ||||||
Disulfide bond | 118↔143 | |||||
Sequence: CPGAIGLFTKDSTEYEAICKGTETKC | ||||||
Disulfide bond | 136↔165 | |||||
Sequence: CKGTETKCINIVGHRYEQFPGDISYNLKGC | ||||||
Disulfide bond | 169↔191 | |||||
Sequence: CPLLSLSNATFEQNRNYLEKVEC | ||||||
Glycosylation | 176 | N-linked (GlcNAc...) asparagine; partial | ||||
Sequence: N |
Post-translational modification
The carbohydrate moiety increases the inhibition capacity of CNF, but is not essential for activity and for oligomerization.
Keywords
- PTM
PTM databases
Expression
Tissue specificity
Expressed by the liver.
Interaction
Subunit
Occurs as a mixture of oligomers (PubMed:24820993).
Tetrameric arrangement appears to be the predominant quaternary structure (PubMed:24820993).
Interacts with phospholipase A2 crotoxin basic subunit CBd; the interaction leads to dissociation of the CA-CB heterodimer and to inhibition of PLA2 activity of the CB subunit (PubMed:10903514).
Tetrameric arrangement appears to be the predominant quaternary structure (PubMed:24820993).
Interacts with phospholipase A2 crotoxin basic subunit CBd; the interaction leads to dissociation of the CA-CB heterodimer and to inhibition of PLA2 activity of the CB subunit (PubMed:10903514).
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length200
- Mass (Da)22,267
- Last updated1996-11-01 v1
- ChecksumAE848DD6EDD9BBFF
Mass Spectrometry
Keywords
- Technical term