Q90358 · PLIGA_CRODU

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).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Molecular Functionphospholipase A2 inhibitor activity
Biological Processregulation of phospholipase A2 activity

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Phospholipase A2 inhibitor CNF
  • Alternative names
    • Crotalus neutralizing factor
      (CNF
      )
    • Crotoxin inhibitor from Crotulus serum
      (CICS
      )
    • Snake blood gamma-PLI
      (Sb-gamma-PLI
      ; gamma-PLI
      )

Organism names

Accessions

  • Primary accession
    Q90358

Subcellular Location

Secreted
Note: Secreted in blood plasma.

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_000002299920-200Phospholipase A2 inhibitor CNF
Disulfide bond22↔46
Disulfide bond25↔32
Disulfide bond39↔67
Disulfide bond73↔94
Disulfide bond95↔100
Disulfide bond118↔143
Disulfide bond136↔165
Disulfide bond169↔191
Glycosylation176N-linked (GlcNAc...) asparagine; partial

Post-translational modification

The carbohydrate moiety increases the inhibition capacity of CNF, but is not essential for activity and for oligomerization.

Keywords

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).

Family & Domains

Sequence similarities

Belongs to the CNF-like-inhibitor family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    200
  • Mass (Da)
    22,267
  • Last updated
    1996-11-01 v1
  • Checksum
    AE848DD6EDD9BBFF
MKYLHTICLLFIFVARGNSRSCDFCHNIGKDCDGYEEECSSPEDVCGKVLLEISSASLSVRTVHKNCFSSSICKLGQFDVNIGHHSYIRGRINCCEKELCEDQPFPGLPLSKPNGYYCPGAIGLFTKDSTEYEAICKGTETKCINIVGHRYEQFPGDISYNLKGCVSSCPLLSLSNATFEQNRNYLEKVECKDAIRLASL

Mass Spectrometry

Molecular mass is 22,201 Da. Determined by MALDI.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U08289
EMBL· GenBank· DDBJ
AAA19162.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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