General Information

  • ID:  hor005862
  • Uniprot ID:  Q27J49
  • Protein name:  C-type natriuretic peptide
  • Gene name:  NA
  • Organism:  Lachesis muta muta (Bushmaster)
  • Family:  Bradykinin-potentiating peptide family; Bradykinin inhibitor peptide family; Natriuretic peptide family
  • Source:  Animal
  • Expression:  Expressed by the venom gland.
  • Disease:  NA
  • Comments:  NA
  • Taxonomy:   Lachesis muta (species), Lachesis (genus), Crotalinae (subfamily), Viperidae (family), Colubroidea (superfamily), Serpentes (infraorder), Toxicofera , Episquamata , Unidentata , Bifurcata , Squamata (order), Lepidosauria (class), Sauria , Sauropsida , Amniota , Tetrapoda , Dipnotetrapodomorpha , Sarcopterygii (superclass), Euteleostomi , Teleostomi , Gnathostomata , Vertebrata , Craniata (subphylum), Chordata (phylum), Deuterostomia , Bilateria , Eumetazoa , Metazoa (kingdom), Opisthokonta , Eukaryota (superkingdom),cellular organisms
  • GO MF:  GO:0004857 enzyme inhibitor activity; GO:0005179 hormone activity; GO:0008191 metalloendopeptidase inhibitor activity; GO:0030414 peptidase inhibitor activity; GO:0090729 toxin activity
  • GO BP:  GO:0007165 signal transduction; GO:0008217 regulation of blood pressure; GO:0035821 modulation of process of another organism; GO:0042311 vasodilation; GO:0097746 blood vessel diameter maintenance
  • GO CC:  GO:0005576 extracellular region

Sequence Information

  • Sequence:  RVGDGCFGLKLDRIGSMSGLGC
  • Length:  22(218-239)
  • Propeptide:  MFVSRLAASGLLLLALLAVSLDGKPVQQWSHKGWPPRPQIPPLVVQQWSQKPWPPGHHIPPVVVQEWPPGHHIPPLVVQQWSQKKWPPGHHIPPLVVQKWDPPPISPPLLKPHESPAGGTTALREELSLGPEAALDTPPAGPDVGPRGSKAPAAPHRLPKSKGASATSAASRPMRDLRTDGKQARQNWGRMMNPDHHAVGGGGGGGGARRLKGLAKKRVGDGCFGLKLDRIGSMSGLGC
  • Signal peptide:  MFVSRLAASGLLLLALLAVSLDG
  • Modification:  NA
  • Glycosylation:  NA
  • Mutagenesis:  NA

Activity

  • Function:  Bradykinin-potentiating peptide both inhibits the activity of the angiotensin-converting enzyme (ACE) and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent (By similarity).
  • Mechanism:  NA
  • Cross BBB:  NA
  • Target:  NA
  • Target Unid:  NA
  • IC50: NA
  • EC50: NA
  • ED50: NA
  • kd: NA
  • Half life: NA

Structure

  • Disulfide bond:  45830
  • Structure ID:  AF-Q27J49-F1(AlphaFold_DB_ID)

  • Structure: (PDB_ID-from https://www.rcsb.org/; AlphaFold_DB_ID-from https://alphafold.ebi.ac.uk/; hordbxxxxxx_AF2.pdb was predicted structure by AlphaFold2; hordbxxxxxx_ESM.pdb was predicted structure by ESMFold)
    •    hor005862_AF2.pdbhor005862_ESM.pdb

Physical Information

Mass: 261640 Formula: C93H157N29O29S3
Absent amino acids: AEHNPQTWY Common amino acids: G
pI: 8.23 Basic residues: 3
Polar residues: 10 Hydrophobic residues: 6
Hydrophobicity: 26.82 Boman Index: -2238
Half-Life: 1 hour Half-Life Yeast: 2 min
Half-Life E.Coli: 2 min Aliphatic Index 84.09
Instability Index: 1451.36 Extinction Coefficient cystines: 125
Absorbance 280nm: 5.95

Literature

  • PubMed ID:  15876444
  • Title:  Identification of novel bradykinin-potentiating peptides and C-type natriuretic peptide from Lachesis muta venom.
  • PubMed ID:  16582429
  • Title:  Lachesis muta (Viperidae) cDNAs reveal diverging pit viper molecules and scaffolds typical of cobra (Elapidae) venoms: implications for snak
  • PubMed ID:  16277978
  • Title: