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MYP_093668
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Basic Information
Unnamed
Antimicrobial
Cardiovascular ▸ Vascular tone modulation ▸ Vasoactive peptide
Cardiovascular ▸ Vascular tone modulation ▸ Vasodilatory activity
Enzyme modulation ▸ Enzyme inhibition ▸ ACE inhibition ▸ ACE inhibitory
Hormonal / Endocrine ▸ Hormone peptide
Metabolic ▸ Appetite and feeding regulation ▸ Feeding regulator
Regulatory peptide ▸ Biological modulation
Regulatory peptide ▸ Biological regulation
Standard
16 amino acids
C84H122N26O21
Standard
Sequence
RPPGFSPFRGKFHSQS
Physicochemical Analysis
1832.03 Da
12.00
2.85
2.59
0.1779
-1.20
0.26
-0.22
101.84
0.00
0.1875
0.00
0.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
755.73
-8.96
26.0
25.0
54.0
131.0
7.0
16.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0105065 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide; DSSP H 0.0%, E 0.0%, T 50.0%, C 50.0% [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial
PaperDADP: the database of anuran defense peptides PMID22467909 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22467909/
RECORD: Rec_0132681 VERIFIED: YES
Provenance & Taxonomy
Bombina maxima [Animal]
Bradykinin
161274
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Hormone Endocrine Vasoactive Vasodilator Metabolic regulation Physiological regulation Receptor modulation ACE inhibitory Feeding regulator
Mammalian: 1 hour; Yeast: 2 min; E. coli: 2 min
PMID20138946 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20138946/
RECORD: Rec_0308255 VERIFIED: YES
Provenance & Taxonomy
Bombina maxima [Animal]
Bradykinin
161274
Structure & Mods
ribosomal mature linear peptide [Linear]
Gene-encoded natural peptide composed of standard L-amino acids [L]
Bio-Activity Profile
Appetite-suppressing Bradykinin receptor-modulating
PaperR. Lai et al. / Peptides 24 (2003) 199-204. Bombinakinin M gene associated peptide, a novel bioactive peptide from skin secretions of the toad Bombina maxima Evidence URLhttps://www.uniprot.org/uniprotkb/Q7T3L1/entry
RECORD: Rec_0410788 VERIFIED: YES
Provenance & Taxonomy
Bombina maxima [Animal]
Bradykinin
161274
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Hormone Endocrine Vasoactive Vasodilator Metabolic regulation Physiological regulation Receptor modulation ACE inhibitory Feeding regulator
vitro relaxation of rat arterial smooth muscle
Mammalian: 1 hour; Yeast: 2 min; E. coli: 2 min
PMID20138946 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20138946/