AMPDB_226 | Temporin-1Ta

1 General Description

AMPDB ID: AMPDB_226

Protein Names: Temporin-1Ta (TA) (Temporin-A)

Protein Family: Frog skin active peptide (FSAP) family; Temporin subfamily

Gene Name: Nil

Source Organism: Rana temporaria (European common frog)

Protein Length: 13 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

FLPLIGRVLSGIL

FASTA format

Counts of Amino Acids

'A': 0, 'R': 1, 'N': 0, 'D': 0, 'C': 0, 'Q': 0, 'E': 0, 'G': 2, 'H': 0, 'I': 2, 'L': 4, 'K': 0, 'M': 0, 'F': 1, 'P': 1, 'S': 1, 'T': 0, 'W': 0, 'Y': 0, 'V': 1

Frequencies of Amino Acids

'A': 0%, 'R': 7.69%, 'N': 0%, 'D': 0%, 'C': 0%, 'Q': 0%, 'E': 0%, 'G': 15.38%, 'H': 0%, 'I': 15.38%, 'L': 30.77%, 'K': 0%, 'M': 0%, 'F': 7.69%, 'P': 7.69%, 'S': 7.69%, 'T': 0%, 'W': 0%, 'Y': 0%, 'V': 7.69%

Missing Amino Acid(s)

A, C, D, E, H, K, M, N, Q, T, W, Y

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

F, P, R, S, V

Hydrophobic Amino Acid(s) Count

Hydrophilic Amino Acid(s) Count

Basic Amino Acid(s) Count

Acidic Amino Acid(s) Count

Modified Amino Acid(s) Count

Modified Amino Acid(s) Frequencies

Computed by biopython (version 1.79) & proteinAnalysis (version 1)

3 Physicochemical Properties

Sl. No.	Properties	Values	Reference
1.	Molecular Mass	1397.77 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	202.308	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	32.331	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	1.808	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.587	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	10.55	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	0.998	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.615, 0.308, 0.308 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.077	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	0, 0	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

S.aureus (Gram-positive)

4.2 Antimicrobial Activity

Amphibian defense peptide, Antibiotic, Antimicrobial, Antiviral protein, Anti-HSV, Anti-MRSA, Anti-parasitic, Anti-gram-Positive

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Hemolytic, Synergistic peptide, Wound healing, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Simmaco M, Mignogna G, Canofeni S, et al. Temporins, antimicrobial peptides from the European red frog Rana temporaria. Eur J Biochem. 1996;242(3):788-92. Published 1996 Dec 15. doi:10.1111/j.1432-1033.1996.0788r.x

PMID: 9022710

Citation 2: Samgina TY, Vasileva ID, Kovalev SV, et al. Differentiation of Central Slovenian and Moscow populations of Rana temporaria frogs using peptide biomarkers of temporins family. Anal Bioanal Chem. 2021;413(21):5333-5347. Published 2021 Sep. doi:10.1007/s00216-021-03506-1

PMID: 34235566

Citation 3: Mangoni ML, Rinaldi AC, Di Giulio A, et al. Structure-function relationships of temporins, small antimicrobial peptides from amphibian skin. Eur J Biochem. 2000;267(5):1447-54. Published 2000 Mar. doi:10.1046/j.1432-1327.2000.01143.x

PMID: 10691983

Citation 4: Rinaldi AC, Di Giulio A, Liberi M, et al. Effects of temporins on molecular dynamics and membrane permeabilization in lipid vesicles. J Pept Res. 2001;58(3):213-20. Published 2001 Sep. doi:10.1034/j.1399-3011.2001.00896.x

PMID: 11576327

Citation 5: Osusky M, Osuska L, Hancock RE, et al. Transgenic potatoes expressing a novel cationic peptide are resistant to late blight and pink rot. Transgenic Res. 2004;13(2):181-90. Published 2004 Apr. doi:10.1023/b:trag.0000026076.72779.60

PMID: 15198205

Citation 6: Chinchar VG, Bryan L, Silphadaung U, et al. Inactivation of viruses infecting ectothermic animals by amphibian and piscine antimicrobial peptides. Virology. 2004;323(2):268-75. Published 2004 Jun 1. doi:10.1016/j.virol.2004.02.029

PMID: 15193922

Citation 7: Mangoni ML, Saugar JM, Dellisanti M, et al. Temporins, small antimicrobial peptides with leishmanicidal activity. J Biol Chem. 2005;280(2):984-90. Published 2005 Jan 14. doi:10.1074/jbc.M410795200

PMID: 15513914

Citation 8: Rosenfeld Y, Barra D, Simmaco M, et al. A synergism between temporins toward Gram-negative bacteria overcomes resistance imposed by the lipopolysaccharide protective layer. J Biol Chem. 2006;281(39):28565-74. Published 2006 Sep 29. doi:10.1074/jbc.M606031200

PMID: 16867990

Citation 9: Simonetti O, Cirioni O, Goteri G, et al. Temporin A is effective in MRSA-infected wounds through bactericidal activity and acceleration of wound repair in a murine model. Peptides. 2008;29(4):520-8. Published 2008 Apr. doi:10.1016/j.peptides.2007.12.011

PMID: 18255189

Citation 10: Di Grazia A, Luca V, Segev-Zarko LA, et al. Temporins A and B stimulate migration of HaCaT keratinocytes and kill intracellular Staphylococcus aureus. Antimicrob Agents Chemother. 2014;58(5):2520-7. Published 2014 May. doi:10.1128/AAC.02801-13

PMID: 24514087

Citation 11: Eggimann GA, Sweeney K, Bolt HL, et al. The role of phosphoglycans in the susceptibility of Leishmania mexicana to the temporin family of anti-microbial peptides. Molecules. 2015;20(2):2775-85. Published 2015 Feb 6. doi:10.3390/molecules20022775

PMID: 25668079

Citation 12: Musale V, Casciaro B, Mangoni ML, et al. Assessment of the potential of temporin peptides from the frog Rana temporaria (Ranidae) as anti-diabetic agents. J Pept Sci. 2018;24(2). Published 2018 Feb. doi:10.1002/psc.3065

PMID: 29349894

Citation 13: Carotenuto A, Malfi S, Saviello MR, et al. A different molecular mechanism underlying antimicrobial and hemolytic actions of temporins A and L. J Med Chem. 2008;51(8):2354-62. Published 2008 Apr 24. doi:10.1021/jm701604t

PMID: 18370376

Citation 14: Saravanan R, Joshi M, Mohanram H, et al. NMR structure of temporin-1 ta in lipopolysaccharide micelles: mechanistic insight into inactivation by outer membrane. PLoS One. 2013;8(9):e72718. Published 2013. doi:10.1371/journal.pone.0072718

PMID: 24039798

5.2 Protein Sequence Databases

5.3 3D Structure Databases

	Sl. no.	PDB ID	Method	Resolution	Access Links	3D View

AlphaFoldDB: P56917

5.4 Nucleotide Sequence Databases

No entries found in GenBank or EMBL

RefSeq: Not found

5.5 Protein-Protein Interaction Databases

STRING: Not found

IntAct: Not found

BioGRID: Not found

5.6 Ligand Databases

BindingDB: Not found

DrugBank: Not found

ChEMBL: Not found

5.7 Family & Domain Databases

InterPro: Not found

PANTHER: Not found

PROSITE: Not found

5.8 Genome Annotation Databases

Ensembl: Not found

5.9 Phylogenomic Databases

GeneTree: Not found

5.10 Enzyme & Pathway Databases

BRENDA: Not found

BioCyc: Not found

5.11 Protein-RNA Interaction Databases

RNAct: Not found

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