AMPDB_228 | Temporin-1Tl

1 General Description

AMPDB ID: AMPDB_228

Protein Names: Temporin-1Tl (TL) (Temporin-L)

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

FVQWFSKFLGRIL

FASTA format

Counts of Amino Acids

'A': 0, 'R': 1, 'N': 0, 'D': 0, 'C': 0, 'Q': 1, 'E': 0, 'G': 1, 'H': 0, 'I': 1, 'L': 2, 'K': 1, 'M': 0, 'F': 3, 'P': 0, 'S': 1, 'T': 0, 'W': 1, 'Y': 0, 'V': 1

Frequencies of Amino Acids

'A': 0%, 'R': 7.69%, 'N': 0%, 'D': 0%, 'C': 0%, 'Q': 7.69%, 'E': 0%, 'G': 7.69%, 'H': 0%, 'I': 7.69%, 'L': 15.38%, 'K': 7.69%, 'M': 0%, 'F': 23.08%, 'P': 0%, 'S': 7.69%, 'T': 0%, 'W': 7.69%, 'Y': 0%, 'V': 7.69%

Missing Amino Acid(s)

A, C, D, E, H, M, N, P, T, Y

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

G, I, K, Q, R, S, V, W

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	1640.99 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	112.308	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	24.046	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	0.823	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.696	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	11.652	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	1.998	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.615, 0.154, 0.154 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.308	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	5500, 5500	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

Gram Negative Bacteria and Gram Positive Bacteria

4.2 Antimicrobial Activity

Amphibian defense peptide, Antibiotic, Antimicrobial, Anti-parasitic, Anti-gram-negative, Anti-gram-Positive

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Cytolysis, Anti-cancer, Cytotoxin, Hemolytic, 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: Rinaldi AC, Mangoni ML, Rufo A, et al. Temporin L: antimicrobial, haemolytic and cytotoxic activities, and effects on membrane permeabilization in lipid vesicles. Biochem J. 2002;368(Pt 1):91-100. Published 2002 Nov 15. doi:10.1042/BJ20020806

PMID: 12133008

Citation 4: Giacometti A, Cirioni O, Ghiselli R, et al. Interaction of antimicrobial peptide temporin L with lipopolysaccharide in vitro and in experimental rat models of septic shock caused by gram-negative bacteria. Antimicrob Agents Chemother. 2006;50(7):2478-86. Published 2006 Jul. doi:10.1128/AAC.01553-05

PMID: 16801429

Citation 5: 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 6: 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 7: 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 8: Bhunia A, Saravanan R, Mohanram H, et al. NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide micelles: mechanistic insights into outer membrane permeabilization and synergistic activity. J Biol Chem. 2011;286(27):24394-406. Published 2011 Jul 8. doi:10.1074/jbc.M110.189662

PMID: 21586570

Citation 9: Manzo G, Ferguson PM, Hind CK, et al. Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. Sci Rep. 2019;9(1):10934. Published 2019 Jul 29. doi:10.1038/s41598-019-47327-w

PMID: 31358802

5.2 Protein Sequence Databases

5.3 3D Structure Databases

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

AlphaFoldDB: P57104

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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