AMPDB_498 | Temporin-SHa

1 General Description

AMPDB ID: AMPDB_498

Protein Names: Temporin-SHa (Temporin-1Sa) (Temp-1Sa)

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

Gene Name: Nil

Source Organism: Pelophylax saharicus (Sahara frog) (Rana saharica)

Protein Length: 50 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

FLGTINLSLCEQERDADEEERRDEPNESNVEVEKRFLSGIVGMLGKLFGK

FASTA format

Counts of Amino Acids

'A': 1, 'R': 4, 'N': 3, 'D': 3, 'C': 1, 'Q': 1, 'E': 9, 'G': 5, 'H': 0, 'I': 2, 'L': 6, 'K': 3, 'M': 1, 'F': 3, 'P': 1, 'S': 3, 'T': 1, 'W': 0, 'Y': 0, 'V': 3

Frequencies of Amino Acids

'A': 2%, 'R': 8%, 'N': 6%, 'D': 6%, 'C': 2%, 'Q': 2%, 'E': 18%, 'G': 10%, 'H': 0%, 'I': 4%, 'L': 12%, 'K': 6%, 'M': 2%, 'F': 6%, 'P': 2%, 'S': 6%, 'T': 2%, 'W': 0%, 'Y': 0%, 'V': 6%

Missing Amino Acid(s)

H, W, Y

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

A, C, M, P, Q, T

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	5699.36 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	81.8	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	42.64	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	-0.668	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.561	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	4.227	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	-5.048	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.28, 0.24, 0.34 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.06	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)

Gram Negative Bacteria and Gram Positive Bacteria

4.2 Antimicrobial Activity

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

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Cytolysis, Hemolytic, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Abbassi F, Oury B, Blasco T, et al. Isolation, characterization and molecular cloning of new temporins from the skin of the North African ranid Pelophylax saharica. Peptides. 2008;29(9):1526-33. Published 2008 Sep. doi:10.1016/j.peptides.2008.05.008

PMID: 18584916

Citation 2: Lombana A, Raja Z, Casale S, et al. Temporin-SHa peptides grafted on gold surfaces display antibacterial activity. J Pept Sci. 2014;20(7):563-9. Published 2014 Jul. doi:10.1002/psc.2654

PMID: 24919960

Citation 3: 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 4: Raja Z, AndrÃ© S, Abbassi F, et al. Insight into the mechanism of action of temporin-SHa, a new broad-spectrum antiparasitic and antibacterial agent. PLoS One. 2017;12(3):e0174024. Published 2017. doi:10.1371/journal.pone.0174024

PMID: 28319176

Citation 5: Roy M, Lebeau L, Chessa C, et al. Comparison of Anti-Viral Activity of Frog Skin Anti-Microbial Peptides Temporin-Sha and [KÂ³]SHa to LL-37 and Temporin-Tb against Herpes Simplex Virus Type 1. Viruses. 2019;11(1). Published 2019 Jan 18. doi:10.3390/v11010077

PMID: 30669255

Citation 6: Abbassi F, Galanth C, Amiche M, et al. Solution structure and model membrane interactions of temporins-SH, antimicrobial peptides from amphibian skin. A NMR spectroscopy and differential scanning calorimetry study. Biochemistry. 2008;47(40):10513-25. Published 2008 Oct 7. doi:10.1021/bi8006884

PMID: 18795798

5.2 Protein Sequence Databases

5.3 3D Structure Databases

AlphaFoldDB: B3KYH4

5.4 Nucleotide Sequence Databases

Sl. no.	Accession(s)	Access Link(s)
1.	AM748899	GenBank \|\| 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: IPR004275

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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