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1.C.16.1.1
Magainin precursor of 333 aas and 1 TMS.  3-d structural determinations and simulations show the oligomeric states, transmembrane helices and tilt angles in the various states of the mature Maganin (Pino-Angeles et al. 2016).  Forms stable heterooligomers with PglA (TC# 1.C.16.1.5) at lower concentrations of the two peptides than allows each one alone to form pores in which PglA, rather than magainin 2 forms the pore (Strandberg et al. 2016). Mixtures of peptides such as magainin 2 and PGLa, which are stored and secreted naturally as a cocktail, exhibit considerably enhanced antimicrobial activities when investigated together in antimicrobial assays and also in pore forming experiments applied to biophysical model systems. Investigations have revealed that these peptides do not form stable complexes but act by specific lipid-mediated interactions and are influenced by the nanoscale properties of phospholipid bilayers (Juhl et al. 2021).

Accession Number:P11006
Protein Name:MAGA
Length:303
Molecular Weight:33380.00
Species:Xenopus laevis (African clawed frog) [8355]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Secreted1
Substrate molecule, water, polyelectrolyte macromolecule

Cross database links:

RefSeq: NP_001081306.1   
Entrez Gene ID: 397766   
KEGG: xla:397766   

Gene Ontology

GO:0005576 C:extracellular region
GO:0019835 P:cytolysis
GO:0042742 P:defense response to bacterium
GO:0050832 P:defense response to fungus
GO:0019836 P:hemolysis by symbiont of host erythrocytes

References (4)

[1] “The cDNA sequence coding for prepro-PGS (prepro-magainins) and aspects of the processing of this prepro-polypeptide.”  Terry A.S.et.al.   2833514
[2] “Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.”  Zasloff M.et.al.   3299384
[3] “Antimicrobial peptides in the stomach of Xenopus laevis.”  Moore K.S.et.al.   1717472
[4] “Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy.”  Bechinger B.et.al.   8298457
Structure:
1D9J   1D9L   1D9M   1D9O   1D9P   1DUM   1F0D   1F0E   1F0F   1F0G   [...more]

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Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MFKGLFICSL IAVICANALP QPEASADEDM DEREVRGIGK FLHSAGKFGK AFVGEIMKSK 
61:	RDAEAVGPEA FADEDLDERE VRGIGKFLHS AKKFGKAFVG EIMNSKRDAE AVGPEAFADE 
121:	DLDEREVRGI GKFLHSAKKF GKAFVGEIMN SKRDAEAVGP EAFADEDLDE REVRGIGKFL 
181:	HSAKKFGKAF VGEIMNSKRD AEAVGPEAFA DEDFDEREVR GIGKFLHSAK KFGKAFVGEI 
241:	MNSKRDAEAV GPEAFADEDL DEREVRGIGK FLHSAKKFGK AFVGEIMNSK RDAEAVDDRR 
301:	WVE