TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family

PylA/PglA (peptide glycine-leucine-amide) precursor of 64 aas and 1 TMS.  3-d structures and simulations have revealed the overall structure, helix orientations, and tilt angles in the homo- and hetero-multimeric pores (Pino-Angeles et al. 2016).  The pore forms stable heterooligomers with magainin 2 (TC# 1.C.16.1.1) in which PglA, rather than magainin 2, forms the pore (Strandberg et al. 2016).  This occurs at lower concentrations of the two peptides than is required for each peptide to form homomeric pores.  Ulmschneider 2017 suggested that cationic antimicrobial peptides (AMPs) such as PGLa translocate across hydrophobic lipid bilayers without formation of peptide-lined channels, explaining why they induce membrane leakage and antimicrobial activity. PGLa spontaneously translocates across the membrane individually on a timescale of tens of microseconds, without forming pores. Instead, short-lived water bridges, with two or three peptides connecting at their termini, may allow both ion translocation and lipid flip-flop via a brushlike mechanism usually involving the C terminus of one peptide (Ulmschneider 2017). Another study suggested that PGLa translocates across the bilayer before membrane permeation (Parvez et al. 2018).

Accession Number:Q99134
Protein Name:PylA/PglA
Molecular Weight:6809.00
Species:Xenopus laevis (African clawed frog) [8355]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Secreted1
Substrate electrolytes, small molecules, water

Cross database links:

RefSeq: NP_001095268.1   
Entrez Gene ID: 779059   
KEGG: xla:779059   

Gene Ontology

GO:0005576 C:extracellular region
GO:0042742 P:defense response to bacterium

References (4)

[1] “A novel peptide designated PYLa and its precursor as predicted from cloned mRNA of Xenopus laevis skin.”  Hoffmann   6688991
[2] “The genes for the frog skin peptides GLa, xenopsin, levitide and caerulein contain a homologous export exon encoding a signal sequence and part of an amphiphilic peptide.”  Kuchler   2465151
[3] “Biosynthesis and degradation of peptides derived from Xenopus laevis prohormones.”  Giovannini   3606567
[4] “Antimicrobial peptides in the stomach of Xenopus laevis.”  Moore   1717472

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)


Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
Window Size: Angle:  
FASTA formatted sequence
61:	RRDS