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1.C.33.1.1
PreProtegrin-2 (prophenin-2; PF-2; PR-2). Exerts antimicrobial activity more effectively against Gram-negative bacteria than Gram-positive bacteria. The high resolution NMR structure has been solved (Usachev et al. 2015).  Its antimicrobial activities have been defined (Yasin et al. 1996, Miyasaki et al. 1997, Miyasaki et al. 1998, Cho et al. 1998)

Accession Number:P51525
Protein Name:PF12
Length:228
Molecular Weight:25855.00
Species:Sus scrofa (Pig) [9823]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Secreted1
Substrate small molecules

Cross database links:

RefSeq: NP_999028.1   
Entrez Gene ID: 396871   
Pfam: PF00666   
KEGG: ssc:396871   

Gene Ontology

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

References (2)

[1] “Molecular cloning of a putative homolog of proline/arginine-rich antibacterial peptides from porcine bone marrow.”  Pungercar J.et.al.   8262247
[2] “Structures of genes for two cathelin-associated antimicrobial peptides: prophenin-2 and PR-39.”  Zhao C.et.al.   7498526

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)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
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FASTA formatted sequence
1:	METQRASLCL GRWSLWLLLL ALVVPSASAQ ALSYREAVLR AVDRLNEQSS EANLYRLLEL 
61:	DQPPKADEDP GTPKPVSFTV KETVCPRPTR RPPELCDFKE NGRVKQCVGT VTLDQIKDPL 
121:	DITCNEGVRR FPWWWPFLRR PRLRRQAFPP PNVPGPRFPP PNVPGPRFPP PNFPGPRFPP 
181:	PNFPGPRFPP PNFPGPPFPP PIFPGPWFPP PPPFRPPPFG PPRFPGRR