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). The cooperativity exhibited by the activities of this and other antimicrobial peptides has been explained as a non-linear concentration dependence characterized by a threshold and a rapid rise to saturation as the concentration exceeds the threshold (Huang 2006).
|
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 |
molecule |
---|
RefSeq: |
NP_999028.1
|
Entrez Gene ID: |
396871
|
Pfam: |
PF00666
|
KEGG: |
ssc:396871
|
|
[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
|
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