General information | DisProt: | DP00567 | Name: | Pilosulin-1 | Synonym(s): | MYR1_MYRPI
Major allergen Myr p 1
Allergen Myr p I
Pilosulin-1 [cleavage product 1]
Pilosulin-1 65->112 [cleavage product 2]
Pilosulin-1 68->112 [cleavage product 3]
Pilosulin-1 71->112 [cleavage product 4]
Pilosulin-1 86->112 [cleavage product 5]
| First appeared in release: | Release 4.1 (07/10/2008) | UniProt: | Q07932 | UniGene: | | SwissProt: | MYR1_MYRPI | TrEMBL: | | NCBI (GI): | 730091 | Source organism: | Myrmecia pilosula (Jack jumper ant) (Australian jumper ant) | Sequence length: | 112 | Percent disordered: | 16% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MKLSCLLLTL TIIFVLTIVH APNVEAKDLA DPESEAVGFA DAFGEADAVG EADPNAGLGS - 60 VFGRLARILG RVIPKVAKKL GPKVAKVLPK VMKEAIPMAV EMAKSQEEQQ PQ
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Functional narrative |
Has strong cytotoxic and hemolytic activities. Is more potent against mononuclear leukocytes than against granulocytes. The synthesized peptide 57-76 shows a potent and broad spectrum antimicrobial activity against both Gram-positive and Gram-negative bacteria, and also against the fungus C.albicans. Adopts an alpha-helical structure.
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | | Location: | 59 - 76 | Length: | 18 | Region sequence: |
GSVFGRLARILGRVIPKV | Modification type: | Native
| PDB: | | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | Modification site
| Functional subclasses: | Unknown
| Detection methods: | References:
- Zelezetsky I, Pag U, Antcheva N, Sahl HG, Tossi A. "Identification and optimization of an antimicrobial peptide from the ant venom toxin pilosulin." Arch Biochem Biophys. 2005; 434(2): 358-64. PubMed: 15639237
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References |
- Street MD, Donovan GR, Baldo BA. "Molecular cloning and characterization of the major allergen Myr p II from the venom of the jumper ant Myrmecia pilosula: Myr p I and Myr p II share a common protein leader sequence." Biochim Biophys Acta. 1996; 1305(1-2): 87-97. PubMed: 8605256
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Comments |
Additional entries may be required for some of the cleavage products.
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