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1.C.81.1.1
Arenicin-1 precursor (202 aas). The processed pore-forming β-hairpin antimicrobial peptide corresponds to residues 182-202 (Andrä et al., 2008; Shenkarev et al., 2011). Low-conductivity pores were detected in the phosphatidylethanolamine-containing lipids and high-conductivity pores in anionic lipids. The measured conductivity levels agreed with the model in which arenicin antimicrobial activity was mediated by the formation of toroidal pores assembled of two, three, or four β-structural peptide dimers and lipid molecules (Shenkarev et al., 2011). 

Accession Number:Q5SC60
Protein Name:Arenicin-1
Length:202
Molecular Weight:22497.00
Species:Arenicola marina (Lugworm) (Rock worm) [6344]
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate molecule

Cross database links:

Pfam: PF04089   

Gene Ontology

GO:0042742 P:defense response to bacterium
GO:0050832 P:defense response to fungus
GO:0031640 P:killing of cells of another organism

References (1)

[1] “Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina.”  Ovchinnikova T.V.et.al.   15527787
Structure:
2JSB   5M9U     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MTSTQSVAVC ATLILAIFCV NDIHCDPIAE ARAAAFGERE ARSDGEWKQF DVNGEKIEVN 
61:	EQENREIIRQ AGGDGVEGSV MVIDHAKGLI SWSIPRAGEC YLIGGVDKQL PDAQELLHYF 
121:	QSAQGSADGE GVESALDYVK AEDRPVTDLN LLAPEVREAC QGKSVYWLEK SSGDNNEPEK 
181:	RRWCVYAYVR VRGVLVRYRR CW