TCDB is operated by the Saier Lab Bioinformatics Group

1.C.81 The Arenicin (Arenicin) Family

The solution structure and the mode of action of arenicin isoform 1, an antimicrobial peptide with a unique 18-residue loop structure, from the lugworm Arenicola marina have been elucidated (Andra et al., 2007). Arenicin folds into a two-stranded anti-parallel β-sheet. It exhibits high antibacterial activity against Gram-negative and positive bacteria, as well as yeast. Bacterial killing occurs within minutes and is accompanied by membrane permeabilisation, membrane detachment, and release of cytoplasmic constituents (Andra et al., 2007).

Arenicin is a hydrophilic protein, 202 aas long with a single N-terminal hydrophobic region. The last 21 residues (182-202 aas) form the processed active peptide. The protein also contains a BRICHOS domain (pfam 64089) found in proteins involved in dementia and cancer. The full length protein is homologous to the chondromodulin-1 precursor (P17404) also called 'leukocyte cell-derived chemotaxin-1' of H. sapiens.

References associated with 1.C.81 family:

Andrä, J., I. Jakovkin, J. Grötzinger, O. Hecht, A.D. Krasnosdembskaya, T. Goldmann, T. Gutsmann, and M. Leippe. (2008). Structure and mode of action of the antimicrobial peptide arenicin. Biochem. J. 410(1): 113-122. 17935487
Cegarra, C., C. Chaves, C. Déon, T.M. Do, B. Dumas, A. Frenzel, P. Kuhn, V. Roudieres, J.C. Guillemot, and D. Lesuisse. (2022). Exploring ITM2A as a new potential target for brain delivery. Fluids Barriers CNS 19: 25. 35313913
Gong, Y., J. Wu, H. Qiang, B. Liu, Z. Chi, T. Chen, B. Yin, X. Peng, and J. Yuan. (2008). BRI3 associates with SCG10 and attenuates NGF-induced neurite outgrowth in PC12 cells. BMB Rep 41: 287-293. 18452648
Mandal, A.K. and D.B. Mount. (2019). Interaction Between ITM2B and GLUT9 Links Urate Transport to Neurodegenerative Disorders. Front Physiol 10: 1323. 31695625
Martin, T.E., C.T. Powell, Z. Wang, S. Bhattacharyya, M.M. Walsh-Reitz, K. Agarwal, and F.G. Toback. (2003). A novel mitogenic protein that is highly expressed in cells of the gastric antrum mucosa. Am. J. Physiol. Gastrointest Liver Physiol 285: G332-343. 12851218
Martins, F., I. Santos, O.A.B. da Cruz E Silva, S. Tambaro, and S. Rebelo. (2021). The role of the integral type II transmembrane protein BRI2 in health and disease. Cell Mol Life Sci. [Epub: Ahead of Print] 34480585
Matsuda, S. and T. Senda. (2019). BRI2 as an anti-Alzheimer gene. Med Mol Morphol 52: 1-7. 29687167
Matsuda, S., Y. Matsuda, and L. D''Adamio. (2009). BRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2. J. Biol. Chem. 284: 15815-15825. 19366692
Mukherjee, S., N. Sengupta, A. Chaudhuri, I. Akbar, N. Singh, S. Chakraborty, A.R. Suryawanshi, A. Bhattacharyya, and A. Basu. (2018). PLVAP and GKN3 Are Two Critical Host Cell Receptors Which Facilitate Japanese Encephalitis Virus Entry Into Neuron.s. Sci Rep 8: 11784. 30082709
Shenkarev, Z.O., S.V. Balandin, K.I. Trunov, A.S. Paramonov, S.V. Sukhanov, L.I. Barsukov, A.S. Arseniev, and T.V. Ovchinnikova. (2011). Molecular mechanism of action of β-hairpin antimicrobial peptide arenicin: oligomeric structure in dodecylphosphocholine micelles and pore formation in planar lipid bilayers. Biochemistry 50: 6255-6265. 21627330
Van den Plas, D. and J. Merregaert. (2004). Constitutive overexpression of the integral membrane protein Itm2A enhances myogenic differentiation of C2C12 cells. Cell Biol Int 28: 199-207. 14984746
Wohlschlegel, J., M. Argentini, C. Michiels, C. Letellier, V. Forster, C. Condroyer, Z. He, G. Thuret, C. Zeitz, T. Léger, and I. Audo. (2021). First identification of ITM2B interactome in the human retina. Sci Rep 11: 17210. 34446781
Yao, W., T. Yin, M.D. Tambini, and L. D''Adamio. (2019). The Familial dementia gene ITM2b/BRI2 facilitates glutamate transmission via both presynaptic and postsynaptic mechanisms. Sci Rep 9: 4862. 30890756