8.B.33.  The TRPA1-activating Peptide, Tx Ueg-12-1 (Tx-Ueg) Family 

This toxin potentiates activation of mammalian TRPA1, a non-selective cation channel involved in perception of pain.  It has an analgesic and anti-inflammatory effect in vivo. It also has antibacterial activity against C. glutamicum (MIC=50 μM) and, to a lesser extent, against S. aureus but not against P. aeruginosa or  E. coli (Logashina et al. 2017). It has been detected in mucus secreted from ectoderm. It has no effect on mammalian TRPV1 orTRPV3. It is said to belongs to the Cnidaria small cysteine-rich protein (SCRiP) family. {ECO:0000305}, but BLAST against the NCBI database does not bring up close homologues.


This family belongs to the Defensin Superfamily.
 

References:

Logashina, Y.A., R.G. Solstad, K.S. Mineev, Y.V. Korolkova, I.V. Mosharova, I.A. Dyachenko, V.A. Palikov, Y.A. Palikova, A.N. Murashev, A.S. Arseniev, S.A. Kozlov, K. Stensvåg, T. Haug, and Y.A. Andreev. (2017). New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties. Toxins (Basel) 9:.
Examples:

TC#NameOrganismal TypeExample
8.B.33.1.1

Sea anemone peptide tau-AnmTx Ueq 12-1 of 45 aas.  The 3-D NMR structure is known (5LAH_A) and reveals an uncommon fold (Logashina et al. 2017).

Tau-AnmTx Ueq 12-1 of Urticina eques

 
8.B.33.1.2

Cyclotide psyleio A of 29 aas.

Cyclotide psyleio A of Psychotria brachyceras

 
8.B.33.1.3

Kalata-B15 of 29 aas.

Kalata-B15 of Oldenlandia affinis