UniProt functional annotation for P0CH43



	UniProt functional annotation for P0CH43

UniProt code: P0CH43.

Organism: Cyriopagopus schmidti (Chinese bird spider) (Haplopelma schmidti).

Taxonomy: Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae; Mygalomorphae; Theraphosidae; Haplopelma.

Function: Selectively activates the heat-activated TRPV1 channel. It binds to TRPV1 in an open state-dependent manner, trapping it there to produce irreversible currents (PubMed:20510930, PubMed:26880553, PubMed:27281200). It binds to the outer edge of the external pore of TRPV1 in a counterclockwise configuration, using a limited protein- protein interface and inserting hydrophobic residues into the bilayer (PubMed:26880553, PubMed:27281200). It also partitions naturally into membranes, with the two lobes exhibiting opposing energetics for membrane partitioning (K1) and channel activation (K2) (PubMed:26880553). In addition, the toxin disrupts a cluster of hydrophobic residues behind the selectivity filter that are critical for channel activation (PubMed:26880553). {ECO:0000269|PubMed:20510930, ECO:0000269|PubMed:26880553, ECO:0000269|PubMed:27281200}.

Subunit: Interacts with TRPV1 (2 toxins (4 moieties) bind 1 channel (homotetramer)). {ECO:0000269|PubMed:24305161}.

Subcellular location: Secreted {ECO:0000269|PubMed:20510930}.

Tissue specificity: Expressed by the venom gland. {ECO:0000305|PubMed:20510930}.

Domain: The presence of 'disulfide through disulfide knots' structurally defines this protein as a knottin. This toxin contains 2 'disulfide through disulfide knots' that are separated by a short linker. Bivalence accounts for irreversible toxin action. {ECO:0000269|PubMed:20510930}.

Similarity: Belongs to the neurotoxin 23 family. Double-knot toxin subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Cyriopagopus schmidti (Chinese bird spider) (Haplopelma schmidti).
Taxonomy:		Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae; Mygalomorphae; Theraphosidae; Haplopelma.



Function:		Selectively activates the heat-activated TRPV1 channel. It binds to TRPV1 in an open state-dependent manner, trapping it there to produce irreversible currents (PubMed:20510930, PubMed:26880553, PubMed:27281200). It binds to the outer edge of the external pore of TRPV1 in a counterclockwise configuration, using a limited protein- protein interface and inserting hydrophobic residues into the bilayer (PubMed:26880553, PubMed:27281200). It also partitions naturally into membranes, with the two lobes exhibiting opposing energetics for membrane partitioning (K1) and channel activation (K2) (PubMed:26880553). In addition, the toxin disrupts a cluster of hydrophobic residues behind the selectivity filter that are critical for channel activation (PubMed:26880553). {ECO:0000269\|PubMed:20510930, ECO:0000269\|PubMed:26880553, ECO:0000269\|PubMed:27281200}.


Subunit:		Interacts with TRPV1 (2 toxins (4 moieties) bind 1 channel (homotetramer)). {ECO:0000269\|PubMed:24305161}.
Subcellular location:		Secreted {ECO:0000269\|PubMed:20510930}.
Tissue specificity:		Expressed by the venom gland. {ECO:0000305\|PubMed:20510930}.
Domain:		The presence of 'disulfide through disulfide knots' structurally defines this protein as a knottin. This toxin contains 2 'disulfide through disulfide knots' that are separated by a short linker. Bivalence accounts for irreversible toxin action. {ECO:0000269\|PubMed:20510930}.
Similarity:		Belongs to the neurotoxin 23 family. Double-knot toxin subfamily. {ECO:0000305}.