ID   TX2_PSACA               Reviewed;          35 AA.
AC   P0C245;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Tau-theraphotoxin-Pc1b;
DE            Short=Tau-TRTX-Pc1b;
DE   AltName: Full=Vanillotoxin-2 {ECO:0000303|PubMed:17093448};
DE            Short=VaTx2 {ECO:0000303|PubMed:17093448};
OS   Psalmopoeus cambridgei (Trinidad chevron tarantula).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Psalmopoeus.
OX   NCBI_TaxID=179874;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, TOXIN TARGET, MASS SPECTROMETRY, SUBCELLULAR
RP   LOCATION, AND AMIDATION AT PHE-35.
RC   TISSUE=Venom;
RX   PubMed=17093448; DOI=10.1038/nature05285;
RA   Siemens J., Zhou S., Piskorowski R., Nikai T., Lumpkin E.A., Basbaum A.I.,
RA   King D., Julius D.;
RT   "Spider toxins activate the capsaicin receptor to produce inflammatory
RT   pain.";
RL   Nature 444:208-212(2006).
CC   -!- FUNCTION: Selectively activates the mammalian capsaicin receptor TRPV1,
CC       a non-selective cation channel expressed by sensory neurons of the pain
CC       pathway. Is more potent than VaTx1, but less potent than VaTx3.
CC       Interacts with distinct regions of the channel than capsaicin, since it
CC       only acts on the extracellular face of the channel, and capsaicin binds
CC       to the cytosolic side. Also activates avian TRPV1, which is insensitive
CC       to capsaicin. Produce weak inhibition on potassium channels
CC       Kv2.1/KCNB1. {ECO:0000269|PubMed:17093448}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17093448}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17093448}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P60992}.
CC   -!- MASS SPECTROMETRY: Mass=3842.0; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:17093448};
CC   -!- MISCELLANEOUS: This toxin does not have effect on TRPV2, TRPV3, TRPV4,
CC       TRPA1, TRPM8, Kv1.2/KCNA2 or Kv4.2/KCND2.
CC       {ECO:0000269|PubMed:17093448}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 62 (Vatx)
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C245; -.
DR   SMR; P0C245; -.
DR   ArachnoServer; AS000252; tau-theraphotoxin-Pc1b.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011696; Huwentoxin-1.
DR   Pfam; PF07740; Toxin_12; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   CHAIN           1..35
FT                   /note="Tau-theraphotoxin-Pc1b"
FT                   /evidence="ECO:0000269|PubMed:17093448"
FT                   /id="PRO_0000262452"
FT   MOD_RES         35
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:17093448"
FT   DISULFID        3..17
FT                   /evidence="ECO:0000250|UniProtKB:P60992"
FT   DISULFID        10..22
FT                   /evidence="ECO:0000250|UniProtKB:P60992"
FT   DISULFID        16..29
FT                   /evidence="ECO:0000250|UniProtKB:P60992"
SQ   SEQUENCE   35 AA;  3852 MW;  B70E717ED06107D1 CRC64;
     GACRWFLGGC KSTSDCCEHL SCKMGLDYCA WDGTF