ID   TX1_PSACA               Reviewed;          35 AA.
AC   P0C244;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Tau/kappa-theraphotoxin-Pc1a;
DE            Short=Tau/kappa-TRTX-Pc1a;
DE   AltName: Full=Vanillotoxin-1 {ECO:0000303|PubMed:17093448};
DE            Short=VaTx1 {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 mammalian TRPV1, the capsaicin
CC       receptor, a non-selective cation channel expressed by sensory neurons
CC       of the pain pathway. Is less potent than VaTx2 and VaTx3. Interacts
CC       with distinct regions of the channel than capsaicin, since it only acts
CC       on the extracellular face of the channel, and capsaicin binds to the
CC       cytosolic side. Also activates avian TRPV1, which is insensitive to
CC       capsaicin. Significantly inhibits potassium channels Kv2.1/KCNB1.
CC       {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=4008.5; 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 and 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; P0C244; -.
DR   SMR; P0C244; -.
DR   TCDB; 8.B.5.3.1; the na(+)/k(+)/ca(2+) channel targeting tarantula huwentoxin (tht) family.
DR   ArachnoServer; AS000226; tau/kappa-theraphotoxin-Pc1a.
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/kappa-theraphotoxin-Pc1a"
FT                   /evidence="ECO:0000269|PubMed:17093448"
FT                   /id="PRO_0000262451"
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;  4019 MW;  A2DB3EA9D0A77A01 CRC64;
     SECRWFMGGC DSTLDCCKHL SCKMGLYYCA WDGTF