ID   NTA_PSACA               Reviewed;          86 AA.
AC   P0C201;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=U1-theraphotoxin-Pc1a {ECO:0000305};
DE            Short=U1-TRTX-Pc1a {ECO:0000305};
DE   AltName: Full=Psalmopeotoxin I {ECO:0000303|PubMed:15304333};
DE   AltName: Full=Psalmopeotoxin-1 {ECO:0000305};
DE   AltName: Full=Psalmopoeus cambridgei Falciparum killer 1 {ECO:0000303|PubMed:16452619};
DE            Short=PcFK1 {ECO:0000303|PubMed:16452619};
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AMIDATION
RP   AT VAL-84, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=15304333; DOI=10.1016/j.febslet.2004.07.019;
RA   Choi S.-J., Parent R., Guillaume C., Deregnaucourt C., Delarbre C.,
RA   Ojcius D.M., Montagne J.-J., Celerier M.-L., Phelipot A., Amiche M.,
RA   Molgo J., Camadro J.-M., Guette C.;
RT   "Isolation and characterization of Psalmopeotoxin I and II: two novel
RT   antimalarial peptides from the venom of the tarantula Psalmopoeus
RT   cambridgei.";
RL   FEBS Lett. 572:109-117(2004).
RN   [2]
RP   STRUCTURE BY NMR OF 52-86, AND DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=16452619; DOI=10.1110/ps.051860606;
RA   Pimentel C., Choi S.-J., Chagot B., Guette C., Camadro J.-M., Darbon H.;
RT   "Solution structure of PcFK1, a spider peptide active against Plasmodium
RT   falciparum.";
RL   Protein Sci. 15:628-634(2006).
CC   -!- FUNCTION: Possesses strong antiplasmodial activity against the intra-
CC       erythrocyte stage of P.falciparum in vitro. IC(50) for inhibiting
CC       P.falciparum growth is 1.59 uM. Interacts with infected and healthy
CC       erythrocytes. Does not lyse erythrocytes, is not cytotoxic to nucleated
CC       mammalian cells, and does not inhibit neuromuscular function. Has
CC       neither antibacterial nor antifungal activity.
CC       {ECO:0000269|PubMed:15304333}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15304333}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15304333}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000269|PubMed:16452619}.
CC   -!- MASS SPECTROMETRY: Mass=3615.60; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15304333};
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family.
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DR   PDB; 1X5V; NMR; -; A=52-84.
DR   PDBsum; 1X5V; -.
DR   AlphaFoldDB; P0C201; -.
DR   BMRB; P0C201; -.
DR   SMR; P0C201; -.
DR   ArachnoServer; AS000318; U1-theraphotoxin-Pc1a.
DR   EvolutionaryTrace; P0C201; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Knottin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..49
FT                   /evidence="ECO:0000305|PubMed:15304333"
FT                   /id="PRO_0000256694"
FT   CHAIN           52..84
FT                   /note="U1-theraphotoxin-Pc1a"
FT                   /evidence="ECO:0000305|PubMed:15304333"
FT                   /id="PRO_0000256695"
FT   MOD_RES         84
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:15304333"
FT   DISULFID        53..70
FT                   /evidence="ECO:0000269|PubMed:16452619,
FT                   ECO:0000312|PDB:1X5V"
FT   DISULFID        60..75
FT                   /evidence="ECO:0000269|PubMed:16452619,
FT                   ECO:0000312|PDB:1X5V"
FT   DISULFID        69..80
FT                   /evidence="ECO:0000269|PubMed:16452619,
FT                   ECO:0000312|PDB:1X5V"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:1X5V"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:1X5V"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:1X5V"
SQ   SEQUENCE   86 AA;  9719 MW;  9E63221359955A21 CRC64;
     MMRVLIVTAV FTFFLVLTSS GHDEDNEQRN ILEGMFLDRA IETPKGLEEK RACGILHDNC
     VYVPAQNPCC RGLQCRYGKC LVQVGR