ID   TX29_PHONI              Reviewed;          32 AA.
AC   P29426;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=U5-ctenitoxin-Pn1a;
DE            Short=U5-CNTX-Pn1a;
DE   AltName: Full=Neurotoxin Tx2-9;
OS   Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Lycosoidea; Ctenidae; Phoneutria.
OX   NCBI_TaxID=6918;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=1397265; DOI=10.1016/0014-5793(92)81318-g;
RA   Cordeiro M.N., Diniz C.R., Valentim A.D.C., von Eickstedt V.R.D.,
RA   Gilroy J., Richardson M.;
RT   "The purification and amino acid sequences of four Tx2 neurotoxins from the
RT   venom of the Brazilian 'armed' spider Phoneutria nigriventer (Keys).";
RL   FEBS Lett. 310:153-156(1992).
RN   [2]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=16278100; DOI=10.1016/j.cbpc.2005.09.010;
RA   Richardson M., Pimenta A.M., Bemquerer M.P., Santoro M.M., Beirao P.S.,
RA   Lima M.E., Figueiredo S.G., Bloch C. Jr., Vasconcelos E.A., Campos F.A.,
RA   Gomes P.C., Cordeiro M.N.;
RT   "Comparison of the partial proteomes of the venoms of Brazilian spiders of
RT   the genus Phoneutria.";
RL   Comp. Biochem. Physiol. 142:173-187(2006).
CC   -!- FUNCTION: Blocks voltage-gated sodium channels (Nav). Causes tail
CC       erection, scratching and a reduction in mobility at a dose level of
CC       1.40 mg/mouse. {ECO:0000269|PubMed:1397265}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1397265,
CC       ECO:0000269|PubMed:16278100}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:1397265, ECO:0000269|PubMed:16278100}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=3742.1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:1397265};
CC   -!- MASS SPECTROMETRY: Mass=3742.1; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:16278100};
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 60 (Tx2-9)
CC       subfamily. {ECO:0000305}.
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DR   PIR; S29217; S29217.
DR   AlphaFoldDB; P29426; -.
DR   SMR; P29426; -.
DR   ArachnoServer; AS000247; U5-ctenitoxin-Pn1a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0017080; F:sodium 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   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Knottin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..32
FT                   /note="U5-ctenitoxin-Pn1a"
FT                   /id="PRO_0000044968"
FT   DISULFID        3..16
FT                   /evidence="ECO:0000250"
FT   DISULFID        9..21
FT                   /evidence="ECO:0000250"
FT   DISULFID        15..30
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   32 AA;  3743 MW;  154479B421385568 CRC64;
     SFCIPFKPCK SDENCCKKFK CKTTGIVKLC RW