TX90B_PHONI
ID TX90B_PHONI Reviewed; 90 AA.
AC P81792;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Omega-ctenitoxin-Pn4a {ECO:0000305};
DE Short=Omega-CNTX-Pn4a {ECO:0000305};
DE AltName: Full=CTK 01512-2 {ECO:0000303|PubMed:27759880};
DE AltName: Full=Neurotoxin Tx3-6 {ECO:0000303|PubMed:16278100, ECO:0000303|PubMed:8446961};
DE Short=PnTx3-6 {ECO:0000303|PubMed:16278100};
DE AltName: Full=Ph-alpha-1-beta toxin {ECO:0000303|PubMed:18774645};
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=12782075; DOI=10.1016/s0041-0101(03)00011-4;
RA Cardoso F.C., Pacifico L.G., Carvalho D.C., Victoria J.M.N., Neves A.L.G.,
RA Chavez-Olortegui C., Gomez M.V., Kalapothakis E.;
RT "Molecular cloning and characterization of Phoneutria nigriventer toxins
RT active on calcium channels.";
RL Toxicon 41:755-763(2003).
RN [2]
RP PROTEIN SEQUENCE OF 36-90, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8446961; DOI=10.1016/0041-0101(93)90354-l;
RA Cordeiro M.N., De Figueiredo S.G., Valentim A.D.C., Diniz C.R.,
RA von Eickstedt V.R.D., Gilroy J., Richardson M.;
RT "Purification and amino acid sequences of six Tx3 type neurotoxins from the
RT venom of the Brazilian 'armed' spider Phoneutria nigriventer (Keys).";
RL Toxicon 31:35-42(1993).
RN [3]
RP PROTEIN SEQUENCE OF 36-90, SUBCELLULAR LOCATION, AND MASS 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).
RN [4]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=12470700; DOI=10.1016/s0197-0186(02)00130-4;
RA Vieira L.B., Kushmerick C., Reis H.J., Diniz C.R., Cordeiro M.N.,
RA Prado M.A.M., Kalapothakis E., Romano-Silva M.A., Gomez M.V.;
RT "PnTx3-6 a spider neurotoxin inhibits K+-evoked increase in [Ca2+](i) and
RT Ca2+-dependent glutamate release in synaptosomes.";
RL Neurochem. Int. 42:277-282(2003).
RN [5]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=15933156; DOI=10.1124/jpet.105.087023;
RA Vieira L.B., Kushmerick C., Hildebrand M.E., Garcia E., Stea A.,
RA Cordeiro M.N., Richardson M., Gomez M.V., Snutch T.P.;
RT "Inhibition of high voltage-activated calcium channels by spider toxin
RT PnTx3-6.";
RL J. Pharmacol. Exp. Ther. 314:1370-1377(2005).
RN [6]
RP FUNCTION, AND BIOASSAY.
RX PubMed=18774645; DOI=10.1016/j.pain.2008.07.014;
RA Souza A.H., Ferreira J., Cordeiro Mdo N., Vieira L.B., De Castro C.J.,
RA Trevisan G., Reis H., Souza I.A., Richardson M., Prado M.A., Prado V.F.,
RA Gomez M.V.;
RT "Analgesic effect in rodents of native and recombinant Ph alpha 1beta
RT toxin, a high-voltage-activated calcium channel blocker isolated from armed
RT spider venom.";
RL Pain 140:115-126(2008).
RN [7]
RP FUNCTION.
RX PubMed=27759880; DOI=10.1111/bph.13652;
RA Tonello R., Fusi C., Materazzi S., Marone I.M., De Logu F., Benemei S.,
RA Goncalves M.C., Coppi E., Castro-Junior C.J., Gomez M.V., Geppetti P.,
RA Ferreira J., Nassini R.;
RT "The peptide Phalpha1beta, from spider venom, acts as a TRPA1 channel
RT antagonist with antinociceptive effects in mice.";
RL Br. J. Pharmacol. 174:57-69(2017).
CC -!- FUNCTION: Potent blocker of nociceptor cation channels TRPA1 and high
CC voltage-activated calcium channels (PubMed:12470700, PubMed:15933156,
CC PubMed:27759880). It acts mainly on P/Q-type (Cav2.1/CACNA1A) calcium
CC channels and has a minor effect on L- (Cav1/CACNA1) and N-type
CC (Cav2.2/CACNA1B) calcium channels (PubMed:12470700, PubMed:15933156).
CC Blocks glutamate release in synaptic transmission mediated by calcium
CC channels (PubMed:12470700). The toxin also inhibits the KCl-induced
CC increase of intrasynaptosomal free calcium (PubMed:12470700). In vivo,
CC it shows analgesic effects in rodent models of pain (PubMed:18774645).
CC In addition, it selectively blocks nocifensive responses evoked by
CC reactive TRPA1 channel agonist (PubMed:27759880). Furthermore, it also
CC reduces the TRPA1 channel-dependent hyperalgesia in a model of
CC neuropathic pain induced by the chemotherapeutic agent BTZ
CC (PubMed:27759880). {ECO:0000269|PubMed:12470700,
CC ECO:0000269|PubMed:15933156, ECO:0000269|PubMed:18774645}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16278100,
CC ECO:0000269|PubMed:8446961}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:16278100, ECO:0000305|PubMed:8446961}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=6035.5; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:16278100};
CC -!- MISCELLANEOUS: Does not target TRPV1 and TRPV4 channels.
CC {ECO:0000269|PubMed:27759880}.
CC -!- SIMILARITY: Belongs to the neurotoxin 09 (Tx3-6) family. {ECO:0000305}.
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DR PIR; F44336; F44336.
DR AlphaFoldDB; P81792; -.
DR SMR; P81792; -.
DR TCDB; 8.B.12.1.5; the spider toxin (stx2) family.
DR ArachnoServer; AS000269; omega-ctenitoxin-Pn4a.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated calcium channel impairing toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..34
FT /evidence="ECO:0000269|PubMed:16278100,
FT ECO:0000269|PubMed:8446961"
FT /id="PRO_0000285665"
FT CHAIN 36..90
FT /note="Omega-ctenitoxin-Pn4a"
FT /evidence="ECO:0000269|PubMed:16278100,
FT ECO:0000269|PubMed:8446961"
FT /id="PRO_0000087641"
FT DISULFID 37..51
FT /evidence="ECO:0000305"
FT DISULFID 44..57
FT /evidence="ECO:0000305"
FT DISULFID 50..72
FT /evidence="ECO:0000305"
FT DISULFID 59..70
FT /evidence="ECO:0000305"
FT DISULFID 80..87
FT /evidence="ECO:0000305"
SQ SEQUENCE 90 AA; 9926 MW; 4CA8F736205AB105 CRC64;
MKCAVLFLSV IALVHIFVVE AEEEPDSDAL VPQERACIPR GEICTDDCEC CGCDNQCYCP
PGSSLGIFKC SCAHANKYFC NRKKEKCKKA
