TX36B_PHONI
ID TX36B_PHONI Reviewed; 82 AA.
AC O76199; P29424;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Delta-ctenitoxin-Pn2c {ECO:0000305};
DE Short=Delta-CNTX-Pn2c {ECO:0000305};
DE AltName: Full=Neurotoxin Pn2-5A {ECO:0000303|PubMed:9839668};
DE AltName: Full=Neurotoxin Tx2-5 {ECO:0000303|PubMed:1397265, ECO:0000303|PubMed:19231838, ECO:0000303|PubMed:9839668};
DE Short=PnTx2-5 {ECO:0000303|PubMed:19231838};
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=9839668; DOI=10.1016/s0041-0101(98)00105-6;
RA Kalapothakis E., Penaforte C.L., Beirao P.S.L., Romano-Silva M.A.,
RA Cruz J.S., Prado M.A.M., Guimaraes P.E.M., Gomez M.V., Prado V.F.;
RT "Cloning of cDNAS encoding neurotoxic peptides from the spider Phoneutria
RT nigriventer.";
RL Toxicon 36:1843-1850(1998).
RN [2]
RP PROTEIN SEQUENCE OF 35-82, FUNCTION, AND SUBCELLULAR LOCATION.
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 [3]
RP PROTEIN SEQUENCE OF 35-82, FUNCTION, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19231838; DOI=10.1021/bi802158p;
RA Matavel A., Fleury C., Oliveira L.C., Molina F., de Lima M.E., Cruz J.S.,
RA Cordeiro M.N., Richardson M., Ramos C.H., Beirao P.S.;
RT "Structure and activity analysis of two spider toxins that alter sodium
RT channel inactivation kinetics.";
RL Biochemistry 48:3078-3088(2009).
RN [4]
RP PROTEIN SEQUENCE OF 35-81, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP BIOASSAY.
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 [5]
RP PROTEIN SEQUENCE OF 35-44.
RC TISSUE=Venom;
RX PubMed=1801316; DOI=10.1016/0041-0101(91)90195-w;
RA Rezende L. Jr., Cordeiro M.N., Oliveira E.B., Diniz C.R.;
RT "Isolation of neurotoxic peptides from the venom of the 'armed' spider
RT Phoneutria nigriventer.";
RL Toxicon 29:1225-1233(1991).
RN [6]
RP PROTEIN SEQUENCE OF 35-39, FUNCTION, AND BIOASSAY.
RX PubMed=15246765; DOI=10.1016/j.toxicon.2004.05.016;
RA Yonamine C.M., Troncone L.R., Camillo M.A.;
RT "Blockade of neuronal nitric oxide synthase abolishes the toxic effects of
RT Tx2-5, a lethal Phoneutria nigriventer spider toxin.";
RL Toxicon 44:169-172(2004).
CC -!- FUNCTION: Reversible inhibitor of voltage-gated sodium channels (Nav).
CC Delays the fast inactivation kinetics of neuronal-type sodium channels.
CC In vivo, it induces rat penile erection (PubMed:15246765). This effect
CC may be due to the neuronal nitric oxide synthase (NOS1), since one of
CC its selective inhibitor completely abolishes all the toxic effects of
CC the toxin (PubMed:15246765). This toxin also causes scratching,
CC lacrimation, hypersalivation, sweating and agitation followed by
CC spastic paralysis of the anterior and posterior extremities and death
CC at dose levels of 0.24 mg/mouse (PubMed:1397265, PubMed:16278100,
CC PubMed:15246765). It is also insecticidal to the larval and adult forms
CC of the house fly (PubMed:1397265). {ECO:0000269|PubMed:1397265,
CC ECO:0000269|PubMed:15246765, ECO:0000269|PubMed:16278100,
CC ECO:0000269|PubMed:19231838}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1397265,
CC ECO:0000269|PubMed:16278100, ECO:0000269|PubMed:19231838}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:1397265, ECO:0000305|PubMed:16278100,
CC ECO:0000305|PubMed:19231838}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=5116.6; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:16278100};
CC -!- MASS SPECTROMETRY: Mass=5112.31; Mass_error=0.41; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19231838};
CC -!- SIMILARITY: Belongs to the neurotoxin 03 (Tx2) family. 06 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF014463; AAC26165.1; -; mRNA.
DR PIR; S29215; S29215.
DR AlphaFoldDB; O76199; -.
DR TCDB; 8.B.12.1.1; the spider toxin (stx2) family.
DR ArachnoServer; AS000242; delta-ctenitoxin-Pn2b.
DR ArachnoServer; AS000241; delta-ctenitoxin-Pn2c.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR035285; CNTX.
DR Pfam; PF17492; D_CNTX; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Knottin; Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..34
FT /evidence="ECO:0000269|PubMed:1397265,
FT ECO:0000269|PubMed:16278100, ECO:0000269|PubMed:1801316,
FT ECO:0000269|PubMed:19231838"
FT /id="PRO_0000035504"
FT CHAIN 35..82
FT /note="Delta-ctenitoxin-Pn2c"
FT /evidence="ECO:0000269|PubMed:1397265,
FT ECO:0000269|PubMed:19231838"
FT /id="PRO_0000035505"
FT DISULFID 37..51
FT /evidence="ECO:0000305"
FT DISULFID 44..57
FT /evidence="ECO:0000305"
FT DISULFID 48..80
FT /evidence="ECO:0000305"
FT DISULFID 50..65
FT /evidence="ECO:0000305"
FT DISULFID 59..63
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="W -> A (in Ref. 2; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="K -> KC (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 82 AA; 8856 MW; 11DAF1EBE78B318F CRC64;
MKVAILFLSI LVLAVASESI EESRDDFAVE ELGRATCAGQ DQTCKVTCDC CGERGECVCG
GPCICRQGNF LIAWYKLASC KK
