TXL1_PHONI
ID TXL1_PHONI Reviewed; 112 AA.
AC P17727;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Mu-ctenitoxin-Pn1a;
DE Short=Mu-CNTX-Pn1a;
DE AltName: Full=Toxin Tx1;
DE Short=PNTx1;
DE Short=PhTx1;
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=8340362; DOI=10.1016/s0021-9258(18)82260-8;
RA Diniz M.R.V., Paine M.J.I., Diniz C.R., Theakston R.D.G., Crampton J.M.;
RT "Sequence of the cDNA coding for the lethal neurotoxin Tx1 from the
RT Brazilian 'armed' spider Phoneutria nigriventer predicts the synthesis and
RT processing of a preprotoxin.";
RL J. Biol. Chem. 268:15340-15342(1993).
RN [2]
RP PROTEIN SEQUENCE OF 34-111, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP 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 [3]
RP PROTEIN SEQUENCE OF 34-110, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=2335228; DOI=10.1016/0014-5793(90)81386-3;
RA Diniz C.R., Cordeiro M.N., Rezende L. Jr., Kelly P., Fischer S.,
RA Reimann F., Oliveira E.B., Richardson M.;
RT "The purification and amino acid sequence of the lethal neurotoxin Tx1 from
RT the venom of the Brazilian 'armed' spider Phoneutria nigriventer.";
RL FEBS Lett. 263:251-253(1990).
RN [4]
RP PROTEIN SEQUENCE OF 34-43.
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 [5]
RP PROTEIN SEQUENCE OF 34-43, MASS SPECTROMETRY, AMIDATION AT GLY-111, AND
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=16505156; DOI=10.1124/mol.105.021147;
RA Martin-Moutot N., Mansuelle P., Alcaraz G., Dos Santos R.G., Cordeiro M.N.,
RA De Lima M.E., Seagar M., Van Renterghem C.;
RT "Phoneutria nigriventer toxin 1: a novel, state-dependent inhibitor of
RT neuronal sodium channels that interacts with mu-conotoxin binding sites.";
RL Mol. Pharmacol. 69:1931-1937(2006).
RN [6]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=9723834; DOI=10.1016/s0041-0101(98)00012-9;
RA Mattiello-Sverzut A.C., Fontana M.D., Diniz C.R., da Cruz-Hofling M.A.;
RT "Pathological changes induced by PhTx1 from Phoneutria nigriventer spider
RT venom in mouse skeletal muscle in vitro.";
RL Toxicon 36:1349-1361(1998).
RN [7]
RP ERRONEOUS FUNCTION.
RC TISSUE=Venom;
RX PubMed=10585642; DOI=10.1590/s0100-879x1999001200019;
RA Santos R.G., Diniz C.R., Cordeiro M.N., De Lima M.E.;
RT "Binding sites and actions of Tx1, a neurotoxin from the venom of the
RT spider Phoneutria nigriventer, in guinea pig ileum.";
RL Braz. J. Med. Biol. Res. 32:1565-1569(1999).
RN [8]
RP FUNCTION, MASS SPECTROMETRY, AND LACK OF AMIDATION AT GLY-111.
RC TISSUE=Venom;
RX PubMed=16908187; DOI=10.1016/j.pep.2006.06.012;
RA Diniz M.R.V., Theakston R.D.G., Crampton J.M., do Nascimento Cordeiro M.,
RA Pimenta A.M.C., De Lima M.E., Diniz C.R.;
RT "Functional expression and purification of recombinant Tx1, a sodium
RT channel blocker neurotoxin from the venom of the Brazilian 'armed' spider,
RT Phoneutria nigriventer.";
RL Protein Expr. Purif. 50:18-24(2006).
CC -!- FUNCTION: Reversible inhibitor of neuronal sodium channels (Nav1.2/
CC SCN2A) that binds in proximity to site 1 and displays increasing
CC affinity as the membrane potential is depolarized. Induces excitatory
CC symptoms and spastic paralysis in mice. {ECO:0000269|PubMed:16505156,
CC ECO:0000269|PubMed:16908187, ECO:0000269|PubMed:9723834}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16278100}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:16278100}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- PTM: Contains 7 disulfide bonds.
CC -!- MASS SPECTROMETRY: Mass=8600.4; Mass_error=1.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16505156};
CC -!- MASS SPECTROMETRY: Mass=8598.92; Mass_error=0.11; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16908187};
CC -!- MASS SPECTROMETRY: Mass=8594.6; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:16278100};
CC -!- TOXIC DOSE: LD(50) is 0.05 mg/kg by intracerebroventricular injection
CC into mice. {ECO:0000269|PubMed:2335228}.
CC -!- SIMILARITY: Belongs to the neurotoxin 04 (omega-agtx) family. 02 (Tx1)
CC subfamily. {ECO:0000305}.
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DR EMBL; X73155; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A47130; A47130.
DR AlphaFoldDB; P17727; -.
DR ArachnoServer; AS000356; mu-ctenitoxin-Pn1a.
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; IPR013605; Toxin_34.
DR Pfam; PF08396; Toxin_34; 1.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..33
FT /evidence="ECO:0000269|PubMed:16278100,
FT ECO:0000269|PubMed:16505156, ECO:0000269|PubMed:1801316,
FT ECO:0000269|PubMed:2335228"
FT /id="PRO_0000035492"
FT CHAIN 34..111
FT /note="Mu-ctenitoxin-Pn1a"
FT /id="PRO_0000035493"
FT MOD_RES 111
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:16505156"
FT DISULFID 39..56
FT /evidence="ECO:0000305"
FT DISULFID 46..62
FT /evidence="ECO:0000305"
FT DISULFID 53..85
FT /evidence="ECO:0000255"
FT DISULFID 55..73
FT /evidence="ECO:0000305"
FT DISULFID 64..71
FT /evidence="ECO:0000305"
FT DISULFID 91..106
FT /evidence="ECO:0000255"
FT DISULFID 102..110
FT /evidence="ECO:0000255"
FT CONFLICT 109
FT /note="N -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 112 AA; 12383 MW; 775F2AB1534D6496 CRC64;
MKLLGIFLVA SFAFVLSFGE EMIEGENPLE DQRAELTSCF PVGHECDGDA SNCNCCGDDV
YCGCGWGRWN CKCKVADQSY AYGICKDKVN CPNRHLWPAK VCKKPCRRNC GG
