ID T3D1B_PIRLC Reviewed; 37 AA. AC P83257; DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 20-JUN-2018, entry version 72. DE RecName: Full=Delta-amaurobitoxin-Pl1b; DE Short=Delta-AMATX-Pl1b; DE AltName: Full=Delta-palutoxin IT2 {ECO:0000303|PubMed:10971590}; DE Short=Delta-paluIT2 {ECO:0000303|PubMed:10971590}; OS Pireneitega luctuosa (Tangled nest spider) (Paracoelotes luctuosus). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Araneae; Araneomorphae; Entelegynae; Amaurobiidae; Pireneitega. OX NCBI_TaxID=185217; RN [1] RP PROTEIN SEQUENCE, FUNCTION, AMIDATION AT SER-37, AND MASS RP SPECTROMETRY. RC TISSUE=Venom; RX PubMed=10971590; DOI=10.1046/j.1432-1327.2000.01653.x; RA Corzo G., Escoubas P., Stankiewicz M., Pelhate M., Kristensen C.P., RA Nakajima T.; RT "Isolation, synthesis and pharmacological characterization of delta- RT palutoxins IT, novel insecticidal toxins from the spider Paracoelotes RT luctuosus (Amaurobiidae)."; RL Eur. J. Biochem. 267:5783-5795(2000). RN [2] RP FUNCTION, TOXIC DOSE, SYNTHESIS, MUTAGENESIS OF VAL-3; ASP-5; GLN-7; RP ARG-8; ARG-8; SER-11; TRP-12; TRP-12; SER-13; TYR-16; ASP-19; TYR-21; RP TYR-22; SER-24; ARG-26; MET-28; TYR-30; ARG-32; ARG-34; ASN-35; ASN-36 RP AND SER-37, AND SITE. RX PubMed=15683238; DOI=10.1021/bi048434k; RA Corzo G., Escoubas P., Villegas E., Karbat I., Gordon D., Gurevitz M., RA Nakajima T., Gilles N.; RT "A spider toxin that induces a typical effect of scorpion alpha-toxins RT but competes with beta-toxins on binding to insect sodium channels."; RL Biochemistry 44:1542-1549(2005). RN [3] RP STRUCTURE BY NMR, AND DISULFIDE BOND. RX PubMed=15726637; DOI=10.1002/prot.20424; RA Ferrat G., Bosmans F., Tytgat J., Pimentel C., Chagot B., Gilles N., RA Nakajima T., Darbon H., Corzo G.; RT "Solution structure of two insect-specific spider toxins and their RT pharmacological interaction with the insect voltage-gated Na+ RT channel."; RL Proteins 59:368-379(2005). CC -!- FUNCTION: Insecticidal toxin. Lethal to lepidopteran larvae. No CC adverse affects when intracerebroventricularly injected in mice at CC a dose of 0.2 ug but causes reversible paralysis of legs when CC injected intracerebroventricularly in mice at a dose of 2.0 ug. CC Binds to site 4 of insect voltage-gated sodium channel (Nav) and CC inhibits channel inactivation. {ECO:0000269|PubMed:10971590, CC ECO:0000269|PubMed:15683238}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000269|PubMed:10971590}. CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot' CC structurally defines this protein as a knottin. CC -!- MASS SPECTROMETRY: Mass=4114.6; Method=MALDI; Range=1-37; CC Evidence={ECO:0000269|PubMed:10971590}; CC -!- TOXIC DOSE: LD(50) is 24.2 ng/mg body weight of lepidoptera CC larvae. {ECO:0000269|PubMed:15683238}. CC -!- SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. CC 02 (aga-3) subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PDB; 1V91; NMR; -; A=1-37. DR PDBsum; 1V91; -. DR ProteinModelPortal; P83257; -. DR SMR; P83257; -. DR ArachnoServer; AS000302; delta-Amaurobitoxin-Pl1b. DR EvolutionaryTrace; P83257; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0019871; F:sodium channel inhibitor activity; IDA:UniProtKB. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IDA:UniProtKB. DR InterPro; IPR016328; Beta/delta-agatoxin_fam. DR PIRSF; PIRSF001882; Curtatoxin; 1. DR PROSITE; PS60015; MU_AGATOXIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Amidation; Direct protein sequencing; Disulfide bond; KW Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Toxin; KW Voltage-gated sodium channel impairing toxin. FT PEPTIDE 1 37 Delta-amaurobitoxin-Pl1b. FT /FTId=PRO_0000044962. FT SITE 8 8 Pharmacophore. FT SITE 12 12 Pharmacophore. FT SITE 19 19 May be involved in voltage sensor FT trapping upon activation of sodium FT channel. {ECO:0000269|PubMed:15726637}. FT SITE 22 22 Pharmacophore. FT SITE 24 24 Pharmacophore. FT SITE 26 26 Pharmacophore. FT SITE 28 28 Pharmacophore. FT SITE 30 30 Pharmacophore. FT SITE 32 32 Pharmacophore. FT SITE 34 34 Pharmacophore. FT MOD_RES 37 37 Serine amide. FT {ECO:0000269|PubMed:10971590}. FT DISULFID 2 18 {ECO:0000269|PubMed:15726637}. FT DISULFID 9 23 {ECO:0000269|PubMed:15726637}. FT DISULFID 17 33 {ECO:0000269|PubMed:15726637}. FT DISULFID 25 31 {ECO:0000269|PubMed:15726637}. FT MUTAGEN 3 3 V->A: Nonsignificant differences nor in FT binding affinity neither in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 5 5 D->A: Nonsignificant differences nor in FT binding affinity neither in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 7 7 Q->A: Nonsignificant differences nor in FT binding affinity neither in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 8 8 R->A: 51-fold decrease in binding FT affinity and nonsignificant differences FT in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 8 8 R->D: More than 80-fold decrease in FT binding affinity and 5-fold decrease in FT toxicity. {ECO:0000269|PubMed:15683238}. FT MUTAGEN 11 11 S->A: Nonsignificant differences nor in FT binding affinity neither in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 12 12 W->A: More than 160-fold decrease in FT binding affinity and nonsignificant FT differences in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 12 12 W->F: 13.5-fold decrease in binding FT affinity and more than 8-fold decrease in FT toxicity. {ECO:0000269|PubMed:15683238}. FT MUTAGEN 13 13 S->A: Nonsignificant differences nor in FT binding affinity neither in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 16 16 Y->A: Nonsignificant differences nor in FT binding affinity neither in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 19 19 D->A: Nonsignificant differences in FT binding affinity and 2.9-fold decrease in FT toxicity. {ECO:0000269|PubMed:15683238}. FT MUTAGEN 21 21 Y->A: Nonsignificant differences nor in FT binding affinity neither in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 22 22 Y->A: 54-fold decrease in binding FT affinity and nonsignificant differences FT in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 24 24 S->A: 40-fold decrease in binding FT affinity and nonsignificant differences FT in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 26 26 R->A: 16-fold decrease in binding FT affinity and nonsignificant differences FT in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 28 28 M->A: 28-fold decrease in binding FT affinity and nonsignificant differences FT in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 30 30 Y->A: 58-fold decrease in binding FT affinity and 5.1-fold decrease in FT toxicity. {ECO:0000269|PubMed:15683238}. FT MUTAGEN 30 30 Y->F: 16-fold decrease in binding FT affinity and nonsignificant differences FT in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 32 32 R->A: 24-fold decrease in binding FT affinity and 2.3-fold decrease in FT toxicity. {ECO:0000269|PubMed:15683238}. FT MUTAGEN 34 34 R->A: 18-fold decrease in binding FT affinity and nonsignificant differences FT in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 35 35 N->A: Nonsignificant differences nor in FT binding affinity neither in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 36 36 N->A: Nonsignificant differences nor in FT binding affinity neither in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT MUTAGEN 37 37 S->A: Nonsignificant differences nor in FT binding affinity neither in lethal dose. FT {ECO:0000269|PubMed:15683238}. FT STRAND 5 8 {ECO:0000244|PDB:1V91}. FT TURN 11 13 {ECO:0000244|PDB:1V91}. FT STRAND 22 24 {ECO:0000244|PDB:1V91}. FT STRAND 27 30 {ECO:0000244|PDB:1V91}. FT STRAND 32 34 {ECO:0000244|PDB:1V91}. SQ SEQUENCE 37 AA; 4124 MW; 861E12C2EB547716 CRC64; ACVGDGQRCA SWSGPYCCDG YYCSCRSMPY CRCRNNS //