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 28-JUN-2023, entry version 81. 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; Araneae; OC Araneomorphae; Entelegynae; Agelenidae; Pireneitega. OX NCBI_TaxID=185217; RN [1] RP PROTEIN SEQUENCE, FUNCTION, AMIDATION AT SER-37, AND MASS 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; ARG-8; RP ARG-8; SER-11; TRP-12; TRP-12; SER-13; TYR-16; ASP-19; TYR-21; TYR-22; RP SER-24; ARG-26; MET-28; TYR-30; ARG-32; ARG-34; ASN-35; ASN-36 AND SER-37, RP 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 but RT 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+ channel."; RL Proteins 59:368-379(2005). CC -!- FUNCTION: Insecticidal toxin. Lethal to lepidopteran larvae. No adverse CC affects when intracerebroventricularly injected in mice at a dose of CC 0.2 ug but causes reversible paralysis of legs when injected CC intracerebroventricularly in mice at a dose of 2.0 ug. Binds to site 4 CC of insect voltage-gated sodium channel (Nav) and inhibits channel CC 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; CC Evidence={ECO:0000269|PubMed:10971590}; CC -!- TOXIC DOSE: LD(50) is 24.2 ng/mg body weight of lepidoptera larvae. CC {ECO:0000269|PubMed:15683238}. CC -!- SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. 02 CC (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 AlphaFoldDB; P83257; -. DR SMR; P83257; -. DR TCDB; 8.B.6.1.9; the ca(2+) channel-targeting spider toxin (cst) family. DR ArachnoServer; AS000302; delta-Amaurobitoxin-Pl1b. DR EvolutionaryTrace; P83257; -. 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; IDA:UniProtKB. DR GO; GO:0035821; P:modulation of process of another organism; IDA:UniProtKB. DR InterPro; IPR016328; Beta/delta-agatoxin_fam. DR Pfam; PF05980; Toxin_7; 1. DR PIRSF; PIRSF001882; Curtatoxin; 1. DR SUPFAM; SSF57059; omega toxin-like; 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 FT /note="Delta-amaurobitoxin-Pl1b" FT /id="PRO_0000044962" FT SITE 8 FT /note="Pharmacophore" FT SITE 12 FT /note="Pharmacophore" FT SITE 19 FT /note="May be involved in voltage sensor trapping upon FT activation of sodium channel" FT /evidence="ECO:0000269|PubMed:15726637" FT SITE 22 FT /note="Pharmacophore" FT SITE 24 FT /note="Pharmacophore" FT SITE 26 FT /note="Pharmacophore" FT SITE 28 FT /note="Pharmacophore" FT SITE 30 FT /note="Pharmacophore" FT SITE 32 FT /note="Pharmacophore" FT SITE 34 FT /note="Pharmacophore" FT MOD_RES 37 FT /note="Serine amide" FT /evidence="ECO:0000269|PubMed:10971590" FT DISULFID 2..18 FT /evidence="ECO:0000269|PubMed:15726637" FT DISULFID 9..23 FT /evidence="ECO:0000269|PubMed:15726637" FT DISULFID 17..33 FT /evidence="ECO:0000269|PubMed:15726637" FT DISULFID 25..31 FT /evidence="ECO:0000269|PubMed:15726637" FT MUTAGEN 3 FT /note="V->A: Nonsignificant differences nor in binding FT affinity neither in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 5 FT /note="D->A: Nonsignificant differences nor in binding FT affinity neither in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 7 FT /note="Q->A: Nonsignificant differences nor in binding FT affinity neither in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 8 FT /note="R->A: 51-fold decrease in binding affinity and FT nonsignificant differences in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 8 FT /note="R->D: More than 80-fold decrease in binding affinity FT and 5-fold decrease in toxicity." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 11 FT /note="S->A: Nonsignificant differences nor in binding FT affinity neither in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 12 FT /note="W->A: More than 160-fold decrease in binding FT affinity and nonsignificant differences in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 12 FT /note="W->F: 13.5-fold decrease in binding affinity and FT more than 8-fold decrease in toxicity." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 13 FT /note="S->A: Nonsignificant differences nor in binding FT affinity neither in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 16 FT /note="Y->A: Nonsignificant differences nor in binding FT affinity neither in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 19 FT /note="D->A: Nonsignificant differences in binding affinity FT and 2.9-fold decrease in toxicity." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 21 FT /note="Y->A: Nonsignificant differences nor in binding FT affinity neither in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 22 FT /note="Y->A: 54-fold decrease in binding affinity and FT nonsignificant differences in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 24 FT /note="S->A: 40-fold decrease in binding affinity and FT nonsignificant differences in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 26 FT /note="R->A: 16-fold decrease in binding affinity and FT nonsignificant differences in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 28 FT /note="M->A: 28-fold decrease in binding affinity and FT nonsignificant differences in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 30 FT /note="Y->A: 58-fold decrease in binding affinity and 5.1- FT fold decrease in toxicity." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 30 FT /note="Y->F: 16-fold decrease in binding affinity and FT nonsignificant differences in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 32 FT /note="R->A: 24-fold decrease in binding affinity and 2.3- FT fold decrease in toxicity." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 34 FT /note="R->A: 18-fold decrease in binding affinity and FT nonsignificant differences in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 35 FT /note="N->A: Nonsignificant differences nor in binding FT affinity neither in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 36 FT /note="N->A: Nonsignificant differences nor in binding FT affinity neither in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT MUTAGEN 37 FT /note="S->A: Nonsignificant differences nor in binding FT affinity neither in lethal dose." FT /evidence="ECO:0000269|PubMed:15683238" FT STRAND 5..8 FT /evidence="ECO:0007829|PDB:1V91" FT TURN 11..13 FT /evidence="ECO:0007829|PDB:1V91" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:1V91" FT STRAND 27..30 FT /evidence="ECO:0007829|PDB:1V91" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:1V91" SQ SEQUENCE 37 AA; 4124 MW; 861E12C2EB547716 CRC64; ACVGDGQRCA SWSGPYCCDG YYCSCRSMPY CRCRNNS //