T3D1A_PIRLC
ID T3D1A_PIRLC Reviewed; 37 AA.
AC P83256;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Delta-amaurobitoxin-Pl1a {ECO:0000303|PubMed:24486516};
DE Short=Delta-AMATX-Pl1a {ECO:0000305};
DE AltName: Full=Delta-palutoxin IT1 {ECO:0000303|PubMed:10971590};
DE Short=Delta-paluIT1 {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, SYNTHESIS, FUNCTION, DISULFIDE BONDS, AMIDATION AT
RP SER-37, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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 BIOTECHNOLOGY, AND RECOMBINANT EXPRESSION AS A CHIMERIC VARIANT.
RX PubMed=24486516; DOI=10.1016/j.ibmb.2014.01.007;
RA Yang S., Pyati P., Fitches E., Gatehouse J.A.;
RT "A recombinant fusion protein containing a spider toxin specific for the
RT insect voltage-gated sodium ion channel shows oral toxicity towards insects
RT of different orders.";
RL Insect Biochem. Mol. Biol. 47:1-11(2014).
RN [3]
RP STRUCTURE BY NMR, DISULFIDE BONDS, AND SYNTHESIS.
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: Binds at site 4 of sodium channels (Nav) and inhibits the
CC fast inactivation of cockroach channels. This toxin is active only on
CC insects. Has a potent activity against S.litura larvae.
CC {ECO:0000269|PubMed:10971590}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10971590}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:10971590}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=4037.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10971590};
CC -!- BIOTECHNOLOGY: Could be considered as a biological insecticide
CC candidate, when fused to Galanthus nivalis agglutinin (GNA), a protein
CC with the potential to cross the insect gut. This chimeric Pl1a/GNA
CC variant shows a gain in toxicity against insects when administered
CC orally, while maintaining similar effects as the wild-type toxin when
CC injected. Transport of Pl1a/GNA variant from gut contents to the
CC hemolymph of cabbage moth larvae, and binding to the nerve chord, has
CC been shown. This variant has been found to be orally toxic against
CC cabbage moth (Mamestra brassicae), housefly (Musca domestica), and the
CC hemipteran Acyrthosiphon pisum. {ECO:0000305|PubMed:24486516}.
CC -!- SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. 02
CC (aga-3) subfamily. {ECO:0000305}.
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DR PIR; A59401; A59401.
DR PDB; 1V90; NMR; -; A=1-37.
DR PDBsum; 1V90; -.
DR AlphaFoldDB; P83256; -.
DR SMR; P83256; -.
DR ArachnoServer; AS000301; delta-Amaurobitoxin-Pl1a.
DR EvolutionaryTrace; P83256; -.
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; IDA:UniProtKB.
DR GO; GO:0044489; P:negative regulation of voltage-gated sodium channel activity in another organism; 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
FT /note="Delta-amaurobitoxin-Pl1a"
FT /evidence="ECO:0000269|PubMed:10971590"
FT /id="PRO_0000044961"
FT SITE 8
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT SITE 12
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT SITE 22
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT SITE 24
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT SITE 26
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT SITE 28
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT SITE 30
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT SITE 32
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT SITE 34
FT /note="Pharmacophore"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:10971590"
FT DISULFID 2..18
FT /evidence="ECO:0000269|PubMed:10971590,
FT ECO:0000269|PubMed:15726637, ECO:0007744|PDB:1V90"
FT DISULFID 9..23
FT /evidence="ECO:0000269|PubMed:10971590,
FT ECO:0000269|PubMed:15726637, ECO:0007744|PDB:1V90"
FT DISULFID 17..33
FT /evidence="ECO:0000269|PubMed:10971590,
FT ECO:0000269|PubMed:15726637, ECO:0007744|PDB:1V90"
FT DISULFID 25..31
FT /evidence="ECO:0000269|PubMed:10971590,
FT ECO:0000269|PubMed:15726637, ECO:0007744|PDB:1V90"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1V90"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1V90"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1V90"
SQ SEQUENCE 37 AA; 4047 MW; E019DABCC25BC11E CRC64;
GCLGEGEKCA DWSGPSCCDG FYCSCRSMPY CRCRNNS
