T3D1B_PIRLC
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 25-MAY-2022, entry version 79.
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}.
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DR PDB; 1V91; NMR; -; A=1-37.
DR PDBsum; 1V91; -.
DR AlphaFoldDB; 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: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 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-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
