TX22G_PLETR
ID TX22G_PLETR Reviewed; 82 AA.
AC P36983;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=U1-plectoxin-Pt1a {ECO:0000305};
DE Short=U1-PLTX-Pt1a {ECO:0000305};
DE AltName: Full=PLT-V/PLT-VI;
DE Short=PLTVI;
DE AltName: Full=Plectoxin V/VI;
DE AltName: Full=Plectoxin-5/6;
DE Flags: Precursor;
OS Plectreurys tristis (Spider) (Plectreurys bispinosus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Haplogynae; Pholcoidea; Plectreuridae; Plectreurys.
OX NCBI_TaxID=33319;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=8763160; DOI=10.1016/0965-1748(95)00070-4;
RA Leisy D.J., Mattson J.D., Quistad G.B., Kramer S.J., van Beek N.,
RA Tsai L.W., Enderlin F.E., Woodworth A.R., Digan M.E.;
RT "Molecular cloning and sequencing of cDNAs encoding insecticidal peptides
RT from the primitive hunting spider, Plectreurys tristis (Simon).";
RL Insect Biochem. Mol. Biol. 26:411-417(1996).
RN [2]
RP PROTEIN SEQUENCE OF 34-79, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8157635; DOI=10.1016/s0021-9258(19)78096-x;
RA Quistad G.B., Skinner W.S.;
RT "Isolation and sequencing of insecticidal peptides from the primitive
RT hunting spider, Plectreurys tristis (Simon).";
RL J. Biol. Chem. 269:11098-11101(1994).
CC -!- FUNCTION: Potent toxin that may paralyze and/or kill insect pests such
CC as H.virescens (lepidoptera), S.exigua (beet armyworm) and M.sexta
CC (tobacco hornworm).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8157635}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:8157635}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- PTM: Plectoxin-5 presumably undergoes post-translational modification
CC to give rise to plectoxin-6.
CC -!- SIMILARITY: Belongs to the neurotoxin 02 (plectoxin) family. 02
CC (plectoxin) subfamily. {ECO:0000305}.
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DR EMBL; U29269; AAC47200.1; -; mRNA.
DR EMBL; U29271; AAC47202.1; -; mRNA.
DR EMBL; U29272; AAC47203.1; -; mRNA.
DR EMBL; U29273; AAC47204.1; -; mRNA.
DR EMBL; U29274; AAC47205.1; -; mRNA.
DR EMBL; U29275; AAC47206.1; -; mRNA.
DR EMBL; U29276; AAC47207.1; -; mRNA.
DR PIR; A53613; A53613.
DR AlphaFoldDB; P36983; -.
DR SMR; P36983; -.
DR ArachnoServer; AS000405; U1-plectoxin-Pt1a.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR004169; Spidertoxin.
DR Pfam; PF02819; Toxin_9; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Knottin; Lipoprotein;
KW Neurotoxin; Palmitate; Secreted; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..33
FT /evidence="ECO:0000269|PubMed:8157635"
FT /id="PRO_0000035533"
FT CHAIN 34..79
FT /note="U1-plectoxin-Pt1a"
FT /evidence="ECO:0000269|PubMed:8157635"
FT /id="PRO_0000035534"
FT PROPEP 80..82
FT /id="PRO_0000035535"
FT LIPID 79
FT /note="O-palmitoyl serine"
FT /evidence="ECO:0000250|UniProtKB:P34079"
FT DISULFID 37..51
FT /evidence="ECO:0000250|UniProtKB:P83559"
FT DISULFID 44..57
FT /evidence="ECO:0000250|UniProtKB:P83559"
FT DISULFID 50..68
FT /evidence="ECO:0000250|UniProtKB:P83559"
FT DISULFID 54..77
FT /evidence="ECO:0000250|UniProtKB:P83559"
FT DISULFID 59..66
FT /evidence="ECO:0000250|UniProtKB:P83559"
FT VARIANT 6..7
FT /note="FS -> LA (in clones PSCI267, PSCI268, PSCI270 and
FT PSCI272)"
FT VARIANT 11
FT /note="V -> I (in clones PSCI268, PSCI270 and PSCI272)"
FT VARIANT 19
FT /note="F -> S (in clones PSCI268, PSCI270 and PSCI272)"
SQ SEQUENCE 82 AA; 9241 MW; F744A5703BC77965 CRC64;
MKHLIFSSAL VCALVVCTFA EEQVNVPFLP DERAVKCIGW QETCNGNLPC CNECVMCECN
IMGQNCRCNH PKATNECESR RR