ID   TX22B_PLETR             Reviewed;          61 AA.
AC   P36984; Q27912;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=U1-plectoxin-Pt1b {ECO:0000305};
DE            Short=U1-PLTX-Pt1b {ECO:0000305};
DE   AltName: Full=Plectoxin VIII;
DE            Short=PLT-VIII;
DE            Short=PLTVIII;
DE   AltName: Full=Plectoxin-8;
DE   Flags: Precursor; Fragment;
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 14-59, 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   -!- SIMILARITY: Belongs to the neurotoxin 02 (plectoxin) family. 02
CC       (plectoxin) subfamily. {ECO:0000305}.
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DR   EMBL; U29277; AAC47208.1; -; mRNA.
DR   AlphaFoldDB; P36984; -.
DR   SMR; P36984; -.
DR   ArachnoServer; AS000409; U1-plectoxin-Pt1b.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036836; Agouti_dom_sf.
DR   InterPro; IPR004169; Spidertoxin.
DR   Pfam; PF02819; Toxin_9; 1.
DR   SUPFAM; SSF57055; SSF57055; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Knottin; Neurotoxin; Secreted;
KW   Toxin.
FT   PROPEP          <1..13
FT                   /evidence="ECO:0000269|PubMed:8157635"
FT                   /id="PRO_0000035536"
FT   CHAIN           14..59
FT                   /note="U1-plectoxin-Pt1b"
FT                   /evidence="ECO:0000269|PubMed:8157635"
FT                   /id="PRO_0000035537"
FT   PROPEP          60..61
FT                   /id="PRO_0000035538"
FT   DISULFID        17..31
FT                   /evidence="ECO:0000250|UniProtKB:P83559"
FT   DISULFID        24..37
FT                   /evidence="ECO:0000250|UniProtKB:P83559"
FT   DISULFID        30..48
FT                   /evidence="ECO:0000250|UniProtKB:P83559"
FT   DISULFID        34..57
FT                   /evidence="ECO:0000250|UniProtKB:P83559"
FT   DISULFID        39..46
FT                   /evidence="ECO:0000250|UniProtKB:P83559"
FT   CONFLICT        27
FT                   /note="Q -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   61 AA;  6853 MW;  DA80929F2FBDEC3C CRC64;
     EEQVNVPFLP DERAVKCIGW QETCNGQLPC CDGCVMCECN IMGQNCRCNH PKMTSECGSR
     R