ID   TXP1_PYETR              Reviewed;         279 AA.
AC   P20798;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 3.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Toxin TxP-I;
DE   AltName: Full=Tox34;
DE   Flags: Precursor;
OS   Pyemotes tritici (Straw itch mite) (Acarus tritici).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Heterostigmata;
OC   Pyemotoidea; Pyemotidae; Pyemotes.
OX   NCBI_TaxID=6950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1840646; DOI=10.1038/352082a0;
RA   Tomalski M.D., Miller L.K.;
RT   "Insect paralysis by baculovirus-mediated expression of a mite neurotoxin
RT   gene.";
RL   Nature 352:82-85(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 28-48.
RX   PubMed=2815110; DOI=10.1016/0041-0101(89)90009-3;
RA   Tomalski M.D., Kutney R., Bruce W.A., Brown M.R., Blum M.S., Travis J.;
RT   "Purification and characterization of insect toxins derived from the mite,
RT   Pyemotes tritici.";
RL   Toxicon 27:1151-1167(1989).
CC   -!- FUNCTION: Part of a complex mixture of neurotoxins which P.tritici
CC       utilizes to capture prey. It has contracting-paralyzing activity in
CC       insects.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Posterior glands which appear to be connected with
CC       the stylet through a series of ducts.
CC   -!- PTM: Contains several disulfide bonds.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA29802.1; Type=Erroneous initiation; Evidence={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   EMBL; M68863; AAA29802.1; ALT_INIT; mRNA.
DR   PIR; S16950; S16950.
DR   AlphaFoldDB; P20798; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR016329; Neurotoxin_TxP-I.
DR   PIRSF; PIRSF001883; Neurotoxin_TxP-I; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Neurotoxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   PROPEP          15..27
FT                   /evidence="ECO:0000269|PubMed:2815110"
FT                   /id="PRO_0000035170"
FT   CHAIN           28..279
FT                   /note="Toxin TxP-I"
FT                   /id="PRO_0000035171"
SQ   SEQUENCE   279 AA;  31676 MW;  731DAFF388C841EC CRC64;
     MNLFFLFIIP TILAVKPFRS FNNISLIDNG NVESVRAVVI DYCDIRHPNN LCKKHFEIDS
     YWNDDTDCFT NIGCKVYGGF DIIGGHTPKV GTVCRLKKGE NKFGYCNSKG NCVERDFKES
     FGISIKIKGI SNKGDDEPAC PQYKNTWINY GKCNEPYYCG TNHGLFYANK RKLDYFPTDG
     EKCNSNNIPY AVCYLGRCHT TGGFFSEFGT IVKNVEIVTL SDGKNSSRRG KHKNLPTSKV
     FDSYSIYDID PKNWKIEDDD KDVTVHENTL DPKSDSRLC