ID   LITD_LATHA              Reviewed;          71 AA.
AC   P0DJE6;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Delta-latroinsectotoxin-Lh1a {ECO:0000305};
DE            Short=Delta-LIT-Lh1a {ECO:0000305};
DE   AltName: Full=Delta-latroinsectotoxin {ECO:0000303|PubMed:22001442};
DE            Short=Delta-LIT {ECO:0000303|PubMed:22001442};
DE   Flags: Fragments;
OS   Latrodectus hasselti (Redback spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Araneoidea; Theridiidae; Latrodectus.
OX   NCBI_TaxID=256736;
RN   [1]
RP   PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom;
RX   PubMed=22001442; DOI=10.1016/j.bcp.2011.09.024;
RA   Graudins A., Little M.J., Pineda S.S., Hains P.G., King G.F., Broady K.W.,
RA   Nicholson G.M.;
RT   "Cloning and activity of a novel alpha-latrotoxin from red-back spider
RT   venom.";
RL   Biochem. Pharmacol. 83:170-183(2012).
CC   -!- FUNCTION: Insecticidal presynaptic neurotoxin that induces massive
CC       neurotransmitter release at insect (but not vertebrate) neuromuscular
CC       junctions. Native toxin forms cation-permeable pores (with high
CC       permeability to calcium) in lipid membranes locust muscle membrane and
CC       artificial lipid bilayers (By similarity). May bind to insect neurexin-
CC       1 homolog, insect adhesion G protein-coupled receptor L1 homolog, and
CC       insect receptor-type tyrosine-protein phosphatase S homolog, and
CC       induces neurotransmitter exocytosis both by forming tetrameric pores in
CC       membranes and signaling via G protein-coupled receptor (By similarity).
CC       Oligomerization is a process independent of divalent cations (By
CC       similarity). {ECO:0000250|UniProtKB:P23631,
CC       ECO:0000250|UniProtKB:Q25338}.
CC   -!- SUBUNIT: Homotetramer in membrane. {ECO:0000250|UniProtKB:Q25338}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22001442}. Target
CC       cell membrane {ECO:0000250|UniProtKB:Q25338}. Note=Forms a membrane
CC       channel in the prey. {ECO:0000250|UniProtKB:Q25338}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:22001442}.
CC   -!- DOMAIN: Two helices (H2 and H8) are predicted to insert into membranes
CC       and form pores by assembling into tetramers. The helices are contained
CC       within a helical bundle domain that undergoes significant
CC       conformational changes during pore formation to allow exposure of the
CC       transmembrane helices and transition of the toxin from a soluble
CC       monomer to a transmembrane tetramer. {ECO:0000250|UniProtKB:Q9XZC0}.
CC   -!- MISCELLANEOUS: Iso and Leu residues are assigned by comparison with
CC       orthologs.
CC   -!- SIMILARITY: Belongs to the cationic peptide 01 (latrotoxin) family. 04
CC       (delta-latroinsectotoxin) subfamily. {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   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   ANK repeat; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Exocytosis; Membrane; Neurotoxin; Presynaptic neurotoxin; Repeat; Secreted;
KW   Target cell membrane; Target membrane; Toxin; Transmembrane.
FT   CHAIN           <1..>71
FT                   /note="Delta-latroinsectotoxin-Lh1a"
FT                   /id="PRO_0000415935"
FT   REPEAT          <25..>36
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255, ECO:0000305"
FT   REPEAT          <37..45
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255, ECO:0000305"
FT   REPEAT          47..>57
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000255, ECO:0000305"
FT   REPEAT          <58..>62
FT                   /note="ANK 4"
FT                   /evidence="ECO:0000255, ECO:0000305"
FT   REPEAT          <63..>71
FT                   /note="ANK 5"
FT                   /evidence="ECO:0000255, ECO:0000305"
FT   NON_CONS        12..13
FT                   /evidence="ECO:0000305"
FT   NON_CONS        24..25
FT                   /evidence="ECO:0000305"
FT   NON_CONS        36..37
FT                   /evidence="ECO:0000305"
FT   NON_CONS        46..47
FT                   /evidence="ECO:0000305"
FT   NON_CONS        57..58
FT                   /evidence="ECO:0000305"
FT   NON_CONS        62..63
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         71
SQ   SEQUENCE   71 AA;  7923 MW;  7C2069531B07B01F CRC64;
     DEEDGEMTLE ERFSEWSEPX TVQGAVDEAE ALLIEKINHX XDVNAKDNLT PLHSAAKTAL
     HAINDDLDMV R