LITD_LATHE
ID LITD_LATHE Reviewed; 147 AA.
AC P0DJE7;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Delta-latroinsectotoxin-Lhe1a {ECO:0000305};
DE Short=Delta-LIT-Lhe1a {ECO:0000305};
DE AltName: Full=Delta-latroinsectotoxin {ECO:0000303|PubMed:22001442};
DE Short=Delta-LIT {ECO:0000303|PubMed:22001442};
DE Flags: Fragments;
OS Latrodectus hesperus (Western black widow spider).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Araneoidea; Theridiidae; Latrodectus.
OX NCBI_TaxID=256737;
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}.
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DR AlphaFoldDB; P0DJE7; -.
DR SMR; P0DJE7; -.
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:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR SUPFAM; SSF48403; SSF48403; 1.
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..>147
FT /note="Delta-latroinsectotoxin-Lhe1a"
FT /id="PRO_0000415936"
FT REPEAT <57..59
FT /note="ANK 7"
FT /evidence="ECO:0000255, ECO:0000305"
FT REPEAT 66..>78
FT /note="ANK 8"
FT /evidence="ECO:0000255, ECO:0000305"
FT REPEAT <79..96
FT /note="ANK 10"
FT /evidence="ECO:0000255, ECO:0000305"
FT REPEAT <98..125
FT /note="ANK 14"
FT /evidence="ECO:0000255, ECO:0000305"
FT NON_CONS 25..26
FT /evidence="ECO:0000305"
FT NON_CONS 56..57
FT /evidence="ECO:0000305"
FT NON_CONS 78..79
FT /evidence="ECO:0000305"
FT NON_CONS 97..98
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 147
SQ SEQUENCE 147 AA; 16531 MW; A349F281725EA804 CRC64;
EPSGNSLSSA LNELLDKNNN YAIPKVAIIF DDFKSSLTGG DDGLIDNVIE VLNTVKVSIN
SVTENNNWTP LHFAIYFKKN PAVSAVLILE NKDIEARTSI MLIVQKLLLE LYNYFINNYA
ETLDEEALFN RLDEQGKLEL ALIMHNK
