LITA_LATHA
ID LITA_LATHA Reviewed; 151 AA.
AC P0DJE5;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Alpha-latroinsectotoxin-Lh1a {ECO:0000305};
DE Short=Alpha-LIT-Lh1a {ECO:0000305};
DE AltName: Full=Alpha-latroinsectotoxin {ECO:0000303|PubMed:22001442};
DE Short=Alpha-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). The toxin forms channels with 0.55-0.58 nm entrance
CC diameter and a relatively small conductance in planar phospholipid
CC membranes (By similarity). {ECO:0000250|UniProtKB:P23631,
CC ECO:0000250|UniProtKB:Q02989, ECO:0000250|UniProtKB:Q25338}.
CC -!- SUBUNIT: Homotetramer in membranes. {ECO:0000250|UniProtKB:Q02989}.
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: The H8 helix is predicted to insert into membranes and form
CC pores by assembling into tetramers. The helix is contained within a
CC helical bundle domain that undergoes significant conformational changes
CC during pore formation to allow exposure of the H8 transmembrane helix
CC and transition of the toxin from a soluble monomer to a transmembrane
CC 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. 02
CC (alpha-latroinsectotoxin) subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DJE5; -.
DR SMR; P0DJE5; -.
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.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 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..>151
FT /note="Alpha-latroinsectotoxin-Lh1a"
FT /id="PRO_0000415934"
FT REPEAT <21..37
FT /note="ANK 1"
FT /evidence="ECO:0000255, ECO:0000305"
FT REPEAT <41..52
FT /note="ANK 2"
FT /evidence="ECO:0000255, ECO:0000305"
FT REPEAT 56..80
FT /note="ANK 3"
FT /evidence="ECO:0000255, ECO:0000305"
FT REPEAT 84..>104
FT /note="ANK 4"
FT /evidence="ECO:0000255, ECO:0000305"
FT REPEAT <105..>116
FT /note="ANK 5"
FT /evidence="ECO:0000255, ECO:0000305"
FT REPEAT <117..>125
FT /note="ANK 6"
FT /evidence="ECO:0000255, ECO:0000305"
FT REPEAT <126..>146
FT /note="ANK 7"
FT /evidence="ECO:0000255, ECO:0000305"
FT REPEAT <147..>151
FT /note="ANK 8"
FT /evidence="ECO:0000255, ECO:0000305"
FT NON_CONS 12..13
FT /evidence="ECO:0000305"
FT NON_CONS 20..21
FT /evidence="ECO:0000305"
FT NON_CONS 40..41
FT /evidence="ECO:0000305"
FT NON_CONS 74..75
FT /evidence="ECO:0000305"
FT NON_CONS 104..105
FT /evidence="ECO:0000305"
FT NON_CONS 116..117
FT /evidence="ECO:0000305"
FT NON_CONS 125..126
FT /evidence="ECO:0000305"
FT NON_CONS 146..147
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 151
SQ SEQUENCE 151 AA; 16680 MW; DEFFA2424553EA5B CRC64;
LVIETIENIA TKLSISISFK TDVTQTLIDI TEIDLNAQDK ILIRNTNAVI NIKSKVGLTP
LHLATLQNNL SVSKGAYLND GDANGMTPLH YAAMTGNLEM VDFLKWTPLH LAILFKQLVI
ELLAKTFFDL AIENGRLNIV AFAVEKYIAA R
