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CTX15_LACTA
ID   CTX15_LACTA             Reviewed;         129 AA.
AC   P85257; B3W6I3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=M-zodatoxin-Lt8e;
DE            Short=M-ZDTX-Lt8e;
DE   AltName: Full=Cytoinsectotoxin-1e {ECO:0000303|PubMed:18215128};
DE            Short=CIT-1e {ECO:0000303|PubMed:18215128};
DE   Flags: Precursor;
GN   Name=cit 1-5;
OS   Lachesana tarabaevi (Spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Entelegynae incertae sedis; Zodariidae;
OC   Lachesana.
OX   NCBI_TaxID=379576;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 61-129, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom {ECO:0000269|PubMed:18215128}, and Venom gland;
RX   PubMed=18215128; DOI=10.1042/bj20071123;
RA   Vassilevski A.A., Kozlov S.A., Samsonova O.V., Egorova N.S., Karpunin D.V.,
RA   Pluzhnikov K.A., Feofanov A.V., Grishin E.V.;
RT   "Cyto-insectotoxins, a novel class of cytolytic and insecticidal peptides
RT   from spider venom.";
RL   Biochem. J. 411:687-696(2008).
RN   [2]
RP   SUBCELLULAR LOCATION, PQM MOTIF, AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:27287558};
RX   PubMed=27287558; DOI=10.1042/bcj20160436;
RA   Kuzmenkov A.I., Sachkova M.Y., Kovalchuk S.I., Grishin E.V.,
RA   Vassilevski A.A.;
RT   "Lachesana tarabaevi, an expert in membrane-active toxins.";
RL   Biochem. J. 473:2495-2506(2016).
CC   -!- FUNCTION: Insecticidal, cytolytic and antimicrobial peptide. Forms
CC       voltage-dependent, ion-permeable channels in membranes. At high
CC       concentration causes cell membrane lysis (By similarity).
CC       {ECO:0000250|UniProtKB:P85253}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18215128,
CC       ECO:0000269|PubMed:27287558}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:18215128}.
CC   -!- DOMAIN: Both the N-terminus (61-94) and the C-terminus (99-129) of the
CC       mature peptide form alpha-helices which probably disrupt target cell
CC       membranes. The linker region (95-98) probably derives from a processing
CC       quadruplet motif (PQM), found in propeptides of many zodatoxins,
CC       hinting at a fusion of two originally separate membrane-active
CC       peptides. {ECO:0000250|UniProtKB:P85253}.
CC   -!- PTM: Cleavage of the propeptide depends on the processing quadruplet
CC       motif (XXXR, with at least one of X being E).
CC       {ECO:0000303|PubMed:27287558}.
CC   -!- MASS SPECTROMETRY: Mass=7921.9; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:27287558};
CC   -!- SIMILARITY: Belongs to the cationic peptide 06 (cytoinsectotoxin)
CC       family. {ECO:0000305}.
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DR   EMBL; FM165478; CAQ63554.1; -; mRNA.
DR   AlphaFoldDB; P85257; -.
DR   SMR; P85257; -.
DR   ArachnoServer; AS000660; M-zodatoxin-Lt8e.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Hemolysis;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..60
FT                   /evidence="ECO:0000269|PubMed:18215128"
FT                   /id="PRO_0000366078"
FT   CHAIN           61..129
FT                   /note="M-zodatoxin-Lt8e"
FT                   /id="PRO_0000337162"
FT   MOTIF           57..60
FT                   /note="Processing quadruplet motif"
FT                   /evidence="ECO:0000303|PubMed:27287558"
SQ   SEQUENCE   129 AA;  14606 MW;  709C93487E5F1475 CRC64;
     MKYFVVALAL VAAFVCIAES KPAESEHELA EVEEENELAD LEDAVWLEHL ADLSDLEEAR
     GFFGNTWKKI KGKSDKIMLK KAVKIMVKKE GISKEEAQAK VDAMSKKQIR LYLLKYYGKK
     ALQKASEKL
 
 
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