CTX13_LACTA
ID CTX13_LACTA Reviewed; 129 AA.
AC P85255; B3W6I1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=M-zodatoxin-Lt8c;
DE Short=M-ZDTX-Lt8c;
DE AltName: Full=Cytoinsectotoxin-1c {ECO:0000303|PubMed:18215128};
DE Short=CIT-1c {ECO:0000303|PubMed:18215128};
DE Flags: Precursor;
GN Name=cit 1-3;
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=7892.4; 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; FM165476; CAQ63552.1; -; mRNA.
DR AlphaFoldDB; P85255; -.
DR SMR; P85255; -.
DR ArachnoServer; AS000552; M-zodatoxin-Lt8c.
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_0000366076"
FT CHAIN 61..129
FT /note="M-zodatoxin-Lt8c"
FT /id="PRO_0000337160"
FT MOTIF 57..60
FT /note="Processing quadruplet motif"
FT /evidence="ECO:0000303|PubMed:27287558"
SQ SEQUENCE 129 AA; 14548 MW; A546EF7EF532A2B1 CRC64;
MKYFVVALAL VAAFACIAES KPAESEHELA EVEEENELAD LEDAVWLEHL ADLSDLEEAR
GFFGNTWKKI KGKADKIMLK KAVKIMVKKE GISKEEAQAK VDAMSKKQIR LYVLKYYGKK
ALQKASEKL
