ID   LAT1_LACTA              Reviewed;          88 AA.
AC   Q1ELT9;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=M-zodatoxin-Lt1a {ECO:0000305};
DE            Short=M-ZDTX-Lt1a {ECO:0000305};
DE   AltName: Full=Latarcin-1 {ECO:0000303|PubMed:16735513};
DE            Short=Ltc-1 {ECO:0000303|PubMed:16735513};
DE            Short=Ltc1;
DE   Flags: Precursor;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 63-87, SYNTHESIS OF 63-87,
RP   FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=16735513; DOI=10.1074/jbc.m602168200;
RA   Kozlov S.A., Vassilevski A.A., Feofanov A.V., Surovoy A.Y., Karpunin D.V.,
RA   Grishin E.V.;
RT   "Latarcins, antimicrobial and cytolytic peptides from the venom of the
RT   spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular
RT   diversity.";
RL   J. Biol. Chem. 281:20983-20992(2006).
RN   [2]
RP   SUBCELLULAR LOCATION, PQM MOTIF, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
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).
RN   [3]
RP   STRUCTURE BY NMR OF 63-88.
RX   PubMed=18293934; DOI=10.1021/bi702203w;
RA   Dubovskii P.V., Volynsky P.E., Polyansky A.A., Karpunin D.V., Chupin V.V.,
RA   Efremov R.G., Arseniev A.S.;
RT   "Three-dimensional structure/hydrophobicity of latarcins specifies their
RT   mode of membrane activity.";
RL   Biochemistry 47:3525-3533(2008).
CC   -!- FUNCTION: Has antimicrobial activity against Gram-positive bacteria
CC       (A.globiformis VKM Ac-1112 (MIC=0.5 uM), and B.subtilis VKM B-501
CC       (MIC=1.0 uM)), Gram-negative bacteria (E.coli DH5-alpha (MIC=1.0 uM),
CC       E.coli MH1 (MIC=0.7 uM), and P.aeruginosa PAO1 (MIC=4.1 uM)), and
CC       yeasts (P.pastoris GS115 (MIC=17 uM), and S.cerevisiae Y190 (MIC>33
CC       uM)). Has a moderate hemolytic activity against rabbit erythrocytes.
CC       Causes paralysis, but is not lethal when injected into insect
CC       (M.domestica) larvae. {ECO:0000269|PubMed:16735513}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16735513,
CC       ECO:0000269|PubMed:27287558}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:16735513}.
CC   -!- DOMAIN: The mature peptide (63-87) probably forms alpha-helices which
CC       disrupt target cell membranes. {ECO:0000303|PubMed:16735513}.
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=3071.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16735513};
CC   -!- MASS SPECTROMETRY: Mass=3074.0; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:27287558};
CC   -!- SIMILARITY: Belongs to the cationic peptide 03 (latarcin) family. 01
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AM232700; CAJ81660.1; -; mRNA.
DR   PDB; 2PCO; NMR; -; A=63-88.
DR   PDBsum; 2PCO; -.
DR   AlphaFoldDB; Q1ELT9; -.
DR   BMRB; Q1ELT9; -.
DR   SMR; Q1ELT9; -.
DR   ArachnoServer; AS000049; M-zodatoxin-Lt1a.
DR   EvolutionaryTrace; Q1ELT9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR018802; Latarcin_precursor.
DR   Pfam; PF10279; Latarcin; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Fungicide; Hemolysis; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..62
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:16735513"
FT                   /id="PRO_0000249734"
FT   PEPTIDE         63..87
FT                   /note="M-zodatoxin-Lt1a"
FT                   /id="PRO_0000249735"
FT   MOTIF           59..62
FT                   /note="Processing quadruplet motif"
FT                   /evidence="ECO:0000303|PubMed:27287558"
FT   HELIX           70..85
FT                   /evidence="ECO:0007829|PDB:2PCO"
SQ   SEQUENCE   88 AA;  10038 MW;  934F07A21BBA90C7 CRC64;
     MKYFVVALAL AVALVCIAES TAYDVNEELE NELDDLSDAA WLAKAAEDLQ ALDDFEESEE
     SRSMWSGMWR RKLKKLRNAL KKKLKGEK