LAT3A_LACTA
ID LAT3A_LACTA Reviewed; 82 AA.
AC Q1ELU3;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=M-zodatoxin-Lt3a {ECO:0000305};
DE Short=M-ZDTX-Lt3a {ECO:0000305};
DE AltName: Full=La47;
DE AltName: Full=Latarcin-3a {ECO:0000303|PubMed:16735513};
DE Short=Ltc-3a {ECO:0000303|PubMed:16735513};
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 62-81, SYNTHESIS OF 62-81,
RP AMIDATION AT ALA-81, FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MASS
RP 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 PROTEIN SEQUENCE OF 62-81, MASS SPECTROMETRY, FUNCTION, SUBCELLULAR
RP LOCATION, AND CIRCULAR DICHROISM.
RC TISSUE=Venom;
RX PubMed=23093034; DOI=10.1038/ja.2012.87;
RA Garcia F., Villegas E., Espino-Solis G.P., Rodriguez A.,
RA Paniagua-Solis J.F., Sandoval-Lopez G., Possani L.D., Corzo G.;
RT "Antimicrobial peptides from arachnid venoms and their microbicidal
RT activity in the presence of commercial antibiotics.";
RL J. Antibiot. 66:3-10(2013).
RN [3]
RP SUBCELLULAR LOCATION, PQM MOTIF, MASS SPECTROMETRY, AND AMIDATION AT
RP ALA-81.
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).
CC -!- FUNCTION: It has antimicrobial activity against Gram-positive bacteria
CC (A.globiformis VKM Ac-1112 (MIC=0.3 uM), and B.subtilis VKM B-501
CC (MIC=1.2 uM)), Gram-negative bacteria (E.coli DH5-alpha (MIC=2.5 uM),
CC E.coli MH1 (MIC=6.0 uM), and P.aeruginosa PAO1 (MIC>40 uM)), and yeasts
CC (P.pastoris GS115 (MIC=20 uM), and S.cerevisiae Y190 (MIC=20 uM)).
CC Causes paralysis, but is not lethal when injected into insect
CC (M.domestica) larvae (PubMed:16735513). A second study reports
CC antibacterial activity against E.coli (MIC=100 uM) and S.aureus (MIC=84
CC uM). Furthermore, increases efficacy of antibiotics (chloramphenicol,
CC streptomycin, kanamycin, novobiocin) when tested against E.coli,
CC probably by facilitating their incorporation into the bacteria
CC (PubMed:23093034). {ECO:0000269|PubMed:16735513,
CC ECO:0000269|PubMed:23093034}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16735513,
CC ECO:0000269|PubMed:23093034, ECO:0000269|PubMed:27287558}. Target cell
CC membrane {ECO:0000305|PubMed:23093034}. Note=Forms a helical membrane
CC channel in the prey. {ECO:0000305|PubMed:23093034}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:23093034}.
CC -!- DOMAIN: The mature peptide (62-81) 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=2481.7; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16735513};
CC -!- MASS SPECTROMETRY: Mass=2484.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:23093034};
CC -!- MASS SPECTROMETRY: Mass=2483.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:27287558};
CC -!- MISCELLANEOUS: Does not have hemolytic activity against rabbit and
CC human erythrocytes. {ECO:0000269|PubMed:16735513,
CC ECO:0000269|PubMed:23093034}.
CC -!- SIMILARITY: Belongs to the cationic peptide 03 (latarcin) family. 03
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: PubMed:23093034 describes a peptide from Lachesana sp. Since
CC the sequence is identical with a peptide from L.tarabaevi and the genus
CC is the same, it is probable that the peptide is from this species.
CC {ECO:0000305}.
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DR EMBL; AM232696; CAJ81656.1; -; mRNA.
DR AlphaFoldDB; Q1ELU3; -.
DR SMR; Q1ELU3; -.
DR ArachnoServer; AS000052; M-zodatoxin-Lt3a.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR InterPro; IPR018802; Latarcin_precursor.
DR Pfam; PF10279; Latarcin; 1.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Direct protein sequencing; Fungicide;
KW Membrane; Secreted; Signal; Target cell membrane; Target membrane; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..61
FT /evidence="ECO:0000255, ECO:0000269|PubMed:16735513,
FT ECO:0000269|PubMed:23093034"
FT /id="PRO_0000249740"
FT PEPTIDE 62..81
FT /note="M-zodatoxin-Lt3a"
FT /evidence="ECO:0000269|PubMed:16735513,
FT ECO:0000269|PubMed:23093034"
FT /id="PRO_0000249741"
FT MOTIF 58..61
FT /note="Processing quadruplet motif"
FT /evidence="ECO:0000303|PubMed:23093034"
FT MOD_RES 81
FT /note="Alanine amide"
FT /evidence="ECO:0000269|PubMed:16735513,
FT ECO:0000269|PubMed:23093034"
SQ SEQUENCE 82 AA; 9417 MW; CAAE22B6EC63755C CRC64;
MKTYAVLLAL VVAFVCIAES TGYPVEDLED DELTELEAEA LLEDLLEDLE LEDLDYNEEA
RSWKSMAKKL KEYMEKLKQR AG
