LAT2A_LACTA
ID LAT2A_LACTA Reviewed; 84 AA.
AC Q1ELU1;
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-Lt2a {ECO:0000305};
DE Short=M-ZDTX-Lt2a {ECO:0000305};
DE AltName: Full=Latarcin-2a {ECO:0000303|PubMed:16735513};
DE Short=Ltc-2a {ECO:0000303|PubMed:16735513};
DE Short=Ltc2a;
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 59-84, SYNTHESIS OF 59-84,
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 59-84.
RX PubMed=16939228; DOI=10.1021/bi060635w;
RA Dubovskii P.V., Volynsky P.E., Polyansky A.A., Chupin V.V., Efremov R.G.,
RA Arseniev A.S.;
RT "Spatial structure and activity mechanism of a novel spider antimicrobial
RT peptide.";
RL Biochemistry 45:10759-10767(2006).
CC -!- FUNCTION: It has antimicrobial activity against Gram-positive bacteria
CC (A.globiformis VKM Ac-1112 (MIC=0.7 uM), and B.subtilis VKM B-501
CC (MIC=0.4 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=6.7 uM)), and
CC yeasts (P.pastoris GS115 (MIC=6.7 uM), and S.cerevisiae Y190 (MIC=54
CC uM)). Also has a strong 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:27287558}.
CC -!- DOMAIN: The mature peptide (59-84) forms alpha-helices which probably
CC disrupt target cell membranes. {ECO:0000269|PubMed:16939228}.
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=2901.0; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16735513};
CC -!- MASS SPECTROMETRY: Mass=2902.7; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:27287558};
CC -!- SIMILARITY: Belongs to the cationic peptide 03 (latarcin) family. 02
CC subfamily. {ECO:0000305}.
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DR EMBL; AM232698; CAJ81658.1; -; mRNA.
DR PDB; 2G9P; NMR; -; A=59-84.
DR PDBsum; 2G9P; -.
DR AlphaFoldDB; Q1ELU1; -.
DR SMR; Q1ELU1; -.
DR ArachnoServer; AS000050; M-zodatoxin-Lt2a.
DR EvolutionaryTrace; Q1ELU1; -.
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..58
FT /evidence="ECO:0000255, ECO:0000269|PubMed:16735513"
FT /id="PRO_0000249736"
FT PEPTIDE 59..84
FT /note="M-zodatoxin-Lt2a"
FT /id="PRO_0000249737"
FT MOTIF 55..58
FT /note="Processing quadruplet motif"
FT /evidence="ECO:0000303|PubMed:27287558"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:2G9P"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:2G9P"
SQ SEQUENCE 84 AA; 9364 MW; B7FA4D69A520E76F CRC64;
MKYFVIALAL AVALVCIAES TAYEVNEELE NELDDLDDAA WLAVAEELQG LEDFEESRGL
FGKLIKKFGR KAISYAVKKA RGKH
