ID   LTX2A_LACTA             Reviewed;         109 AA.
AC   B3EWF4; K7WSN2;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Latartoxin-2a {ECO:0000303|PubMed:23088912};
DE            Short=LtTx-2a {ECO:0000303|PubMed:23088912};
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 38-108, FUNCTION,
RP   SUBCELLULAR LOCATION, DISULFIDE BONDS, MASS SPECTROMETRY, TOXIC DOSE, AND
RP   AMIDATION AT VAL-108.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=23088912; DOI=10.1016/j.bbamem.2012.10.014;
RA   Kuzmenkov A.I., Fedorova I.M., Vassilevski A.A., Grishin E.V.;
RT   "Cysteine-rich toxins from Lachesana tarabaevi spider venom with
RT   amphiphilic C-terminal segments.";
RL   Biochim. Biophys. Acta 1828:724-731(2013).
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).
CC   -!- FUNCTION: Insect toxin. Causes paralysis in larvae of C.vicina by
CC       depolarizing membranes at the neuromuscular junction.
CC       {ECO:0000269|PubMed:23088912}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23088912,
CC       ECO:0000269|PubMed:27287558}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:23088912}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- PTM: Contains 5 disulfide bonds. {ECO:0000269|PubMed:23088912}.
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=8333.8; Mass_error=0.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23088912};
CC   -!- MASS SPECTROMETRY: Mass=8334.0; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:27287558};
CC   -!- TOXIC DOSE: LD(50) is 35 ug/g in flesh fly larvae (S.carnaria).
CC       {ECO:0000269|PubMed:23088912}.
CC   -!- TOXIC DOSE: LD(50) is 30 ug/g in house crickets (Acheta domesticus).
CC       {ECO:0000269|PubMed:23088912}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 11 (latartoxin)
CC       subfamily. {ECO:0000255}.
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DR   EMBL; JQ513644; AFX65329.1; -; mRNA.
DR   AlphaFoldDB; B3EWF4; -.
DR   SMR; B3EWF4; -.
DR   ArachnoServer; AS001731; U2-zodatoxin-Lt2a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond; Knottin; Neurotoxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..37
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000269|PubMed:23088912"
FT                   /id="PRO_0000421845"
FT   PEPTIDE         38..108
FT                   /note="Latartoxin-2a"
FT                   /id="PRO_0000421846"
FT   MOTIF           34..37
FT                   /note="Processing quadruplet motif"
FT                   /evidence="ECO:0000303|PubMed:27287558"
FT   MOD_RES         108
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:23088912"
FT   DISULFID        39..56
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        46..67
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        55..81
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        69..79
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        72..93
FT                   /evidence="ECO:0000303|PubMed:23088912"
SQ   SEQUENCE   109 AA;  12585 MW;  E8D9D1A872BD6C28 CRC64;
     MKVLVIIALC LVAFQSALSK KIENFESYIE DLKSEARECI PLYNDCTAFK YNNNCCKDPE
     KKYQYKCSCI VCKEGKEQCT CQRKETVESM MKCVRFVKKV GEKVIEKVG