LTX1A_LACTA
ID LTX1A_LACTA Reviewed; 85 AA.
AC B3EWF2; K7WU35;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Latartoxin-1a {ECO:0000303|PubMed:23088912};
DE Short=LtTx-1a {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 26-85, FUNCTION,
RP SUBCELLULAR LOCATION, DOMAIN, DISULFIDE BONDS, MASS SPECTROMETRY, AND TOXIC
RP DOSE.
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 C-terminal part (65-85) forms an alpha-helix which probably
CC disrupts target membranes. {ECO:0000269|PubMed:23088912}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000269|PubMed:23088912, ECO:0000305}.
CC -!- PTM: Contains 4 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=6569.7; Mass_error=0.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:23088912};
CC -!- MASS SPECTROMETRY: Mass=6570.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:27287558};
CC -!- TOXIC DOSE: LD(50) is 45 ug/g in flesh fly larvae (S.carnaria).
CC {ECO:0000269|PubMed:23088912}.
CC -!- TOXIC DOSE: LD(50) is 50 ug/g in house crickets (Acheta domesticus).
CC {ECO:0000269|PubMed:23088912}.
CC -!- SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. {ECO:0000255}.
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DR EMBL; JQ513641; AFX65326.1; -; mRNA.
DR EMBL; JQ513642; AFX65327.1; -; mRNA.
DR AlphaFoldDB; B3EWF2; -.
DR SMR; B3EWF2; -.
DR ArachnoServer; AS001847; U1-zodatoxin-Lt1a.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR019553; Spider_toxin_CSTX_knottin.
DR Pfam; PF10530; Toxin_35; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Knottin; Neurotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..25
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:23088912"
FT /id="PRO_0000421841"
FT PEPTIDE 26..85
FT /note="Latartoxin-1a"
FT /id="PRO_0000421842"
FT MOTIF 22..25
FT /note="Processing quadruplet motif"
FT /evidence="ECO:0000303|PubMed:27287558"
FT DISULFID 27..42
FT /evidence="ECO:0000250|UniProtKB:P58604"
FT DISULFID 34..47
FT /evidence="ECO:0000250|UniProtKB:P58604"
FT DISULFID 41..64
FT /evidence="ECO:0000250|UniProtKB:P58604"
FT DISULFID 49..62
FT /evidence="ECO:0000250|UniProtKB:P58604"
SQ SEQUENCE 85 AA; 9293 MW; C7F6B93BC28C30DA CRC64;
MKVLVFAIVC SVLLQVVLSA DEEARECIPT KHDCTNDRKN CCPGHECKCY NTQIGGSKKE
QCGCKKSLLA KAKNFGGKVI TIFKA
