LAT4B_LACTA
ID LAT4B_LACTA Reviewed; 179 AA.
AC Q1ELU4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=M-zodatoxin-Lt4b {ECO:0000305};
DE Short=M-ZDTX-Lt4b {ECO:0000305};
DE Contains:
DE RecName: Full=Repetitive polypeptide element type 1c {ECO:0000303|PubMed:27287558};
DE Short=Rpe 1c {ECO:0000303|PubMed:27287558};
DE Contains:
DE RecName: Full=Repetitive polypeptide element type 1d {ECO:0000303|PubMed:27287558};
DE Short=Rpe 1d {ECO:0000303|PubMed:27287558};
DE Contains:
DE RecName: Full=M-zodatoxin-Lt4b peptide {ECO:0000305};
DE AltName: Full=Latarcin-4b {ECO:0000303|PubMed:16735513};
DE Short=Ltc-4b {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] {ECO:0000305, ECO:0000312|EMBL:CAJ81655.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 155-178, SYNTHESIS OF
RP 155-178, AMIDATION AT PHE-178, FUNCTION OF M-ZODATOXIN-LT4B, SUBCELLULAR
RP LOCATION, DOMAIN, 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 PROTEIN SEQUENCE OF 44-61; 72-89; 100-117 AND 128-145, FUNCTION OF
RP REPETITIVE POLYPEPTIDE ELEMENT TYPE 1C, SUBCELLULAR LOCATION, PQM MOTIF,
RP MASS SPECTROMETRY, AND AMIDATION AT GLN-61; GLN-89; GLN-117 AND GLN-145.
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: M-zodatoxin-Lt4b: Has antimicrobial activity against Gram-
CC positive bacteria (A.globiformis VKM Ac-1112 (MIC=0.3 uM), and
CC B.subtilis VKM B-501 (MIC=1.1 uM)), Gram-negative bacteria (E.coli DH5-
CC alpha (MIC=4.4 uM), E.coli MH1 (MIC=4.4 uM), and P.aeruginosa PAO1
CC (MIC=>35 uM)), and yeasts (P.pastoris GS115 (MIC=>35 uM), and
CC S.cerevisiae Y190 (MIC=35 uM)). Does not have hemolytic activity
CC against rabbit erythrocytes. Causes paralysis, but is not lethal when
CC injected into insect (M.domestica) larvae.
CC {ECO:0000269|PubMed:16735513}.
CC -!- FUNCTION: [Repetitive polypeptide element type 1c]: Shows no
CC antimicrobial activity against Gram-positive bacterium B.subtilis B-501
CC or Gram-negative bacterium E.coli DH5-alpha at concentration up to 20
CC uM. {ECO:0000269|PubMed:27287558}.
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, ECO:0000305|PubMed:27287558}.
CC -!- DOMAIN: M-zodatoxin-Lt4a: Probably forms an alpha-helix which disrupts
CC target cell membranes. {ECO:0000303|PubMed:16735513}.
CC -!- PTM: Cleavage of the propeptide depends on the processing quadruplet
CC motif (PQM) (XXXR, with at least one of X being E) and the inverted PQM
CC (RXXX, with at least one of X being E). {ECO:0000303|PubMed:27287558}.
CC -!- MASS SPECTROMETRY: [M-zodatoxin-Lt4b peptide]: Mass=2882.3;
CC Method=MALDI; Note=M-zodatoxin-Lt4b peptide.;
CC Evidence={ECO:0000269|PubMed:16735513};
CC -!- MASS SPECTROMETRY: [M-zodatoxin-Lt4b peptide]: Mass=2884.7;
CC Method=MALDI; Note=M-zodatoxin-Lt4b peptide.;
CC Evidence={ECO:0000269|PubMed:27287558};
CC -!- MASS SPECTROMETRY: [Repetitive polypeptide element type 1c]:
CC Mass=2113.6; Method=MALDI; Note=Repetitive polypeptide element type
CC 1c.; Evidence={ECO:0000269|PubMed:27287558};
CC -!- MASS SPECTROMETRY: Mass=2127.7; Method=MALDI; Note=Repetitive
CC polypeptide element type 1d. The measured ranges are 72-89, 100-117,
CC 128-145.; Evidence={ECO:0000269|PubMed:27287558};
CC -!- SIMILARITY: Belongs to the cationic peptide 03 (latarcin) family. 04
CC subfamily. {ECO:0000305}.
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DR EMBL; AM232695; CAJ81655.1; -; mRNA.
DR AlphaFoldDB; Q1ELU4; -.
DR SMR; Q1ELU4; -.
DR ArachnoServer; AS000055; M-zodatoxin-Lt4b.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR InterPro; IPR018802; Latarcin_precursor.
DR Pfam; PF10279; Latarcin; 2.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Direct protein sequencing; Fungicide;
KW Repeat; Secreted; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..43
FT /evidence="ECO:0000255, ECO:0000269|PubMed:16735513"
FT /id="PRO_0000249746"
FT PEPTIDE 44..61
FT /note="Repetitive polypeptide element type 1c"
FT /evidence="ECO:0000269|PubMed:27287558"
FT /id="PRO_0000434688"
FT PROPEP 63..71
FT /evidence="ECO:0000269|PubMed:27287558"
FT /id="PRO_0000434689"
FT PEPTIDE 72..89
FT /note="Repetitive polypeptide element type 1d"
FT /evidence="ECO:0000269|PubMed:27287558"
FT /id="PRO_0000434690"
FT PROPEP 91..99
FT /evidence="ECO:0000269|PubMed:27287558"
FT /id="PRO_0000434691"
FT PEPTIDE 100..117
FT /note="Repetitive polypeptide element type 1c"
FT /evidence="ECO:0000269|PubMed:27287558"
FT /id="PRO_0000434692"
FT PROPEP 119..127
FT /evidence="ECO:0000269|PubMed:27287558"
FT /id="PRO_0000434693"
FT PEPTIDE 128..145
FT /note="Repetitive polypeptide element type 1c"
FT /evidence="ECO:0000269|PubMed:27287558"
FT /id="PRO_0000434694"
FT PROPEP 147..154
FT /evidence="ECO:0000269|PubMed:27287558"
FT /id="PRO_0000434695"
FT PEPTIDE 155..178
FT /note="M-zodatoxin-Lt4b peptide"
FT /evidence="ECO:0000269|PubMed:16735513"
FT /id="PRO_0000249747"
FT MOTIF 40..43
FT /note="Processing quadruplet motif 1"
FT /evidence="ECO:0000303|PubMed:27287558"
FT MOTIF 63..66
FT /note="Inverted processing quadruplet motif 1"
FT /evidence="ECO:0000303|PubMed:27287558"
FT MOTIF 68..71
FT /note="Processing quadruplet motif 2"
FT /evidence="ECO:0000303|PubMed:27287558"
FT MOTIF 91..94
FT /note="Inverted processing quadruplet motif 2"
FT /evidence="ECO:0000303|PubMed:27287558"
FT MOTIF 96..99
FT /note="Processing quadruplet motif 3"
FT /evidence="ECO:0000303|PubMed:27287558"
FT MOTIF 119..122
FT /note="Inverted processing quadruplet motif 3"
FT /evidence="ECO:0000303|PubMed:27287558"
FT MOTIF 124..127
FT /note="Processing quadruplet motif 4"
FT /evidence="ECO:0000303|PubMed:27287558"
FT MOTIF 147..150
FT /note="Inverted processing quadruplet motif 4"
FT /evidence="ECO:0000303|PubMed:27287558"
FT MOTIF 151..154
FT /note="Processing quadruplet motif 5"
FT /evidence="ECO:0000303|PubMed:27287558"
FT MOD_RES 61
FT /note="Glutamine amide"
FT /evidence="ECO:0000269|PubMed:27287558"
FT MOD_RES 89
FT /note="Glutamine amide"
FT /evidence="ECO:0000269|PubMed:27287558"
FT MOD_RES 117
FT /note="Glutamine amide"
FT /evidence="ECO:0000269|PubMed:27287558"
FT MOD_RES 145
FT /note="Glutamine amide"
FT /evidence="ECO:0000269|PubMed:27287558"
FT MOD_RES 178
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16735513"
SQ SEQUENCE 179 AA; 20364 MW; A6D4CFDD58A437C7 CRC64;
MKFSIIALAL AVAFVCVAES RSEEEGYDVS EEIQAEELEE AARGGINRKL MEMVNKLRKV
QGREDSEDAG RAGINRKLME MVNKLRKVQG REDTEEAGRG GINRKLMEMV NKLRKVQGRE
DSEEAGRGGI NRKLMEMVNK LRKVQGREDT EEARSLKDKV KSMGEKLKQY IQTWKAKFG
