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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //