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 22-NOV-2017, entry version 29. 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; OC Araneae; Araneomorphae; Entelegynae; Entelegynae incertae sedis; OC Zodariidae; 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, RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, AND MASS RP 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., RA Karpunin D.V., 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 RP MOTIF, MASS SPECTROMETRY, AND AMIDATION AT GLN-61; GLN-89; GLN-117 AND RP GLN-145. RC TISSUE=Venom {ECO:0000303|PubMed:27287558}; 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 CC Gram-positive bacteria (A.globiformis VKM Ac-1112 (MIC=0.3 ug/ml), CC and B.subtilis VKM B-501 (MIC=1.1 ug/ml)), Gram-negative bacteria CC (E.coli DH5-alpha (MIC=4.4 ug/ml), E.coli MH1 (MIC=4.4 ug/ml), and CC P.aeruginosa PAO1 (MIC=>35 ug/ml)), and yeasts (P.pastoris GS115 CC (MIC=>35 ug/ml), and S.cerevisiae Y190 (MIC=35 ug/ml)). Does not CC have hemolytic activity against rabbit erythrocytes. Causes CC paralysis, but is not lethal when injected into insect CC (M.domestica) larvae. {ECO:0000269|PubMed:16735513}. CC -!- FUNCTION: Repetitive polypeptide element type 1c: Shows no CC antimicrobial activity against Gram-positive bacterium B.subtilis CC B-501 or Gram-negative bacterium E.coli DH5-alpha at concentration CC up to 20 ug/ml. {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:0000269|PubMed:16735513}. CC -!- DOMAIN: M-zodatoxin-Lt4a: Probably forms an alpha-helix which CC disrupts target cell membranes. {ECO:0000303|PubMed:16735513}. CC -!- PTM: Cleavage of the propeptide depends on the processing CC quadruplet motif (PQM) (XXXR, with at least one of X being E) and CC the inverted PQM (RXXX, with at least one of X being E). CC {ECO:0000303|PubMed:27287558}. CC -!- MASS SPECTROMETRY: Mass=2882.3; Method=MALDI; Range=155-178; CC Note=M-zodatoxin-Lt4b peptide.; CC Evidence={ECO:0000269|PubMed:16735513}; CC -!- MASS SPECTROMETRY: Mass=2884.7; Method=MALDI; Range=155-178; CC Note=M-zodatoxin-Lt4b peptide.; CC Evidence={ECO:0000269|PubMed:27287558}; CC -!- MASS SPECTROMETRY: Mass=2113.6; Method=MALDI; Range=44-61; CC Note=Repetitive polypeptide element type 1c.; CC Evidence={ECO:0000269|PubMed:27287558}; CC -!- MASS SPECTROMETRY: Mass=2127.7; Method=MALDI; Range=72-89, 100- CC 117, 128-145; Note=Repetitive polypeptide element type 1d.; CC Evidence={ECO:0000269|PubMed:27287558}; CC -!- SIMILARITY: Belongs to the latarcin superfamily. Lt4 family. CC {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 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 other 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; KW Fungicide; Repeat; Secreted; Signal; Toxin. FT SIGNAL 1 22 {ECO:0000255}. FT PROPEP 23 43 {ECO:0000255, FT ECO:0000269|PubMed:16735513}. FT /FTId=PRO_0000249746. FT PEPTIDE 44 61 Repetitive polypeptide element type 1c. FT {ECO:0000269|PubMed:27287558}. FT /FTId=PRO_0000434688. FT PROPEP 63 71 {ECO:0000269|PubMed:27287558}. FT /FTId=PRO_0000434689. FT PEPTIDE 72 89 Repetitive polypeptide element type 1d. FT {ECO:0000269|PubMed:27287558}. FT /FTId=PRO_0000434690. FT PROPEP 91 99 {ECO:0000269|PubMed:27287558}. FT /FTId=PRO_0000434691. FT PEPTIDE 100 117 Repetitive polypeptide element type 1c. FT {ECO:0000269|PubMed:27287558}. FT /FTId=PRO_0000434692. FT PROPEP 119 127 {ECO:0000269|PubMed:27287558}. FT /FTId=PRO_0000434693. FT PEPTIDE 128 145 Repetitive polypeptide element type 1c. FT {ECO:0000269|PubMed:27287558}. FT /FTId=PRO_0000434694. FT PROPEP 147 154 {ECO:0000269|PubMed:27287558}. FT /FTId=PRO_0000434695. FT PEPTIDE 155 178 M-zodatoxin-Lt4b peptide. FT {ECO:0000269|PubMed:16735513}. FT /FTId=PRO_0000249747. FT MOTIF 40 43 Processing quadruplet motif 1. FT {ECO:0000303|PubMed:27287558}. FT MOTIF 63 66 Inverted processing quadruplet motif 1. FT {ECO:0000303|PubMed:27287558}. FT MOTIF 68 71 Processing quadruplet motif 2. FT {ECO:0000303|PubMed:27287558}. FT MOTIF 91 94 Inverted processing quadruplet motif 2. FT {ECO:0000303|PubMed:27287558}. FT MOTIF 96 99 Processing quadruplet motif 3. FT {ECO:0000303|PubMed:27287558}. FT MOTIF 119 122 Inverted processing quadruplet motif 3. FT {ECO:0000303|PubMed:27287558}. FT MOTIF 124 127 Processing quadruplet motif 4. FT {ECO:0000303|PubMed:27287558}. FT MOTIF 147 150 Inverted processing quadruplet motif 4. FT {ECO:0000303|PubMed:27287558}. FT MOTIF 151 154 Processing quadruplet motif 5. FT {ECO:0000303|PubMed:27287558}. FT MOD_RES 61 61 Glutamine amide. FT {ECO:0000269|PubMed:27287558}. FT MOD_RES 89 89 Glutamine amide. FT {ECO:0000269|PubMed:27287558}. FT MOD_RES 117 117 Glutamine amide. FT {ECO:0000269|PubMed:27287558}. FT MOD_RES 145 145 Glutamine amide. FT {ECO:0000269|PubMed:27287558}. FT MOD_RES 178 178 Phenylalanine amide. FT {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 //