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 16-JUN-2009, entry version 13. DE RecName: Full=Latarcin-4b; DE Short=Ltc-4b; DE Flags: Precursor; OS Lachesana tarabaevi (Spider). OC Eukaryota; Metazoa; 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 155-178, SYNTHESIS OF RP 155-178, AMIDATION AT PHE-178, FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, 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., 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). CC -!- FUNCTION: Has antimicrobial activity against Gram-positive CC bacteria (A.globiformis VKM Ac-1112 (MIC=0.3 ug/ml), and CC 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 larvae. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- MASS SPECTROMETRY: Mass=2882.3; Method=MALDI; Range=155-178; CC Source=PubMed:16735513; CC -!- SIMILARITY: Belongs to the latarcin family. 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 GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 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:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR018802; Latarcin_precursor. DR Pfam; PF10279; Latarcin; 1. PE 1: Evidence at protein level; KW Amidation; Antibiotic; Antimicrobial; Direct protein sequencing; KW Fungicide; Repeat; Secreted; Signal; Toxin. FT SIGNAL 1 22 Potential. FT PROPEP 23 154 FT /FTId=PRO_0000249746. FT PEPTIDE 155 178 Latarcin-4b. FT /FTId=PRO_0000249747. FT REPEAT 44 66 Repetitive polypeptide element type 4. FT REPEAT 72 94 Repetitive polypeptide element type 5. FT REPEAT 100 122 Repetitive polypeptide element type 6. FT REPEAT 128 150 Repetitive polypeptide element type 7. FT MOTIF 40 43 Processing quadruplet motif 1. FT MOTIF 68 71 Processing quadruplet motif 2. FT MOTIF 96 99 Processing quadruplet motif 3. FT MOTIF 124 127 Processing quadruplet motif 4. FT MOTIF 151 154 Processing quadruplet motif 5. FT MOD_RES 178 178 Phenylalanine amide. 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 //