ID   LYS1_LYCSI              Reviewed;          24 AA.
AC   P0DV70;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 1.
DT   03-AUG-2022, entry version 2.
DE   RecName: Full=Lycosin-I {ECO:0000303|PubMed:22882120, ECO:0000303|PubMed:23638903, ECO:0000303|PubMed:26937786};
DE   AltName: Full=Anticancer peptide {ECO:0000303|PubMed:26937786};
DE   AltName: Full=Cell penetrating peptide {ECO:0000303|PubMed:26937786};
OS   Lycosa singoriensis (Wolf spider) (Aranea singoriensis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Lycosoidea; Lycosidae; Lycosa.
OX   NCBI_TaxID=434756;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=22882120; DOI=10.2174/156652412803833643;
RA   Liu Z., Deng M., Xiang J., Ma H., Hu W., Zhao Y., Li D.W., Liang S.;
RT   "A novel spider peptide toxin suppresses tumor growth through dual
RT   signaling pathways.";
RL   Curr. Mol. Med. 12:1350-1360(2012).
RN   [2]
RP   FUNCTION.
RX   PubMed=23638903; DOI=10.2174/15665240113139990045;
RA   Tan H., Ding X., Meng S., Liu C., Wang H., Xia L., Liu Z., Liang S.;
RT   "Antimicrobial potential of Lycosin-I, a cationic and amphiphilic peptide
RT   from the venom of the spider Lycosa singorensis.";
RL   Curr. Mol. Med. 13:900-910(2013).
RN   [3]
RP   FUNCTION.
RX   PubMed=25199777; DOI=10.1128/aac.03279-14;
RA   Wang L., Wang Y.J., Liu Y.Y., Li H., Guo L.X., Liu Z.H., Shi X.L., Hu M.;
RT   "In vitro potential of Lycosin-I as an alternative antimicrobial drug for
RT   treatment of multidrug-resistant Acinetobacter baumannii infections.";
RL   Antimicrob. Agents Chemother. 58:6999-7002(2014).
RN   [4]
RP   SUBUNIT.
RX   PubMed=26937786; DOI=10.1021/acs.jpcb.5b12618;
RA   Tan H., Luo W., Wei L., Chen B., Li W., Xiao L., Manzhos S., Liu Z.,
RA   Liang S.;
RT   "Quantifying the distribution of the stoichiometric composition of
RT   anticancer peptide Lycosin-I on the lipid membrane with single molecule
RT   spectroscopy.";
RL   J. Phys. Chem. B 120:3081-3088(2016).
RN   [5]
RP   BIOTECHNOLOGY.
RX   PubMed=28839471; DOI=10.7150/thno.19780;
RA   Tan H., Huang Y., Xu J., Chen B., Zhang P., Ye Z., Liang S., Xiao L.,
RA   Liu Z.;
RT   "Spider toxin peptide Lycosin-I functionalized gold nanoparticles for in
RT   vivo tumor targeting and therapy.";
RL   Theranostics 7:3168-3178(2017).
RN   [6]
RP   FUNCTION.
RX   PubMed=30269852; DOI=10.1016/j.micres.2018.08.012;
RA   Tan L., Bai L., Wang L., He L., Li G., Du W., Shen T., Xiang Z., Wu J.,
RA   Liu Z., Hu M.;
RT   "Antifungal activity of spider venom-derived peptide lycosin-I against
RT   Candida tropicalis.";
RL   Microbiol. Res. 216:120-128(2018).
RN   [7]
RP   FUNCTION, AND SYNTHESIS.
RX   PubMed=29248696; DOI=10.1016/j.peptides.2017.12.011;
RA   Ma B., Xi Z., Li J., Gao T., Liao R., Wang S., Li X., Tang Y., Wang Z.,
RA   Hou S., Jiang J., Deng M., Duan Z., Tang X., Jiang L.;
RT   "Vasodilator and hypotensive effects of the spider peptide Lycosin-I in
RT   vitro and in vivo.";
RL   Peptides 99:108-114(2018).
RN   [8]
RP   FUNCTION.
RX   PubMed=30682337; DOI=10.1016/j.exppara.2019.01.009;
RA   Tang Y., Hou S., Li X., Wu M., Ma B., Wang Z., Jiang J., Deng M., Duan Z.,
RA   Tang X., Liu Y., Wang W., Han X., Jiang L.;
RT   "Anti-parasitic effect on Toxoplasma gondii induced by a spider peptide
RT   lycosin-I.";
RL   Exp. Parasitol. 198:17-25(2019).
CC   -!- FUNCTION: Antimicrobial peptide that inhibits many reference strains of
CC       bacteria and fungi (PubMed:23638903, PubMed:30269852). Is potent
CC       against Candida species and multidrug-resistant Acinetobacter baumannii
CC       (MDRAB) (PubMed:25199777, PubMed:30269852). Is probably localized in
CC       the cytoplasm after being transported through the cell wall and
CC       membrane (PubMed:30269852). Is able to interact with cell membranes and
CC       enter into cell plasma to activate the mitochondrial death pathway to
CC       sensitize cancer cells for apoptosis, as well as up-regulates p27 to
CC       inhibit cell proliferation (PubMed:22882120). It shows very low effect
CC       on normal cells, such as erythrocytes, Hek293t cells (PubMed:22882120).
CC       It also potently inhibits tumor cell growth in vitro, and suppresses
CC       various tumor growth in vivo when tested in human cancer xenograft
CC       models (PubMed:22882120). It interacts with the cell membrane and is
CC       then internalized into the cytoplasm of cancer cells to initiate the
CC       programmable cell death (PubMed:22882120). In addition, this peptide
CC       has the therapeutic effects of anti-hypertension by endothelium-
CC       dependent vasodilatation via the NO/sGC/cGMP signaling pathway
CC       (PubMed:29248696). In vivo, this peptide also shows a significant
CC       ability to inhibit T.gondii invasion and proliferation, making it a
CC       potential alternative agent for the treatment of toxoplasmosis
CC       (PubMed:30682337). {ECO:0000269|PubMed:22882120,
CC       ECO:0000269|PubMed:23638903, ECO:0000269|PubMed:25199777,
CC       ECO:0000269|PubMed:29248696, ECO:0000269|PubMed:30269852,
CC       ECO:0000269|PubMed:30682337}.
CC   -!- SUBUNIT: Monomer in solution. Small size oligomers on the lipid
CC       membranes. {ECO:0000269|PubMed:26937786}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22882120}. Target
CC       cell membrane {ECO:0000269|PubMed:26937786}. Note=Lipid membranes
CC       induce the formation of amphipathic-helix conformation of lycosin-I and
CC       subsequently stable aggregates of peptide molecules on bilayer, which
CC       are believed to be crucial for the cell penetrating ability of lycosin-
CC       I. {ECO:0000305|PubMed:26937786}.
CC   -!- BIOTECHNOLOGY: When conjugated to gold nanoparticles (LGNPs) or gold
CC       nanorods (LGNRs), this peptide has great potential in cancer-targeting
CC       delivery and photothermal therapy. {ECO:0000269|PubMed:28839471}.
CC   -!- SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 05
CC       subfamily. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; 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   GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Fungicide;
KW   Hypotensive agent; Membrane; Secreted; Target cell membrane;
KW   Target membrane; Vasoactive.
FT   PEPTIDE         1..24
FT                   /note="Lycosin-I"
FT                   /evidence="ECO:0000269|PubMed:22882120"
FT                   /id="PRO_0000455434"
SQ   SEQUENCE   24 AA;  2889 MW;  6ADADDFDB944A6C6 CRC64;
     RKGWFKAMKS IAKFIAKEKL KEHL