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MPSIN_ARGMO
ID   MPSIN_ARGMO             Reviewed;         113 AA.
AC   Q09JR4;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Antimicrobial peptide microplusin {ECO:0000250|UniProtKB:Q86LE5};
DE   Flags: Precursor;
GN   ORFNames=AM-189 {ECO:0000303|PubMed:18070664};
OS   Argas monolakensis (Mono lake bird tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Argasidae; Argas.
OX   NCBI_TaxID=34602;
RN   [1] {ECO:0000312|EMBL:ABI52699.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=18070664; DOI=10.1016/j.ibmb.2007.09.003;
RA   Mans B.J., Andersen J.F., Francischetti I.M., Valenzuela J.G., Schwan T.G.,
RA   Pham V.M., Garfield M.K., Hammer C.H., Ribeiro J.M.C.;
RT   "Comparative sialomics between hard and soft ticks: implications for the
RT   evolution of blood-feeding behavior.";
RL   Insect Biochem. Mol. Biol. 38:42-58(2008).
CC   -!- FUNCTION: Has bacteriostatic activity against Gram-positive bacteria,
CC       but not against Gram-negative bacteria. Has fungistatic activity
CC       against some but not all fungi. Binds and sequesters copper and iron
CC       ions. Copper-chelating activity is crucial for antimicrobial activity
CC       against M.luteus (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q86LE5}.
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DR   EMBL; DQ886782; ABI52699.1; -; mRNA.
DR   AlphaFoldDB; Q09JR4; -.
DR   SMR; Q09JR4; -.
DR   PRIDE; Q09JR4; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0016531; F:copper chaperone activity; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0046911; F:metal chelating activity; ISS:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; ISS:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Copper; Disulfide bond; Fungicide; Immunity;
KW   Innate immunity; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250|UniProtKB:Q86LE5"
FT   CHAIN           20..113
FT                   /note="Antimicrobial peptide microplusin"
FT                   /evidence="ECO:0000250|UniProtKB:Q86LE5"
FT                   /id="PRO_0000392948"
FT   DISULFID        25..71
FT                   /evidence="ECO:0000250|UniProtKB:Q86LE5"
FT   DISULFID        38..99
FT                   /evidence="ECO:0000250|UniProtKB:Q86LE5"
FT   DISULFID        60..65
FT                   /evidence="ECO:0000250|UniProtKB:Q86LE5"
SQ   SEQUENCE   113 AA;  12968 MW;  6C8298A6B3F49DCB CRC64;
     MKSLLVLALL AFGAVLVSAH HLEMCEKSTD ELREQLVCHR QHATGAFNAK LDQVNRQLRC
     NNDICTFKKL CDAPDFLTEL RKYFTESEIN ELHELANQCD PDAHHDHPHC HPH
 
 
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