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