ID   MPSIN_IXOSC             Reviewed;         107 AA.
AC   B7PCF6;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Antimicrobial peptide microplusin {ECO:0000250|UniProtKB:Q86LE5};
DE   Flags: Precursor;
GN   ORFNames=ISCW002113;
OS   Ixodes scapularis (Black-legged tick) (Deer tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=6945;
RN   [1] {ECO:0000312|EMBL:EEC04278.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wikel {ECO:0000312|EMBL:EEC04278.1};
RC   TISSUE=Embryo {ECO:0000269|Ref.1};
RG   Ixodes scapularis Genome Project Consortium;
RA   Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA   Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA   Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA   Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT   "Annotation of Ixodes scapularis.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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 is crucial for antimicrobial activity against
CC       M.luteus (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q86LE5}.
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; DS683675; EEC04278.1; -; Genomic_DNA.
DR   RefSeq; XP_002409778.1; XM_002409734.1.
DR   AlphaFoldDB; B7PCF6; -.
DR   SMR; B7PCF6; -.
DR   KEGG; isc:IscW_ISCW002113; -.
DR   VEuPathDB; VectorBase:ISCI008209; -.
DR   VEuPathDB; VectorBase:ISCW002113; -.
DR   HOGENOM; CLU_170585_0_0_1; -.
DR   PhylomeDB; B7PCF6; -.
DR   Proteomes; UP000001555; Unassembled WGS sequence.
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; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250|UniProtKB:Q86LE5"
FT   CHAIN           20..107
FT                   /note="Antimicrobial peptide microplusin"
FT                   /evidence="ECO:0000250|UniProtKB:Q86LE5"
FT                   /id="PRO_0000392950"
FT   REGION          86..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        25..60
FT                   /evidence="ECO:0000250|UniProtKB:Q86LE5"
FT   DISULFID        38..88
FT                   /evidence="ECO:0000250|UniProtKB:Q86LE5"
FT   DISULFID        49..54
FT                   /evidence="ECO:0000250|UniProtKB:Q86LE5"
SQ   SEQUENCE   107 AA;  11661 MW;  3A18922578A5DFDE CRC64;
     MKSLLVCLVL AVVVLVASGH HVELCKKNDA ELKEALTCIT SKLPAALGCN DKSCVFEKLC
     KEGDLDEALK KHFTEAEVQT LHTTATDCDH SHGHEHSHGH EHGHGHH