MPSIN_RHIMP
ID MPSIN_RHIMP Reviewed; 110 AA.
AC Q86LE5;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Antimicrobial peptide microplusin {ECO:0000303|PubMed:14642886};
DE Short=Microplusin {ECO:0000303|PubMed:14642886};
DE Flags: Precursor;
OS Rhipicephalus microplus (Cattle tick) (Boophilus microplus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC Rhipicephalus; Boophilus.
OX NCBI_TaxID=6941;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO48942.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-110, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC STRAIN=Porto Alegre {ECO:0000269|PubMed:14642886};
RC TISSUE=Hemolymph {ECO:0000269|PubMed:14642886};
RX PubMed=14642886; DOI=10.1016/j.dci.2003.08.001;
RA Fogaca A.C., Lorenzini D.M., Kaku L.M., Esteves E., Bulet P., Daffre S.;
RT "Cysteine-rich antimicrobial peptides of the cattle tick Boophilus
RT microplus: isolation, structural characterization and tissue expression
RT profile.";
RL Dev. Comp. Immunol. 28:191-200(2004).
RN [2] {ECO:0000305}
RP STRUCTURE BY NMR IN COMPLEX WITH COPPER, DISULFIDE BONDS, AND
RP COPPER-BINDING.
RX PubMed=19828445; DOI=10.1074/jbc.m109.016410;
RA Silva F.D., Rezende C.A., Rossi D.C., Esteves E., Dyszy F.H., Schreier S.,
RA Gueiros-Filho F., Campos C.B., Pires J.R., Daffre S.;
RT "Structure and mode of action of microplusin, a copper II-chelating
RT antimicrobial peptide from the cattle tick Rhipicephalus (Boophilus)
RT microplus.";
RL J. Biol. Chem. 284:34735-34746(2009).
CC -!- FUNCTION: Has bacteriostatic activity against the Gram-positive
CC bacterium M.luteus, but not against Gram-negative bacterium E.coli
CC SBS363. Has fungistatic activity against C.neoformans, but not
CC C.albicans. Binds and sequesters copper and iron ions. Copper-chelating
CC is crucial for antimicrobial activity against M.luteus.
CC {ECO:0000269|PubMed:14642886}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14642886}.
CC -!- TISSUE SPECIFICITY: Expressed in the hemocytes, fat body and ovaries.
CC {ECO:0000269|PubMed:14642886}.
CC -!- MASS SPECTROMETRY: Mass=10204; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:14642886};
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DR EMBL; AY233212; AAO48942.1; -; mRNA.
DR PDB; 2KNJ; NMR; -; A=21-110.
DR PDBsum; 2KNJ; -.
DR AlphaFoldDB; Q86LE5; -.
DR BMRB; Q86LE5; -.
DR SMR; Q86LE5; -.
DR EnsemblMetazoa; XM_037413837.1; XP_037269734.1; LOC119161398.
DR VEuPathDB; VectorBase:LOC119161398; -.
DR EvolutionaryTrace; Q86LE5; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0016531; F:copper chaperone activity; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0046911; F:metal chelating activity; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA: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 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Copper; Direct protein sequencing;
KW Disulfide bond; Fungicide; Immunity; Innate immunity; Metal-binding;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:14642886"
FT CHAIN 21..110
FT /note="Antimicrobial peptide microplusin"
FT /evidence="ECO:0000269|PubMed:14642886"
FT /id="PRO_0000392949"
FT DISULFID 26..72
FT /evidence="ECO:0000269|PubMed:19828445"
FT DISULFID 39..100
FT /evidence="ECO:0000269|PubMed:19828445"
FT DISULFID 61..66
FT /evidence="ECO:0000269|PubMed:19828445"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:2KNJ"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:2KNJ"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:2KNJ"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:2KNJ"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:2KNJ"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2KNJ"
SQ SEQUENCE 110 AA; 12182 MW; 42B815904D9B0D98 CRC64;
MKAIFVSALL VVALVASTSA HHQELCTKGD DALVTELECI RLRISPETNA AFDNAVQQLN
CLNRACAYRK MCATNNLEQA MSVYFTNEQI KEIHDAATAC DPEAHHEHDH
