ID   DEFI_RHIMP              Reviewed;          74 AA.
AC   Q86LE4;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Defensin {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:AAO48943.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-74, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   STRAIN=Porto Alegre {ECO:0000269|PubMed:14642886};
RC   TISSUE=Hemocyte {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).
CC   -!- FUNCTION: Antibacterial peptide mostly active against Gram-positive
CC       bacteria. {ECO:0000250|UniProtKB:Q86QI5, ECO:0000255|PROSITE-
CC       ProRule:PRU00710}.
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=4285; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:14642886};
CC   -!- SIMILARITY: Belongs to the invertebrate defensin family. Type 2
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00710}.
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DR   EMBL; AY233213; AAO48943.1; -; mRNA.
DR   AlphaFoldDB; Q86LE4; -.
DR   SMR; Q86LE4; -.
DR   EnsemblMetazoa; XM_037413367.1; XP_037269264.1; LOC119161044.
DR   VEuPathDB; VectorBase:LOC119161044; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; 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   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR001542; Defensin_invertebrate/fungal.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   Pfam; PF01097; Defensin_2; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Defensin;
KW   Direct protein sequencing; Disulfide bond; Immunity; Innate immunity;
KW   Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..34
FT                   /evidence="ECO:0000269|PubMed:14642886"
FT                   /id="PRO_0000392946"
FT   CHAIN           37..74
FT                   /note="Defensin"
FT                   /evidence="ECO:0000269|PubMed:14642886"
FT                   /id="PRO_0000392947"
FT   DISULFID        40..61
FT                   /evidence="ECO:0000250|UniProtKB:I1T3C7"
FT   DISULFID        47..69
FT                   /evidence="ECO:0000250|UniProtKB:I1T3C7"
FT   DISULFID        51..71
FT                   /evidence="ECO:0000250|UniProtKB:I1T3C7"
SQ   SEQUENCE   74 AA;  8249 MW;  30B313222AB52952 CRC64;
     MRGIYICLVF VLVCGLVSGL ADVPAESEMA HLRVRRGFGC PFNQGACHRH CRSIRRRGGY
     CAGLIKQTCT CYRN