ID   DEF2_ORNSA              Reviewed;          37 AA.
AC   P0DV61;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 1.
DT   03-AUG-2022, entry version 2.
DE   RecName: Full=Tick defensin 2 {ECO:0000303|PubMed:23553969};
DE   AltName: Full=OsDef2 {ECO:0000303|PubMed:23553969};
OS   Ornithodoros savignyi (African eyed tampan) (Soft tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Argasidae; Ornithodoros.
OX   NCBI_TaxID=69826;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND SYNTHESIS OF 16-37.
RX   PubMed=23553969; DOI=10.1002/psc.2505;
RA   Prinsloo L., Naidoo A., Serem J., Taute H., Sayed Y., Bester M., Neitz A.,
RA   Gaspar A.;
RT   "Structural and functional characterization of peptides derived from the
RT   carboxy-terminal region of a defensin from the tick Ornithodoros
RT   savignyi.";
RL   J. Pept. Sci. 19:325-332(2013).
CC   -!- FUNCTION: Antibacterial peptide mostly active against Gram-positive
CC       bacteria (MIC=0.24 ug/ml on Bacillus subtilis, and MIC=0.94 ug/ml on
CC       Micrococcus luteus, MIC>120 ug/ml on both Escherichia coli and
CC       Pseudomonas aeruginosa). {ECO:0000269|PubMed:23553969}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23553969}.
CC   -!- MISCELLANEOUS: Two peptides derived from the C-terminal region have
CC       been synthesized. The peptide Os consist of residues 16-37, while the
CC       peptide Os-C is an analog in which the three cysteine residues are
CC       omitted. Both peptides show potent bactericidal activity, and high
CC       antioxidant activity. {ECO:0000269|PubMed:23553969}.
CC   -!- SIMILARITY: Belongs to the invertebrate defensin family. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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; Defensin; Direct protein sequencing;
KW   Disulfide bond; Immunity; Innate immunity; Secreted.
FT   CHAIN           1..37
FT                   /note="Tick defensin 2"
FT                   /evidence="ECO:0000269|PubMed:23553969"
FT                   /id="PRO_0000455161"
FT   DISULFID        4..26
FT                   /evidence="ECO:0000250|UniProtKB:I1T3C7"
FT   DISULFID        11..34
FT                   /evidence="ECO:0000250|UniProtKB:I1T3C7"
FT   DISULFID        15..36
FT                   /evidence="ECO:0000250|UniProtKB:I1T3C7"
SQ   SEQUENCE   37 AA;  4186 MW;  107966FFC6051ED4 CRC64;
     GYGCPFNQYQ CHSHCKGIRG YKGGYCKGAF KQTCKCY