ID   DEF5_MESMA              Reviewed;          62 AA.
AC   P0DQU0;
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=Defensin BmKDfsin5 {ECO:0000303|PubMed:24129506, ECO:0000303|PubMed:31954123};
DE   Flags: Precursor;
OS   Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX   NCBI_TaxID=34649;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle;
RX   PubMed=24129506; DOI=10.1038/ncomms3602;
RA   Cao Z., Yu Y., Wu Y., Hao P., Di Z., He Y., Chen Z., Yang W., Shen Z.,
RA   He X., Sheng J., Xu X., Pan B., Feng J., Yang X., Hong W., Zhao W., Li Z.,
RA   Huang K., Li T., Kong Y., Liu H., Jiang D., Zhang B., Hu J., Hu Y.,
RA   Wang B., Dai J., Yuan B., Feng Y., Huang W., Xing X., Zhao G., Li X.,
RA   Li Y., Li W.;
RT   "The genome of Mesobuthus martensii reveals a unique adaptation model of
RT   arthropods.";
RL   Nat. Commun. 4:2602-2602(2013).
RN   [2]
RP   FUNCTION, SYNTHESIS OF 25-62, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Hemolymph, and Venom gland;
RX   PubMed=31954123; DOI=10.1016/j.ijbiomac.2020.01.133;
RA   Meng L., Zhao Y., Qu D., Xie Z., Guo X., Zhu Z., Chen Z., Zhang L., Li W.,
RA   Cao Z., Tian C., Wu Y.;
RT   "Ion channel modulation by scorpion hemolymph and its defensin ingredients
RT   highlights origin of neurotoxins in telson formed in Paleozoic scorpions.";
RL   Int. J. Biol. Macromol. 148:351-363(2020).
CC   -!- FUNCTION: Antibacterial peptide active against Gram-positive bacteria
CC       (including S.aureus ATCC25923 (MIC=2.5 uM), M.luteus AB93113 (MIC=2.5
CC       uM), and the antibiotic-resistant S.epidermidis PRSE P1389 (MIC=1.25
CC       uM)), but not against Gram-negative bacteria (including E.coli and
CC       P.aeruginosa). Has also weak blocking activity on Kv1.1/KCNA1 (8.7%
CC       inhibition), Kv1.2/KCNA2 (10.2% inhibition), Kv1.3/KCNA3 (9.0%
CC       inhibition), KCa3.1/KCNN4/IK (9.1% inhibition), KCa2.3/KCNN3/SK3 (46.3%
CC       inhibition) and Kv11.1/KCNH2/ERG1 (16.9% inhibition) channels (tested
CC       at 1 uM) (PubMed:31954123). It inhibits potassium channel current by
CC       interacting with the pore region (By similarity).
CC       {ECO:0000250|UniProtKB:A0A384E0Y8, ECO:0000269|PubMed:31954123}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31954123}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in non-venom gland (hemolymph) and
CC       moderately expressed in venom gland. {ECO:0000269|PubMed:31954123}.
CC   -!- SIMILARITY: Belongs to the invertebrate defensin family. Type 2
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00710}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Antibiotic; Antimicrobial;
KW   Calcium-activated potassium channel impairing toxin; Defensin;
KW   Disulfide bond; Immunity; Innate immunity; Ion channel impairing toxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..62
FT                   /note="Defensin BmKDfsin5"
FT                   /evidence="ECO:0000305|PubMed:24129506"
FT                   /id="PRO_0000455529"
FT   DISULFID        28..49
FT                   /evidence="ECO:0000250|UniProtKB:A0A384E0Y8"
FT   DISULFID        35..57
FT                   /evidence="ECO:0000250|UniProtKB:A0A384E0Y8"
FT   DISULFID        39..59
FT                   /evidence="ECO:0000250|UniProtKB:A0A384E0Y8"
SQ   SEQUENCE   62 AA;  7017 MW;  A18A0C5AD32BCB3C CRC64;
     MKVIALFFLF AFIFCTLEVA IVEAGFGCPL NQGACHRHCL SIRRRGGYCS GFFKQTCTCY
     RN