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DEF3_MESMA
ID   DEF3_MESMA              Reviewed;          62 AA.
AC   A0A384E0Y8;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 2.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Defensin BmKDfsin3 {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] {ECO:0000312|PDB:5XA6}
RP   STRUCTURE BY NMR, FUNCTION, SYNTHESIS OF 25-62, DISULFIDE BONDS, AND TISSUE
RP   SPECIFICITY.
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) (PubMed:31954123). Also blocks the currents of
CC       Kv1.1/KCNA1 (57% inhibition), Kv1.2/KCNA2 (27.5% inhibition),
CC       Kv1.3/KCNA3 (IC(50)=23.4 nM, 84.3% inhibition), KCa3.1/KCNN4/IK (15%
CC       inhibition), KCa2.3/KCNN3/SK3 (87.5% inhibition) and Kv11.1/KCNH2/ERG1
CC       (30.4% inhibition) channels (tested at 1 uM) (PubMed:31954123). It
CC       inhibits potassium channel current by interacting with the pore region
CC       (PubMed:31954123). {ECO:0000269|PubMed:31954123}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:31954123}.
CC   -!- TISSUE SPECIFICITY: Low expression in both venom and non-venom glands
CC       (hemolymph). {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   PDB; 5XA6; NMR; -; A=25-62.
DR   PDBsum; 5XA6; -.
DR   SMR; A0A384E0Y8; -.
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   1: Evidence at protein level;
KW   3D-structure; 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 BmKDfsin3"
FT                   /evidence="ECO:0000305|PubMed:24129506"
FT                   /id="PRO_0000455527"
FT   DISULFID        28..49
FT                   /evidence="ECO:0000269|PubMed:31954123,
FT                   ECO:0007744|PDB:5XA6"
FT   DISULFID        35..57
FT                   /evidence="ECO:0000269|PubMed:31954123,
FT                   ECO:0007744|PDB:5XA6"
FT   DISULFID        39..59
FT                   /evidence="ECO:0000269|PubMed:31954123,
FT                   ECO:0007744|PDB:5XA6"
SQ   SEQUENCE   62 AA;  7149 MW;  A9E6178EBE7E6D44 CRC64;
     MKTIVILFVL ALVFCTLEMG MVEAGFGCPF NQGKCHRHCR SIRRRGGYCD GFLKQRCVCY
     RK
 
 
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