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DEF1_MESMA
ID   DEF1_MESMA              Reviewed;          61 AA.
AC   P0DQT7;
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 BmKDfsin1 {ECO:0000303|PubMed:24129506};
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).
CC   -!- FUNCTION: Antibacterial peptide active against Gram-positive bacteria,
CC       but not on Gram-negative bacteria (By similarity). Has also weak
CC       blocking activity on Kv1.1/KCNA1, Kv1.2/KCNA2, Kv1.3/KCNA3,
CC       KCa3.1/KCNN4/IK, KCa2.3/KCNN3/SK3 and Kv11.1/KCNH2/ERG1 channels
CC       (tested at 1 uM) (By similarity). It inhibits potassium channel current
CC       by interacting with the pore region (By similarity).
CC       {ECO:0000250|UniProtKB:A0A384E0Y8, ECO:0000250|UniProtKB:P0DQU0}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24129506}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in non-venom gland (hemolymph) and
CC       moderately expressed in venom gland. {ECO:0000250|UniProtKB:P0DQU0}.
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   3: Inferred from homology;
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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..61
FT                   /note="Defensin BmKDfsin1"
FT                   /evidence="ECO:0000305|PubMed:24129506"
FT                   /id="PRO_0000455525"
FT   DISULFID        29..50
FT                   /evidence="ECO:0000250|UniProtKB:A0A384E0Y8"
FT   DISULFID        36..58
FT                   /evidence="ECO:0000250|UniProtKB:A0A384E0Y8"
FT   DISULFID        40..60
FT                   /evidence="ECO:0000250|UniProtKB:A0A384E0Y8"
SQ   SEQUENCE   61 AA;  6720 MW;  91CBFF2C7E3BC6B4 CRC64;
     MKTIVLLFVL VLVFALLVKM GMVEAEHGCP DNEDECHEHC KSIGKSGGYC VGPHKQTCRC
     N
 
 
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