ID   KBX33_OPICA             Reviewed;          95 AA.
AC   Q5WQZ7;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Opiscorpine-3 {ECO:0000303|PubMed:15241551};
DE   Flags: Precursor;
OS   Opistophthalmus carinatus (African yellow leg scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Opistophthalminae;
OC   Opistophthalmus.
OX   NCBI_TaxID=190115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15241551; DOI=10.1007/s00018-004-4149-1;
RA   Zhu S., Tytgat J.;
RT   "The scorpine family of defensins: gene structure, alternative
RT   polyadenylation and fold recognition.";
RL   Cell. Mol. Life Sci. 61:1751-1763(2004).
CC   -!- FUNCTION: Has antimicrobial activity against yeasts and bacteria.
CC       {ECO:0000250|UniProtKB:Q5WR03}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:15241551}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15241551}.
CC   -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY423487; AAQ94358.1; -; Genomic_DNA.
DR   EMBL; AY423484; AAQ94355.1; -; mRNA.
DR   AlphaFoldDB; Q5WQZ7; -.
DR   SMR; Q5WQZ7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR029237; Long_scorpion_toxin.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   Pfam; PF14866; Toxin_38; 1.
DR   SUPFAM; SSF57095; Scorpion toxin-like; 1.
DR   PROSITE; PS51862; BSPN_CSAB; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Disulfide bond; Fungicide; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..95
FT                   /note="Opiscorpine-3"
FT                   /evidence="ECO:0000305|PubMed:15241551"
FT                   /id="PRO_5000092276"
FT   DOMAIN          55..95
FT                   /note="BetaSPN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        58..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        68..87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        72..89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ   SEQUENCE   95 AA;  10383 MW;  95FC10548CB9475F CRC64;
     MNNKLTALIF LGLLAIASCK WLNEKSIQNK IDEKIGKNFL GGMAKAVVHK LAKNEFMCVA
     NVDMTKSCDT HCQKASGEKG YCHGTKCKCG VPLSY
//