ID   WAPC_OXYMI              Reviewed;          74 AA.
AC   B5L5M9;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Omwaprin-c {ECO:0000250|UniProtKB:B5G6G7};
DE   AltName: Full=Oxywaprin-c {ECO:0000312|EMBL:ACC77766.1};
DE   Flags: Precursor;
OS   Oxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX   NCBI_TaxID=111177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Venom gland;
RX   PubMed=18979207; DOI=10.1007/s00018-008-8573-5;
RA   St Pierre L., Earl S.T., Filippovich I., Sorokina N., Masci P.P.,
RA   De Jersey J., Lavin M.F.;
RT   "Common evolution of waprin and Kunitz-like toxin families in Australian
RT   venomous snakes.";
RL   Cell. Mol. Life Sci. 65:4039-4054(2008).
CC   -!- FUNCTION: Damages membranes of susceptible bacteria. Has antibacterial
CC       activity against the Gram-positive bacteria B.megaterium and S.warneri.
CC       After 45 minutes of treatment with this protein, B.megaterium have no
CC       visible pili and are smooth. Has no antibacterial activity against the
CC       Gram-positive bacteria B.thuringiensis, S.aureus, S.clavuligerus and B.
CC       anthracis, or the Gram-negative bacteria E.coli and A.tumefaciens. Has
CC       no hemolytic activity. Does not inhibit the proteinases elastase and
CC       cathepsin G. Is not toxic to mice. {ECO:0000250|UniProtKB:P83952}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18979207}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:18979207}.
CC   -!- SIMILARITY: Belongs to the snake waprin family. {ECO:0000305}.
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DR   EMBL; EU401817; ACC77766.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5L5M9; -.
DR   SMR; B5L5M9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.75.10; -; 1.
DR   InterPro; IPR036645; Elafin-like_sf.
DR   InterPro; IPR008197; WAP_dom.
DR   Pfam; PF00095; WAP; 1.
DR   PRINTS; PR00003; 4DISULPHCORE.
DR   SMART; SM00217; WAP; 1.
DR   SUPFAM; SSF57256; SSF57256; 1.
DR   PROSITE; PS51390; WAP; 1.
PE   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..74
FT                   /note="Omwaprin-c"
FT                   /id="PRO_5000395617"
FT   DOMAIN          27..71
FT                   /note="WAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        34..59
FT                   /evidence="ECO:0000250|UniProtKB:P83952"
FT   DISULFID        42..63
FT                   /evidence="ECO:0000250|UniProtKB:P83952"
FT   DISULFID        46..58
FT                   /evidence="ECO:0000250|UniProtKB:P83952"
FT   DISULFID        52..67
FT                   /evidence="ECO:0000250|UniProtKB:P83952"
SQ   SEQUENCE   74 AA;  8148 MW;  B85B76E7A60FA88F CRC64;
     MSSGGLLLLL GLLTLWAEVT PISGQDRPKK PGLCPPRPQK PCVKECKNDW SCPGQQKCCN
     YGCIDECRDP IFVN