ID   WAPA_DEMVE              Reviewed;          74 AA.
AC   B5L5P8; B5L5M6;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Veswaprin-a;
DE   Flags: Precursor;
OS   Demansia vestigiata (Lesser black whip snake) (Demansia atra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Notechinae; Demansia.
OX   NCBI_TaxID=412038;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   St Pierre L.;
RT   "Waprins: a distinct toxin family from the venom of Australian Elapid
RT   snakes.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Damages membranes of susceptible bacteria. Has no hemolytic
CC       activity. Not toxic to mice. Does not inhibit the proteinases elastase
CC       and cathepsin G. {ECO:0000250|UniProtKB:P83952}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the snake waprin family. {ECO:0000305}.
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DR   EMBL; EU401836; ACC77785.1; -; Genomic_DNA.
DR   EMBL; EU401814; ACC77763.1; -; mRNA.
DR   AlphaFoldDB; B5L5P8; -.
DR   SMR; B5L5P8; -.
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   2: Evidence at transcript level;
KW   Antibiotic; Antimicrobial; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..74
FT                   /note="Veswaprin-a"
FT                   /id="PRO_5000395636"
FT   DOMAIN          27..71
FT                   /note="WAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        34..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        42..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        46..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        52..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   CONFLICT        17..25
FT                   /note="AEVTPISGQ -> EVLTPVSSK (in Ref. 2; ACC77763)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   74 AA;  8148 MW;  B85B76E7A60FA88F CRC64;
     MSSGGLLLLL GLLTLWAEVT PISGQDRPKK PGLCPPRPQK PCVKECKNDW SCPGQQKCCN
     YGCIDECRDP IFVN