WAP1_ERYPO
ID WAP1_ERYPO Reviewed; 60 AA.
AC A7X4L4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Waprin-Lio1;
DE Flags: Precursor; Fragment;
OS Erythrolamprus poecilogyrus (Water snake) (Liophis poecilogyrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Dipsadidae; Erythrolamprus.
OX NCBI_TaxID=338838;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=17855442; DOI=10.1074/mcp.m700094-mcp200;
RA Fry B.G., Scheib H., van der Weerd L., Young B., McNaughtan J.,
RA Ramjan S.F.R., Vidal N., Poelmann R.E., Norman J.A.;
RT "Evolution of an arsenal: structural and functional diversification of the
RT venom system in the advanced snakes (Caenophidia).";
RL Mol. Cell. Proteomics 7:215-246(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU029744; ABU68544.1; -; mRNA.
DR AlphaFoldDB; A7X4L4; -.
DR SMR; A7X4L4; -.
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 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..8
FT /evidence="ECO:0000305"
FT CHAIN 9..60
FT /note="Waprin-Lio1"
FT /id="PRO_0000314686"
FT DOMAIN 9..59
FT /note="WAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 16..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 29..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 33..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 39..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT NON_TER 1
SQ SEQUENCE 60 AA; 6381 MW; 152BEA9D5CACBFB2 CRC64;
MLLGTTSAQV VRPGSCPNVD VPIPPLGLCR TTCQTDANCQ EGRKCCKNGC GFMTCETARF