ID   VKT1_PHIOL              Reviewed;          98 AA.
AC   A7X3V7;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Kunitz-type serine protease inhibitor kunitoxin-Phi1;
DE   Flags: Precursor;
OS   Philodryas olfersii (Green snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Dipsadidae; Philodryas.
OX   NCBI_TaxID=120305;
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: Serine protease inhibitor. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type 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; EU029688; ABU68488.1; -; mRNA.
DR   AlphaFoldDB; A7X3V7; -.
DR   SMR; A7X3V7; -.
DR   MEROPS; I02.022; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00109; KU; 1.
DR   Gene3D; 4.10.410.10; -; 1.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57362; SSF57362; 1.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Protease inhibitor; Secreted; Serine protease inhibitor;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..98
FT                   /note="Kunitz-type serine protease inhibitor kunitoxin-
FT                   Phi1"
FT                   /id="PRO_0000377475"
FT   DOMAIN          39..89
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            49..50
FT                   /note="Reactive bond for chymotrypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        48..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        64..85
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   98 AA;  11021 MW;  FBC6DC70E8A4BFE6 CRC64;
     MWARVLLLGV LLSLLADLHA ASGGDAGGQK TWNPRISDCE LPPEKGPCNN LELRWFYNLK
     SKRCERFFYG GCYGNANNFK EINECDRRCV SPDINKPG