ID   VKT2_PSERS              Reviewed;          83 AA.
AC   E7FL12;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Kunitz serine protease inhibitor Pr-mulgin 2;
DE   Flags: Precursor;
OS   Pseudechis rossignolii (Papuan pigmy mulga snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudechis.
OX   NCBI_TaxID=1489342;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=22024014; DOI=10.1016/j.toxicon.2011.10.005;
RA   Inagaki H., Kimoto H., Yamauchi Y., Toriba M., Kubo T.;
RT   "Functional characterization of Kunitz-type protease inhibitor Pr-mulgins
RT   identified from New Guinean Pseudechis australis.";
RL   Toxicon 59:74-80(2012).
CC   -!- FUNCTION: Serine protease inhibitor that acts against trypsin
CC       (EC(50)=10 nM, Ki=5nM), chymotrypsin (EC(50)=100 nM, Ki=40 nM), and
CC       plasmin (EC(50)=100 nM, Ki=40 nM). {ECO:0000269|PubMed:22024014}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not inhibit serine proteases (elastase, kallikrein,
CC       and pepsin), cysteine protease (cathepsin G), and MMP (1, 3, 7, 8, 9,
CC       10, 12, 13, and 14), as well as voltage-gated potassium channels
CC       (Shaker and rKv1.1/KCNA1). {ECO:0000305|PubMed:22024014}.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; AB576155; BAJ76675.1; -; mRNA.
DR   AlphaFoldDB; E7FL12; -.
DR   SMR; E7FL12; -.
DR   MEROPS; I02.052; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin 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; Toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..83
FT                   /note="Kunitz serine protease inhibitor Pr-mulgin 2"
FT                   /id="PRO_0000429463"
FT   DOMAIN          31..81
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            41..42
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        40..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        56..77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   83 AA;  9241 MW;  E374BF41DA63EEB2 CRC64;
     MSSGGLLLLL GLLTLWEGLT PVSSKDRPHF CHLPHDPGPC KGNFQAFYYH PVRRTCLEFI
     YGGCQGNPNN FKTIDECKRT CAA