ID   VKT1_PSERS              Reviewed;          83 AA.
AC   E7FL11;
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 1;
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], FUNCTION, AND MUTAGENESIS OF 73-THR--GLY-75.
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: Specifically inhibits MMP2 activity (EC(50)=100 nM and Ki=60
CC       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 (trypsin,
CC       chymotrypsin, elastase, kallikrein, plasmin and pepsin), cysteine
CC       protease (cathepsin G), and MMP (1, 3, 7, 8, 9, 10, 12, 13, and 14), as
CC       well as voltage-gated potassium channels (Shaker, Shal, Shaw, and
CC       rKv1.1/KCNA1). {ECO:0000305|PubMed:22024014}.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; AB576154; BAJ76674.1; -; mRNA.
DR   AlphaFoldDB; E7FL11; -.
DR   SMR; E7FL11; -.
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   1: Evidence at protein 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 1"
FT                   /id="PRO_0000429462"
FT   DOMAIN          31..81
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
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"
FT   MUTAGEN         73..75
FT                   /note="TIE->SRG: Decrease in inhibitory activity on MMP-2."
FT                   /evidence="ECO:0000269|PubMed:22024014"
SQ   SEQUENCE   83 AA;  9232 MW;  61138BA35408EF75 CRC64;
     MSSGGLLLLL GLLTLWEVLT PVSSKDRPRF CELPADPGPC NGLFQAFYYN PVQRKCLKFR
     YGGCKGNPNT FKTIEECKRT CAA