ID   VKT3L_BUNMU             Reviewed;          83 AA.
AC   B4ESA4;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Kunitz-type serine protease inhibitor PILP-3;
DE   AltName: Full=Protease inhibitor-like protein 3;
DE   Flags: Precursor;
OS   Bungarus multicinctus (Many-banded krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   TISSUE=Liver;
RX   PubMed=18471842; DOI=10.1016/j.toxicon.2008.03.025;
RA   Chang L.-S., Wang J.-J., Cheng Y.-C., Chou W.-M.;
RT   "Genomic DNAs encoding Bungarus multicinctis protease inhibitor-like
RT   proteins.";
RL   Toxicon 51:1490-1495(2008).
RN   [2]
RP   FUNCTION.
RX   PubMed=19706303; DOI=10.1016/j.toxicon.2009.08.012;
RA   Chou W.M., Liu W.H., Chen K.C., Chang L.S.;
RT   "Structure-function studies on inhibitory activity of Bungarus multicinctus
RT   protease inhibitor-like protein on matrix metalloprotease-2, and invasion
RT   and migration of human neuroblastoma SK-N-SH cells.";
RL   Toxicon 55:353-360(2010).
CC   -!- FUNCTION: Binds and inhibits MMP-2 and shows an activity in inhibiting
CC       migration and invasion of neuroblastoma. Intact C-terminus is crucial
CC       to the activities of this protein (PubMed:19706303).
CC       {ECO:0000269|PubMed:18471842, ECO:0000269|PubMed:19706303}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not inhibit chymotrypsin or trypsin.
CC       {ECO:0000305|PubMed:18471842}.
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; AM939783; CAP74383.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4ESA4; -.
DR   SMR; B4ESA4; -.
DR   MEROPS; I02.031; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Disulfide bond; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW   Protease inhibitor; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..83
FT                   /note="Kunitz-type serine protease inhibitor PILP-3"
FT                   /id="PRO_5000388069"
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 chymotrypsin"
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;  9227 MW;  811FF9D23DA533F1 CRC64;
     MSSGGLLLLL GLLTLWAELT PVSSRKRHQF CNVPPEPGRC NANVRAFYYN PRLRKCIEFS
     YGGCGGNANN FKSRGECKRT CAE