ID   VPI_MESMA               Reviewed;          89 AA.
AC   Q86RQ7; Q95P91;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Venom peptide BmKAPI {ECO:0000303|PubMed:12457884};
DE   AltName: Full=Ascaris-type protease inhibitor {ECO:0000305};
DE            Short=BmAPI;
DE   AltName: Full=Putative anticoagulant peptide BmAP1;
DE   Flags: Precursor;
OS   Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX   NCBI_TaxID=34649;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=12457884; DOI=10.1016/s0041-0101(02)00134-4;
RA   Zeng X.-C., Wang S.-X., Li W.-X.;
RT   "Identification of BmKAPi, a novel type of scorpion venom peptide with
RT   peculiar disulfide bridge pattern from Buthus martensii Karsch.";
RL   Toxicon 40:1719-1722(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=11923087; DOI=10.1016/s1096-4959(02)00020-9;
RA   Zhu S.-Y., Li W.-X.;
RT   "Precursors of three unique cysteine-rich peptides from the scorpion Buthus
RT   martensii Karsch.";
RL   Comp. Biochem. Physiol. 131B:749-756(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 23-89.
RC   TISSUE=Venom gland;
RX   PubMed=23533574; DOI=10.1371/journal.pone.0057529;
RA   Chen Z., Wang B., Hu J., Yang W., Cao Z., Zhuo R., Li W., Wu Y.;
RT   "SjAPI, the first functionally characterized Ascaris-type protease
RT   inhibitor from animal venoms.";
RL   PLoS ONE 8:E57529-E57529(2013).
CC   -!- FUNCTION: Serine protease inhibitor. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12457884}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:12457884}.
CC   -!- SIMILARITY: Belongs to the serine protease inhibitor-like (TIL domain-
CC       containing) family. {ECO:0000305}.
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DR   EMBL; AF462308; AAO26744.1; -; mRNA.
DR   EMBL; AF155367; AAK61817.1; -; mRNA.
DR   AlphaFoldDB; Q86RQ7; -.
DR   SMR; Q86RQ7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   Pfam; PF01826; TIL; 1.
DR   SUPFAM; SSF57567; SSF57567; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Protease inhibitor; Secreted; Serine protease inhibitor;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..89
FT                   /note="Venom peptide BmKAPI"
FT                   /id="PRO_0000034313"
FT   DOMAIN          28..86
FT                   /note="TIL"
FT   DISULFID        28..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        37..62
FT                   /evidence="ECO:0000250"
FT   DISULFID        41..55
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..86
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..80
FT                   /evidence="ECO:0000250"
FT   CONFLICT        31
FT                   /note="N -> D (in Ref. 2; AAK61817)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   89 AA;  10104 MW;  40986883CA294BFB CRC64;
     MKFVFASFAL FVIFLCFSQS LSQSYFRCRD NEVFDNCISN CGPPRCSNIL NTYPCTNLGP
     LCTPGCKCKD GRVYDNQGRC VLQTECFQK