ID   BDEL_HIRME              Reviewed;          59 AA.
AC   P82107;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Bdellastasin;
DE   AltName: Full=Bdellin A;
OS   Hirudo medicinalis (Medicinal leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Hirudo.
OX   NCBI_TaxID=6421;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RX   PubMed=9578479; DOI=10.1046/j.1432-1327.1998.2530212.x;
RA   Moser M., Auerswald E., Mentele R., Eckerskorn C., Fritz H., Fink E.;
RT   "Bdellastasin, a serine protease inhibitor of the antistasin family from
RT   the medical leech (Hirudo medicinalis). Primary structure, expression in
RT   yeast, and characterization of native and recombinant inhibitor.";
RL   Eur. J. Biochem. 253:212-220(1998).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-59 OF COMPLEX WITH PIG TRYPSIN.
RX   PubMed=10771427; DOI=10.1107/s0907444900003048;
RA   Rester U., Moser M., Huber R., Bode W.;
RT   "L-isoaspartate 115 of porcine beta-trypsin promotes crystallization of its
RT   complex with bdellastasin.";
RL   Acta Crystallogr. D 56:581-588(2000).
CC   -!- FUNCTION: Strong inhibitor of mammalian trypsin, plasmin and acrosin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MASS SPECTROMETRY: Mass=6332.6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9578479};
CC   -!- SIMILARITY: Belongs to the protease inhibitor I15 (antistasin) family.
CC       {ECO:0000305}.
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DR   PDB; 1C9P; X-ray; 2.80 A; B=1-59.
DR   PDB; 1C9T; X-ray; 3.30 A; G/H/I/J/K/L=1-59.
DR   PDB; 1EJA; X-ray; 2.70 A; B=1-59.
DR   PDBsum; 1C9P; -.
DR   PDBsum; 1C9T; -.
DR   PDBsum; 1EJA; -.
DR   AlphaFoldDB; P82107; -.
DR   SMR; P82107; -.
DR   EvolutionaryTrace; P82107; -.
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; IPR004094; Antistasin-like.
DR   InterPro; IPR011061; Hirudin/antistatin.
DR   Pfam; PF02822; Antistasin; 1.
DR   SUPFAM; SSF57262; SSF57262; 1.
DR   PROSITE; PS51252; ANTISTASIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Secreted; Serine protease inhibitor.
FT   CHAIN           1..59
FT                   /note="Bdellastasin"
FT                   /id="PRO_0000155195"
FT   DOMAIN          28..54
FT                   /note="Antistasin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT   SITE            34..35
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   DISULFID        10..21
FT   DISULFID        15..26
FT   DISULFID        28..48
FT   DISULFID        33..52
FT   DISULFID        37..54
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:1EJA"
FT   STRAND          13..15
FT                   /evidence="ECO:0007829|PDB:1EJA"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:1EJA"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:1EJA"
FT   STRAND          31..34
FT                   /evidence="ECO:0007829|PDB:1EJA"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:1C9P"
FT   STRAND          49..54
FT                   /evidence="ECO:0007829|PDB:1C9P"
SQ   SEQUENCE   59 AA;  6343 MW;  43BA5BB2D0E403A9 CRC64;
     FDVNSHTTPC GPVTCSGAQM CEVDKCVCSD LHCKVKCEHG FKKDDNGCEY ACICADAPQ