ID   PIGU_HIRNI              Reviewed;          48 AA.
AC   P81499;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Piguamerin;
OS   Hirudo nipponia (Korean blood-sucking leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Hirudo.
OX   NCBI_TaxID=42736;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=9688284; DOI=10.1046/j.1432-1327.1998.2540692.x;
RA   Kim D.R., Kang K.W.;
RT   "Amino acid sequence of piguamerin, an antistasin-type protease inhibitor
RT   from the blood sucking leech Hirudo nipponia.";
RL   Eur. J. Biochem. 254:692-697(1998).
CC   -!- FUNCTION: Inhibits plasma and tissue kallikrein, and trypsin. May be
CC       involved in leech hematophagia.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I15 (antistasin) family.
CC       {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   AlphaFoldDB; P81499; -.
DR   SMR; P81499; -.
DR   MEROPS; I15.001; -.
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   Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW   Serine protease inhibitor.
FT   CHAIN           1..48
FT                   /note="Piguamerin"
FT                   /id="PRO_0000155197"
FT   DOMAIN          19..47
FT                   /note="Antistasin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00582"
FT   SITE            27..28
FT                   /note="Reactive bond"
FT   DISULFID        3..14
FT                   /evidence="ECO:0000250"
FT   DISULFID        8..19
FT                   /evidence="ECO:0000250"
FT   DISULFID        21..41
FT                   /evidence="ECO:0000250"
FT   DISULFID        26..45
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..47
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   48 AA;  5101 MW;  0331C2D807F32FDC CRC64;
     TDCGGKTCSE AQVCKDGKCV CVIGQCRKYC PNGFKKDENG CTFPCTCA