ID   HIRM1_POEMA             Reviewed;          84 AA.
AC   Q07558;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Hirudin-HM1;
DE   Flags: Precursor;
OS   Poecilobdella manillensis (Mexican medical leech) (Hirudinaria
OS   manillensis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Poecilobdella.
OX   NCBI_TaxID=1348078;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-84.
RX   PubMed=7685281; DOI=10.1111/j.1432-1033.1993.tb17924.x;
RA   Scacheri E., Nitti G., Valsasina B., Orsini G., Visco C., Ferrera M.,
RA   Sawyer R.T., Sarmientos P.;
RT   "Novel hirudin variants from the leech Hirudinaria manillensis. Amino acid
RT   sequence, cDNA cloning and genomic organization.";
RL   Eur. J. Biochem. 214:295-304(1993).
CC   -!- FUNCTION: Hirudin is a potent thrombin-specific protease inhibitor. It
CC       forms a stable non-covalent complex with alpha-thrombin, thereby
CC       abolishing its ability to cleave fibrinogen.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I14 (hirudin) family.
CC       {ECO:0000305}.
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DR   EMBL; X72785; CAA51292.1; -; Genomic_DNA.
DR   PIR; S33328; S33328.
DR   AlphaFoldDB; Q07558; -.
DR   SMR; Q07558; -.
DR   MEROPS; I14.001; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.10.10; -; 1.
DR   InterPro; IPR024793; Hirudin.
DR   InterPro; IPR011061; Hirudin/antistatin.
DR   InterPro; IPR000429; Prot_inh_hirudin.
DR   Pfam; PF00713; Hirudin; 1.
DR   PIRSF; PIRSF001640; Hirudin; 1.
DR   PRINTS; PR00777; HIRUDIN.
DR   SUPFAM; SSF57262; SSF57262; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:7685281"
FT   CHAIN           21..84
FT                   /note="Hirudin-HM1"
FT                   /id="PRO_0000013442"
FT   REGION          21..23
FT                   /note="Interaction with thrombin active site"
FT                   /evidence="ECO:0000250"
FT   REGION          59..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..84
FT                   /note="Interaction with fibrinogen-binding exosite of
FT                   thrombin"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        63
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        26..34
FT                   /evidence="ECO:0000250"
FT   DISULFID        36..48
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..57
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   84 AA;  8934 MW;  3AD737E7D72D4C1D CRC64;
     MFSLKLFVVF LAVCICVSQA VSYTDCTESG QNYCLCVGGN LCGGGKHCEM DGSGNKCVDG
     EGTPKPKSQT EGDFEEIPDE DILN