ID   HIRPA_HIRME             Reviewed;          66 AA.
AC   P09944;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Hirudin-PA;
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 SULFATION AT TYR-64.
RX   PubMed=3768144; DOI=10.1515/bchm3.1986.367.2.803;
RA   Dodt J., Machleidt W., Seemueller U., Maschler R., Fritz H.;
RT   "Isolation and characterization of hirudin isoinhibitors and sequence
RT   analysis of hirudin PA.";
RL   Biol. Chem. Hoppe-Seyler 367:803-811(1986).
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   PIR; A24350; A24350.
DR   PDB; 1IHT; X-ray; 2.10 A; I=55-60.
DR   PDBsum; 1IHT; -.
DR   AlphaFoldDB; P09944; -.
DR   SMR; P09944; -.
DR   Allergome; 9843; Hir me Hirudin.
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   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Protease inhibitor; Secreted; Serine protease inhibitor; Sulfation.
FT   CHAIN           1..66
FT                   /note="Hirudin-PA"
FT                   /id="PRO_0000195640"
FT   REGION          1..3
FT                   /note="Interaction with thrombin active site"
FT                   /evidence="ECO:0000250"
FT   REGION          39..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..66
FT                   /note="Interaction with fibrinogen-binding exosite of
FT                   thrombin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         64
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:3768144"
FT   CARBOHYD        45
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        6..14
FT                   /evidence="ECO:0000250"
FT   DISULFID        16..28
FT                   /evidence="ECO:0000250"
FT   DISULFID        22..39
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   66 AA;  7026 MW;  FA1B80B7F4FEA317 CRC64;
     ITYTDCTESG QNLCLCEGSN VCGKGNKCIL GSQGKDNQCV TGEGTPKPQS HNQGDFEPIP
     EDAYDE